|
Name |
Accession |
Description |
Interval |
E-value |
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
55-342 |
1.15e-47 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 172.06 E-value: 1.15e-47
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 55 ILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNV 134
Cdd:COG0666 3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 135 ADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLGCKDRKGYGLLHTAAA 214
Cdd:COG0666 83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 215 SGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGALcLELLVNN 294
Cdd:COG0666 163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLLEA 241
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1034579110 295 GADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPL 342
Cdd:COG0666 242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
86-365 |
1.42e-46 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 168.98 E-value: 1.42e-46
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 86 EKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLLNKGASL 165
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 166 NVCDKKERQPLHWAAFLGHLEVLKLLVARGADLGCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIA 245
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 246 CYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGALcLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILI 325
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI-VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1034579110 326 QNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADTA 365
Cdd:COG0666 240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
36-300 |
4.87e-45 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 164.74 E-value: 4.87e-45
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 36 QDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAA 115
Cdd:COG0666 17 LLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAAR 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 116 NRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARG 195
Cdd:COG0666 97 NGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 196 ADLGCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPL 275
Cdd:COG0666 177 ADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTAL 256
|
250 260
....*....|....*....|....*
gi 1034579110 276 HVAAVSTNGALCLELLVNNGADVNY 300
Cdd:COG0666 257 LLAAAAGAALIVKLLLLALLLLAAA 281
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
35-275 |
3.65e-43 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 158.96 E-value: 3.65e-43
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 35 SQDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAA 114
Cdd:COG0666 49 LADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAA 128
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 115 ANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVAR 194
Cdd:COG0666 129 YNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 195 GADLGCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTP 274
Cdd:COG0666 209 GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
.
gi 1034579110 275 L 275
Cdd:COG0666 289 L 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
185-488 |
2.13e-37 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 142.40 E-value: 2.13e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 185 LEVLKLLVARGADLGCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANV 264
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 265 NQPNDKGFTPLHvAAVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHV 344
Cdd:COG0666 81 NAKDDGGNTLLH-AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 345 AARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRKLlssgqlysivsslsnehvLSAGFDINTPDNLGRT 424
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL------------------LEAGADVNAKDNDGKT 221
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034579110 425 CLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKG 488
Cdd:COG0666 222 ALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
55-416 |
6.99e-37 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 149.06 E-value: 6.99e-37
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 55 ILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVN--ARDKLwqTPLHVAAANRATKCAEALAPLLSSL 132
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNiiALDDL--SVLECAVDSKNIDTIKAIIDNRSNI 237
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 133 NVADRSgrsaLHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVL-KLLVARGADLGCKDRKGYGLLHT 211
Cdd:PHA02876 238 NKNDLS----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYL 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 212 AAASG-QIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDA-VAIELVNAGANVNQPNDKGFTPLHVAAVStNGALCLE 289
Cdd:PHA02876 314 MAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVR-NNVVIIN 392
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 290 LLVNNGADVNYQSKEGKSPLHMaAIHGR--FTRSQILIQNGSEIDCADKFGNTPLHVAARYGHEL-LISTLMTNGADTAR 366
Cdd:PHA02876 393 TLLDYGADIEALSQKIGTALHF-ALCGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNA 471
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|
gi 1034579110 367 RGIHDMFPLHLAVlfGFSDCCRKLLSSGqlysivSSLSNEHVLSAGFDIN 416
Cdd:PHA02876 472 INIQNQYPLLIAL--EYHGIVNILLHYG------AELRDSRVLHKSLNDN 513
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
41-316 |
2.49e-34 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 138.23 E-value: 2.49e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 41 RTPLHA--AAYVGDVP-ILQLLLMSGANVNAKDTLWLTPLHRAAASRN-EKVLGLLLAHSADVNARDKLWQTPLHVAaan 116
Cdd:PHA03095 48 KTPLHLylHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVY--- 124
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 117 ratkcaealaplLSSLNVadrsgrsalhhavhsgHLETVNLLLNKGASLNVCDKKERQPLHwaAFLGH----LEVLKLLV 192
Cdd:PHA03095 125 ------------LSGFNI----------------NPKVIRLLLRKGADVNALDLYGMTPLA--VLLKSrnanVELLRLLI 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 193 ARGADLGCKDRKGYGLLHTAAASGQI--EVVKYLLRMGAEIDEPNAFGNTALHIACYLG--QDAVAIELVNAGANVNQPN 268
Cdd:PHA03095 175 DAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARN 254
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1034579110 269 DKGFTPLHVAAVSTNGALCLELLvNNGADVNYQSKEGKSPLHMAAIHG 316
Cdd:PHA03095 255 RYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGNTPLSLMVRNN 301
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
532-811 |
1.29e-33 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 131.61 E-value: 1.29e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 532 LEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNCLEDVESTIPVSPLHLAAYNGHCEALKTLAETLVNLD 611
Cdd:COG0666 2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 612 VRDHKGRTALFLATERGSTECVEVLTAHGASALIKErKRKWTPLHAAAASGHTDSLHLLIDSGerADItDVMDAYGQTPL 691
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD-KDGETPLHLAAYNGNLEIVKLLLEAG--ADV-NAQDNDGNTPL 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 692 MLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFVLCRDFKGRTPIHLASACGHTAVLRT 771
Cdd:COG0666 158 HLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
|
250 260 270 280
....*....|....*....|....*....|....*....|
gi 1034579110 772 LLQAALstdpLDAGVDYSGYSPMHWASYTGHEDCLELLLE 811
Cdd:COG0666 238 LLEAGA----DLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
288-621 |
1.40e-33 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 131.23 E-value: 1.40e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 288 LELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADTARR 367
Cdd:COG0666 4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 368 GIHDMFPLHLAVLFGFSDCCRKLLSsgqlysivsslsnehvlsAGFDINTPDNLGRTCLHAAASGGNVECLNLLLSSGAD 447
Cdd:COG0666 84 DDGGNTLLHAAARNGDLEIVKLLLE------------------AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD 145
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 448 LRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAASDtyrraephtpsshdaeedeplkesrRKE 527
Cdd:COG0666 146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG-------------------------HLE 200
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 528 AffcLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNclEDVESTIPVSPLHLAAYNGHCEALKTLAETL 607
Cdd:COG0666 201 I---VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD--LNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
|
330
....*....|....
gi 1034579110 608 VNLDVRDHKGRTAL 621
Cdd:COG0666 276 LLLAAALLDLLTLL 289
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
667-997 |
5.42e-33 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 129.69 E-value: 5.42e-33
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 667 LHLLIDSGERADITDVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFV 746
Cdd:COG0666 1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 747 LCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDpldaGVDYSGYSPMHWASYTGHEDCLELLLEHspfsylegnpftpl 826
Cdd:COG0666 81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN----ARDKDGETPLHLAAYNGNLEIVKLLLEA-------------- 142
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 827 hcavinnqdsttemllgalGAKiVNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAV 906
Cdd:COG0666 143 -------------------GAD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 907 EFLLYRGkADLTVLDENKNTALHLACSKGHEKCALMILAEtqdLGLINATNSALQMPLHIAARNGLASVVQALLSHGATV 986
Cdd:COG0666 203 KLLLEAG-ADVNAKDNDGKTALDLAAENGNLEIVKLLLEA---GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
|
330
....*....|.
gi 1034579110 987 LAVDEEGHTPA 997
Cdd:COG0666 279 AAALLDLLTLL 289
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
91-358 |
2.16e-31 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 129.37 E-value: 2.16e-31
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 91 LLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSS---LNVADRSGRSALH-HAVHSGHLETVNLLLNKGASLN 166
Cdd:PHA03095 32 RLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAgadVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVN 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 167 VCDKKERQPLHwaAFLG----HLEVLKLLVARGADLGCKDRKGYGLLHTAAASGQ--IEVVKYLLRMGAEIDEPNAFGNT 240
Cdd:PHA03095 112 AKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 241 ALHIAC-YLGQDA-VAIELVNAGANVNQPNDKGFTPLHVAAV-STNGALCLELLVNNGADVNYQSKEGKSPLHMAAIHGR 317
Cdd:PHA03095 190 LLHHHLqSFKPRArIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNN 269
|
250 260 270 280
....*....|....*....|....*....|....*....|.
gi 1034579110 318 FTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLM 358
Cdd:PHA03095 270 PRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
772-1014 |
1.16e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 122.76 E-value: 1.16e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 772 LLQAALSTDPLDAGVDYSGYSPMHWASYTGHEDCLELLLEHSPFSYLEGNPFTPLHCAVINNQDSTTEMLLGALGAKIvN 851
Cdd:COG0666 3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI-N 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 852 SRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLLYRGkADLTVLDENKNTALHLA 931
Cdd:COG0666 82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLA 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 932 CSKGHEKCALMILAETQDlglINATNSALQMPLHIAARNGLASVVQALLSHGATVLAVDEEGHTPALACAPNKDVADCLA 1011
Cdd:COG0666 161 AANGNLEIVKLLLEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237
|
...
gi 1034579110 1012 LIL 1014
Cdd:COG0666 238 LLE 240
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
705-1014 |
4.19e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 121.21 E-value: 4.19e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 705 LLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFVLCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDA 784
Cdd:COG0666 6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 785 GvdysGYSPMHWASYTGHEDCLELLLEHspfsylegnpftplhcavinnqdsttemllgalGAKiVNSRDAKGRTPLHAA 864
Cdd:COG0666 86 G----GNTLLHAAARNGDLEIVKLLLEA---------------------------------GAD-VNARDKDGETPLHLA 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 865 AFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLLYRGkADLTVLDENKNTALHLACSKGHEKCALMIL 944
Cdd:COG0666 128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENGHLEIVKLLL 206
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 945 AETQDlglINATNSALQMPLHIAARNGLASVVQALLSHGATVLAVDEEGHTPALACAPNKDVADCLALIL 1014
Cdd:COG0666 207 EAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
587-859 |
9.68e-30 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 120.06 E-value: 9.68e-30
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 587 PLHLAAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGAsALIKERKRKWTPLHAAAASGHTDS 666
Cdd:COG0666 24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-DINAKDDGGNTLLHAAARNGDLEI 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 667 LHLLIDSGerADItDVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFV 746
Cdd:COG0666 103 VKLLLEAG--ADV-NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 747 LCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAgvdySGYSPMHWASYTGHEDCLELLLEHSPFSYLEGNPFTPL 826
Cdd:COG0666 180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN----DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
|
250 260 270
....*....|....*....|....*....|...
gi 1034579110 827 HCAVINNQDSTTEMLLGALGAKIVNSRDAKGRT 859
Cdd:COG0666 256 LLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
511-757 |
4.74e-29 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 118.13 E-value: 4.74e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 511 SHDAEEDEPLKESRRKEAFFCLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNCleDVESTIPVSPLHL 590
Cdd:COG0666 49 LADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV--NARDKDGETPLHL 126
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 591 AAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKErKRKWTPLHAAAASGHTDSLHLL 670
Cdd:COG0666 127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD-NDGETPLHLAAENGHLEIVKLL 205
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 671 IDSGerADITDVmDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFVLCRD 750
Cdd:COG0666 206 LEAG--ADVNAK-DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
|
....*..
