|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
485-782 |
1.92e-46 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 168.21 E-value: 1.92e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 485 ASLGHSEADRQLLEAAKAGDVETVKKLCTVQSVNCRDIEGRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLH 564
Cdd:COG0666 13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 565 NACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDLvkdgdtdiqdllr 644
Cdd:COG0666 93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL------------- 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 645 gdaalldAAKKGCLARVKKL-SSPDNVNCRDTQGRhsTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYG 723
Cdd:COG0666 160 -------AAANGNLEIVKLLlEAGADVNARDNDGE--TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENG 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 755563780 724 HVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPL 782
Cdd:COG0666 231 NLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
60-343 |
2.62e-43 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 159.35 E-value: 2.62e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 60 TPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLQHGADPNARDNWNYTPLHEAAIKGKIDV 139
Cdd:COG0666 56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 140 CIVLLQHGAEPTIRNTDGRTaldladpsakavltgdykkdellesarsgneekmmalltplnvnchasdgrkstPLHLAA 219
Cdd:COG0666 136 VKLLLEAGADVNAQDNDGNT------------------------------------------------------PLHLAA 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 220 GYNRVKIVQLLLHHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRIEVCSLLLSY 299
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....
gi 755563780 300 GADPTLLNCHNKSAIDLAPTAQLKERLSYEFKGHSLLQAAREAD 343
Cdd:COG0666 242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
25-307 |
2.84e-42 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 156.27 E-value: 2.84e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 25 ARELFEACRNGDVERVKRLVTPEKVNSRDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHA 104
Cdd:COG0666 54 GALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 105 EVVNLLLQHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRtaldladpsakavltgdykkdelles 184
Cdd:COG0666 134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE-------------------------- 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 185 arsgneekmmalltplnvnchasdgrksTPLHLAAGYNRVKIVQLLLHHGADVHAKDKGDLVPLHNACSYGHYEVTELLV 264
Cdd:COG0666 188 ----------------------------TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 755563780 265 KHGACVNAMDLWQFTPLHEAASKNRIEVCSLLLSYGADPTLLN 307
Cdd:COG0666 240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
528-784 |
8.28e-42 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 154.73 E-value: 8.28e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 528 TPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEI 607
Cdd:COG0666 23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 608 CKLLLQHGADPTKKNRDGNTPLdlvkdgdtdiqdllrgdaalldaakkgclarvkklsspdnvncrdtqgrhstplHLAA 687
Cdd:COG0666 103 VKLLLEAGADVNARDKDGETPL------------------------------------------------------HLAA 128
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 688 GYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAH 767
Cdd:COG0666 129 YNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
|
250
....*....|....*..
gi 755563780 768 GADPTLKNQEGQTPLDL 784
Cdd:COG0666 209 GADVNAKDNDGKTALDL 225
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
28-245 |
6.49e-39 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 146.64 E-value: 6.49e-39
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 28 LFEACRNGDVERVKRLVT-PEKVNSRDTAGRksTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEV 106
Cdd:COG0666 91 LHAAARNGDLEIVKLLLEaGADVNARDKDGE--TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 107 VNLLLQHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLAdpsakavltgdykkdellesAR 186
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA--------------------AE 228
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*....
gi 755563780 187 SGNEEkMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLHHGADVHAKDKGDL 245
Cdd:COG0666 229 NGNLE-IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
347-716 |
1.31e-38 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 145.48 E-value: 1.31e-38
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 347 IKKHLSLEMVNFKHPQTHETALHCAAASPYPKRKQICELLLRKGANTNEKTKEFLTPLHVASENAHNDVVEVVVKHEAKV 426
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 427 NALDSLGQTSLHRAAHCGHLQTCRLLLSYGCDPNIISLQGFTalqmgnenvqqllqegaslghseadrqlleaakagdve 506
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGET-------------------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 507 tvkklctvqsvncrdiegrqstPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVN 586
Cdd:COG0666 123 ----------------------PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 587 VADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDL-VKDGDTDIQDLLRGDAALLDAAKKgclarvkkls 665
Cdd:COG0666 181 ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLaAENGNLEIVKLLLEAGADLNAKDK---------- 250
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|.
gi 755563780 666 spdnvncrdtqgRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPL 716
Cdd:COG0666 251 ------------DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
53-317 |
2.10e-36 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 139.32 E-value: 2.10e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 53 DTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLQHGADPNARDNWNYTPLHEAA 132
Cdd:COG0666 16 LLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAA 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 133 IKGKIDVCIVLLQHGAEPTIRNTDGRTaldladpsakavltgdykkdellesarsgneekmmalltplnvnchasdgrks 212
Cdd:COG0666 96 RNGDLEIVKLLLEAGADVNARDKDGET----------------------------------------------------- 122
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 213 tPLHLAAGYNRVKIVQLLLHHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRIEV 292
Cdd:COG0666 123 -PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201
|
250 260
....*....|....*....|....*
gi 755563780 293 CSLLLSYGADPTLLNCHNKSAIDLA 317
Cdd:COG0666 202 VKLLLEAGADVNAKDNDGKTALDLA 226
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
160-470 |
2.12e-36 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 139.32 E-value: 2.12e-36
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 160 ALDLADPSAKAVLTGDYKKDELLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLHHGADVHA 239
Cdd:COG0666 36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 240 KDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRIEVCSLLLSYGADPTLLNCHNksaidlapt 319
Cdd:COG0666 116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDG--------- 186
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 320 aqlkerlsyefkghsllqaareadvtrikkhlslemvnfkhpqthETALHCAAASpypKRKQICELLLRKGANTNEKTKE 399
Cdd:COG0666 187 ---------------------------------------------ETPLHLAAEN---GHLEIVKLLLEAGADVNAKDND 218
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755563780 400 FLTPLHVASENAHNDVVEVVVKHEAKVNALDSLGQTSLHRAAHCGHLQTCRLLLSYGCDPNIISLQGFTAL 470
Cdd:COG0666 219 GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
494-784 |
1.36e-30 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 126.68 E-value: 1.36e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 494 RQLLEAAKAgDVETVKKLC-TVQSVNCRDIEGRqsTPLHFAAGYN---RVSVVEYLLQHGADVHAKDKGGLVPLH----N 565
Cdd:PHA03095 17 DYLLNASNV-TVEEVRRLLaAGADVNFRGEYGK--TPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHlylyN 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 566 ACSYghyEVAELLVKHGAVVNVADLWKFTPLHeAAAKGK---YEICKLLLQHGADPTKKNRDGNTPLD-LVKDGDTDIqD 641
Cdd:PHA03095 94 ATTL---DVIKLLIKAGADVNAKDKVGRTPLH-VYLSGFninPKVIRLLLRKGADVNALDLYGMTPLAvLLKSRNANV-E 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 642 LLRgdaALLDAakkGCLARVKKLsspdnvncrdtqgRHSTPLHLAAGY--NNLEVAEYLLQHGADVNAQDKGGLIPLHNA 719
Cdd:PHA03095 169 LLR---LLIDA---GADVYAVDD-------------RFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSM 229
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755563780 720 ASYG---HVDVAALLIKyNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDL 784
Cdd:PHA03095 230 ATGSsckRSLVLPLLIA-GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSL 296
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
73-458 |
2.03e-30 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 128.26 E-value: 2.03e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 73 VVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLQHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAE--- 149
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNink 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 150 ------PTIRNTDGRTALDLADPSAKAVLTGDYKKDELLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAA--GY 221
Cdd:PHA02876 240 ndlsllKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAknGY 319
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 222 NRVKIvQLLLHHGADVHAKDKGDLVPLHNACSYGHYEVTEL-LVKHGACVNAMDLWQFTPLHEAASKNRIEVCSLLLSYG 300
Cdd:PHA02876 320 DTENI-RTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 301 ADPTLLNchnksaidlaptaqlkerlsyefkghsllqaareadvtrikkhlslemvnfkhpQTHETALHCA--AASPYPK 378
Cdd:PHA02876 399 ADIEALS------------------------------------------------------QKIGTALHFAlcGTNPYMS 424
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 379 RKQicelLLRKGANTNEKTKEFLTPLHVA-SENAHNDVVEVVVKHEAKVNALDSLGQTSLHRAahCGHLQTCRLLLSYGC 457
Cdd:PHA02876 425 VKT----LIDRGANVNSKNKDLSTPLHYAcKKNCKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGA 498
|
.
gi 755563780 458 D 458
Cdd:PHA02876 499 E 499
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
191-629 |
1.56e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 119.29 E-value: 1.56e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 191 EKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLHHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACV 270
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 271 NAMDLWQFTPLHEAASKNRIEVCSLLLSYGADPtllnchnksaidlaptaqlkerlsyefkghsllqaareadvtrikkh 350
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV----------------------------------------------- 113
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 351 lslemvnfkhpqthetalhcaaaspypkrkqicelllrkgantNEKTKEFLTPLHVASENAHNDVVEVVVKHEAKVNALD 430
Cdd:COG0666 114 -------------------------------------------NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQD 150
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 431 SLGQTSLHRAAHCGHLQTCRLLLSYGCDPNIislqgftalqmgnenvqqllqegaslghseadrqlleaakagdvetvkk 510
Cdd:COG0666 151 NDGNTPLHLAAANGNLEIVKLLLEAGADVNA------------------------------------------------- 181
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 511 lctvqsvncRDIEGRqsTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADL 590
Cdd:COG0666 182 ---------RDNDGE--TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
|
410 420 430
....*....|....*....|....*....|....*....
gi 755563780 591 WKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPL 629
Cdd:COG0666 251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
525-743 |
1.70e-29 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 122.47 E-value: 1.70e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 525 RQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHY-----EVAELLVKHGAVVNVADLWKFTPLHEA 599
Cdd:PHA03100 34 KPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 600 AAK--GKYEICKLLLQHGADPTKKNRDGNTPLDLVKDG---DTDIQDLLRGDAALLDAAKkgclaRVKKL-SSPDNVNCR 673
Cdd:PHA03100 114 ISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESnkiDLKILKLLIDKGVDINAKN-----RVNYLlSYGVPINIK 188
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 674 DTQGrhSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDK 743
Cdd:PHA03100 189 DVYG--FTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
378-782 |
3.45e-29 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 124.41 E-value: 3.45e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 378 KRKQICELLLRKGANTNE----KTKEFLTPLHVASENAHND---VVEVVVKHEAKVNALDSLGQTSLHRAAHCGHLQTCR 450
Cdd:PHA02876 116 KLDEACIHILKEAISGNDihydKINESIEYMKLIKERIQQDellIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVN 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 451 LLLSYGCDPNIISLQGFTALQMGN-----ENVQQLLQEGASLghSEADRQLLEAAKAGDVETVKKLCTVQ-SVNcrDIEG 524
Cdd:PHA02876 196 LLLSYGADVNIIALDDLSVLECAVdskniDTIKAIIDNRSNI--NKNDLSLLKAIRNEDLETSLLLYDAGfSVN--SIDD 271
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 525 RQSTPLHFAAGYNRVS-VVEYLLQHGADVHAKDKGGLVPLHNACSYGH-YEVAELLVKHGAVVNVADLWKFTPLHEAAAK 602
Cdd:PHA02876 272 CKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTL 351
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 603 GKY-EICKLLLQHGAdptkknrdgntpldlvkdgdtdiqdllrgdaalldaakkgclarvkklsspdNVNCRDTQGRhsT 681
Cdd:PHA02876 352 DRNkDIVITLLELGA----------------------------------------------------NVNARDYCDK--T 377
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 682 PLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAAsYGHVDVAAL--LIKYNACVNATDKWAFTPLHEAAQKG-RT 758
Cdd:PHA02876 378 PIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL-CGTNPYMSVktLIDRGANVNSKNKDLSTPLHYACKKNcKL 456
|
410 420
....*....|....*....|....
gi 755563780 759 QLCALLLAHGADPTLKNQEGQTPL 782
Cdd:PHA02876 457 DVIEMLLDNGADVNAINIQNQYPL 480
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
382-722 |
3.48e-26 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 112.75 E-value: 3.48e-26
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 382 ICELLLRKGANTNEKTKEFLTPLHVASENAHNDVVEVVVKHEAKVNALDSLGQTSLHRAAHCGHLQTCRLLLSYGCDPNI 461
Cdd:PHA02874 17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 462 ISLQgftalQMGNENVQQLLQEGAslghseadrqlleaakagdvetvkklctvqSVNCRDIEGRqsTPLHFAAGYNRVSV 541
Cdd:PHA02874 97 LPIP-----CIEKDMIKTILDCGI------------------------------DVNIKDAELK--TFLHYAIKKGDLES 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 542 VEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKK 621
Cdd:PHA02874 140 IKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK 219
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 622 NRDGNTPLDLVKDGDTDIQDLLRGDAAlldaakkgclarvkklsspdnVNCRDTQGrhSTPLHLAAGYN-NLEVAEYLLQ 700
Cdd:PHA02874 220 CKNGFTPLHNAIIHNRSAIELLINNAS---------------------INDQDIDG--STPLHHAINPPcDIDIIDILLY 276
|
330 340
....*....|....*....|..
gi 755563780 701 HGADVNAQDKGGLIPLHNAASY 722
Cdd:PHA02874 277 HKADISIKDNKGENPIDTAFKY 298
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
259-652 |
2.16e-25 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 112.46 E-value: 2.16e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 259 VTELLVKHGACVNAMDLWQFTPLHEAASKNRIEVCSLLLSYGADPTLLNCHNKSAIDLAPTAQ--------LKERLSYEF 330
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKnidtikaiIDNRSNINK 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 331 KGHSLLQAAREADV-TRIKKHLSLEMVNfKHPQTHETALHCAAASPYPKRkqICELLLRKGANTNEKTKEFLTPLHVASE 409
Cdd:PHA02876 240 NDLSLLKAIRNEDLeTSLLLYDAGFSVN-SIDDCKNTPLHHASQAPSLSR--LVPKLLERGADVNAKNIKGETPLYLMAK 316
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 410 NAHN-DVVEVVVKHEAKVNALDSLGQTSLHRAahcghlqtcrlllsygcdpniislqgfTALQMGNENVQQLLQEGASlg 488
Cdd:PHA02876 317 NGYDtENIRTLIMLGADVNAADRLYITPLHQA---------------------------STLDRNKDIVITLLELGAN-- 367
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 489 hseadrqlleaakagdvetvkklctvqsVNCRDIegRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNA-C 567
Cdd:PHA02876 368 ----------------------------VNARDY--CDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlC 417
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 568 SYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKG-KYEICKLLLQHGADPTKKNRDGNTPLDLVKDGDTDIQDLLRGD 646
Cdd:PHA02876 418 GTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGIVNILLHYG 497
|
....*.