gi 1034579110 751 FKGRTPI 757
Cdd:COG0666 283 LDLLTLL 289
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
152-444 |
5.03e-29 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 122.06 E-value: 5.03e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 152 LETVNLLLNKGASLNVCDKKERQPLHwaAFLGH-----LEVLKLLVARGADLGCKDRKGYGLLHTAAASGQ-IEVVKYLL 225
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLH--LYLHYssekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLI 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 226 RMGAEIDEPNAFGNTALHIacYLGQDAVA---IE-LVNAGANVNQPNDKGFTPLHVAAVSTNGAL-CLELLVNNGADVNY 300
Cdd:PHA03095 105 KAGADVNAKDKVGRTPLHV--YLSGFNINpkvIRlLLRKGADVNALDLYGMTPLAVLLKSRNANVeLLRLLIDAGADVYA 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 301 QSKEGKSPLHmaaIHGRFTRS-----QILIQNGSEIDCADKFGNTPLHVAARYG--HELLISTLMTNGADTARRGIHDMF 373
Cdd:PHA03095 183 VDDRFRSLLH---HHLQSFKPrarivRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQT 259
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034579110 374 PLHLAVLFGFSDCCRKLlssgqlysivsslsnehvLSAGFDINTPDNLGRTCLHAAASGGNVECLNLLLSS 444
Cdd:PHA03095 260 PLHYAAVFNNPRACRRL------------------IALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
38-372 |
6.15e-29 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 121.22 E-value: 6.15e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 38 QERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVNArdklwqtpLHVAAANR 117
Cdd:PHA02874 33 DETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI--------LPIPCIEK 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 118 atkcaEALAPLLSS---LNVADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVAR 194
Cdd:PHA02874 105 -----DMIKTILDCgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEK 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 195 GADLGCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNdkGFTP 274
Cdd:PHA02874 180 GAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDID--GSTP 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 275 LHVAAVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAAIH-GRFTRSQILIQNGSEIDCADKFGNTPL--HVaaryghE 351
Cdd:PHA02874 258 LHHAINPPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKDIIANAVLIKEADKLKDSDFleHI------E 331
|
330 340
....*....|....*....|.
gi 1034579110 352 LLISTLMTNGADTARRGIHDM 372
Cdd:PHA02874 332 IKDNKEFSDFIKECNEEIEDM 352
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
655-955 |
1.44e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 116.98 E-value: 1.44e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 655 LHAAAASGHTDSLHLLIDSGERADITDVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCED 734
Cdd:COG0666 22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLE 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 735 CLAALLDHDAFVLCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAgvdySGYSPMHWASYTGHEDCLELLLEHsp 814
Cdd:COG0666 102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN----DGNTPLHLAAANGNLEIVKLLLEA-- 175
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 815 fsylegnpftplhcavinnqdsttemllgalGAKiVNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTAL 894
Cdd:COG0666 176 -------------------------------GAD-VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034579110 895 MTAAENGQTAAVEFLLYRGkADLTVLDENKNTALHLACSKGHEKCALMILAETQDLGLINA 955
Cdd:COG0666 224 DLAAENGNLEIVKLLLEAG-ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
20-300 |
3.92e-28 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 118.61 E-value: 3.92e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 20 IAPLPRAHTPCSFLPSQDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLH-----RAAASRNEKVLGLLLA 94
Cdd:PHA03100 15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 95 HSADVNARDKLWQTPLHVAAANratkcaealapllsslnvadrsgrsalhhavHSGHLETVNLLLNKGASLNVCDKKERQ 174
Cdd:PHA03100 95 YGANVNAPDNNGITPLLYAISK-------------------------------KSNSYSIVEYLLDNGANVNIKNSDGEN 143
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 175 PLHWAAFLGH--LEVLKLLVARGADLGCKDRkgygllhtaaasgqievVKYLLRMGAEIDEPNAFGNTALHIACYlgqdA 252
Cdd:PHA03100 144 LLHLYLESNKidLKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVY----N 202
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1034579110 253 VAIELVNA----GANVNQPNDKGFTPLHVAAVSTNGALcLELLVNNGADVNY 300
Cdd:PHA03100 203 NNPEFVKYlldlGANPNLVNKYGDTPLHIAILNNNKEI-FKLLLNNGPSIKT 253
|
|
| ANKYR |
COG0666 |
Ankyrin repeat [Signal transduction mechanisms]; |
409-724 |
4.10e-28 |
|
Ankyrin repeat [Signal transduction mechanisms];
Pssm-ID: 440430 [Multi-domain] Cd Length: 289 Bit Score: 115.44 E-value: 4.10e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 409 LSAGFDINTPDNLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKG 488
Cdd:COG0666 41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 489 CSPLHYAAASDTYRRAEphtpsshdaeedeplkesrrkeaffcleFLLDNGADPSLRDRQGYTavhyaaaygnrqnlell 568
Cdd:COG0666 121 ETPLHLAAYNGNLEIVK----------------------------LLLEAGADVNAQDNDGNT----------------- 155
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 569 lemsfncledvestipvsPLHLAAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKEr 648
Cdd:COG0666 156 ------------------PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD- 216
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034579110 649 KRKWTPLHAAAASGHTDSLHLLIDSGERADITdvmDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTAL 724
Cdd:COG0666 217 NDGKTALDLAAENGNLEIVKLLLEAGADLNAK---DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
185-475 |
6.23e-28 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 118.97 E-value: 6.23e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 185 LEVLKLLVARGADLGCKDRKGYGLLHTAAASGQ---IEVVKYLLRMGAEIDEPNAFGNTALHiaCYLgQDAVAIE----L 257
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLH--LYL-YNATTLDviklL 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 258 VNAGANVNQPNDKGFTPLHVAAVSTNGALC-LELLVNNGADVNYQSKEGKSPLHmaaIHGRFTRSQI-----LIQNGSEI 331
Cdd:PHA03095 104 IKAGADVNAKDKVGRTPLHVYLSGFNINPKvIRLLLRKGADVNALDLYGMTPLA---VLLKSRNANVellrlLIDAGADV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 332 DCADKFGNTPLHVAARYGH--ELLISTLMTNGADTARRGIHDMFPLHlaVLFGFSDCCRkllssgqlySIVSSLsnehvL 409
Cdd:PHA03095 181 YAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNTPLH--SMATGSSCKR---------SLVLPL-----L 244
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034579110 410 SAGFDINTPDNLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYqCAVTLV 475
Cdd:PHA03095 245 IAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNG-RAVRAA 309
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
218-659 |
7.49e-28 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 118.59 E-value: 7.49e-28
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 218 IEVVKYLLRMGAEIDEPNAFGNTALH--IACYLGQDAVAIE-LVNAGANVNQPNDKGFTPLHVAAVSTNGALCLELLVNN 294
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKDIVRlLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 295 GADVNYQskegksplhmaaihgrftrsqiliqngseidcaDKFGNTPLHVAAR--YGHELLISTLMTNGADTARRGIHDM 372
Cdd:PHA03095 107 GADVNAK---------------------------------DKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGM 153
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 373 FPLHlaVLFGFSDCCRKLLssgqlysivsslsnEHVLSAGFDINTPDNLGRTCLH--AAASGGNVECLNLLLSSGADLRR 450
Cdd:PHA03095 154 TPLA--VLLKSRNANVELL--------------RLLIDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAA 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 451 RDKFGRTPLHYAAANGSYQCAVT--LVTAGAGVNEADCKGCSPLHYAAASDtyrraephtpsshdaeedeplkesrrKEA 528
Cdd:PHA03095 218 TDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFN--------------------------NPR 271
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 529 FFCleFLLDNGADPSLRDRQGYTAvhyaaaygnrqnlelLLEMSFNCLEDVEST-IPVSPlhlaaynghceALKTLAETL 607
Cdd:PHA03095 272 ACR--RLIALGADINAVSSDGNTP---------------LSLMVRNNNGRAVRAaLAKNP-----------SAETVAATL 323
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|..
gi 1034579110 608 VNLDVRDHKGRTAlflaterGSTECVEVLTAHGASALIKERKRKwtpLHAAA 659
Cdd:PHA03095 324 NTASVAGGDIPSD-------ATRLCVAKVVLRGAFSLLPEPIRA---YHADF 365
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
147-492 |
3.02e-27 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 119.01 E-value: 3.02e-27
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 147 VHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLGCKDRKGYGLLHTAAASGQIEVVKYLLR 226
Cdd:PHA02876 153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIID 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 227 MGAEIDEP-----NAFGNTALHiacylgqdaVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGALCLELLVNNGADVNYQ 301
Cdd:PHA02876 233 NRSNINKNdlsllKAIRNEDLE---------TSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAK 303
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 302 SKEGKSPLHMAAIHGRFTRS-QILIQNGSEIDCADKFGNTPLHVAARYG-HELLISTLMTNGADTARRGIHDMFPLHLAV 379
Cdd:PHA02876 304 NIKGETPLYLMAKNGYDTENiRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAA 383
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 380 LfgfsdccrkllssGQLYSIVSSLsnehvLSAGFDINTPDNLGRTCLHAAASGGN-VECLNLLLSSGADLRRRDKFGRTP 458
Cdd:PHA02876 384 V-------------RNNVVIINTL-----LDYGADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTP 445
|
330 340 350
....*....|....*....|....*....|....*
gi 1034579110 459 LHYAAANG-SYQCAVTLVTAGAGVNEADCKGCSPL 492
Cdd:PHA02876 446 LHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPL 480
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
147-462 |
3.76e-24 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 106.97 E-value: 3.76e-24
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 147 VHSGHLETV-NLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLGCKDRKGYGLLHTAAASGQIEVVKYLL 225
Cdd:PHA02874 9 IYSGDIEAIeKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 226 RMGAEidepnafgNTALHIACyLGQDAVAIeLVNAGANVNQPNDKGFTPLHVAaVSTNGALCLELLVNNGADVNYQSKEG 305
Cdd:PHA02874 89 DNGVD--------TSILPIPC-IEKDMIKT-ILDCGIDVNIKDAELKTFLHYA-IKKGDLESIKMLFEYGADVNIEDDNG 157
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 306 KSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGfsd 385
Cdd:PHA02874 158 CYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN--- 234
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034579110 386 ccrkllssgqlYSIVSSLSNEHvlsagfDINTPDNLGRTCLHAAAS-GGNVECLNLLLSSGADLRRRDKFGRTPLHYA 462
Cdd:PHA02874 235 -----------RSAIELLINNA------SINDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
340-624 |
1.44e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 101.96 E-value: 1.44e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 340 TPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRKLLSSGQLYSI--VSSLSNEHV---LSAGFD 414
Cdd:PHA02874 37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIlpIPCIEKDMIktiLDCGID 116
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 415 INTPDNLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHY 494
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 495 AAASDTYRraephtpsshdaeedeplkesrrkeaffCLEFLLDNGADPSLRDRQGYTAVHYAAAYgNRQNLELLLEMSFN 574
Cdd:PHA02874 197 AAEYGDYA----------------------------CIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLINNASI 247
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1034579110 575 CLEDVESTipvSPLHLA-AYNGHCEALKTLAETLVNLDVRDHKGRTALFLA 624
Cdd:PHA02874 248 NDQDIDGS---TPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
74-357 |
2.93e-22 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 101.50 E-value: 2.93e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 74 LTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAaanratkCAE----ALAPLLSSLNVADRS-GRSALHHAVH 148
Cdd:PHA02878 38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHII-------CKEpnklGMKEMIRSINKCSVFyTLVAIKDAFN 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 149 SGHLETVN-LLLNKGASLNVCDKKERQPLHWAAFLgHLEVLKLLVARGADLGCKDR-KGYGLLHTAAASGQIEVVKYLLR 226
Cdd:PHA02878 111 NRNVEIFKiILTNRYKNIQTIDLVYIDKKSKDDII-EAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLS 189
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 227 MGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGALCLELLVNNGADVNYQSK-EG 305
Cdd:PHA02878 190 YGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYiLG 269
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034579110 306 KSPLHMaAIHGRfTRSQILIQNGSEIDCADKFGNTPLHVAA--RYGHE---LLISTL 357
Cdd:PHA02878 270 LTALHS-SIKSE-RKLKLLLEYGADINSLNSYKLTPLSSAVkqYLCINigrILISNI 324
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
575-984 |
2.51e-20 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 96.67 E-value: 2.51e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 575 CLEDVESTIPVSPLHLAAYNGHCEALKTLAETL---------------VNLDVRDHKGRTALFLATERGSTECVEVLTAH 639
Cdd:PHA02876 121 CIHILKEAISGNDIHYDKINESIEYMKLIKERIqqdelliaemlleggADVNAKDIYCITPIHYAAERGNAKMVNLLLSY 200
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 640 GASALIKERKrKWTPLHAAAASGHTDSLHLLIDSGERADITDVmdaygqtPLMLAIMNGHVDCVHLLLEKGSTADAADLR 719
Cdd:PHA02876 201 GADVNIIALD-DLSVLECAVDSKNIDTIKAIIDNRSNINKNDL-------SLLKAIRNEDLETSLLLYDAGFSVNSIDDC 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 720 GRTALHRGAVT-GCEDCLAALLDHDAFVLCRDFKGRTPIHLASACGH-TAVLRTLLQAalstdpldaGVDYSGYSPMHwa 797
Cdd:PHA02876 273 KNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIML---------GADVNAADRLY-- 341
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 798 sytghedclelllehspfsylegnpFTPLHCAVINNQDSTTEMLLGALGAKiVNSRDAKGRTPLHAAAFADNVSGLRMLL 877
Cdd:PHA02876 342 -------------------------ITPLHQASTLDRNKDIVITLLELGAN-VNARDYCDKTPIHYAAVRNNVVIINTLL 395
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 878 QHQAEVNATDHTGRTALMTA--AENGQTaAVEFLLYRGkADLTVLDENKNTALHLACSKgheKCALMILAETQDLGL-IN 954
Cdd:PHA02876 396 DYGADIEALSQKIGTALHFAlcGTNPYM-SVKTLIDRG-ANVNSKNKDLSTPLHYACKK---NCKLDVIEMLLDNGAdVN 470
|
410 420 430
....*....|....*....|....*....|
gi 1034579110 955 ATNSALQMPLHIAArnGLASVVQALLSHGA 984
Cdd:PHA02876 471 AINIQNQYPLLIAL--EYHGIVNILLHYGA 498
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
185-465 |
6.23e-20 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 93.96 E-value: 6.23e-20
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 185 LEVLKLLVARGADLGCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIAC---YLGQDAVAIE--LVN 259
Cdd:PHA03100 15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikYNLTDVKEIVklLLE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 260 AGANVNQPNDKGFTPLHVAAVSTNGALCL-ELLVNNGADVNYQSKEGKSPLHMAA--IHGRFTRSQILIQNGSEIDCADK 336
Cdd:PHA03100 95 YGANVNAPDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNR 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 337 FgntplhvaaryghellistlmtngadtarrgihDMFplhlavlfgfsdccrkllssgqlysivsslsnehvLSAGFDIN 416
Cdd:PHA03100 175 V---------------------------------NYL-----------------------------------LSYGVPIN 186
|
250 260 270 280
....*....|....*....|....*....|....*....|....*....
gi 1034579110 417 TPDNLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAAN 465
Cdd:PHA03100 187 IKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILN 235
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
588-897 |
2.01e-19 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 92.33 E-value: 2.01e-19
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 588 LHLAAYNGHCEALKTLAETLVN-LDVRDHKGRTALFLATERGSTECVEVLTAHGASalIKERKRKW-TPLHAAAASGHTD 665
Cdd:PHA02874 5 LRMCIYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGAD--INHINTKIpHPLLTAIKIGAHD 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 666 SLHLLIDSGERADITDVMDAYGQTplmlaimnghvdcVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAF 745
Cdd:PHA02874 83 IIKLLIDNGVDTSILPIPCIEKDM-------------IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGAD 149
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 746 VLCRDFKGRTPIHLASACGHTAVLRTLLQ--AALSTDpldagvDYSGYSPMHWASYTGHEDCLELLLEH-SPFSYLEGNP 822
Cdd:PHA02874 150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLEkgAYANVK------DNNGESPLHNAAEYGDYACIKLLIDHgNHIMNKCKNG 223
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034579110 823 FTPLHCAVINNQdSTTEMLlgaLGAKIVNSRDAKGRTPLH-AAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTA 897
Cdd:PHA02874 224 FTPLHNAIIHNR-SAIELL---INNASINDQDIDGSTPLHhAINPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
143-379 |
1.42e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 90.32 E-value: 1.42e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 143 LHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAF----LGHLEVLKLLVARgaDLGCKDRKgyglLHTAAASGQI 218
Cdd:PHA02878 41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKepnkLGMKEMIRSINKC--SVFYTLVA----IKDAFNNRNV 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 219 EVVKYLLrmgaeIDEPNAFGNTALHIACYLGQDAVaIE------LVNAGANVNQPN-DKGFTPLHVAAVSTNGALcLELL 291
Cdd:PHA02878 115 EIFKIIL-----TNRYKNIQTIDLVYIDKKSKDDI-IEaeitklLLSYGADINMKDrHKGNTALHYATENKDQRL-TELL 187
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 292 VNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHEL-LISTLMTNGAD-TARRGI 369
Cdd:PHA02878 188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYdILKLLLEHGVDvNAKSYI 267
|
250
....*....|
gi 1034579110 370 HDMFPLHLAV 379
Cdd:PHA02878 268 LGLTALHSSI 277
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
41-299 |
2.19e-18 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 88.89 E-value: 2.19e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 41 RTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSA--DVNARDKlwqtplhvaaanra 118
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDI-------------- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 119 tkcaealapllsslnvadrsgRSALHHAVHSGHLETVNLLLNKGASLN-VCDKKERQPLHWAAFLGHLEVLKLLVARGAD 197
Cdd:PHA02875 69 ---------------------ESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGAD 127
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 198 LGCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHV 277
Cdd:PHA02875 128 PDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALC 207
|
250 260
....*....|....*....|..
gi 1034579110 278 AAVSTNGALCLELLVNNGADVN 299
Cdd:PHA02875 208 YAIENNKIDIVRLFIKRGADCN 229
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
588-681 |
2.32e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.93 E-value: 2.32e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 588 LHLAAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHgasALIKERKRKWTPLHAAAASGHTDSL 667
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 1034579110 668 HLLIDSGERADITD 681
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
143-235 |
4.24e-18 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 80.16 E-value: 4.24e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 143 LHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARgADLGCKDrKGYGLLHTAAASGQIEVVK 222
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1034579110 223 YLLRMGAEIDEPN 235
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
653-1014 |
4.90e-18 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 88.54 E-value: 4.90e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 653 TPLHAAAASGHTDSLHLLIDSGERADITDVM------------DAYGQTPLMLAIMNGHVDC---VHLLLEKGSTADAAD 717
Cdd:PHA03095 1 DEEDESVDIIMEAALYDYLLNASNVTVEEVRrllaagadvnfrGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 718 LRGRTALH---RGAVTgcEDCLAALLDHDAFVLCRDFKGRTPIH--LASACGHTAVLRTLLQAALSTDPLDAgvdySGYS 792
Cdd:PHA03095 81 RCGFTPLHlylYNATT--LDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDL----YGMT 154
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 793 PMHwaSYTGHEDC----LELLLEH-SPFSYLEGNPFTPLHCAVINNQDSTTEM-LLGALGAKiVNSRDAKGRTPLHAAAF 866
Cdd:PHA03095 155 PLA--VLLKSRNAnvelLRLLIDAgADVYAVDDRFRSLLHHHLQSFKPRARIVrELIRAGCD-PAATDMLGNTPLHSMAT 231
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 867 ADNVSGLRM--LLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLLYRGkADLTVLDENKNTALHLACSKGHEKCALMIL 944
Cdd:PHA03095 232 GSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG-ADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034579110 945 AETQDLGLINATnsalqmpLHIAARNGLASVVQALLSHGATVLAVDEEGHTPALACAPNKD-VADCLALIL 1014
Cdd:PHA03095 311 AKNPSAETVAAT-------LNTASVAGGDIPSDATRLCVAKVVLRGAFSLLPEPIRAYHADfIRECEAEIA 374
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
176-268 |
1.32e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 78.62 E-value: 1.32e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 176 LHWAAFLGHLEVLKLLVARGADLGCKDRKGYGLLHTAAASGQIEVVKYLLRmGAEIDEPNaFGNTALHIACYLGQDAVAI 255
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1034579110 256 ELVNAGANVNQPN 268
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
520-928 |
1.62e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 87.81 E-value: 1.62e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 520 LKESRRKEAFFCLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLemSFNCLEDVESTIPVSPLHLAAYNGHCEA 599
Cdd:PHA02876 149 IKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLL--SYGADVNIIALDDLSVLECAVDSKNIDT 226
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 600 LKTLAETLVNLDVRDhkgrTALFLATERGSTECVEVLTAHGASA-LIKERKRkwTPLHAAAasgHTDSLHLLIDS-GERA 677
Cdd:PHA02876 227 IKAIIDNRSNINKND----LSLLKAIRNEDLETSLLLYDAGFSVnSIDDCKN--TPLHHAS---QAPSLSRLVPKlLERG 297
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 678 DITDVMDAYGQTPLMLAIMNGH-VDCVHLLLEKGSTADAADLRGRTALHRGA-VTGCEDCLAALLDHDAFVLCRDFKGRT 755
Cdd:PHA02876 298 ADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKT 377
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 756 PIHLASACGHTAVLRTLLQAALSTDPLDAGVDysgySPMHWASYTghedclelllehspfsyleGNPFTPLHCAVINNQD 835
Cdd:PHA02876 378 PIHYAAVRNNVVIINTLLDYGADIEALSQKIG----TALHFALCG-------------------TNPYMSVKTLIDRGAN 434
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 836 sttemllgalgakiVNSRDAKGRTPLHAAAFAD-NVSGLRMLLQHQAEVNATDHTGRTALMTAAenGQTAAVEFLLYRGK 914
Cdd:PHA02876 435 --------------VNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGA 498
|
410
....*....|....*.