gi 755563780 647 AALLDA 652
Cdd:PHA02876 498 AELRDS 503
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
57-358 |
2.96e-25 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 109.75 E-value: 2.96e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 57 RKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHA-----EVVNLLLQHGADPNARDNWNYTPLHEA 131
Cdd:PHA03100 34 KPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYA 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 132 AIKGKIDVCIV--LLQHGAeptirntdgrtaldladpsakavltgdykkdellesarsgneekmmalltplNVNCHASDG 209
Cdd:PHA03100 114 ISKKSNSYSIVeyLLDNGA----------------------------------------------------NVNIKNSDG 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 210 RksTPLHLAAGYNRV--KIVQLLLHHGADVHAKDKgdlvplhnacsyghyevTELLVKHGACVNAMDLWQFTPLHEAASK 287
Cdd:PHA03100 142 E--NLLHLYLESNKIdlKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYN 202
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755563780 288 NRIEVCSLLLSYGADPTLLNCHNKSAIDLAptaqLKERLSYEFKghSLLQAAreADVTRIKKHLSLEMVNF 358
Cdd:PHA03100 203 NNPEFVKYLLDLGANPNLVNKYGDTPLHIA----ILNNNKEIFK--LLLNNG--PSIKTIIETLLYFKDKD 265
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
207-472 |
3.59e-25 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 109.37 E-value: 3.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 207 SDGRKSTPLHLAAGYNRVKIVQLLLHHGADVHAKDKGDLVPLHNACSYGHY-----EVTELLVKHGACVNAMDLWQFTPL 281
Cdd:PHA03100 31 SYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPL 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 282 HEAASK--NRIEVCSLLLSYGADPTLLNCHNksaidlaptaqlkerlsyefkghsllqaareadvtrikkhlslemvnfk 359
Cdd:PHA03100 111 LYAISKksNSYSIVEYLLDNGANVNIKNSDG------------------------------------------------- 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 360 hpqthETALHCAAASPYPKRKqICELLLRKGANTNEKTKefltplhvasenahndvVEVVVKHEAKVNALDSLGQTSLHR 439
Cdd:PHA03100 142 -----ENLLHLYLESNKIDLK-ILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHY 198
|
250 260 270
....*....|....*....|....*....|...
gi 755563780 440 AAHCGHLQTCRLLLSYGCDPNIISLQGFTALQM 472
Cdd:PHA03100 199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI 231
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
29-317 |
7.59e-25 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 108.96 E-value: 7.59e-25
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 29 FEACRNGDVERVKRLV-TPEKVNSRDTAGRksTPLHFAAGFG---RKDVVEYLLQNGANVQARDDGGLIPLH----NACS 100
Cdd:PHA03095 19 LLNASNVTVEEVRRLLaAGADVNFRGEYGK--TPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHlylyNATT 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 101 fghAEVVNLLLQHGADPNARDNWNYTPLHeAAIKGK-IDVCIV--LLQHGAEPTIRNTDGRTALDLadpsakavltgdyk 177
Cdd:PHA03095 97 ---LDVIKLLIKAGADVNAKDKVGRTPLH-VYLSGFnINPKVIrlLLRKGADVNALDLYGMTPLAV-------------- 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 178 kdeLLESARSgnEEKMMALLTPLNVNCHASDGRKSTPLHLAAGY--NRVKIVQLLLHHGADVHAKDKGDLVPLHNACSYG 255
Cdd:PHA03095 159 ---LLKSRNA--NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGS 233
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755563780 256 HYEVTEL--LVKHGACVNAMDLWQFTPLHEAASKNRIEVCSLLLSYGADPTLLNCHNKSAIDLA 317
Cdd:PHA03095 234 SCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
502-830 |
3.53e-24 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 106.59 E-value: 3.53e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 502 AGDVETVKKLCTVQSvNCRDIEGRQS-TPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVK 580
Cdd:PHA02874 11 SGDIEAIEKIIKNKG-NCINISVDETtTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 581 HGA-----------------------VVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDL-VKDGD 636
Cdd:PHA02874 90 NGVdtsilpipciekdmiktildcgiDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIaIKHNF 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 637 TDIQDLLrgdaalldaAKKGCLARVKKlsspDNVNcrdtqgrhsTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPL 716
Cdd:PHA02874 170 FDIIKLL---------LEKGAYANVKD----NNGE---------SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL 227
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 717 HNAASYGHvDVAALLIKyNACVNATDKWAFTPLHEAAQ-KGRTQLCALLLAHGADPTLKNQEGQTPLDLVSSLLCR---- 791
Cdd:PHA02874 228 HNAIIHNR-SAIELLIN-NASINDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKdpvi 305
|
330 340 350
....*....|....*....|....*....|....*....
gi 755563780 792 SQICVNHWNRSAFSPLPLRSLTRAVKWKEAKFCPPWIYE 830
Cdd:PHA02874 306 KDIIANAVLIKEADKLKDSDFLEHIEIKDNKEFSDFIKE 344
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
408-735 |
9.26e-24 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 105.88 E-value: 9.26e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 408 SENAHNDVVEVVVKHEAKVNALDSLGQTSLHRAAHCGH---LQTCRLLLSYGCDPNIISLQGFTALQ--MGNENVQQLLQ 482
Cdd:PHA03095 22 ASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHlyLYNATTLDVIK 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 483 egaslghseadrqLLEAAKAgdvetvkklctvqSVNCRDIEGRqsTPLH-FAAGYN-RVSVVEYLLQHGADVHAKDKGGL 560
Cdd:PHA03095 102 -------------LLIKAGA-------------DVNAKDKVGR--TPLHvYLSGFNiNPKVIRLLLRKGADVNALDLYGM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 561 VPLH------NACSyghyEVAELLVKHGAVVNVADLWKFTPLHEAA--AKGKYEICKLLLQHGADPTKKNRDGNTPLDLV 632
Cdd:PHA03095 154 TPLAvllksrNANV----ELLRLLIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSM 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 633 KDG----DTDIQDLLRGDAAlldaakkgclarvkklsspdnVNCRDTQGRhsTPLHLAAGYNNLEVAEYLLQHGADVNAQ 708
Cdd:PHA03095 230 ATGssckRSLVLPLLIAGIS---------------------INARNRYGQ--TPLHYAAVFNNPRACRRLIALGADINAV 286
|
330 340
....*....|....*....|....*..
gi 755563780 709 DKGGLIPLHNAASYGHVDVAALLIKYN 735
Cdd:PHA03095 287 SSDGNTPLSLMVRNNNGRAVRAALAKN 313
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
378-629 |
2.05e-23 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 103.98 E-value: 2.05e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 378 KRKQICELLLRKGANTNEKTKEFLTPLHVASENAHN-----DVVEVVVKHEAKVNALDSLGQTSLHRAA--HCGHLQTCR 450
Cdd:PHA03100 46 RNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVE 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 451 LLLSYGCDPNIISLQGFTALQMgnenvqqllqegaslghseadrqlleaakagdvetvkklctVQSVNCRDIEgrqstpl 530
Cdd:PHA03100 126 YLLDNGANVNIKNSDGENLLHL-----------------------------------------YLESNKIDLK------- 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 531 hfaagynrvsVVEYLLQHGADVHAKDKgglvplhnacsyghyevAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKL 610
Cdd:PHA03100 158 ----------ILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKY 210
|
250
....*....|....*....
gi 755563780 611 LLQHGADPTKKNRDGNTPL 629
Cdd:PHA03100 211 LLDLGANPNLVNKYGDTPL 229
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
530-622 |
1.00e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 90.18 E-value: 1.00e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 530 LHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWkfTPLHEAAAKGKYEICK 609
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR--TALHYAARSGHLEIVK 78
|
90
....*....|...
gi 755563780 610 LLLQHGADPTKKN 622
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
356-653 |
1.40e-21 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 98.94 E-value: 1.40e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 356 VNFKHPQThETALHCAAASPYPKRKQICELLLRKGANTNEKTKEFLTPLHVASENAHN-DVVEVVVKHEAKVNALDSLGQ 434
Cdd:PHA03095 40 VNFRGEYG-KTPLHLYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGR 118
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 435 TSLHraAHCG----HLQTCRLLLSYGCDPNIISLQGFTALQ--MGNENVqqllqegaslghseadrqlleaakagDVETV 508
Cdd:PHA03095 119 TPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNA--------------------------NVELL 170
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 509 KKLCTVQS-VNCRDIEGRqsTPLHFAAGY--NRVSVVEYLLQHGADVHAKDKGGLVPLHNA---CSYGHYEVAELLVKhG 582
Cdd:PHA03095 171 RLLIDAGAdVYAVDDRFR--SLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMatgSSCKRSLVLPLLIA-G 247
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755563780 583 AVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDLVkdgdtdiqdLLRGDAALLDAA 653
Cdd:PHA03095 248 ISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM---------VRNNNGRAVRAA 309
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
401-778 |
1.53e-21 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 99.18 E-value: 1.53e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 401 LTPLHVASENAHNDVVEVVVKHEAKVNALDSLGQTSLHRAahCGHlqtcrlllsygcdPNIISLqgftalqmgnenvQQL 480
Cdd:PHA02878 38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHII--CKE-------------PNKLGM-------------KEM 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 481 LQEGASLGHSEADRQLLEAAKAGDVETVKKLCTVQSVNCRDIEGRQSTPLHFAAGYNrVSVVEYLLQHGADVHAKDK-GG 559
Cdd:PHA02878 90 IRSINKCSVFYTLVAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIE-AEITKLLLSYGADINMKDRhKG 168
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 560 LVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNtpldlvkdgdtdi 639
Cdd:PHA02878 169 NTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGN------------- 235
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 640 qdllrgdaalldaakkgclarvkklsspdnvncrdtqgrhsTPLHLAAGY-NNLEVAEYLLQHGADVNAQDK-GGLIPLH 717
Cdd:PHA02878 236 -----------------------------------------TPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALH 274
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755563780 718 naASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQK------GRTQLCALLLAHGADPTLKNQEG 778
Cdd:PHA02878 275 --SSIKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQylciniGRILISNICLLKRIKPDIKNSEG 339
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
683-775 |
3.56e-21 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 88.63 E-value: 3.56e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 683 LHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWafTPLHEAAQKGRTQLCA 762
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR--TALHYAARSGHLEIVK 78
|
90
....*....|...