gi 1034579110 915 A--DLTVLDENKNTAL 928
Cdd:PHA02876 499 ElrDSRVLHKSLNDNM 514
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
110-202 |
2.42e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 77.85 E-value: 2.42e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 110 LHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLLNKgASLNVCDKKeRQPLHWAAFLGHLEVLK 189
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1034579110 190 LLVARGADLGCKD 202
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
598-906 |
2.47e-17 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 86.23 E-value: 2.47e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 598 EALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEV---LTAHGASALIKERKrKWTPLHAAAASGHT-DSLHLLIDS 673
Cdd:PHA03095 28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERC-GFTPLHLYLYNATTlDVIKLLIKA 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 674 GerADITDVmDAYGQTPL--MLAIMNGHVDCVHLLLEKGSTADAADLRGRTALH-----RGAvtgCEDCLAALLDHDAFV 746
Cdd:PHA03095 107 G--ADVNAK-DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvllksRNA---NVELLRLLIDAGADV 180
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 747 LCRDFKGRTP--IHLASACGHTAVLRTLLqaALSTDPldAGVDYSGYSPMHwaSYTGHEDCLELLLehSPFsylegnpft 824
Cdd:PHA03095 181 YAVDDRFRSLlhHHLQSFKPRARIVRELI--RAGCDP--AATDMLGNTPLH--SMATGSSCKRSLV--LPL--------- 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 825 plhcaVINNQDsttemllgalgakiVNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTA 904
Cdd:PHA03095 244 -----LIAGIS--------------INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGR 304
|
..
gi 1034579110 905 AV 906
Cdd:PHA03095 305 AV 306
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
655-750 |
4.43e-17 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 77.08 E-value: 4.43e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 655 LHAAAASGHTDSLHLLIDSGERADitdVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADaaDLRGRTALHRGAVTGCED 734
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADAN---LQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLE 75
|
90
....*....|....*.
gi 1034579110 735 CLAALLDHDAFVLCRD 750
Cdd:pfam12796 76 IVKLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
532-729 |
6.79e-17 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 84.27 E-value: 6.79e-17
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 532 LEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLleMSFNCLEDVESTIPVSPLHLAAYNGHCEALKTL--AETLVN 609
Cdd:PHA02875 18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLL--MKHGAIPDVKYPDIESELHDAVEEGDVKAVEELldLGKFAD 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 610 lDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKERKRkWTPLHAAAASGHTDSLHLLIDsgERAdITDVMDAYGQT 689
Cdd:PHA02875 96 -DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDK-FSPLHLAVMMGDIKGIELLID--HKA-CLDIEDCCGCT 170
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1034579110 690 PLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAV 729
Cdd:PHA02875 171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAI 210
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
435-788 |
1.40e-16 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 83.92 E-value: 1.40e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 435 VECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCA---VTLVTAGAGVNEADCKGCSPLHYAAasdtyrraephtpsS 511
Cdd:PHA03095 27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGFTPLHLYL--------------Y 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 512 HDAEEDeplkesrrkeaffCLEFLLDNGADPSLRDRQGYTAVHyaaaygnrqnlelllemsfncledvestipvspLHLA 591
Cdd:PHA03095 93 NATTLD-------------VIKLLIKAGADVNAKDKVGRTPLH---------------------------------VYLS 126
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 592 AYNGHCEALKTLAETLVNLDVRDHKGRTAL--FLATERGSTECVEVLTAHGASALIKERKRKwTPLHAAAASGHTDS--L 667
Cdd:PHA03095 127 GFNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFR-SLLHHHLQSFKPRAriV 205
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 668 HLLIDSGERADITDVmdaYGQTPLMLAIMngHVDCVHL----LLEKGSTADAADLRGRTALHRGAVTG----CEDCLAAL 739
Cdd:PHA03095 206 RELIRAGCDPAATDM---LGNTPLHSMAT--GSSCKRSlvlpLLIAGISINARNRYGQTPLHYAAVFNnpraCRRLIALG 280
|
330 340 350 360
....*....|....*....|....*....|....*....|....*....
gi 1034579110 740 LDhdafVLCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAGVDY 788
Cdd:PHA03095 281 AD----INAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNT 325
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
209-301 |
1.45e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 75.92 E-value: 1.45e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 209 LHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNaGANVNqPNDKGFTPLHVAAVSTNGAlCL 288
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVN-LKDNGRTALHYAARSGHLE-IV 77
|
90
....*....|...
gi 1034579110 289 ELLVNNGADVNYQ 301
Cdd:pfam12796 78 KLLLEKGADINVK 90
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
861-954 |
4.04e-16 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 74.38 E-value: 4.04e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 861 LHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLLYRGKADltvLDENKNTALHLACSKGHEKCA 940
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77
|
90
....*....|....
gi 1034579110 941 LMILAETQDLGLIN 954
Cdd:pfam12796 78 KLLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
246-562 |
1.00e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 80.78 E-value: 1.00e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 246 CYLGQDAVAIE--LVNAGANVNQPNDKGFTPLhVAAVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQI 323
Cdd:PHA02874 8 CIYSGDIEAIEkiIKNKGNCINISVDETTTPL-IDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKL 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 324 LIQNGSE-----IDCADKfgntplhvaarygheLLISTLMTNGADTARRGIHDMFPLHLAVlfgfsdccrkllSSGQLYS 398
Cdd:PHA02874 87 LIDNGVDtsilpIPCIEK---------------DMIKTILDCGIDVNIKDAELKTFLHYAI------------KKGDLES 139
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 399 IvsslsnEHVLSAGFDINTPDNLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAG 478
Cdd:PHA02874 140 I------KMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG 213
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 479 AGVNEADCKGCSPLHYAAASDtyRRAEP-----HTPSSHDAEEDEPLKESRRkeaFFC----LEFLLDNGADPSLRDRQG 549
Cdd:PHA02874 214 NHIMNKCKNGFTPLHNAIIHN--RSAIEllinnASINDQDIDGSTPLHHAIN---PPCdidiIDILLYHKADISIKDNKG 288
|
330
....*....|...
gi 1034579110 550 YTAVHYAAAYGNR 562
Cdd:PHA02874 289 ENPIDTAFKYINK 301
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
621-717 |
1.06e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 73.23 E-value: 1.06e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 621 LFLATERGSTECVEVLTAHGASALIKErKRKWTPLHAAAASGHTDSLHLLIDSGeRADITDvmdaYGQTPLMLAIMNGHV 700
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD----NGRTALHYAARSGHL 74
|
90
....*....|....*..
gi 1034579110 701 DCVHLLLEKGSTADAAD 717
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
739-992 |
1.37e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 81.65 E-value: 1.37e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 739 LLDHDAFVLCRDFKGRTPIHLASACGHTAVLRTLLQ--AALSTDPLDagvdysGYSPMHWASYTGHEDCLELLLEHSpfS 816
Cdd:PHA02876 164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSygADVNIIALD------DLSVLECAVDSKNIDTIKAIIDNR--S 235
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 817 YLEGNPFTPLHcaVINNQDSTTEMLLGALGAKiVNSRDAKGRTPLHAAAFADNVSGL-RMLLQHQAEVNATDHTGRTALM 895
Cdd:PHA02876 236 NINKNDLSLLK--AIRNEDLETSLLLYDAGFS-VNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLY 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 896 TAAENG-QTAAVEFLLYRGkADLTVLDENKNTALHLACSKGHEKCALMILAEtqdLGL-INATNSALQMPLHIAARNGLA 973
Cdd:PHA02876 313 LMAKNGyDTENIRTLIMLG-ADVNAADRLYITPLHQASTLDRNKDIVITLLE---LGAnVNARDYCDKTPIHYAAVRNNV 388
|
250
....*....|....*....
gi 1034579110 974 SVVQALLSHGATVLAVDEE 992
Cdd:PHA02876 389 VIINTLLDYGADIEALSQK 407
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
894-990 |
5.23e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 71.30 E-value: 5.23e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 894 LMTAAENGQTAAVEFLLYRGkADLTVLDENKNTALHLACSKGHEKCAlMILAETQDLGLINATNSalqmPLHIAARNGLA 973
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIV-KLLLEHADVNLKDNGRT----ALHYAARSGHL 74
|
90
....*....|....*..
gi 1034579110 974 SVVQALLSHGATVLAVD 990
Cdd:pfam12796 75 EIVKLLLEKGADINVKD 91
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
36-227 |
6.91e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 78.47 E-value: 6.91e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 36 QDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAA 115
Cdd:PHA02874 120 KDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 116 NRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHlETVNLLLNKgASLNVCDKKERQPLHWA-AFLGHLEVLKLLVAR 194
Cdd:PHA02874 200 YGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAiNPPCDIDIIDILLYH 277
|
170 180 190
....*....|....*....|....*....|...
gi 1034579110 195 GADLGCKDRKGYGLLHTAaasgqievVKYLLRM 227
Cdd:PHA02874 278 KADISIKDNKGENPIDTA--------FKYINKD 302
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
375-485 |
7.43e-15 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 70.92 E-value: 7.43e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 375 LHLAVLFGFSDCCRKLLSSGqlysivsslsnehvlsagFDINTPDNLGRTCLHAAASGGNVECLNLLLSSgADLRRRDKf 454
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENG------------------ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN- 60
|
90 100 110
....*....|....*....|....*....|.
gi 1034579110 455 GRTPLHYAAANGSYQCAVTLVTAGAGVNEAD 485
Cdd:pfam12796 61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
396-717 |
8.71e-15 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 77.78 E-value: 8.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 396 LYSIVS-------SLSNEHVLSAGFDINTPDNLGRT-CLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGS 467
Cdd:PHA03100 1 LYSYIVltksriiKVKNIKYIIMEDDLNDYSYKKPVlPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKY 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 468 YQCAVT-----LVTAGAGVNEADCKGCSPLHYAAasdtyrraephtpsshdaeedeplkeSRRKEAFFCLEFLLDNGADP 542
Cdd:PHA03100 81 NLTDVKeivklLLEYGANVNAPDNNGITPLLYAI--------------------------SKKSNSYSIVEYLLDNGANV 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 543 SLRDRQGYTAVHYAAAYgNRQNLELllemsfncledvestipvsplhlaaynghceaLKTLAETLVNLDVRDHkgrtalf 622
Cdd:PHA03100 135 NIKNSDGENLLHLYLES-NKIDLKI--------------------------------LKLLIDKGVDINAKNR------- 174
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 623 latergstecVEVLTAHGASALIKErKRKWTPLHAAAASGHTDSLHLLIDSGerADITDVMDaYGQTPLMLAIMNGHVDC 702
Cdd:PHA03100 175 ----------VNYLLSYGVPINIKD-VYGFTPLHYAVYNNNPEFVKYLLDLG--ANPNLVNK-YGDTPLHIAILNNNKEI 240
|
330
....*....|....*
gi 1034579110 703 VHLLLEKGSTADAAD 717
Cdd:PHA03100 241 FKLLLNNGPSIKTII 255
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
426-546 |
1.12e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 70.53 E-value: 1.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 426 LHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGvnEADCKGCSPLHYAAasdtyrrae 505
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAA--------- 69
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1034579110 506 phtpsshdaeedeplkESRRKEaffCLEFLLDNGADPSLRD 546
Cdd:pfam12796 70 ----------------RSGHLE---IVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
691-774 |
1.21e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 70.14 E-value: 1.21e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 691 LMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHdaFVLCRDFKGRTPIHLASACGHTAVLR 770
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDNGRTALHYAARSGHLEIVK 78
|
....
gi 1034579110 771 TLLQ 774
Cdd:pfam12796 79 LLLE 82
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
44-136 |
1.99e-14 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 69.76 E-value: 1.99e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 44 LHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHsADVNARDKLWqTPLHVAAANRATKCAE 123
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78
|
90
....*....|...
gi 1034579110 124 ALAPLLSSLNVAD 136
Cdd:pfam12796 79 LLLEKGADINVKD 91
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
41-176 |
4.12e-14 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 76.07 E-value: 4.12e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 41 RTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAAnrATK 120
Cdd:PHA02878 169 NTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVG--YCK 246
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 121 CAEALAPLLS-SLNVADRS---GRSALHHAVHSGhlETVNLLLNKGASLNVCDKKERQPL 176
Cdd:PHA02878 247 DYDILKLLLEhGVDVNAKSyilGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPL 304
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
73-283 |
4.33e-14 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 76.59 E-value: 4.33e-14
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 73 WLTPLHRAAASRN-EKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEAL---APLLssLNVADRS----GRSALH 144
Cdd:cd22192 17 SESPLLLAAKENDvQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLmeaAPEL--VNEPMTSdlyqGETALH 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 145 HAVHSGHLETVNLLLNKGASL---------------NVCDKKErQPLHWAAFLGHLEVLKLLVARGADLGCKDRkgygll 209
Cdd:cd22192 95 IAVVNQNLNLVRELIARGADVvspratgtffrpgpkNLIYYGE-HPLSFAACVGNEEIVRLLIEHGADIRAQDS------ 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 210 htaaasgqievvkyllrmgaeidepnaFGNTALHI---------ACYL---------GQDAVAIELVnaganvnqPNDKG 271
Cdd:cd22192 168 ---------------------------LGNTVLHIlvlqpnktfACQMydlilsydkEDDLQPLDLV--------PNNQG 212
|
250
....*....|..
gi 1034579110 272 FTPLHVAAVSTN 283
Cdd:cd22192 213 LTPFKLAAKEGN 224
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
595-871 |
1.21e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 74.26 E-value: 1.21e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 595 GHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKERKRKwTPLHAAAASGHTDSLHLLIDSG 674
Cdd:PHA02875 13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIE-SELHDAVEEGDVKAVEELLDLG 91
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 675 ERADitDVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFVLCRDFKGR 754
Cdd:PHA02875 92 KFAD--DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGC 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 755 TPIHLASACGHTAVLRTLLQAAlstdpldAGVDYSGYSP----MHWASYTGHEDCLELLLEHSP----FSYLEGNPFTPL 826
Cdd:PHA02875 170 TPLIIAMAKGDIAICKMLLDSG-------ANIDYFGKNGcvaaLCYAIENNKIDIVRLFIKRGAdcniMFMIEGEECTIL 242
|
250 260 270 280
....*....|....*....|....*....|....*....|....*.
gi 1034579110 827 HcaVINNQDSTTEM-LLGALGAKIVNSRDAKgrTPLHAAAFADNVS 871
Cdd:PHA02875 243 D--MICNMCTNLESeAIDALIADIAIRIHKK--TIRRDEGFKNNMS 284
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
140-407 |
1.89e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 73.49 E-value: 1.89e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 140 RSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLGCKDRKGYGLLHTAAASGQIE 219
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 220 VVKYLLRMGAEIDEpnafgntalhiACYlgqdavaielvnaganvnqpnDKGFTPLHVAAVSTNGALcLELLVNNGADVN 299
Cdd:PHA02875 83 AVEELLDLGKFADD-----------VFY---------------------KDGMTPLHLATILKKLDI-MKLLIARGADPD 129
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 300 YQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADT---ARRGihDMFPLH 376
Cdd:PHA02875 130 IPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIdyfGKNG--CVAALC 207
|
250 260 270
....*....|....*....|....*....|.
gi 1034579110 377 LAVLFGFSDCCRKLLSSGQLYSIVSSLSNEH 407
Cdd:PHA02875 208 YAIENNKIDIVRLFIKRGADCNIMFMIEGEE 238
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
47-283 |
2.77e-13 |
|
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: 74.35 E-value: 2.77e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 47 AAYVGDVPILQLLLMSGA--NVNAKDTLWLTPLHRAAA-SRNEKVLGLLLAHSADVNARDKLwqtpLHVAAANRATKCAE 123
Cdd:TIGR00870 24 AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGDTL----LHAISLEYVDAVEA 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 124 ALAPLL-------SSLNVADRS------GRSALHHAVHSGHLETVNLLLNKGASLNV------CDKKERQ--------PL 176
Cdd:TIGR00870 100 ILLHLLaafrksgPLELANDQYtseftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVdsfyhgesPL 179
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 177 HWAAFLGHLEVLKLLVARGADLGCKDRKGYGLLHtaaasgqievvkyLLRMGAEidepNAFGNTALHIACY------LGQ 250
Cdd:TIGR00870 180 NAAACLGSPSIVALLSEDPADILTADSLGNTLLH-------------LLVMENE----FKAEYEELSCQMYnfalslLDK 242
|
250 260 270
....*....|....*....|....*....|....*
gi 1034579110 251 --DAVAIELVnaganvnqPNDKGFTPLHVAAVSTN 283
Cdd:TIGR00870 243 lrDSKELEVI--------LNHQGLTPLKLAAKEGR 269
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
440-760 |
8.35e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 72.79 E-value: 8.35e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 440 LLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAASDTYRraephtpsshdaeedep 519
Cdd:PHA02876 163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNID----------------- 225
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 520 lkesrrkeaffCLEFLLDNGADPSLRDRQGYTAVhyaaaygNRQNLE--LLLE---MSFNCLEDVESTipvsPLHLAAYN 594
Cdd:PHA02876 226 -----------TIKAIIDNRSNINKNDLSLLKAI-------RNEDLEtsLLLYdagFSVNSIDDCKNT----PLHHASQA 283
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 595 GHCEAL-KTLAETLVNLDVRDHKGRTALFLATERG-STECVEVLTAHGASALIKERKRKwTPLHAAAA-SGHTDSLHLLI 671
Cdd:PHA02876 284 PSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYI-TPLHQASTlDRNKDIVITLL 362
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 672 DSGERadiTDVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRgAVTGCEDCLA--ALLDHDAFVLCR 749
Cdd:PHA02876 363 ELGAN---VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHF-ALCGTNPYMSvkTLIDRGANVNSK 438
|
330
....*....|.
gi 1034579110 750 DFKGRTPIHLA 760
Cdd:PHA02876 439 NKDLSTPLHYA 449
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
208-344 |
8.98e-13 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 72.35 E-value: 8.98e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 208 LLHTAAASGQIEVVKYLLRM-GAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGAN-VNQPND----KGFTPLHVAAVS 281
Cdd:cd22192 20 PLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVVN 99
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034579110 282 TNGALcLELLVNNGADVN-------YQSKEGKS-------PLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHV 344
Cdd:cd22192 100 QNLNL-VRELIARGADVVspratgtFFRPGPKNliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
532-788 |
9.17e-13 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 71.62 E-value: 9.17e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 532 LEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNclEDVESTIPVSPLHLAAYNGHC-----EALKTLAET 606
Cdd:PHA03100 18 IKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGAD--INSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 607 LVNLDVRDHKGRTALFLA--TERGSTECVEVLTAHGASALIKeRKRKWTPLHAAAASGHTDS--LHLLIDSGerADItDV 682
Cdd:PHA03100 96 GANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIK-NSDGENLLHLYLESNKIDLkiLKLLIDKG--VDI-NA 171
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 683 MDAygqtplmlaimnghvdcVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFVLCRDFKGRTPIHLASA 762
Cdd:PHA03100 172 KNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234
|
250 260
....*....|....*....|....*.
gi 1034579110 763 CGHTAVLRTLLQAALSTDPLDAGVDY 788
Cdd:PHA03100 235 NNNKEIFKLLLNNGPSIKTIIETLLY 260
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
342-452 |
1.12e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 64.75 E-value: 1.12e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 342 LHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRKLLSSgqlysivsslsnehvlsagFDINTPDNl 421
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-------------------ADVNLKDN- 60
|
90 100 110
....*....|....*....|....*....|.
gi 1034579110 422 GRTCLHAAASGGNVECLNLLLSSGADLRRRD 452
Cdd:pfam12796 61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
309-394 |
1.26e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 64.75 E-value: 1.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 309 LHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGAdtARRGIHDMFPLHLAVLFGFSDCCR 388
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
|
....*.
gi 1034579110 389 KLLSSG 394
Cdd:pfam12796 79 LLLEKG 84
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
232-476 |
1.40e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 71.45 E-value: 1.40e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 232 DEPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTN---------------------------- 283
Cdd:PHA02878 31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNklgmkemirsinkcsvfytlvaikdafn 110
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 284 -----------------------------------GALCLELLVNNGADVNYQSKE-GKSPLHMAAIHGRFTRSQILIQN 327
Cdd:PHA02878 111 nrnveifkiiltnrykniqtidlvyidkkskddiiEAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSY 190
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 328 GSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVlfgfsdccrkllSSGQLYSIVSSLsneh 407
Cdd:PHA02878 191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV------------GYCKDYDILKLL---- 254
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034579110 408 vLSAGFDINTPDN-LGRTCLHAAASGGNVecLNLLLSSGADLRRRDKFGRTPLHYAAANGS-YQCAVTLVT 476
Cdd:PHA02878 255 -LEHGVDVNAKSYiLGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAVKQYLcINIGRILIS 322
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
275-363 |
1.46e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 64.37 E-value: 1.46e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 275 LHVAAVStNGALCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGsEIDCADKfGNTPLHVAARYGHELLI 354
Cdd:pfam12796 1 LHLAAKN-GNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIV 77
|
....*....