gi 755563780 763 LLLAHGADPTLKN 775
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
93-303 |
4.85e-21 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 96.60 E-value: 4.85e-21
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 93 IPLHNACSFGHAEVVNLLLQHGADPNARDNWNYTPLhEAAIKGKIDVCI-VLLQHGAEPTIRNTDGRTALDladpsaKAV 171
Cdd:PHA02875 4 VALCDAILFGELDIARRLLDIGINPNFEIYDGISPI-KLAMKFRDSEAIkLLMKHGAIPDVKYPDIESELH------DAV 76
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 172 LTGDYKKDELLesarsgneekmmalltpLNVNCHASD---GRKSTPLHLAAGYNRVKIVQLLLHHGADVHAKDKGDLVPL 248
Cdd:PHA02875 77 EEGDVKAVEEL-----------------LDLGKFADDvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL 139
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*
gi 755563780 249 HNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRIEVCSLLLSYGADP 303
Cdd:PHA02875 140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
62-154 |
1.52e-20 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 87.09 E-value: 1.52e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 62 LHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLQHgADPNARDNwNYTPLHEAAIKGKIDVCI 141
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 755563780 142 VLLQHGAEPTIRN 154
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
28-161 |
6.85e-20 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 91.17 E-value: 6.85e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 28 LFEACRNGDVERVKRLVtpEK---VNSRDTAGRksTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHA 104
Cdd:COG0666 157 LHLAAANGNLEIVKLLL--EAgadVNARDNDGE--TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNL 232
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 755563780 105 EVVNLLLQHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTAL 161
Cdd:COG0666 233 EIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
21-317 |
2.76e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 91.56 E-value: 2.76e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 21 VEPSARELFEACRNGDVERVKRLVTP-EKVNSRDTagRKSTPLHFAAGFGRKDVVEYLLQNGAnvqardDGGLIPLHNAc 99
Cdd:PHA02874 32 VDETTTPLIDAIRSGDAKIVELFIKHgADINHINT--KIPHPLLTAIKIGAHDIIKLLIDNGV------DTSILPIPCI- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 100 sfgHAEVVNLLLQHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLADPSakavltgdykkd 179
Cdd:PHA02874 103 ---EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKH------------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 180 ellesarsgNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLHHGADVHAKDKGDLVPLHNACSYGHyEV 259
Cdd:PHA02874 168 ---------NFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SA 237
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 755563780 260 TELLVKHgACVNAMDLWQFTPLHEAASKN-RIEVCSLLLSYGADPTLLNCHNKSAIDLA 317
Cdd:PHA02874 238 IELLINN-ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
61-329 |
3.49e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 91.87 E-value: 3.49e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 61 PLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACS----FGHAEVVNLLLQ--------------HGADPNA--- 119
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKepnkLGMKEMIRSINKcsvfytlvaikdafNNRNVEIfki 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 120 ----RDNWNYT----PLHEAAIKGKIDVCIV--LLQHGAEPTIRNTD-GRTALDLADPSAkavltgDYKKDELLesarsg 188
Cdd:PHA02878 120 iltnRYKNIQTidlvYIDKKSKDDIIEAEITklLLSYGADINMKDRHkGNTALHYATENK------DQRLTELL------ 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 189 neekmmaLLTPLNVNchASDGRKSTPLHLAAGYNRVKIVQLLLHHGADVHAKDKGDLVPLHNACSY-GHYEVTELLVKHG 267
Cdd:PHA02878 188 -------LSYGANVN--IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHG 258
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755563780 268 ACVNAMD-LWQFTPLHEAASKNRieVCSLLLSYGADPTLLNCHNKSAIDLAptaqLKERLSYE 329
Cdd:PHA02878 259 VDVNAKSyILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSA----VKQYLCIN 315
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
215-307 |
5.55e-19 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 82.47 E-value: 5.55e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 215 LHLAAGYNRVKIVQLLLHHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHgACVNaMDLWQFTPLHEAASKNRIEVCS 294
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 755563780 295 LLLSYGADPTLLN 307
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
271-614 |
1.39e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 89.94 E-value: 1.39e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 271 NAMDLWQFTPLHEAASKNRIEVCSLLLSYGAD----------PTLLNCH--NKSAIDLAPTAQLKERLSYEFKGHSLLQA 338
Cdd:PHA02878 31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNvnqpdhrdltPLHIICKepNKLGMKEMIRSINKCSVFYTLVAIKDAFN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 339 AREADVTRIkkhlsLEMVNFKHPQTHETALHCAAASPYPKRKQICELLLRKGANTNEKTKEFL-TPLHVASENAHNDVVE 417
Cdd:PHA02878 111 NRNVEIFKI-----ILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTE 185
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 418 VVVKHEAKVNALDSLGQTSLHRAAHcghlqtcrlllsygcdpniislqgftalQMGNENVQQLLQEGASLGHseadrqll 497
Cdd:PHA02878 186 LLLSYGANVNIPDKTNNSPLHHAVK----------------------------HYNKPIVHILLENGASTDA-------- 229
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 498 eaakagdvetvKKLCTvqsvncrdiegrqSTPLHFAAGY-NRVSVVEYLLQHGADVHAKDK-GGLVPLHnaCSYGHYEVA 575
Cdd:PHA02878 230 -----------RDKCG-------------NTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALH--SSIKSERKL 283
|
330 340 350 360
....*....|....*....|....*....|....*....|
gi 755563780 576 ELLVKHGAVVNVADLWKFTPLHEAAAK-GKYEICKLLLQH 614
Cdd:PHA02878 284 KLLLEYGADINSLNSYKLTPLSSAVKQyLCINIGRILISN 323
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
437-629 |
1.95e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 88.89 E-value: 1.95e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 437 LHRAAHC-----GHLQTCRLLLSYGCDPNIISLQGFTALQMG-----NENVQQLLQEGA--SLGHSEADRQLLEAAKAGD 504
Cdd:PHA02875 1 MDQVALCdailfGELDIARRLLDIGINPNFEIYDGISPIKLAmkfrdSEAIKLLMKHGAipDVKYPDIESELHDAVEEGD 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 505 VETVKKLCTVQSVNCRDIEGRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAV 584
Cdd:PHA02875 81 VKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 755563780 585 VNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPL 629
Cdd:PHA02875 161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
222-597 |
3.32e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 88.18 E-value: 3.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 222 NRVKIVQLLLHHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLH----EAASKNR-IEVCSLL 296
Cdd:PHA03100 13 IKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsnIKYNLTDvKEIVKLL 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 297 LSYGADPTllNCHNKSAidlaptaqlkerlsyefkgHSLLQAAreadvtrIKKHLSLEMVnfkhpqthetalhcaaaspy 376
Cdd:PHA03100 93 LEYGANVN--APDNNGI-------------------TPLLYAI-------SKKSNSYSIV-------------------- 124
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 377 pkrkqicELLLRKGANTNEKTKEFLTPLHVASENAHND--VVEVVVKHEAKVNALDSLgqtslhraahcghlqtcRLLLS 454
Cdd:PHA03100 125 -------EYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKNRV-----------------NYLLS 180
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 455 YGCDPNIISLQGFtalqmgnenvqqllqegaslghseadrqlleaakagdvetvkklctvqsvncrdiegrqsTPLHFAA 534
Cdd:PHA03100 181 YGVPINIKDVYGF------------------------------------------------------------TPLHYAV 200
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755563780 535 GYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVAD----LWKFTPLH 597
Cdd:PHA03100 201 YNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIetllYFKDKDLN 267
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
28-121 |
3.77e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.16 E-value: 3.77e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 28 LFEACRNGDVERVKRLVTPEK-VNSRDTAGRksTPLHFAAGFGRKDVVEYLLQNgANVQARDDgGLIPLHNACSFGHAEV 106
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGAdANLQDKNGR--TALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEI 76
|
90
....*....|....*
gi 755563780 107 VNLLLQHGADPNARD 121
Cdd:pfam12796 77 VKLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
561-795 |
7.92e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 86.97 E-value: 7.92e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 561 VPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPL-DLVKDGDT-D 638
Cdd:PHA02875 4 VALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELhDAVEEGDVkA 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 639 IQDLLRGDAALLDAA-KKGclarvkklsspdnvncrdtqgrhSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLH 717
Cdd:PHA02875 84 VEELLDLGKFADDVFyKDG-----------------------MTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLH 140
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 718 NAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPL----------DLVSS 787
Cdd:PHA02875 141 LAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAAlcyaiennkiDIVRL 220
|
....*...
gi 755563780 788 LLCRSQIC 795
Cdd:PHA02875 221 FIKRGADC 228
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
529-814 |
4.12e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 85.32 E-value: 4.12e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 529 PLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYE-VAELLvkhgAVVNVADL-WKFTPLHEAAAKGKYE 606
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLgMKEMI----RSINKCSVfYTLVAIKDAFNNRNVE 115
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 607 ICKLLLqhgADPTKKNRDgntpLDLVKDGDTDIQDLLRGDAALLdaakkgclarvkKLSSPDNVNCRDtQGRHSTPLHLA 686
Cdd:PHA02878 116 IFKIIL---TNRYKNIQT----IDLVYIDKKSKDDIIEAEITKL------------LLSYGADINMKD-RHKGNTALHYA 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 687 AGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRT-QLCALLL 765
Cdd:PHA02878 176 TENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLL 255
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 755563780 766 AHGADPTLKNQ-EGQTPLDL------VSSLLCRSQICVNHWNRSAFSPLPLRSLTR 814
Cdd:PHA02878 256 EHGVDVNAKSYiLGLTALHSsikserKLKLLLEYGADINSLNSYKLTPLSSAVKQY 311
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
72-289 |
1.25e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 83.47 E-value: 1.25e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 72 DVVEYLLQNGAN-VQARDDGGLIPLHNACSFGHAEVVNLLLQHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAE- 149
Cdd:PHA02874 15 EAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDt 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 150 -----PTIRNTDGRTALDladpSAKAVLTGDYKKDELLESARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRV 224
Cdd:PHA02874 95 silpiPCIEKDMIKTILD----CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFF 170
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755563780 225 KIVQLLLHHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNR 289
Cdd:PHA02874 171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR 235
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
48-254 |
1.93e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 82.70 E-value: 1.93e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 48 KVNSRDtagRKS-TPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLQHGADPNARDNWNYT 126
Cdd:PHA02874 116 DVNIKD---AELkTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGES 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 127 PLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLADPSAKAVLtgdykkdELLESARSGNEEKMmalltplnvncha 206
Cdd:PHA02874 193 PLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI-------ELLINNASINDQDI------------- 252
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 755563780 207 sDGrkSTPLHLAAGYN-RVKIVQLLLHHGADVHAKDKGDLVPLHNACSY 254
Cdd:PHA02874 253 -DG--STPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKY 298
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
437-556 |
2.39e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.77 E-value: 2.39e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 437 LHRAAHCGHLQTCRLLLSYGCDPNIISLQGFTALQMgnenvqqllqegaslghseadrqlleAAKAGDVETVKKLCTVQS 516
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHL--------------------------AAKNGHLEIVKLLLEHAD 54
|
90 100 110 120
....*....|....*....|....*....|....*....|
gi 755563780 517 VNCRDiegRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKD 556
Cdd:pfam12796 55 VNLKD---NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
247-676 |
2.83e-16 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 82.32 E-value: 2.83e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 247 PLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRIEVCSLLLSYGADPTLLN--CHNKSAI----DLAPTA 320
Cdd:PHA02874 38 PLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPipCIEKDMIktilDCGIDV 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 321 QLKERLSYEFkghsLLQAAREADvtrikkhlsLEMVNfkhpqthetalhcaaaspypkrkqiceLLLRKGANTNEKTKEF 400
Cdd:PHA02874 118 NIKDAELKTF----LHYAIKKGD---------LESIK---------------------------MLFEYGADVNIEDDNG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 401 LTPLHVASENAHNDVVEVVVKHEAKVNALDSLGQTSLHRAAHCGHLQTCRLLLSYGCDPNIISLQGFTALQ---MGNENV 477
Cdd:PHA02874 158 CYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHnaiIHNRSA 237
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 478 QQLLQEGAslghseadrqlleaakagdvetvkklctvqSVNCRDIEGrqSTPLHFAAGYN-RVSVVEYLLQHGADVHAKD 556
Cdd:PHA02874 238 IELLINNA------------------------------SINDQDIDG--STPLHHAINPPcDIDIIDILLYHKADISIKD 285
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 557 KGGLVPLHNACSY-GHYEVAELLVKHGAVVNVADLWKFTPLHEaaakgkyeicklllqhgadptKKNRDGNTPL-DLVKD 634
Cdd:PHA02874 286 NKGENPIDTAFKYiNKDPVIKDIIANAVLIKEADKLKDSDFLE---------------------HIEIKDNKEFsDFIKE 344
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 755563780 635 GDTDIQDLLR----GDAALLDAakkgCLARVK------KLSSPDNVNCRDTQ 676
Cdd:PHA02874 345 CNEEIEDMKKtkcgCDKNIFDL----CLIRIKhkfdgnEDSIKDYLNCLDDN 392
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
596-709 |
5.41e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.00 E-value: 5.41e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 596 LHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDLvkdgdtdiqdllrgdaalldAAKKGCLARVKKLSSPDNVNCRDt 675
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHL--------------------AAKNGHLEIVKLLLEHADVNLKD- 59
|
90 100 110
....*....|....*....|....*....|....
gi 755563780 676 qgRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQD 709
Cdd:pfam12796 60 --NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
95-241 |
1.40e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 72.84 E-value: 1.40e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 95 LHNACSFGHAEVVNLLLQHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGaeptirntdgrtaldladpsakavltg 174
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--------------------------- 53
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755563780 175 dykkdellesarsgneekmmalltplNVNChasDGRKSTPLHLAAGYNRVKIVQLLLHHGADVHAKD 241
Cdd:pfam12796 54 --------------------------DVNL---KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
71-184 |
1.48e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 80.09 E-value: 1.48e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 71 KDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLQHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGA-- 148
Cdd:PHA03100 172 KNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPsi 251
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 755563780 149 ---EPTI-----RNTDGRTALDLADPSAKAVLTGD---YKKDELLES 184
Cdd:PHA03100 252 ktiIETLlyfkdKDLNTITKIKMLKKSIMYMFLLDpgfYKNRKLIEN 298
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
368-461 |
4.02e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 71.30 E-value: 4.02e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 368 LHCAAASPYPkrkQICELLLRKGANTNEKTKEFLTPLHVASENAHNDVVEVVVKHeAKVNALDSlGQTSLHRAAHCGHLQ 447
Cdd:pfam12796 1 LHLAAKNGNL---ELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE 75
|
90
....*....|....
gi 755563780 448 TCRLLLSYGCDPNI 461
Cdd:pfam12796 76 IVKLLLEKGADINV 89
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
26-298 |
4.17e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 79.15 E-value: 4.17e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 26 RELFEACRNGDVERVKRLVTPEKVNSRDTAGRKSTPLHFAAGFGRKdVVEYLLQNGANVQARD-DGGLIPLHNACSFGHA 104
Cdd:PHA02878 103 VAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAE-ITKLLLSYGADINMKDrHKGNTALHYATENKDQ 181
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 105 EVVNLLLQHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGrtaldladpsakavltgdykkdelles 184
Cdd:PHA02878 182 RLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCG--------------------------- 234
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 185 arsgneekmmalltplnvnchasdgrkSTPLHLAAGY-NRVKIVQLLLHHGADVHAKDK-GDLVPLHnaCSYGHYEVTEL 262
Cdd:PHA02878 235 ---------------------------NTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTALH--SSIKSERKLKL 285
|
250 260 270
....*....|....*....|....*....|....*..
gi 755563780 263 LVKHGACVNAMDLWQFTPLHEAASKNR-IEVCSLLLS 298
Cdd:PHA02878 286 LLEYGADINSLNSYKLTPLSSAVKQYLcINIGRILIS 322
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
678-787 |
2.39e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 76.24 E-value: 2.39e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 678 RHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHV-----DVAALLIKYNACVNATDKWAFTPLHEA 752
Cdd:PHA03100 34 KPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYA 113
|
90 100 110
....*....|....*....|....*....|....*..
gi 755563780 753 AQKGRTQ--LCALLLAHGADPTLKNQEGQTPLDLVSS 787
Cdd:PHA03100 114 ISKKSNSysIVEYLLDNGANVNIKNSDGENLLHLYLE 150
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
59-269 |
4.53e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 72.61 E-value: 4.53e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 59 STPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLQHGADPNARDNWNYTPLHEAAIKGK-I 137
Cdd:PHA02878 169 NTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKdY 248
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 138 DVCIVLLQHGaeptirntdgrtaldlADPSAKAVLTGdykkdellesarsgneekmmalLTPLNVNCHASDgrkstplhl 217
Cdd:PHA02878 249 DILKLLLEHG----------------VDVNAKSYILG----------------------LTALHSSIKSER--------- 281
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 755563780 218 aagynrvkIVQLLLHHGADVHAKDKGDLVPLHNAC-SYGHYEVTELLVKHGAC 269
Cdd:PHA02878 282 --------KLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRILISNICL 326
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
679-732 |
7.11e-13 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 63.83 E-value: 7.11e-13
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 755563780 679 HSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLI 732
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
522-755 |
9.16e-13 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 72.21 E-value: 9.16e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 522 IEGRQSTPlhfaagYNRVSVVEYLLQHGADVHAKDKGGLV--------------PLHNACSYGHYEVAELLVKHGAVVNV 587
Cdd:PLN03192 480 IEAMQTRQ------EDNVVILKNFLQHHKELHDLNVGDLLgdnggehddpnmasNLLTVASTGNAALLEELLKAKLDPDI 553
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 588 ADLWKFTPLHEAAAKGkYEICKL-LLQHGADPTKKNRDGNTPL-DLVKDGDTDIQDLLRGDAALLDAAKKGCLarvkkls 665
Cdd:PLN03192 554 GDSKGRTPLHIAASKG-YEDCVLvLLKHACNVHIRDANGNTALwNAISAKHHKIFRILYHFASISDPHAAGDL------- 625
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 666 spdnvncrdtqgrhstpLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNA---CVNATD 742
Cdd:PLN03192 626 -----------------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAdvdKANTDD 688
|
250
....*....|...
gi 755563780 743 KWAFTPLHEAAQK 755
Cdd:PLN03192 689 DFSPTELRELLQK 701
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
60-273 |
3.17e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 69.63 E-value: 3.17e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 60 TPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLQHGA---DPNARDnwNYTPLHEAAIKGK 136
Cdd:PHA02875 37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 137 IDVCIVLLQHGAEPTIRNTDGRTALDLadpsakAVLTGDYKKDELLESARSgneekmmalltPLNVnchaSDGRKSTPLH 216
Cdd:PHA02875 115 LDIMKLLIARGADPDIPNTDKFSPLHL------AVMMGDIKGIELLIDHKA-----------CLDI----EDCCGCTPLI 173
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 755563780 217 LAAGYNRVKIVQLLLHHGADV-HAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAM 273
Cdd:PHA02875 174 IAMAKGDIAICKMLLDSGANIdYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNIM 231
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
27-150 |
7.54e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 68.48 E-value: 7.54e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 27 ELFEACRNGDVERVKRLVTPEKVNSRDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEV 106
Cdd:PHA02875 71 ELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG 150
|
90 100 110 120
....*....|....*....|....*....|....*....|....
gi 755563780 107 VNLLLQHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEP 150
Cdd:PHA02875 151 IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
59-111 |
8.42e-12 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 60.75 E-value: 8.42e-12
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 755563780 59 STPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLL 111
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
79-281 |
1.19e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 68.74 E-value: 1.19e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 79 QNGANVQARDDGGLIplhNACSFGHAEVVNLLLQHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGR 158
Cdd:PLN03192 516 NGGEHDDPNMASNLL---TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGN 592
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 159 TALdladpsAKAVLTGDYKKDELL-ESARSGNEEKMMALLtplnvnChasdgrkstplhLAAGYNRVKIVQLLLHHGADV 237
Cdd:PLN03192 593 TAL------WNAISAKHHKIFRILyHFASISDPHAAGDLL------C------------TAAKRNDLTAMKELLKQGLNV 648
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 755563780 238 HAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQ-FTPL 281
Cdd:PLN03192 649 DSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDDdFSPT 693
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
526-579 |
1.22e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 60.37 E-value: 1.22e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 755563780 526 QSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLV 579
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
496-700 |
7.07e-11 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 65.80 E-value: 7.07e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 496 LLEAAKAGDVETVKKLCTVQSVncrDIEGRQS---TPLHFAAGYNRVSVVEYLLQHG---------ADVHAkdkgGLVPL 563
Cdd:cd22192 21 LLLAAKENDVQAIKKLLKCPSC---DLFQRGAlgeTALHVAALYDNLEAAVVLMEAApelvnepmtSDLYQ----GETAL 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 564 HNACSYGHYEVAELLVKHGAVVNVA------------DLWKFT--PLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPL 629
Cdd:cd22192 94 HIAVVNQNLNLVRELIARGADVVSPratgtffrpgpkNLIYYGehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755563780 630 D-LV----KDGDTDIQDLLrgdaalldaakkgcLARVKklssPDNVNCRDTQGRHS--TPLHLAAGYNNLEVAEYLLQ 700
Cdd:cd22192 174 HiLVlqpnKTFACQMYDLI--------------LSYDK----EDDLQPLDLVPNNQglTPFKLAAKEGNIVMFQHLVQ 233
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
224-476 |
1.86e-10 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 64.09 E-value: 1.86e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 224 VKIVQLLLHHGADVHAKDKGDLVPL----HNACSYGH-YEVTELLVKHGACVNAMDLWQFTPLHEAASK---NRIEVCSL 295
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLctilSNIKDYKHmLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 296 LLSYGADPTLLNCHNKSAIDLaptaqlkerlsyefkghsLLQAAREADVTRIKkhLSLEM---VNFKHPQTHETALHCAA 372
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQV------------------YLQSNHHIDIEIIK--LLLEKgvdINTHNNKEKYDTLHCYF 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 373 ASPYPK-RKQICELLLRKGANTNEKTK-------EFLTPLHVASENAHNDVVEVVVKHeAKVNALDSLGQTSLHRAAHCG 444
Cdd:PHA02798 191 KYNIDRiDADILKLFVDNGFIINKENKshkkkfmEYLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLYYSVSHN 269
|
250 260 270
....*....|....*....|....*....|..
gi 755563780 445 HLQTCRLLLSYGCDPNIISLQGFTALQMGNEN 476
Cdd:PHA02798 270 NRKIFEYLLQLGGDINIITELGNTCLFTAFEN 301
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
53-164 |
3.45e-10 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 64.12 E-value: 3.45e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 53 DTAGRksTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLQ--HGADPNARDNWnytpLHE 130
Cdd:PLN03192 555 DSKGR--TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfaSISDPHAAGDL----LCT 628
|
90 100 110
....*....|....*....|....*....|....
gi 755563780 131 AAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLA 164
Cdd:PLN03192 629 AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA 662
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
244-485 |
4.01e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 63.09 E-value: 4.01e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 244 DLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRIEVCSLLLSYGADPtllnchnksaidlaptaqlk 323
Cdd:PHA02875 2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIP-------------------- 61
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 324 erlSYEFKG--HSLLQAAREADVTRIKKHLSL-EMVNFKHPQTHETALHCAAASpypKRKQICELLLRKGANTNEKTKEF 400
Cdd:PHA02875 62 ---DVKYPDieSELHDAVEEGDVKAVEELLDLgKFADDVFYKDGMTPLHLATIL---KKLDIMKLLIARGADPDIPNTDK 135
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 401 LTPLHVASENAHNDVVEVVVKHEAKVNALDSLGQTSLHRAAHCGHLQTCRLLLSYGCDPNIISLQG-FTALQMGNEN--- 476
Cdd:PHA02875 136 FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENnki 215
|
250
....*....|.
gi 755563780 477 --VQQLLQEGA 485
Cdd:PHA02875 216 diVRLFIKRGA 226
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
28-237 |
5.59e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 63.16 E-value: 5.59e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 28 LFEACRNG-DVERVKRLVT-PEKVNSRDTAgrKSTPLHFAAGFGR-KDVVEYLLQNGANVQARDDGGLIPLHNACSFGHA 104
Cdd:PHA02876 311 LYLMAKNGyDTENIRTLIMlGADVNAADRL--YITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAVRNNV 388
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 105 EVVNLLLQHGADPNARDNWNYTPLHEAAIKGKIDVCI-VLLQHGAEPTIRNTDGRTALDLAdpsakavltgdykkdelle 183
Cdd:PHA02876 389 VIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVkTLIDRGANVNSKNKDLSTPLHYA------------------- 449
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....
gi 755563780 184 sARSGNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNrvKIVQLLLHHGADV 237
Cdd:PHA02876 450 -CKKNCKLDVIEMLLDNGADVNAINIQNQYPLLIALEYH--GIVNILLHYGAEL 500
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
594-784 |
5.67e-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: 63.11 E-value: 5.67e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 594 TPLHEAAAKGKYE-ICKLLLQHGADPTKKNRDGNTPLDLVKDGDTDiqdllrgDAA--LLDAAkkgclarvkklssPDNV 670
Cdd:cd22192 19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNL-------EAAvvLMEAA-------------PELV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 671 NCRDT----QGRhsTPLHLAAGYNNLEVAEYLLQHGADVNA---------QDKGGLI-----PLHNAASYGHVDVAALLI 732
Cdd:cd22192 79 NEPMTsdlyQGE--TALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLI 156
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755563780 733 KYNACVNATDKWAFTPLH----EAAQKGRTQLCALLLAhgADP--------TLKNQEGQTPLDL 784
Cdd:cd22192 157 EHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILS--YDKeddlqpldLVPNNQGLTPFKL 218
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
102-167 |
9.64e-10 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 62.22 E-value: 9.64e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755563780 102 GHAEVVNLLLQHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLADPS 167
Cdd:PTZ00322 93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
28-164 |
9.91e-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: 62.34 E-value: 9.91e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 28 LFEACRNGDVERVKRLVT------------------------------------PEKVNSRDT----AGRksTPLHFAAG 67
Cdd:cd22192 21 LLLAAKENDVQAIKKLLKcpscdlfqrgalgetalhvaalydnleaavvlmeaaPELVNEPMTsdlyQGE--TALHIAVV 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 68 FGRKDVVEYLLQNGANVQ-ARDDG--------GLI-----PLHNACSFGHAEVVNLLLQHGADPNARDNWNYTPLHE-AA 132
Cdd:cd22192 99 NQNLNLVRELIARGADVVsPRATGtffrpgpkNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIlVL 178
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 755563780 133 IKGKIDVCIV---LLQHGAE------PTIRNTDGRTALDLA 164
Cdd:cd22192 179 QPNKTFACQMydlILSYDKEddlqplDLVPNNQGLTPFKLA 219
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
212-264 |
1.03e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 54.97 E-value: 1.03e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 755563780 212 STPLHLAAGYNRVKIVQLLLHHGADVHAKDKGDLVPLHNACSYGHYEVTELLV 264
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
384-596 |
1.10e-09 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 62.19 E-value: 1.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 384 ELLLRKGANTNEKTKEFLTPLHVASENAHNDVVEVVVKHEAKVNALDSLGQTSLHRAAHCGHLQTCRLLLSYG--CDPNI 461
Cdd:PLN03192 542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAsiSDPHA 621
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 462 islqgftalqmgnenvqqllqegaslghseadrqlleaakAGDVetvkkLCTvqsvncrdiegrqstplhfAAGYNRVSV 541
Cdd:PLN03192 622 ----------------------------------------AGDL-----LCT-------------------AAKRNDLTA 637
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*.
gi 755563780 542 VEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLW-KFTPL 596
Cdd:PLN03192 638 MKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDdDFSPT 693
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
495-581 |
1.65e-09 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 61.45 E-value: 1.65e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 495 QLLEAAKAGDVETVKKLCTVQS-VNCRDIEGRqsTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHYE 573
Cdd:PTZ00322 85 ELCQLAASGDAVGARILLTGGAdPNCRDYDGR--TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFRE 162
|
....*...
gi 755563780 574 VAELLVKH 581
Cdd:PTZ00322 163 VVQLLSRH 170
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
94-144 |
2.67e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.82 E-value: 2.67e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 755563780 94 PLHNACSFGHAEVVNLLLQHGADPNARDNWNYTPLHEAAIKGKIDVCIVLL 144
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
74-248 |
3.07e-09 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 60.07 E-value: 3.07e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 74 VEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLQHGADPNARDNWNYTPLHeaAIKGKIDVCI----VLLQHGAE 149
Cdd:PHA02946 55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY--YLSGTDDEVIerinLLVQYGAK 132
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 150 ptIRNTDGRTA----LDLADPSAK-----------AVLTGDYKKDELLESARSGN-EEKMMALLTPLNVNCHASDGRKST 213
Cdd:PHA02946 133 --INNSVDEEGcgplLACTDPSERvfkkimsigfeARIVDKFGKNHIHRHLMSDNpKASTISWMMKLGISPSKPDHDGNT 210
|
170 180 190
....*....|....*....|....*....|....*..
gi 755563780 214 PLHLAAG--YNRVKIVQLLLhHGADVHAKDKGDLVPL 248
Cdd:PHA02946 211 PLHIVCSktVKNVDIINLLL-PSTDVNKQNKFGDSPL 246
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
247-297 |
3.73e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.43 E-value: 3.73e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 755563780 247 PLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRIEVCSLLL 297
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
110-164 |
4.20e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 53.12 E-value: 4.20e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 755563780 110 LLQHG-ADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLA 164
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
74-149 |
4.21e-09 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 60.30 E-value: 4.21e-09
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755563780 74 VEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLQHGADPNARDNWNYTPLHEAAIKGKIDVCIVLLQHGAE 149
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
77-131 |
4.86e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 53.12 E-value: 4.86e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 755563780 77 LLQNG-ANVQARDDGGLIPLHNACSFGHAEVVNLLLQHGADPNARDNWNYTPLHEA 131
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
72-306 |
5.73e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 59.46 E-value: 5.73e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 72 DVVEYLLQNGANVQARDDGGLIP----LHNACSFGHA-EVVNLLLQHGADPNARDNWNYTP----LHEAAIKGKiDVCIV 142
Cdd:PHA02798 52 DIVKLFINLGANVNGLDNEYSTPlctiLSNIKDYKHMlDIVKILIENGADINKKNSDGETPlyclLSNGYINNL-EILLF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 143 LLQHGAEPTIRNTDGRTALDLadpsakAVLTGDYKKDELLEsarsgneekmMALLTPLNVNCHaSDGRKSTPLHLAAGYN 222
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQV------YLQSNHHIDIEIIK----------LLLEKGVDINTH-NNKEKYDTLHCYFKYN 193
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 223 ----RVKIVQLLLHHGADVHAKDKGD-------LVPLHNACSYGHYEVTELLVKHgACVNAMDLWQFTPLHEAASKNRIE 291
Cdd:PHA02798 194 idriDADILKLFVDNGFIINKENKSHkkkfmeyLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLYYSVSHNNRK 272
|
250
....*....|....*
gi 755563780 292 VCSLLLSYGADPTLL 306
Cdd:PHA02798 273 IFEYLLQLGGDINII 287
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
571-784 |
6.64e-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: 59.71 E-value: 6.64e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 571 HYEVAELLVKHGAVVNVADlwkfTPLHeAAAKGKYEICKLLLQHgadpTKKNRDGNTPLDLVKDGDTDiqDLLRGdaall 650
Cdd:TIGR00870 65 NLELTELLLNLSCRGAVGD----TLLH-AISLEYVDAVEAILLH----LLAAFRKSGPLELANDQYTS--EFTPG----- 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 651 daakkgclarvkklsspdnvncrdtqgrhSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKG--------------GLIPL 716
Cdd:TIGR00870 129 -----------------------------ITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 717 HNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAA---------QKGRTQLCALLLAHGA--DPTLK-----NQEGQT 780
Cdd:TIGR00870 180 NAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenefkaeyEELSCQMYNFALSLLDklRDSKElevilNHQGLT 259
|
....