gi 1034579110 355 STLMTNGAD 363
Cdd:pfam12796 78 KLLLEKGAD 86
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
535-760 |
1.49e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 71.15 E-value: 1.49e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 535 LLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNC-LEDVESTIPVsplHLAAYNGHCEALKTLAETLVNLDVR 613
Cdd:PHA02874 110 ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVnIEDDNGCYPI---HIAIKHNFFDIIKLLLEKGAYANVK 186
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 614 DHKGRTALFLATERGSTECVEVLTAHGASALIKeRKRKWTPLHAAAasghtdslhllidsgeraditdvmdAYGQTPLML 693
Cdd:PHA02874 187 DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK-CKNGFTPLHNAI-------------------------IHNRSAIEL 240
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034579110 694 AIMNghvdcvhlllekgSTADAADLRGRTALHRGAVTGCE-DCLAALLDHDAFVLCRDFKGRTPIHLA 760
Cdd:PHA02874 241 LINN-------------ASINDQDIDGSTPLHHAINPPCDiDIIDILLYHKADISIKDNKGENPIDTA 295
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
554-646 |
1.88e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 63.98 E-value: 1.88e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 554 HYAAAYGNRQNLELLLEMSFNCleDVESTIPVSPLHLAAYNGHCEALKTLAETlVNLDVRDHkGRTALFLATERGSTECV 633
Cdd:pfam12796 2 HLAAKNGNLELVKLLLENGADA--NLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIV 77
|
90
....*....|...
gi 1034579110 634 EVLTAHGASALIK 646
Cdd:pfam12796 78 KLLLEKGADINVK 90
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
264-570 |
2.28e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 70.46 E-value: 2.28e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 264 VNQPNDKGFTPLHVAAVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAA-IHGRFTR----SQILIQNGSEIDCADKFG 338
Cdd:PHA03100 27 LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnIKYNLTDvkeiVKLLLEYGANVNAPDNNG 106
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 339 NTPLHVAA--RYGHELLISTLMTNGADT---ARRGIHdmfPLHLAVlfgfSDCCRKLlssgqlySIVSSLsnehvLSAGF 413
Cdd:PHA03100 107 ITPLLYAIskKSNSYSIVEYLLDNGANVnikNSDGEN---LLHLYL----ESNKIDL-------KILKLL-----IDKGV 167
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 414 DINTPDNLgrtclhaaasggnveclNLLLSSGADlrrrdkfgrtplhyaaangsyqcavtlvtagagVNEADCKGCSPLH 493
Cdd:PHA03100 168 DINAKNRV-----------------NYLLSYGVP---------------------------------INIKDVYGFTPLH 197
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034579110 494 YAAasdtyrraephtpsSHDAEEdeplkesrrkeaFFclEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLE 570
Cdd:PHA03100 198 YAV--------------YNNNPE------------FV--KYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
458-760 |
3.78e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 69.91 E-value: 3.78e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 458 PLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAAsdtyrraEPHTPSshdaeedepLKESRRKEaffcleflld 537
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICK-------EPNKLG---------MKEMIRSI---------- 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 538 ngadpsLRDRQGYTAVHYAAAYGNRqNLELLLEMSFNCLeDVESTIPVSPLHLAAYNGHCEA--LKTLAETLVNLDVRD- 614
Cdd:PHA02878 94 ------NKCSVFYTLVAIKDAFNNR-NVEIFKIILTNRY-KNIQTIDLVYIDKKSKDDIIEAeiTKLLLSYGADINMKDr 165
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 615 HKGRTALFLATERGSTECVEVLTAHGASALIKERKRKwTPLHAAAASGHTDSLHLLIDSGERadiTDVMDAYGQTPLMLA 694
Cdd:PHA02878 166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNN-SPLHHAVKHYNKPIVHILLENGAS---TDARDKCGNTPLHIS 241
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 695 ImnGHV---DCVHLLLEKGSTADA-ADLRGRTALHRGAVTgcEDCLAALLDHDAFVLCRDFKGRTPIHLA 760
Cdd:PHA02878 242 V--GYCkdyDILKLLLEHGVDVNAkSYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
341-591 |
4.27e-12 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 69.91 E-value: 4.27e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 341 PLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAV----LFGFSDCCRKLLS---SGQLYSIVSSLSNEHV----- 408
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnKLGMKEMIRSINKcsvFYTLVAIKDAFNNRNVeifki 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 409 -LSAGFDINTPDNLGRTCLHAAASGGNVECLNLLLSSGADLRRRDK-FGRTPLHYAAANGSYQCAVTLVTAGAGVNEADC 486
Cdd:PHA02878 120 iLTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 487 KGCSPLHYAaasdtyrraephtpsshdaeedepLKESRRKeaffCLEFLLDNGADPSLRDRQGYTAVHYAAAY-GNRQNL 565
Cdd:PHA02878 200 TNNSPLHHA------------------------VKHYNKP----IVHILLENGASTDARDKCGNTPLHISVGYcKDYDIL 251
|
250 260
....*....|....*....|....*..
gi 1034579110 566 ELLLEMSFNCleDVESTI-PVSPLHLA 591
Cdd:PHA02878 252 KLLLEHGVDV--NAKSYIlGLTALHSS 276
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
80-235 |
6.24e-12 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 69.90 E-value: 6.24e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 80 AAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLL 159
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034579110 160 NKGASLNvcDKKERQPLHWAAFLGHLEVLKLLVARGADLGCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPN 235
Cdd:PLN03192 612 HFASISD--PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
794-887 |
7.29e-12 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 62.44 E-value: 7.29e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 794 MHWASYTGHEDCLELLLE-HSPFSYLEGNPFTPLHCAVINNQDSTTEMLLGALGAKIVNsrdaKGRTPLHAAAFADNVSG 872
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLEnGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD----NGRTALHYAARSGHLEI 76
|
90
....*....|....*
gi 1034579110 873 LRMLLQHQAEVNATD 887
Cdd:pfam12796 77 VKLLLEKGADINVKD 91
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
245-489 |
1.36e-11 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 67.71 E-value: 1.36e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 245 ACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAaVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQIL 324
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLA-MKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 325 IQNGSEI-DCADKFGNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGfsdccrkllssgqlysivssl 403
Cdd:PHA02875 88 LDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG--------------------- 146
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 404 snehvlsagfDINTpdnlgrtclhaaasggnvecLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNE 483
Cdd:PHA02875 147 ----------DIKG--------------------IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDY 196
|
....*.
gi 1034579110 484 ADCKGC 489
Cdd:PHA02875 197 FGKNGC 202
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
669-918 |
1.46e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 68.74 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 669 LLIDSGERaDITDVMDAygqtPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFVLC 748
Cdd:PLN03192 512 LLGDNGGE-HDDPNMAS----NLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI 586
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 749 RDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAGvdysgyspmhwasytghedclELLLEhspfsylegnpftplhc 828
Cdd:PLN03192 587 RDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG---------------------DLLCT----------------- 628
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 829 avinnqdsttemllgalgakivnsrdakgrtplhaAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEF 908
Cdd:PLN03192 629 -----------------------------------AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRL 673
|
250
....*....|
gi 1034579110 909 LLYRGkADLT 918
Cdd:PLN03192 674 LIMNG-ADVD 682
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
531-614 |
2.17e-11 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 60.90 E-value: 2.17e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 531 CLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNCLEDVESTipvsPLHLAAYNGHCEALKTLAETLVNL 610
Cdd:pfam12796 12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT----ALHYAARSGHLEIVKLLLEKGADI 87
|
....
gi 1034579110 611 DVRD 614
Cdd:pfam12796 88 NVKD 91
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
112-275 |
4.99e-11 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 67.20 E-value: 4.99e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 112 VAAANRATKCAEALAPLLSSL-------NVADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGH 184
Cdd:PLN03192 524 NMASNLLTVASTGNAALLEELlkakldpDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKH 603
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 185 LEVLKLL--VARGADlgckDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGA 262
Cdd:PLN03192 604 HKIFRILyhFASISD----PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
|
170
....*....|....
gi 1034579110 263 NVNQPN-DKGFTPL 275
Cdd:PLN03192 680 DVDKANtDDDFSPT 693
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
422-475 |
5.80e-11 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 58.44 E-value: 5.80e-11
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1034579110 422 GRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLV 475
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
256-459 |
9.03e-11 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 65.46 E-value: 9.03e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 256 ELVNAGANVNQPNDKGFTPLHVAAVSTNGALcLELLVNNGADVNYQSKEGKSPLHMAAIHGR--FTRSQILIQNGSEID- 332
Cdd:PHA02946 57 ELLHRGYSPNETDDDGNYPLHIASKINNNRI-VAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINn 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 333 CADKFGNTPLhVAARYGHELLISTLMTNGadtarrgihdmFPLHLAVLFGFSDCCRKLLSSGQLYSIVSSLsnehvLSAG 412
Cdd:PHA02946 136 SVDEEGCGPL-LACTDPSERVFKKIMSIG-----------FEARIVDKFGKNHIHRHLMSDNPKASTISWM-----MKLG 198
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 1034579110 413 FDINTPDNLGRTCLHAAASG--GNVECLNLLLSSgADLRRRDKFGRTPL 459
Cdd:PHA02946 199 ISPSKPDHDGNTPLHIVCSKtvKNVDIINLLLPS-TDVNKQNKFGDSPL 246
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
273-460 |
1.02e-10 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 65.80 E-value: 1.02e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 273 TPLHVAAvSTNGALCLE-LLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSE-----IDCADKFGNTPLHVAA 346
Cdd:cd22192 19 SPLLLAA-KENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 347 RYGHELLISTLMTNGADTA---------RRGIHDMFplhlavLFGfsdccrkllssgqlysivsslsnEHVLSagFdint 417
Cdd:cd22192 98 VNQNLNLVRELIARGADVVspratgtffRPGPKNLI------YYG-----------------------EHPLS--F---- 142
|
170 180 190 200
....*....|....*....|....*....|....*....|...