gi 755563780 781 PLDL 784
Cdd:TIGR00870 260 PLKL 263
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
562-612 |
7.26e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.28 E-value: 7.26e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 755563780 562 PLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLL 612
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
200-427 |
8.32e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 58.85 E-value: 8.32e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 200 LNVNCHASDGrkSTPLHLAAGYNRVKIVQLLLHHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNamDLWQ-- 277
Cdd:PHA02875 26 INPNFEIYDG--ISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD--DVFYkd 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 278 -FTPLHEAASKNRIEVCSLLLSYGADPTLLNCHNKSAIDLAPtaqlkerLSYEFKGHSLLQAAREAdvtrikkhLSLEmv 356
Cdd:PHA02875 102 gMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAV-------MMGDIKGIELLIDHKAC--------LDIE-- 164
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755563780 357 nfkhpqthetalHCAAASPY-----PKRKQICELLLRKGANTNEKTKE-FLTPLHVASENAHNDVVEVVVKHEAKVN 427
Cdd:PHA02875 165 ------------DCCGCTPLiiamaKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLFIKRGADCN 229
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
162-269 |
8.87e-09 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 59.14 E-value: 8.87e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 162 DLADPSAKAVLTGdykkdELLESARSGNEEKMMALLTP-LNVNCHASDGRksTPLHLAAGYNRVKIVQLLLHHGADVHAK 240
Cdd:PTZ00322 72 EVIDPVVAHMLTV-----ELCQLAASGDAVGARILLTGgADPNCRDYDGR--TPLHIACANGHVQVVRVLLEFGADPTLL 144
|
90 100
....*....|....*....|....*....
gi 755563780 241 DKGDLVPLHNACSYGHYEVTELLVKHGAC 269
Cdd:PTZ00322 145 DKDGKTPLELAEENGFREVVQLLSRHSQC 173
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
567-737 |
1.41e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 58.76 E-value: 1.41e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 567 CSYGHYEVAELLVKhGAVVNVADLWKFTPLHEAAAKgKYEICKLLLQHGADPTKKNRDGNTPLDLVKDGDTD--IQDLLR 644
Cdd:PTZ00322 6 CSVASSAFAAQLFF-GTEGSRKRRAKPISFERMAAI-QEEIARIDTHLEALEATENKDATPDHNLTTEEVIDpvVAHMLT 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 645 GDAALLDAAKKGCLARVKkLSSPDNVNCRDTQGRhsTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGH 724
Cdd:PTZ00322 84 VELCQLAASGDAVGARIL-LTGGADPNCRDYDGR--TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF 160
|
170
....*....|...
gi 755563780 725 VDVAALLIKYNAC 737
Cdd:PTZ00322 161 REVVQLLSRHSQC 173
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
669-786 |
1.44e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 58.54 E-value: 1.44e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 669 NVNCRDTQGRhsTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIK--------------- 733
Cdd:PHA02876 170 DVNAKDIYCI--TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDnrsninkndlsllka 247
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755563780 734 ------------YNA--CVNATDKWAFTPLHEAAQK-GRTQLCALLLAHGADPTLKNQEGQTPLDLVS 786
Cdd:PHA02876 248 irnedletslllYDAgfSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMA 315
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
668-717 |
2.38e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 51.19 E-value: 2.38e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 755563780 668 DNVNCRDTQGRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLH 717
Cdd:pfam13857 5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
684-767 |
2.97e-08 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 57.60 E-value: 2.97e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 684 HLAAGYNNLEvAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCAL 763
Cdd:PTZ00322 88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
....
gi 755563780 764 LLAH 767
Cdd:PTZ00322 167 LSRH 170
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
526-760 |
3.88e-08 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 56.94 E-value: 3.88e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 526 QSTPLHFAAGYNRVSVVEYLL-QHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHG-AVVNVA---DLWK-FTPLHEA 599
Cdd:cd22192 17 SESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApELVNEPmtsDLYQgETALHIA 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 600 AAKGKYEICKLLLQHGADPTKknrdgntpldlvkdgdtdiqdllrgdaalldaakkgclARVKKLSSPDNVNCRDTQGRH 679
Cdd:cd22192 97 VVNQNLNLVRELIARGADVVS--------------------------------------PRATGTFFRPGPKNLIYYGEH 138
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 680 stPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAA----LLIKYNACVNA------TDKWAFTPL 749
Cdd:cd22192 139 --PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACqmydLILSYDKEDDLqpldlvPNNQGLTPF 216
|
250
....*....|.
gi 755563780 750 HEAAQKGRTQL 760
Cdd:cd22192 217 KLAAKEGNIVM 227
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
715-765 |
7.32e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.58 E-value: 7.32e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 755563780 715 PLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLL 765
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
60-172 |
7.33e-08 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 56.24 E-value: 7.33e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 60 TPLHFAAGFGRKDVVEYLLQNGANVQARDDG--------------GLIPLHNACSFGHAEVVNLLLQHGADPNARDNWNY 125
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADILTADSLGN 209
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755563780 126 TPLHEAAIKGKID------VCIV---LLQHGAEP-------TIRNTDGRTALDLADPSAKAVL 172
Cdd:TIGR00870 210 TLLHLLVMENEFKaeyeelSCQMynfALSLLDKLrdskeleVILNHQGLTPLKLAAKEGRIVL 272
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
216-299 |
1.04e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 55.67 E-value: 1.04e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 216 HLAAGYNRVKIvQLLLHHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNRIEVCSL 295
Cdd:PTZ00322 88 QLAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
....
gi 755563780 296 LLSY 299
Cdd:PTZ00322 167 LSRH 170
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
335-430 |
1.12e-07 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 50.11 E-value: 1.12e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 335 LLQAAREADVTRIKKHLSLEMVNFKHPQTHETALHCAAASpypKRKQICELLLRKgANTNEKTKEFlTPLHVASENAHND 414
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKN---GHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLE 75
|
90
....*....|....*.
gi 755563780 415 VVEVVVKHEAKVNALD 430
Cdd:pfam12796 76 IVKLLLEKGADINVKD 91
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
516-564 |
1.29e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 48.88 E-value: 1.29e-07
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 755563780 516 SVNCRDIEGRQSTPLHFAAGYNRVSVVEYLLQHGADVHAKDKGGLVPLH 564
Cdd:pfam13857 6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
573-750 |
1.53e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 54.84 E-value: 1.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 573 EVAELLVKHGAVVNVADLWKFTPLHEAAA-----KGKYEICKLLLQHGADPTKKNRDGNTPLdlvkdgdtdiqdllrgda 647
Cdd:PHA02798 52 DIVKLFINLGANVNGLDNEYSTPLCTILSnikdyKHMLDIVKILIENGADINKKNSDGETPL------------------ 113
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 648 alldaakkGCLarvkklsspdnvncrdtqgrhstplhLAAGY-NNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGH-- 724
Cdd:PHA02798 114 --------YCL--------------------------LSNGYiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhi 159
|
170 180
....*....|....*....|....*...
gi 755563780 725 -VDVAALLIKYNACVNATDKW-AFTPLH 750
Cdd:PHA02798 160 dIEIIKLLLEKGVDINTHNNKeKYDTLH 187
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
531-614 |
3.81e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 53.75 E-value: 3.81e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 531 HFAAGYNRVSVvEYLLQHGADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKL 610
Cdd:PTZ00322 88 QLAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
....
gi 755563780 611 LLQH 614
Cdd:PTZ00322 167 LSRH 170
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
126-299 |
4.03e-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: 53.86 E-value: 4.03e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 126 TPLHEAAIKGKID-VCIVLLQHGAEPTIRNTDGRTALDLAdpsakaVLtgdYKKDE----LLESARsgneekmmallTPL 200
Cdd:cd22192 19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVA------AL---YDNLEaavvLMEAAP-----------ELV 78
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 201 NVNCHASDGRKSTPLHLAAGYNRVKIVQLLLHHGADVHA---------KDKGDLV-----PLHNACSYGHYEVTELLVKH 266
Cdd:cd22192 79 NEPMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEH 158
|
170 180 190
....*....|....*....|....*....|....*..
gi 755563780 267 GACVNAMDLWQFTPLHEAASK-NRIEVC---SLLLSY 299
Cdd:cd22192 159 GADIRAQDSLGNTVLHILVLQpNKTFACqmyDLILSY 195
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
681-710 |
5.12e-07 |
|
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: 46.51 E-value: 5.12e-07
10 20 30
....*....|....*....|....*....|.
gi 755563780 681 TPLHLAAG-YNNLEVAEYLLQHGADVNAQDK 710
Cdd:pfam00023 4 TPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
446-706 |
5.23e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 53.30 E-value: 5.23e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 446 LQTCRLLLSyGCDPNIISLQgFTALQ-------MGNENVQQLLQEGASLGHSEADRQLleaakagdvetvkKLCTVQSvN 518
Cdd:PHA02798 18 LSTVKLLIK-SCNPNEIVNE-YSIFQkylqrdsPSTDIVKLFINLGANVNGLDNEYST-------------PLCTILS-N 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 519 CRDiegrqstplhfaagYN-RVSVVEYLLQHGADVHAKDKGGLVPLHNACSYGHY---EVAELLVKHGAVVNVADLWKFT 594
Cdd:PHA02798 82 IKD--------------YKhMLDIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFT 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 595 PLHEAAAKGKY---EICKLLLQHGAD-PTKKNRDGNTPLDL-----VKDGDTDIQDLLRGDAALLD----AAKKGCLA-- 659
Cdd:PHA02798 148 MLQVYLQSNHHidiEIIKLLLEKGVDiNTHNNKEKYDTLHCyfkynIDRIDADILKLFVDNGFIINkenkSHKKKFMEyl 227
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 660 --------RVKK-----LSSPDNVNCRDTQGrhSTPLHLAAGYNNLEVAEYLLQHGADVN 706
Cdd:PHA02798 228 nsllydnkRFKKnildfIFSYIDINQVDELG--FNPLYYSVSHNNRKIFEYLLQLGGDIN 285
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
477-766 |
5.64e-07 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 53.55 E-value: 5.64e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 477 VQQLLQEGASLGHSEADR----QLLEAAKAGDVETVKKLctVQSVNCRDIEGRqsTPLHfAAGYNRVSVVEYLLQHGADV 552
Cdd:TIGR00870 33 VYRDLEEPKKLNINCPDRlgrsALFVAAIENENLELTEL--LLNLSCRGAVGD--TLLH-AISLEYVDAVEAILLHLLAA 107
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 553 HAKdkGGLVPLHNACSYGHYEVAEllvkhgavvnvadlwkfTPLHEAAAKGKYEICKLLLQHGAD-PTKKNRDgntplDL 631
Cdd:TIGR00870 108 FRK--SGPLELANDQYTSEFTPGI-----------------TALHLAAHRQNYEIVKLLLERGASvPARACGD-----FF 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 632 VKdgdTDIQDLLRgdaalldaakkgclarvkklsspdnvncrdtQGRHstPLHLAAGYNNLEVAEYLLQHGADVNAQDKG 711
Cdd:TIGR00870 164 VK---SQGVDSFY-------------------------------HGES--PLNAAACLGSPSIVALLSEDPADILTADSL 207
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755563780 712 GLIPLH-------NAASY------------GHVDVAALLIKYNACVNATDkwaFTPLHEAAQKGRTQLCALLLA 766
Cdd:TIGR00870 208 GNTLLHllvmeneFKAEYeelscqmynfalSLLDKLRDSKELEVILNHQG---LTPLKLAAKEGRIVLFRLKLA 278
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
401-453 |
5.85e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.88 E-value: 5.85e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 755563780 401 LTPLHVASENAHNDVVEVVVKHEAKVNALDSLGQTSLHRAAHCGHLQTCRLLL 453
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
578-632 |
6.09e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.96 E-value: 6.09e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 755563780 578 LVKHGAV-VNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDLV 632
Cdd:pfam13857 1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
539-782 |
6.60e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 52.91 E-value: 6.60e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 539 VSVVEYLLQHGADVHAKDKGGLVPL----HNACSYGH-YEVAELLVKHGAVVNVADLWKFTPLHEAAAKG---KYEICKL 610
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLctilSNIKDYKHmLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLF 130
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 611 LLQHGADPTKKNRDGNTPLDL-VKDG---DTDIQDLLrgdaalldaakkgclarvkkLSSPDNVNCRDTQGRHSTpLHLA 686
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQVyLQSNhhiDIEIIKLL--------------------LEKGVDINTHNNKEKYDT-LHCY 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 687 AGYN----NLEVAEYLLQHGADVNAQDKGG-------LIPLHNAASYGHVDVAALLIKYnACVNATDKWAFTPLHEAAQK 755
Cdd:PHA02798 190 FKYNidriDADILKLFVDNGFIINKENKSHkkkfmeyLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLYYSVSH 268
|
250 260
....*....|....*....|....*..