gi 1034579110 418 pdnlgrtclhaAASGGNVECLNLLLSSGADLRRRDKFGRTPLH 460
Cdd:cd22192 143 -----------AACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
|
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
35-103 |
1.70e-10 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 58.59 E-value: 1.70e-10
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034579110 35 SQDQERRTPLHAAAYVGDVPILQLLLmSGANVNAKDTLWlTPLHRAAASRNEKVLGLLLAHSADVNARD 103
Cdd:pfam12796 25 LQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDNGR-TALHYAARSGHLEIVKLLLEKGADINVKD 91
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
139-192 |
1.86e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 57.28 E-value: 1.86e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1034579110 139 GRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLV 192
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
658-933 |
3.34e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 63.47 E-value: 3.34e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 658 AAASGHTDSLHLLIDSGERADITdVMDAYgqTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLA 737
Cdd:PHA02875 9 AILFGELDIARRLLDIGINPNFE-IYDGI--SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 738 ALLDHDAF---VLCRDfkGRTPIHLASACGHTAVLRTLLqaALSTDPLDAGVDYsgYSPMHWASYTGHEDCLELLLEHSP 814
Cdd:PHA02875 86 ELLDLGKFaddVFYKD--GMTPLHLATILKKLDIMKLLI--ARGADPDIPNTDK--FSPLHLAVMMGDIKGIELLIDHKA 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 815 FSYLEgnpftplhcavinnqdsttemllgalgakivnsrDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTAL 894
Cdd:PHA02875 160 CLDIE----------------------------------DCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1034579110 895 M-TAAENGQTAAVEFLLYRGkAD---LTVLDENKNTALHLACS 933
Cdd:PHA02875 206 LcYAIENNKIDIVRLFIKRG-ADcniMFMIEGEECTILDMICN 247
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
42-167 |
3.88e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 63.09 E-value: 3.88e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 42 TPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKC 121
Cdd:PHA02875 104 TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183
|
90 100 110 120
....*....|....*....|....*....|....*....|....*..
gi 1034579110 122 AEALAPLLSSLNVADRSGR-SALHHAVHSGHLETVNLLLNKGASLNV 167
Cdd:PHA02875 184 CKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNI 230
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
850-1010 |
6.66e-10 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 62.67 E-value: 6.66e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 850 VNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLLYRGkADLTVLDENKNTALH 929
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLH 195
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 930 LACSKGHEKCALMILAETQDlgLINATNSALqMPLHIAARNGLASVvqALLSHGATVLAVDEEGHTP---ALACAPNKDV 1006
Cdd:PHA02874 196 NAAEYGDYACIKLLIDHGNH--IMNKCKNGF-TPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPlhhAINPPCDIDI 270
|
....
gi 1034579110 1007 ADCL 1010
Cdd:PHA02874 271 IDIL 274
|
|
| PHA03095 |
PHA03095 |
ankyrin-like protein; Provisional |
37-167 |
7.39e-10 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222980 [Multi-domain] Cd Length: 471 Bit Score: 62.73 E-value: 7.39e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 37 DQERRTPLHA-AAYVGDVP-ILQLLLMSGANVNAKDTLWLTPLHRAAASRNEK--VLGLLLAHSADVNARDKLWQTPLHV 112
Cdd:PHA03095 184 DDRFRSLLHHhLQSFKPRArIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHY 263
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*
gi 1034579110 113 AAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLLNKGASLNV 167
Cdd:PHA03095 264 AAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAET 318
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
172-225 |
8.45e-10 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 55.36 E-value: 8.45e-10
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1034579110 172 ERQPLHWAAFLGHLEVLKLLVARGADLGCKDRKGYGLLHTAAASGQIEVVKYLL 225
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
50-345 |
1.05e-09 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 62.16 E-value: 1.05e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 50 VGDVPILQL--LLMSGANVN---AKDTLWLTPLHRAAASRneKVLGLLLAHSADVNARDKLWQTPLhvaaanratkCAea 124
Cdd:PHA02798 12 FSDNVKLSTvkLLIKSCNPNeivNEYSIFQKYLQRDSPST--DIVKLFINLGANVNGLDNEYSTPL----------CT-- 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 125 lapLLSslNVADrsgrsalhhavHSGHLETVNLLLNKGASLNVCDKKERQPLHWA---AFLGHLEVLKLLVARGADLGCK 201
Cdd:PHA02798 78 ---ILS--NIKD-----------YKHMLDIVKILIENGADINKKNSDGETPLYCLlsnGYINNLEILLFMIENGADTTLL 141
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 202 DRKGYGLLHTAAASG---QIEVVKYLLRMGAEIDE-PNAFGNTALHiaCYLGQDAVAIE------LVNAGANVNQPND-- 269
Cdd:PHA02798 142 DKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDINThNNKEKYDTLH--CYFKYNIDRIDadilklFVDNGFIINKENKsh 219
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034579110 270 -KGFTPLHVAAVSTNGALCLELL--VNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVA 345
Cdd:PHA02798 220 kKKFMEYLNSLLYDNKRFKKNILdfIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
131-311 |
1.12e-09 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 61.99 E-value: 1.12e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 131 SLNVADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGH--LEVLKLLVARGADLGCK-DRKGYG 207
Cdd:PHA02946 64 SPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNSvDEEGCG 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 208 LLhTAAASGQIEVVKYLLRMGAEIDEPNAFGNTalHIACYLGQD---AVAIE-LVNAGANVNQPNDKGFTPLHVAAVSTN 283
Cdd:PHA02946 144 PL-LACTDPSERVFKKIMSIGFEARIVDKFGKN--HIHRHLMSDnpkASTISwMMKLGISPSKPDHDGNTPLHIVCSKTV 220
|
170 180
....*....|....*....|....*...
gi 1034579110 284 GALCLELLVNNGADVNYQSKEGKSPLHM 311
Cdd:PHA02946 221 KNVDIINLLLPSTDVNKQNKFGDSPLTL 248
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
652-707 |
2.63e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 53.82 E-value: 2.63e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034579110 652 WTPLHAAAASGHTDSLHLLIDSGerADItDVMDAYGQTPLMLAIMNGHVDCVHLLL 707
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKG--ADI-NAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
857-1019 |
4.20e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 60.00 E-value: 4.20e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 857 GRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLLYRGKADLTVLDENKNTALHLACSKGH 936
Cdd:PHA02875 35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKK 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 937 EKCALMILAETQDLGLINATNSAlqmPLHIAARNGLASVVQALLSHGATVLAVDEEGHTPALACAPNKDVADCLALILST 1016
Cdd:PHA02875 115 LDIMKLLIARGADPDIPNTDKFS---PLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
|
...
gi 1034579110 1017 MKP 1019
Cdd:PHA02875 192 ANI 194
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
338-575 |
6.74e-09 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 59.23 E-value: 6.74e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 338 GNTPLHVAARYGHELLISTLMTNGA--DTARRGIHDmfPLHLAVLFGFSDCCRKLLSSGqlysivsSLSNEHVLSAGfdi 415
Cdd:PHA02875 35 GISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIES--ELHDAVEEGDVKAVEELLDLG-------KFADDVFYKDG--- 102
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 416 NTPdnlgrtcLHAAASGGNVECLNLLLSSGAD--LRRRDKFgrTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLH 493
Cdd:PHA02875 103 MTP-------LHLATILKKLDIMKLLIARGADpdIPNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLI 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 494 YAAAsdtyrraephtpsshdaeedeplkesrRKEAFFClEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNL-ELLLEMS 572
Cdd:PHA02875 174 IAMA---------------------------KGDIAIC-KMLLDSGANIDYFGKNGCVAALCYAIENNKIDIvRLFIKRG 225
|
...
gi 1034579110 573 FNC 575
Cdd:PHA02875 226 ADC 228
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
577-718 |
7.17e-09 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 59.88 E-value: 7.17e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 577 EDVESTIPVSPLHLAAyNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKE--------- 647
Cdd:PLN03192 519 EHDDPNMASNLLTVAS-TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDangntalwn 597
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 648 ------RKRKWTPLHAAAASGHTDSLHLLIDSGERADIT------------DVMDAYGQTPLMLAIMNGHVDCVHLLLEK 709
Cdd:PLN03192 598 aisakhHKIFRILYHFASISDPHAAGDLLCTAAKRNDLTamkellkqglnvDSEDHQGATALQVAMAEDHVDMVRLLIMN 677
|
....*....
gi 1034579110 710 GSTADAADL 718
Cdd:PLN03192 678 GADVDKANT 686
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
428-569 |
7.23e-09 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 59.88 E-value: 7.23e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 428 AAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPL--------------- 492
Cdd:PLN03192 531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifril 610
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034579110 493 -HYAAASDtyrraePHTPSshdaeedEPLKESRRKEAFFCLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLL 569
Cdd:PLN03192 611 yHFASISD------PHAAG-------DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
857-910 |
8.51e-09 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 52.66 E-value: 8.51e-09
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1034579110 857 GRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLL 910
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
48-275 |
1.61e-08 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 58.14 E-value: 1.61e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 48 AYVG----DVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKcae 123
Cdd:PHA02946 43 AYCGikglDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEV--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 124 alapllsslnvadrsgrsalhhavhsghLETVNLLLNKGASL-NVCDKKERQPLhWAAFLGHLEVLKLLVARGADLGCKD 202
Cdd:PHA02946 120 ----------------------------IERINLLVQYGAKInNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVD 170
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034579110 203 RKGYGLLHTAAASG--QIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAV-AIELVNAGANVNQPNDKGFTPL 275
Cdd:PHA02946 171 KFGKNHIHRHLMSDnpKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKNVdIINLLLPSTDVNKQNKFGDSPL 246
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
721-913 |
1.86e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 58.08 E-value: 1.86e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 721 RTALHRGAVTGCEDCLAALLD---HDAFVLcrdFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAGVDysgySPMHWA 797
Cdd:PHA02875 3 QVALCDAILFGELDIARRLLDigiNPNFEI---YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIE----SELHDA 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 798 SYTGHEDCLELLLEHSPFS----YLEGNpfTPLHCAVINNQDSTTEMLLGALGAKIVNSRDAKgrTPLHAAAFADNVSGL 873
Cdd:PHA02875 76 VEEGDVKAVEELLDLGKFAddvfYKDGM--TPLHLATILKKLDIMKLLIARGADPDIPNTDKF--SPLHLAVMMGDIKGI 151
|
170 180 190 200
....*....|....*....|....*....|....*....|
gi 1034579110 874 RMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLLYRG 913
Cdd:PHA02875 152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
765-991 |
2.70e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 57.37 E-value: 2.70e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 765 HTAVLRTLLQAALSTDPLDAGVDYSGYSPMHWASYTGHEDCLELLLEHS--PFSYLEGNpFTPLH-----CAVINNQDST 837
Cdd:PHA03100 10 SRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGadINSSTKNN-STPLHylsniKYNLTDVKEI 88
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 838 TEMLLgALGAkIVNSRDAKGRTPLHAAAFA--DNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQ--TAAVEFLLYRG 913
Cdd:PHA03100 89 VKLLL-EYGA-NVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKG 166
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 914 ---------------KADLTVLDENKNTALHLACSKGHEKCALMILaetqDLGL-INATNSALQMPLHIAARNGLASVVQ 977
Cdd:PHA03100 167 vdinaknrvnyllsyGVPINIKDVYGFTPLHYAVYNNNPEFVKYLL----DLGAnPNLVNKYGDTPLHIAILNNNKEIFK 242
|
250
....*....|....