gi 755563780 756 GRTQLCALLLAHGADPTLKNQEGQTPL 782
Cdd:PHA02798 269 NNRKIFEYLLQLGGDINIITELGNTCL 295
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
698-752 |
8.85e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.57 E-value: 8.85e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 755563780 698 LLQHG-ADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEA 752
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
181-335 |
9.77e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 52.56 E-value: 9.77e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 181 LLESARSGN----EEKMMALLTPlnvncHASDGRKSTPLHLAAGYNRVKIVQLLLHHGADVHAKDKGDLVPLHNACSYGH 256
Cdd:PLN03192 529 LLTVASTGNaallEELLKAKLDP-----DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKH 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 257 YEVTEL-------------------------------LVKHGACVNAMDLWQFTPLHEAASKNRIEVCSLLLSYGADPTL 305
Cdd:PLN03192 604 HKIFRIlyhfasisdphaagdllctaakrndltamkeLLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
|
170 180 190
....*....|....*....|....*....|
gi 755563780 306 LNCHNksaiDLAPTaQLKERLSYEFKGHSL 335
Cdd:PLN03192 684 ANTDD----DFSPT-ELRELLQKRELGHSI 708
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
738-785 |
1.22e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.19 E-value: 1.22e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 755563780 738 VNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLV 785
Cdd:pfam13857 9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
594-630 |
1.26e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 46.11 E-value: 1.26e-06
10 20 30
....*....|....*....|....*....|....*..
gi 755563780 594 TPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLD 630
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALH 39
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
27-113 |
1.98e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.44 E-value: 1.98e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 27 ELFEACRNGDVERVKRLVTP-EKVNSRDTAGRksTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAE 105
Cdd:PTZ00322 85 ELCQLAASGDAVGARILLTGgADPNCRDYDGR--TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFRE 162
|
....*...
gi 755563780 106 VVNLLLQH 113
Cdd:PTZ00322 163 VVQLLSRH 170
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
60-171 |
2.34e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 51.18 E-value: 2.34e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 60 TPLHFAAGFG--RKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLQHGADPNARDNWNYTPLHEAAIKGki 137
Cdd:PHA03095 224 TPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNN-- 301
|
90 100 110
....*....|....*....|....*....|....
gi 755563780 138 DVCIVllqhgaeptirntdgRTALDLAdPSAKAV 171
Cdd:PHA03095 302 NGRAV---------------RAALAKN-PSAETV 319
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
503-629 |
2.69e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 49.05 E-value: 2.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 503 GDVETVKK-LCTVQSVNcrdieGRQSTPLH--FAAGYNRVSVVEYLLQHGADVHAKDKG-GLVPLHNACSYG---HYEVA 575
Cdd:PHA02859 32 DDIEGVKKwIKFVNDCN-----DLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRDnNLSALHHYLSFNknvEPEIL 106
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*.
gi 755563780 576 ELLVKHGAVVNVADLWKFTPLHE--AAAKGKYEICKLLLQHGADPTKKNRDGNTPL 629
Cdd:PHA02859 107 KILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLIDSGVSFLNKDFDNNNIL 162
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
196-249 |
2.93e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 45.03 E-value: 2.93e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 755563780 196 LLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLHHGADVHAKDKGDLVPLH 249
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
545-599 |
4.05e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 44.64 E-value: 4.05e-06
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 755563780 545 LLQHG-ADVHAKDKGGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEA 599
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
717-806 |
5.58e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 50.28 E-value: 5.58e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 717 HNAASyGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDL--------VSSL 788
Cdd:PTZ00322 88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELaeengfreVVQL 166
|
90
....*....|....*...
gi 755563780 789 LCRSQICvnHWNRSAFSP 806
Cdd:PTZ00322 167 LSRHSQC--HFELGANAK 182
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
213-242 |
5.82e-06 |
|
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: 43.82 E-value: 5.82e-06
10 20 30
....*....|....*....|....*....|.
gi 755563780 213 TPLHLAAG-YNRVKIVQLLLHHGADVHAKDK 242
Cdd:pfam00023 4 TPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
528-557 |
8.29e-06 |
|
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: 43.43 E-value: 8.29e-06
10 20 30
....*....|....*....|....*....|.
gi 755563780 528 TPLHFAAG-YNRVSVVEYLLQHGADVHAKDK 557
Cdd:pfam00023 4 TPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
58-152 |
1.22e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 48.83 E-value: 1.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 58 KSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLQHGADPN-ARDNWNYTPLHEAAIKGK 136
Cdd:PHA02875 135 KFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNK 214
|
90
....*....|....*.
gi 755563780 137 IDVCIVLLQHGAEPTI 152
Cdd:PHA02875 215 IDIVRLFIKRGADCNI 230
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
91-122 |
1.42e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 42.66 E-value: 1.42e-05
10 20 30
....*....|....*....|....*....|...
gi 755563780 91 GLIPLHNAC-SFGHAEVVNLLLQHGADPNARDN 122
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
681-707 |
1.48e-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: 42.63 E-value: 1.48e-05
10 20
....*....|....*....|....*..
gi 755563780 681 TPLHLAAGYNNLEVAEYLLQHGADVNA 707
Cdd:pfam13606 4 TPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
60-172 |
1.54e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 48.72 E-value: 1.54e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 60 TPLHFAAGFGRKDVVEYLLQNGANVQARDDG-------------GLIPLHNACSFGHAEVVNLLLQHGADP---NARDNW 123
Cdd:cd21882 75 TALHIAIENRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSL 154
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 755563780 124 NYTPLH---EAAIKGKIDVCIV------LLQHGA--EPT-----IRNTDGRTALDLADPSAKAVL 172
Cdd:cd21882 155 GNTVLHalvLQADNTPENSAFVcqmynlLLSYGAhlDPTqqleeIPNHQGLTPLKLAAVEGKIVM 219
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
681-707 |
1.65e-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: 42.19 E-value: 1.65e-05
10 20
....*....|....*....|....*..
gi 755563780 681 TPLHLAAGYNNLEVAEYLLQHGADVNA 707
Cdd:smart00248 4 TPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
679-788 |
1.93e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 48.06 E-value: 1.93e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 679 HSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRT 758
Cdd:PHA02875 2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81
|
90 100 110
....*....|....*....|....*....|..
gi 755563780 759 QLCALLLAHG--ADPTLKnQEGQTPLDLVSSL 788
Cdd:PHA02875 82 KAVEELLDLGkfADDVFY-KDGMTPLHLATIL 112
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
263-317 |
2.01e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 42.72 E-value: 2.01e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 755563780 263 LVKHGAC-VNAMDLWQFTPLHEAASKNRIEVCSLLLSYGADPTLLNCHNKSAIDLA 317
Cdd:pfam13857 1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
632-787 |
2.22e-05 |
|
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: 48.26 E-value: 2.22e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 632 VKDGDTDIQDLLrgdaalLDAAKKGclarvKKLSSPDNVNCRDTQGRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKG 711
Cdd:cd22196 58 LHNGQNDTISLL------LDIAEKT-----GNLKEFVNAAYTDSYYKGQTALHIAIERRNMHLVELLVQNGADVHARASG 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 712 --------------GLIPLHNAASYGHVDVAALLIK---YNACVNATDKWAFTPLH---EAAQ------KGRTQLCALLL 765
Cdd:cd22196 127 effkkkkggpgfyfGELPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLHalvEVADntpentKFVTKMYNEIL 206
|
170 180
....*....|....*....|....*....
gi 755563780 766 AHGAD--PTLK-----NQEGQTPLDLVSS 787
Cdd:cd22196 207 ILGAKirPLLKleeitNKKGLTPLKLAAK 235
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
458-631 |
3.19e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 47.94 E-value: 3.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 458 DPNIISlQGFTALQMGNEN-VQQLLQEG--ASLGHSEADRQLLEAAKAGDVETV----KKLCtvqSVNCRDIEGRQSTPL 530
Cdd:PLN03192 522 DPNMAS-NLLTVASTGNAAlLEELLKAKldPDIGDSKGRTPLHIAASKGYEDCVlvllKHAC---NVHIRDANGNTALWN 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 531 HFAAGYNRVSVVEYLLQHGADVHAkdkGGLVpLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKL 610
Cdd:PLN03192 598 AISAKHHKIFRILYHFASISDPHA---AGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRL 673
|
170 180
....*....|....*....|..
gi 755563780 611 LLQHGADPTKKNRDGN-TPLDL 631
Cdd:PLN03192 674 LIMNGADVDKANTDDDfSPTEL 695
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
124-164 |
3.44e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.88 E-value: 3.44e-05
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 755563780 124 NYTPLHEAAIKGKIDVCIVLLQHGAEPTIRNTDGRTALDLA 164
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
416-493 |
3.66e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 47.59 E-value: 3.66e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 416 VEVVVKHEAKVNALDSLGQTSLHRAAHCGHLQTCRLLLSYGCDPNIISLQGFTALQMGNEN----VQQLLQeGASLGHSE 491
Cdd:PTZ00322 98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENgfreVVQLLS-RHSQCHFE 176
|
..
gi 755563780 492 AD 493
Cdd:PTZ00322 177 LG 178
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
727-783 |
5.74e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 46.98 E-value: 5.74e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 755563780 727 VAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLD 783
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLE 216
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
262-317 |
5.76e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.82 E-value: 5.76e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 755563780 262 LLVKHGACVNAMDLWQFTPLHEAASKNRIEVCSLLLSYGADPTLLNCHNKSAIDLA 317
Cdd:PTZ00322 100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
91-119 |
6.19e-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: 6.19e-05
10 20
....*....|....*....|....*....
gi 755563780 91 GLIPLHNACSFGHAEVVNLLLQHGADPNA 119
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
43-96 |
6.52e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.18 E-value: 6.52e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 755563780 43 LVTPEKVNSRDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLH 96
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
60-89 |
6.58e-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: 6.58e-05
10 20 30
....*....|....*....|....*....|.
gi 755563780 60 TPLHFAAG-FGRKDVVEYLLQNGANVQARDD 89
Cdd:pfam00023 4 TPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
426-472 |
6.59e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.18 E-value: 6.59e-05
10 20 30 40
....*....|....*....|....*....|....*....|....*..
gi 755563780 426 VNALDSLGQTSLHRAAHCGHLQTCRLLLSYGCDPNIISLQGFTALQM 472
Cdd:pfam13857 9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
528-554 |
7.84e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 40.32 E-value: 7.84e-05
10 20
....*....|....*....|....*..
gi 755563780 528 TPLHFAAGYNRVSVVEYLLQHGADVHA 554
Cdd:pfam13606 4 TPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
658-814 |
7.91e-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: 46.33 E-value: 7.91e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 658 LARVKKLSSPD---NVNCRDTQGRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKG--------------GLIPLHNAA 720
Cdd:cd22193 52 LDIAEKTDNLKrfiNAEYTDEYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAA 131
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 721 SYGHVDVAALLIK---YNACVNATDKWAFTPLH---EAAQKGRTQ------LCALLLAHGAD--PTLK-----NQEGQTP 781
Cdd:cd22193 132 CTNQPDIVQYLLEnehQPADIEAQDSRGNTVLHalvTVADNTKENtkfvtrMYDMILIRGAKlcPTVEleeirNNDGLTP 211
|
170 180 190
....*....|....*....|....*....|....
gi 755563780 782 LDLVSSLlcrSQICV-NHWNRSAFSPLPLRSLTR 814
Cdd:cd22193 212 LQLAAKM---GKIEIlKYILQREIKEPELRHLSR 242
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
385-455 |
8.03e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.43 E-value: 8.03e-05
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755563780 385 LLLRKGANTNEKTKEFLTPLHVASENAHNDVVEVVVKHEAKVNALDSLGQTSLHRAAHCGHLQTCRLLLSY 455
Cdd:PTZ00322 100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
380-568 |
8.67e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 46.20 E-value: 8.67e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 380 KQICELLLRKGANTNEKTKEFLTPLHVASENAHNDVVEVVVKHEAKVNALDSLGQTSLHRAAhcghlqtcrlllsyGCDP 459
Cdd:PHA02946 52 ERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLS--------------GTDD 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 460 NIIslqgftalqmgnENVQQLLQEGASLGHS--EADRQLLEAAKAGDVETVKKLCTVQ-SVNCRDIEGRQSTPLHFAAGY 536
Cdd:PHA02946 118 EVI------------ERINLLVQYGAKINNSvdEEGCGPLLACTDPSERVFKKIMSIGfEARIVDKFGKNHIHRHLMSDN 185
|
170 180 190
....*....|....*....|....*....|..
gi 755563780 537 NRVSVVEYLLQHGADVHAKDKGGLVPLHNACS 568
Cdd:PHA02946 186 PKASTISWMMKLGISPSKPDHDGNTPLHIVCS 217
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
364-459 |
9.43e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 44.42 E-value: 9.43e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 364 HETALHCAAASPYPKrKQICELLLRKGANTNEKTKEF-LTPLH---VASENAHNDVVEVVVKHEAKVNALDSLGQTSLHR 439
Cdd:PHA02859 51 YETPIFSCLEKDKVN-VEILKFLIENGADVNFKTRDNnLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLLHM 129
|
90 100
....*....|....*....|..
gi 755563780 440 -AAHCG-HLQTCRLLLSYGCDP 459
Cdd:PHA02859 130 yMCNFNvRINVIKLLIDSGVSF 151
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
213-301 |
9.76e-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: 46.23 E-value: 9.76e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 213 TPLHLAAGYNRVKIVQLLLHHGADVHAKDKGDLV---PLHNACSYGHY-----------EVTELLVKHGACVNAMDLWQF 278
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPARACGDFFvksQGVDSFYHGESplnaaaclgspSIVALLSEDPADILTADSLGN 209
|
90 100 110
....*....|....*....|....*....|..
gi 755563780 279 TPLH------EAASKNRIEVCS---LLLSYGA 301
Cdd:TIGR00870 210 TLLHllvmenEFKAEYEELSCQmynFALSLLD 241
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
431-639 |
1.10e-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: 1.10e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 431 SLGQTSLHRAA---HCGHLQTCRLLLSygCDPNIISLQGFTALQMGNEnvqqlLQEGASLGHSEADRQLLEAAKAgdveT 507
Cdd:cd21882 24 ATGKTCLHKAAlnlNDGVNEAIMLLLE--AAPDSGNPKELVNAPCTDE-----FYQGQTALHIAIENRNLNLVRL----L 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 508 VKKLCTVQSVNCRDIEGRQ--------STPLHFAAGYNRVSVVEYLLQHGAD---VHAKDKGGLVPLHnacsyghyevae 576
Cdd:cd21882 93 VENGADVSARATGRFFRKSpgnlfyfgELPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLH------------ 160
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755563780 577 llvkhgAVVNVADLwkfTPLHEAAAKGKYEickLLLQHGA--DPTKK-----NRDGNTPLDLV-KDGDTDI 639
Cdd:cd21882 161 ------ALVLQADN---TPENSAFVCQMYN---LLLSYGAhlDPTQQleeipNHQGLTPLKLAaVEGKIVM 219
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
593-623 |
1.13e-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: 39.97 E-value: 1.13e-04
10 20 30
....*....|....*....|....*....|..
gi 755563780 593 FTPLHEAAAK-GKYEICKLLLQHGADPTKKNR 623
Cdd:pfam00023 3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
376-553 |
1.15e-04 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 45.60 E-value: 1.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 376 YPKRKQICELLLRKGANTNEKTKEFLTPLHVASENAHNDVVEVV---VKHEAKVNALDSLGQTSLHRAAHCGH---LQTC 449
Cdd:PHA02798 85 YKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILlfmIENGADTTLLDKDGFTMLQVYLQSNHhidIEII 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 450 RLLLSYGCDPNIIS-LQGFTALQMG--------NENVQQLLQEGASLGHSEaDRQ-----------LLEAAKAGDVETVK 509
Cdd:PHA02798 165 KLLLEKGVDINTHNnKEKYDTLHCYfkynidriDADILKLFVDNGFIINKE-NKShkkkfmeylnsLLYDNKRFKKNILD 243
|
170 180 190 200
....*....|....*....|....*....|....*....|....
gi 755563780 510 KLCTVQSVNCRDIEGrqSTPLHFAAGYNRVSVVEYLLQHGADVH 553
Cdd:PHA02798 244 FIFSYIDINQVDELG--FNPLYYSVSHNNRKIFEYLLQLGGDIN 285
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
679-750 |
1.24e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 44.04 E-value: 1.24e-04
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755563780 679 HSTPLH--LAAGYNNLEVAEYLLQHGADVNAQDKG-GLIPLHNAASYG---HVDVAALLIKYNACVNATDKWAFTPLH 750
Cdd:PHA02859 51 YETPIFscLEKDKVNVEILKFLIENGADVNFKTRDnNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLH 128
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
435-481 |
1.25e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.34 E-value: 1.25e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 755563780 435 TSLHRAAHCGHLQTCRLLLSYGCDPNIISLQGFTALQM----GNENVQQLL 481
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFaasnGNVEVLKLL 53
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
496-546 |
1.47e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 40.34 E-value: 1.47e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 755563780 496 LLEAAKAGDVETVKKL-CTVQSVNCRDIEGRqsTPLHFAAGYNRVSVVEYLL 546
Cdd:pfam13637 5 LHAAAASGHLELLRLLlEKGADINAVDGNGE--TALHFAASNGNVEVLKLLL 54
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
157-278 |
1.57e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411980 [Multi-domain] Cd Length: 649 Bit Score: 45.57 E-value: 1.57e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 157 GRTALdladpsAKAVLTGDYKKDE----LLESARSGNEEKMMalltplnVNCHASDG--RKSTPLHLAAGYNRVKIVQLL 230
Cdd:cd22196 47 GKTCL------LKAMLNLHNGQNDtislLLDIAEKTGNLKEF-------VNAAYTDSyyKGQTALHIAIERRNMHLVELL 113
|
90 100 110 120
....*....|....*....|....*....|....*....|....*...
gi 755563780 231 LHHGADVHAKDKGDLVPLhNACSYGHYeVTELLVKHGACVNAMDLWQF 278
Cdd:cd22196 114 VQNGADVHARASGEFFKK-KKGGPGFY-FGELPLSLAACTNQLDIVKF 159
|
|
| PHA02743 |
PHA02743 |
Viral ankyrin protein; Provisional |
521-616 |
1.61e-04 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 222925 [Multi-domain] Cd Length: 166 Bit Score: 43.27 E-value: 1.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 521 DIEGRQSTplHFAAGYNRVSVV---EYLLQHGADVHAKDKG-GLVPLHNACSYGHYEVAELLVKH-GAVVNVADLWKFTP 595
Cdd:PHA02743 54 DHHGRQCT--HMVAWYDRANAVmkiELLVNMGADINARELGtGNTLLHIAASTKNYELAEWLCRQlGVNLGAINYQHETA 131
|
90 100
....*....|....*....|.
gi 755563780 596 LHEAAAKGKYEICKLLLQHGA 616
Cdd:PHA02743 132 YHIAYKMRDRRMMEILRANGA 152
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
213-239 |
1.69e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 39.55 E-value: 1.69e-04
10 20
....*....|....*....|....*..
gi 755563780 213 TPLHLAAGYNRVKIVQLLLHHGADVHA 239
Cdd:pfam13606 4 TPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
49-170 |
1.93e-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: 45.17 E-value: 1.93e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 49 VNS--RDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDG--------------GLIPLHNACSFGHAEVVNLLLQ 112
Cdd:cd22193 65 INAeyTDEYYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLE 144
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755563780 113 HG---ADPNARDNWNYTPLH---EAAIKGKIDVCIV------LLQHGAE-------PTIRNTDGRTALDLADPSAKA 170
Cdd:cd22193 145 NEhqpADIEAQDSRGNTVLHalvTVADNTKENTKFVtrmydmILIRGAKlcptvelEEIRNNDGLTPLQLAAKMGKI 221
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
47-169 |
2.03e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411980 [Multi-domain] Cd Length: 649 Bit Score: 45.18 E-value: 2.03e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 47 EKVNS--RDTAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQARDDG--------------GLIPLHNACSFGHAEVVNLL 110
Cdd:cd22196 81 EFVNAayTDSYYKGQTALHIAIERRNMHLVELLVQNGADVHARASGeffkkkkggpgfyfGELPLSLAACTNQLDIVKFL 160
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 755563780 111 LQH---GADPNARDNWNYTPLH---EAAIKGKIDVCIV------LLQHGAE--PTIR-----NTDGRTALDLADPSAK 169
Cdd:cd22196 161 LENphsPADISARDSMGNTVLHalvEVADNTPENTKFVtkmyneILILGAKirPLLKleeitNKKGLTPLKLAAKTGK 238
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
229-284 |
2.21e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.02 E-value: 2.21e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 755563780 229 LLLHHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEA 284
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
593-620 |
2.95e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 38.72 E-value: 2.95e-04
10 20
....*....|....*....|....*...
gi 755563780 593 FTPLHEAAAKGKYEICKLLLQHGADPTK 620
Cdd:smart00248 3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
188-271 |
3.39e-04 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 44.27 E-value: 3.39e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 188 GNEEKMMALLTPLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLHHGADVHAKDKGDLVPLHnACSYGHYEVTE---LLV 264
Cdd:PHA02946 49 GLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY-YLSGTDDEVIErinLLV 127
|
....*..
gi 755563780 265 KHGACVN 271
Cdd:PHA02946 128 QYGAKIN 134
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
385-440 |
3.51e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.25 E-value: 3.51e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 755563780 385 LLLRKGANTNEKTKEFLTPLHVASENAHNDVVEVVVKHEAKVNALDSLGQTSLHRA 440
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
648-699 |
3.57e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.18 E-value: 3.57e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 755563780 648 ALLDAAKKGCLARVKKL-SSPDNVNCRDTQGRhsTPLHLAAGYNNLEVAEYLL 699
Cdd:pfam13637 4 ALHAAAASGHLELLRLLlEKGADINAVDGNGE--TALHFAASNGNVEVLKLLL 54
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
153-305 |
4.04e-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: 44.10 E-value: 4.04e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 153 RNTDGRTALdladpsAKAVLTGDYKKDE----LLESARSGNEEKMMAlltplNVNCHASDGRKSTPLHLAAGYNRVKIVQ 228
Cdd:cd21882 22 RGATGKTCL------HKAALNLNDGVNEaimlLLEAAPDSGNPKELV-----NAPCTDEFYQGQTALHIAIENRNLNLVR 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 229 LLLHHGADVHAKDKGDL-------------VPLHNACSYGHYEVTELLVKHG---ACVNAMDLWQFTPLH---EAASK-- 287
Cdd:cd21882 91 LLVENGADVSARATGRFfrkspgnlfyfgeLPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLHalvLQADNtp 170
|
170 180
....*....|....*....|....
gi 755563780 288 -NRIEVCS---LLLSYGA--DPTL 305
Cdd:cd21882 171 eNSAFVCQmynLLLSYGAhlDPTQ 194
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
105-308 |
4.21e-04 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 44.13 E-value: 4.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 105 EVVNLLLQHGADPNARDNWNYTPLHEAAIKGKIDVCIV--LLQHGAEPTIRNTDGRTaldladPSAKAVLTGDYKKDELl 182
Cdd:PHA02716 193 DILEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASVIkkIIELGGDMDMKCVNGMS------PIMTYIINIDNINPEI- 265
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 183 esarsgneekmmalltpLNVNCHASDGRKSTP----LHL---AAGYNRVKIVQLLLHHGADVHAKDKGDLVPLHNAC--S 253
Cdd:PHA02716 266 -----------------TNIYIESLDGNKVKNipmiLHSyitLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHQYIlrH 328
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755563780 254 YGHYEVTELLVKHGACVNAMDLWQFTPLH--------------EAASKNRIEVCSLLLSYGADPTLLNC 308
Cdd:PHA02716 329 NISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvvnildpETDNDIRLDVIQCLISLGADITAVNC 397
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
94-119 |
5.75e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 38.01 E-value: 5.75e-04
10 20
....*....|....*....|....*.
gi 755563780 94 PLHNACSFGHAEVVNLLLQHGADPNA 119
Cdd:pfam13606 5 PLHLAARNGRLEIVKLLLENGADINA 30
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
213-239 |
6.22e-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: 6.22e-04
10 20
....*....|....*....|....*..
gi 755563780 213 TPLHLAAGYNRVKIVQLLLHHGADVHA 239
Cdd:smart00248 4 TPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
213-310 |
6.45e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 42.11 E-value: 6.45e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 213 TPLH--LAAGYNRVKIVQLLLHHGADVHAKDKGD-LVPLHNACSYG---HYEVTELLVKHGACVNAMDLWQFTPLHEAAS 286
Cdd:PHA02859 53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRDNnLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHMYMC 132
|
90 100
....*....|....*....|....*.
gi 755563780 287 K--NRIEVCSLLLSYGADPTLLNCHN 310
Cdd:PHA02859 133 NfnVRINVIKLLIDSGVSFLNKDFDN 158
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
594-787 |
6.87e-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: 43.33 E-value: 6.87e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 594 TPLHEAA---AKGKYEICKLLLQhgADPtkknrDGNTPLDLVKDGDTDiqDLLRGDAALLDAAKKGCLARVKKL-SSPDN 669
Cdd:cd21882 28 TCLHKAAlnlNDGVNEAIMLLLE--AAP-----DSGNPKELVNAPCTD--EFYQGQTALHIAIENRNLNLVRLLvENGAD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 670 VNCRDTQ-------------GRHstPLHLAAGYNNLEVAEYLLQHGAD---VNAQDKGGLIPLHnaasyghvdvaALLIK 733
Cdd:cd21882 99 VSARATGrffrkspgnlfyfGEL--PLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLH-----------ALVLQ 165
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755563780 734 YNacvNATDKWAFTplheaaqkgrTQLCALLLAHGA--DPTLK-----NQEGQTPLDLVSS 787
Cdd:cd21882 166 AD---NTPENSAFV----------CQMYNLLLSYGAhlDPTQQleeipNHQGLTPLKLAAV 213
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
747-787 |
6.98e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.41 E-value: 6.98e-04
10 20 30 40
....*....|....*....|....*....|....*....|.
gi 755563780 747 TPLHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLVSS 787
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAAS 43
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
528-554 |
7.49e-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: 7.49e-04
10 20
....*....|....*....|....*..
gi 755563780 528 TPLHFAAGYNRVSVVEYLLQHGADVHA 554
Cdd:smart00248 4 TPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
212-302 |
7.62e-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: 43.08 E-value: 7.62e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 212 STPLHLAAGYNRVKIVQ-LLLHHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKhgaCV-----NAM--DLWQ-FTPLH 282
Cdd:cd22192 18 ESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME---AApelvnEPMtsDLYQgETALH 94
|
90 100
....*....|....*....|
gi 755563780 283 EAASKNRIEVCSLLLSYGAD 302
Cdd:cd22192 95 IAVVNQNLNLVRELIARGAD 114
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
60-86 |
7.88e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 37.62 E-value: 7.88e-04
10 20
....*....|....*....|....*..
gi 755563780 60 TPLHFAAGFGRKDVVEYLLQNGANVQA 86
Cdd:pfam13606 4 TPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
682-809 |
1.29e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 42.35 E-value: 1.29e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 682 PLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGH--VDVAALLIKYNACV-NATDKWAFTPL--------- 749
Cdd:PHA02946 75 PLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKInNSVDEEGCGPLlactdpser 154
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 750 -------------------------HEAAQKGRTQLCALLLAHGADPTLKNQEGQTPLDLVSSLLCRS---------QIC 795
Cdd:PHA02946 155 vfkkimsigfearivdkfgknhihrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKNvdiinlllpSTD 234
|
170
....*....|....
gi 755563780 796 VNHWNRSAFSPLPL 809
Cdd:PHA02946 235 VNKQNKFGDSPLTL 248
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
693-790 |
1.51e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 41.51 E-value: 1.51e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 693 EVAEYLLQHGADVNAQDKGGLI----PLHNAASYGHVDVAALLIKYNACVNATDKWA-FTPLHEAAQKGRTQLCALLLAH 767
Cdd:PHA02884 47 DIIDAILKLGADPEAPFPLSENsktnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkITPLYISVLHGCLKCLEILLSY 126
|
90 100
....*....|....*....|...
gi 755563780 768 GADPTLKNQEGQTPLDLvSSLLC 790
Cdd:PHA02884 127 GADINIQTNDMVTPIEL-ALMIC 148
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
41-170 |
1.61e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 42.05 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 41 KRLVTPEKVNSrdtAGRKSTPLHFAAGFGRKDVVEYLLQNGANVQA-----------RDDG---GLIPLHNACSFGHAEV 106
Cdd:cd22194 127 DRFINAEYTEE---AYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpkyKHEGfyfGETPLALAACTNQPEI 203
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 755563780 107 VNLLLQHGADPNA-RDNWNYTPLHEAAI-----KGKIDVCI-----VLLQHGAE--PTIRNTDGRTALDLADPSAKA 170
Cdd:cd22194 204 VQLLMEKESTDITsQDSRGNTVLHALVTvaedsKTQNDFVKrmydmILLKSENKnlETIRNNEGLTPLQLAAKMGKA 280
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
49-238 |
1.94e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 41.74 E-value: 1.94e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 49 VNSRDTAGRksTPLHFAAGFG---RKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHA---EVVNLLLQHGADPNARDN 122
Cdd:PHA02798 102 INKKNSDGE--TPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNN 179
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 123 W-NYTPLHeAAIK---GKIDVCIVLLQhgaeptirnTDGRTALDLADPSAKAVLTgDYKKDeLLESARSGNEEKMMALLT 198
Cdd:PHA02798 180 KeKYDTLH-CYFKyniDRIDADILKLF---------VDNGFIINKENKSHKKKFM-EYLNS-LLYDNKRFKKNILDFIFS 247
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 755563780 199 PLNVNchASDGRKSTPLHLAAGYNRVKIVQLLLHHGADVH 238
Cdd:PHA02798 248 YIDIN--QVDELGFNPLYYSVSHNNRKIFEYLLQLGGDIN 285
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
562-587 |
2.08e-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: 2.08e-03
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
278-305 |
2.10e-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: 2.10e-03
10 20
....*....|....*....|....*...
gi 755563780 278 FTPLHEAASKNRIEVCSLLLSYGADPTL 305
Cdd:smart00248 3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
433-461 |
2.13e-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: 36.50 E-value: 2.13e-03
10 20 30
....*....|....*....|....*....|
gi 755563780 433 GQTSLHRAA-HCGHLQTCRLLLSYGCDPNI 461
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
60-84 |
2.30e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.41 E-value: 2.30e-03
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
594-618 |
2.35e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 36.08 E-value: 2.35e-03
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
28-161 |
2.60e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 40.19 E-value: 2.60e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 28 LFEACRNGDVERVKRLVTpekvNSRDTAGRKSTPLH--FAAGFGRKDVVEYLLQNGANVQARDDG-GLIPLHNACSFG-- 102
Cdd:PHA02859 25 LFYYVEKDDIEGVKKWIK----FVNDCNDLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRDnNLSALHHYLSFNkn 100
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755563780 103 -HAEVVNLLLQHGADPNARDNWNYTPLHE--AAIKGKIDVCIVLLQHGAEPTIRNTDGRTAL 161
Cdd:PHA02859 101 vEPEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLIDSGVSFLNKDFDNNNIL 162
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
749-782 |
2.85e-03 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 37.79 E-value: 2.85e-03
10 20 30
....*....|....*....|....*....|....
gi 755563780 749 LHEAAQKGRTQLCALLLAHGADPTLKNQEGQTPL 782
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTAL 34
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
433-461 |
3.03e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 36.08 E-value: 3.03e-03
10 20
....*....|....*....|....*....
gi 755563780 433 GQTSLHRAAHCGHLQTCRLLLSYGCDPNI 461
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
225-301 |
3.03e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 41.19 E-value: 3.03e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755563780 225 KIVQLLLHHGADVHAKDKGDLVPLHNACSYGHYEVTELLVKHGACVNAMDLWQFTPLHEAASKNR--IEVCSLLLSYGA 301
Cdd:PHA02946 53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGA 131
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
61-145 |
3.06e-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: 41.22 E-value: 3.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 61 PLHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLH-----NACSFGHAEVV----NLLLQHGAD----------PNARD 121
Cdd:TIGR00870 178 PLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHllvmeNEFKAEYEELScqmyNFALSLLDKlrdskeleviLNHQG 257
|
90 100
....*....|....*....|....
gi 755563780 122 NwnyTPLHEAAIKGKIDVCIVLLQ 145
Cdd:TIGR00870 258 L---TPLKLAAKEGRIVLFRLKLA 278
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
534-629 |
3.36e-03 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 41.05 E-value: 3.36e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 534 AGYNRVSVVEYLLQHGADVHAKDKGGLVPLHNAC--SYGHYEVAELLVKHGAVVNVADLWKFTPLH-------------- 597
Cdd:PHA02716 292 ARNIDISVVYSFLQPGVKLHYKDSAGRTCLHQYIlrHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvvnildp 371
|
90 100 110
....*....|....*....|....*....|..
gi 755563780 598 EAAAKGKYEICKLLLQHGADPTKKNRDGNTPL 629
Cdd:PHA02716 372 ETDNDIRLDVIQCLISLGADITAVNCLGYTPL 403
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
712-743 |
3.67e-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: 3.67e-03
10 20 30
....*....|....*....|....*....|...
gi 755563780 712 GLIPLHNAA-SYGHVDVAALLIKYNACVNATDK 743
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| TRPV2 |
cd22197 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ... |
181-275 |
4.05e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411981 [Multi-domain] Cd Length: 640 Bit Score: 40.99 E-value: 4.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 181 LLESARSGNEEKMmalltpLNVNCHASDGRKSTPLHLAAGYNRVKIVQLLLHHGADVHAKDKGDLVPLH-NACSYghyeV 259
Cdd:cd22197 70 LEIDKDSGNPKPL------VNAQCTDEYYRGHSALHIAIEKRSLQCVKLLVENGADVHARACGRFFQKKqGTCFY----F 139
|
90
....*....|....*.
gi 755563780 260 TELLVKHGACVNAMDL 275
Cdd:cd22197 140 GELPLSLAACTKQWDV 155
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
562-587 |
4.11e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 35.70 E-value: 4.11e-03
10 20
....*....|....*....|....*.
gi 755563780 562 PLHNACSYGHYEVAELLVKHGAVVNV 587
Cdd:pfam13606 5 PLHLAARNGRLEIVKLLLENGADINA 30
|
|
| PHA02743 |
PHA02743 |
Viral ankyrin protein; Provisional |
186-301 |
4.86e-03 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 222925 [Multi-domain] Cd Length: 166 Bit Score: 38.64 E-value: 4.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 186 RSGNEEKMMALLTPLNVNCHA-----SDGRKSTplHLAAGYNR---VKIVQLLLHHGADVHAKDK--GDLVpLHNACSYG 255
Cdd:PHA02743 29 RTGNIYELMEVAPFISGDGHLlhrydHHGRQCT--HMVAWYDRanaVMKIELLVNMGADINARELgtGNTL-LHIAASTK 105
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 755563780 256 HYEVTELLVKH-GACVNAMDLWQFTPLHEAASKNRIEVCSLLLSYGA 301
Cdd:PHA02743 106 NYELAEWLCRQlGVNLGAINYQHETAYHIAYKMRDRRMMEILRANGA 152
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
686-771 |
5.09e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 40.62 E-value: 5.09e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 686 AAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNAASYGHVDVAALLIKYNACVNATDKWAFTPLHEAAQKGRTQLCALL- 764
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILy 611
|
....*...
gi 755563780 765 -LAHGADP 771
Cdd:PLN03192 612 hFASISDP 619
|
|
| PHA02730 |
PHA02730 |
ankyrin-like protein; Provisional |
71-308 |
5.28e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165098 [Multi-domain] Cd Length: 672 Bit Score: 40.39 E-value: 5.28e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 71 KDVVEYLLQNGANVQARDDGGLIPLHNACSFG--HAEVVNLLLQHGADPNARDNWNyTPLHEAAIKGKIDVCIVLLQHGA 148
Cdd:PHA02730 215 KDVIKCLIDNNVSIHGRDEGGSLPIQYYWSCStiDIEIVKLLIKDVDTCSVYDDIS-QPYIRGVLADYLNKRFRVTPYNV 293
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 149 EPTIRN--TDGRTALDLADPSAKAVLTGDYKK---DELLESARSGNEEKMMALL-----------TPLnVNCHASDGR-- 210
Cdd:PHA02730 294 DMEIVNllIEGRHTLIDVMRSITSYDSREYNHyiiDNILKRFRQQDESIVQAMLinylhygdmvsIPI-LRCMLDNGAtm 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 211 -KST----PLHLAAGYNR----VKIVQLLLH---HGADVHAKDKGDL------VPLHNACSYGHYE-----VTELLVKHG 267
Cdd:PHA02730 373 dKTTdnnyPLHDYFVNNNnivdVNVVRFIVEnngHMAINHVSNNGRLcmygliLSRFNNCGYHCYEtilidVFDILSKYM 452
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 755563780 268 ACVNAMDLWQFTPLHEAASKNRIEVCSLLLSYGADPTLLNC 308
Cdd:PHA02730 453 DDIDMIDNENKTLLYYAVDVNNIQFARRLLEYGASVNTTSR 493
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
72-161 |
6.21e-03 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 40.28 E-value: 6.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 72 DVVEYLLQNGANVQARDDGGLIPLHNAC--SFGHAEVVNLLLQHGADPNARDNWNYTPLH--------------EAAIKG 135
Cdd:PHA02716 298 SVVYSFLQPGVKLHYKDSAGRTCLHQYIlrHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvvnildpETDNDI 377
|
90 100
....*....|....*....|....*.
gi 755563780 136 KIDVCIVLLQHGAEPTIRNTDGRTAL 161
Cdd:PHA02716 378 RLDVIQCLISLGADITAVNCLGYTPL 403
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
358-598 |
6.57e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 40.25 E-value: 6.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 358 FKHPQTHETALHCAAASPYPKRKQiCELLLRKGANTNEKTKEFL------------TPLHVASENAHNDVVEVVVKHEAK 425
Cdd:cd21882 20 YQRGATGKTCLHKAALNLNDGVNE-AIMLLLEAAPDSGNPKELVnapctdefyqgqTALHIAIENRNLNLVRLLVENGAD 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 426 VNA-------------LDSLGQTSLHRAAHCGHLQTCRLLLSYGCDPNIISLQGftalQMGNENVQQL-LQEGASLGHSE 491
Cdd:cd21882 99 VSAratgrffrkspgnLFYFGELPLSLAACTNQEEIVRLLLENGAQPAALEAQD----SLGNTVLHALvLQADNTPENSA 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 492 ADRQLLEAAKAGDvetvKKLCTVQSVNcrDIEGRQS-TPLHFAAGYNRVSVVEYLLQ---HGADVHAKDK---------- 557
Cdd:cd21882 175 FVCQMYNLLLSYG----AHLDPTQQLE--EIPNHQGlTPLKLAAVEGKIVMFQHILQrefSGPYQPLSRKftewtygpvt 248
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 755563780 558 GGLVPLHNACSYGHYEVAELLVKHGAVVNVADLWKFTPLHE 598
Cdd:cd21882 249 SSLYDLSEIDSWEKNSVLELIAFSKKREARHQMLVQEPLNE 289
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
124-152 |
7.05e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 34.87 E-value: 7.05e-03
10 20
....*....|....*....|....*....
gi 755563780 124 NYTPLHEAAIKGKIDVCIVLLQHGAEPTI 152
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
169-303 |
7.06e-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: 40.13 E-value: 7.06e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 169 KAVLTGDYKKDELLESARSGNEEKmmALLTPL-NVNCHASDGRKSTPLHLAAGYNRVKIVQLLLHHGADVHAKDKGDLV- 246
Cdd:cd22194 100 KALLNINENTKEIVRILLAFAEEN--GILDRFiNAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFFn 177
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 755563780 247 PLHNacsyghyevtellvkhgacvnaMDLWQF--TPLHEAASKNRIEVCSLLLSYGADP 303
Cdd:cd22194 178 PKYK----------------------HEGFYFgeTPLALAACTNQPEIVQLLMEKESTD 214
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
576-749 |
8.10e-03 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 39.65 E-value: 8.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 576 ELLVKHGAVVNVADLWKFTPLHEAAAKGKYEICKLLLQHGADPTKKNRDGNTPLDLVKDGDTDIQD----LLRGDAALLD 651
Cdd:PHA02946 56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIErinlLVQYGAKINN 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755563780 652 AA-KKGC---LA------RV--KKLSSPDNVNCRDTQGRHSTPLHLAAGYNNLEVAEYLLQHGADVNAQDKGGLIPLHNA 719
Cdd:PHA02946 136 SVdEEGCgplLActdpseRVfkKIMSIGFEARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIV 215
|
170 180 190
....*....|....*....|....*....|..
gi 755563780 720 AS--YGHVDVAALLIKyNACVNATDKWAFTPL 749
Cdd:PHA02946 216 CSktVKNVDIINLLLP-STDVNKQNKFGDSPL 246
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
62-130 |
8.12e-03 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 39.85 E-value: 8.12e-03
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755563780 62 LHFAAGFGRKDVVEYLLQNGANVQARDDGGLIPLHNACSFGHAEVVNLLLQHGAD---PNARDNWNYTPLHE 130
Cdd:PLN03192 626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADvdkANTDDDFSPTELRE 697
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
559-589 |
8.73e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 34.57 E-value: 8.73e-03
10 20 30
....*....|....*....|....*....|..
gi 755563780 559 GLVPLHNAC-SYGHYEVAELLVKHGAVVNVAD 589
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
746-775 |
9.08e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 34.57 E-value: 9.08e-03
10 20 30
....*....|....*....|....*....|.
gi 755563780 746 FTPLHEAA-QKGRTQLCALLLAHGADPTLKN 775
Cdd:pfam00023 3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| |