gi 1034579110 978 ALLSHGATVLAVDE 991
Cdd:PHA03100 243 LLLNNGPSIKTIIE 256
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
200-346 |
4.47e-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: 57.40 E-value: 4.47e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 200 CKDRKGYGLLHTAAASGQ-IEVVKYLLRMGAEIDEpnafGNTALHIACYLGQDAV----AIELVNAGANVNQP--ND--- 269
Cdd:TIGR00870 47 CPDRLGRSALFVAAIENEnLELTELLLNLSCRGAV----GDTLLHAISLEYVDAVeailLHLLAAFRKSGPLElaNDqyt 122
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 270 ----KGFTPLHVAAVsTNGALCLELLVNNGADVNYQSK--------------EGKSPLHMAAIHGRFTRSQILIQNGSEI 331
Cdd:TIGR00870 123 seftPGITALHLAAH-RQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADI 201
|
170
....*....|....*
gi 1034579110 332 DCADKFGNTPLHVAA 346
Cdd:TIGR00870 202 LTADSLGNTLLHLLV 216
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
336-493 |
6.99e-08 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 56.56 E-value: 6.99e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 336 KFGNTPLHVAARYGHELLISTLMT-NGADTARRGIHDMFPLHLAVLFGFSDCCRKLLSSgqlysiVSSLSNEHVLSAGFd 414
Cdd:cd22192 15 RISESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEA------APELVNEPMTSDLY- 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 415 intpdnLGRTCLHAAASGGNVECLNLLLSSGADL----------RRRDK----FGRTPLHYAAANGSYQCAVTLVTAGAG 480
Cdd:cd22192 88 ------QGETALHIAVVNQNLNLVRELIARGADVvspratgtffRPGPKnliyYGEHPLSFAACVGNEEIVRLLIEHGAD 161
|
170
....*....|...
gi 1034579110 481 VNEADCKGCSPLH 493
Cdd:cd22192 162 IRAQDSLGNTVLH 174
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
40-93 |
7.06e-08 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.97 E-value: 7.06e-08
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1034579110 40 RRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLL 93
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
841-996 |
8.59e-08 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 56.04 E-value: 8.59e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 841 LLGALGAKIVNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLLYRGkADLTVL 920
Cdd:PHA02878 152 LLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDAR 230
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034579110 921 DENKNTALHLACSKGHEKCALMILAETQdlGLINATNSALQM-PLHIAARNglASVVQALLSHGATVLAVDEEGHTP 996
Cdd:PHA02878 231 DKCGNTPLHISVGYCKDYDILKLLLEHG--VDVNAKSYILGLtALHSSIKS--ERKLKLLLEYGADINSLNSYKLTP 303
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
54-236 |
1.16e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 56.06 E-value: 1.16e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 54 PILQLLLMSGANVNAKDTLWLTPLHRAAASRNEkvLGLLLAHSADVNARDKLWQTPLHVAAANratkcaEALAP-LLSSL 132
Cdd:PTZ00322 11 SAFAAQLFFGTEGSRKRRAKPISFERMAAIQEE--IARIDTHLEALEATENKDATPDHNLTTE------EVIDPvVAHML 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 133 NVAdrsgrsaLHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLGCKDRKGYGLLHTA 212
Cdd:PTZ00322 83 TVE-------LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
|
170 180
....*....|....*....|....
gi 1034579110 213 AASGQIEVVKYLLRMGAEIDEPNA 236
Cdd:PTZ00322 156 EENGFREVVQLLSRHSQCHFELGA 179
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
427-530 |
1.30e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 55.67 E-value: 1.30e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 427 HAAASGGNVEcLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAASDTYRRAE- 505
Cdd:PTZ00322 88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQl 166
|
90 100
....*....|....*....|....*..
gi 1034579110 506 --PHTPSSHDAEEDEPLKESRRKEAFF 530
Cdd:PTZ00322 167 lsRHSQCHFELGANAKPDSFTGKPPSL 193
|
|
| PHA02798 |
PHA02798 |
ankyrin-like protein; Provisional |
152-447 |
1.34e-07 |
|
ankyrin-like protein; Provisional
Pssm-ID: 222931 [Multi-domain] Cd Length: 489 Bit Score: 55.61 E-value: 1.34e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 152 LETVNLLLNKGASLNVCDKKERQPL-----HWAAFLGHLEVLKLLVARGADLGCKDRKG----YGLLHTAAASgQIEVVK 222
Cdd:PHA02798 51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGetplYCLLSNGYIN-NLEILL 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 223 YLLRMGAEIDEPNAFGNTALHI----ACYLGQDAVAIeLVNAGANVNQPNDK-GFTPLHV---AAVSTNGALCLELLVNN 294
Cdd:PHA02798 130 FMIENGADTTLLDKDGFTMLQVylqsNHHIDIEIIKL-LLEKGVDINTHNNKeKYDTLHCyfkYNIDRIDADILKLFVDN 208
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 295 GADVNYQSKegksplhmaaihgrFTRSQILiqngseidcadkfgntplhvaaryghELLISTLMTNgadtaRRGIHDMFP 374
Cdd:PHA02798 209 GFIINKENK--------------SHKKKFM--------------------------EYLNSLLYDN-----KRFKKNILD 243
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034579110 375 LhlavLFGFSDCCRK-LLSSGQLYSIVSSLSN---EHVLSAGFDINTPDNLGRTCLHAAASGGNVECLNLLLSSGAD 447
Cdd:PHA02798 244 F----IFSYIDINQVdELGFNPLYYSVSHNNRkifEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
73-125 |
1.43e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 49.20 E-value: 1.43e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1034579110 73 WLTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEAL 125
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
824-996 |
1.48e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 54.97 E-value: 1.48e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 824 TPLHCAVINNQDSTTEMLLgALGAKiVNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQT 903
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLF-EYGAD-VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDY 203
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 904 AAVEFLLYRGkADLTVLDENKNTALHLACSKGHEKCALMILAETqdlglINATNSALQMPLHIAARNGLA-SVVQALLSH 982
Cdd:PHA02874 204 ACIKLLIDHG-NHIMNKCKNGFTPLHNAIIHNRSAIELLINNAS-----INDQDIDGSTPLHHAINPPCDiDIIDILLYH 277
|
170
....*....|....
gi 1034579110 983 GATVLAVDEEGHTP 996
Cdd:PHA02874 278 KADISIKDNKGENP 291
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
868-1014 |
1.55e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 55.64 E-value: 1.55e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 868 DNVSGLRMLLQHQAEVNA--------------TDHTGRTALMTAAENGQTAAVEFLLyRGKADLTVLDENKNTALHLACS 933
Cdd:PLN03192 489 DNVVILKNFLQHHKELHDlnvgdllgdnggehDDPNMASNLLTVASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAAS 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 934 KGHEKCALMILAETQDLGLINAT-NSAL---------------------QMP------LHIAARNGLASVVQALLSHGAT 985
Cdd:PLN03192 568 KGYEDCVLVLLKHACNVHIRDANgNTALwnaisakhhkifrilyhfasiSDPhaagdlLCTAAKRNDLTAMKELLKQGLN 647
|
170 180
....*....|....*....|....*....
gi 1034579110 986 VLAVDEEGHTpALACAPNKDVADCLALIL 1014
Cdd:PLN03192 648 VDSEDHQGAT-ALQVAMAEDHVDMVRLLI 675
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
217-470 |
2.00e-07 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 55.30 E-value: 2.00e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 217 QIEVVKYLLRMG-AEID-EPNAFGNTALHiaCYLGQDAVAIE----LVNAGANVNQPNDKGFTPLHVAAVSTN-GALCLE 289
Cdd:PHA02716 154 DLDLIKYMVDVGiVNLNyVCKKTGYGILH--AYLGNMYVDIDilewLCNNGVNVNLQNNHLITPLHTYLITGNvCASVIK 231
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 290 LLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDcADKFGNTP--LHV---AARYGHELLISTLMTNGA-- 362
Cdd:PHA02716 232 KIIELGGDMDMKCVNGMSPIMTYIINIDNINPEITNIYIESLD-GNKVKNIPmiLHSyitLARNIDISVVYSFLQPGVkl 310
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 363 ---DTARRGIhdmfpLHLAVLfgfsdccRKLLSSgqlySIVSSLsNEHvlsaGFDINTPDNLGRTCLHAAAS-------- 431
Cdd:PHA02716 311 hykDSAGRTC-----LHQYIL-------RHNIST----DIIKLL-HEY----GNDLNEPDNIGNTVLHTYLSmlsvvnil 369
|
250 260 270 280
....*....|....*....|....*....|....*....|....*
gi 1034579110 432 ------GGNVECLNLLLSSGADLRRRDKFGRTPLhyaaanGSYQC 470
Cdd:PHA02716 370 dpetdnDIRLDVIQCLISLGADITAVNCLGYTPL------TSYIC 408
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
586-759 |
2.53e-07 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 54.63 E-value: 2.53e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 586 SPLHLAAYNGHCEALKTLAETlvnldvrdhkGRTALFlatERGstecvevltAHGASALikerkrkwtplHAAAASGHTD 665
Cdd:cd22192 19 SPLLLAAKENDVQAIKKLLKC----------PSCDLF---QRG---------ALGETAL-----------HVAALYDNLE 65
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 666 SLHLLIDSGERAdITDVM--DAY-GQTPLMLAIMNGHVDCVHLLLEKGstADAADLR----------------GRTALHR 726
Cdd:cd22192 66 AAVVLMEAAPEL-VNEPMtsDLYqGETALHIAVVNQNLNLVRELIARG--ADVVSPRatgtffrpgpknliyyGEHPLSF 142
|
170 180 190
....*....|....*....|....*....|...
gi 1034579110 727 GAVTGCEDCLAALLDHDAFVLCRDFKGRTPIHL 759
Cdd:cd22192 143 AACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
722-813 |
2.86e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 54.52 E-value: 2.86e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 722 TALHRGAVTGCEdcLAA---------LLDHDAFVLCRDFKGRTPIHLASACGHTAVLRTLLQaaLSTDPldAGVDYSGYS 792
Cdd:PTZ00322 77 VVAHMLTVELCQ--LAAsgdavgariLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLE--FGADP--TLLDKDGKT 150
|
90 100
....*....|....*....|.
gi 1034579110 793 PMHWASYTGHEDCLELLLEHS 813
Cdd:PTZ00322 151 PLELAEENGFREVVQLLSRHS 171
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
657-789 |
3.33e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 54.49 E-value: 3.33e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 657 AAAASGHTDSLHLLIDSGERADITDvmdAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTAL------------ 724
Cdd:PLN03192 531 TVASTGNAALLEELLKAKLDPDIGD---SKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkif 607
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 725 ------------HRGAVTGCE-------DCLAALLDHDAFVLCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAG 785
Cdd:PLN03192 608 rilyhfasisdpHAAGDLLCTaakrndlTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
|
....
gi 1034579110 786 VDYS 789
Cdd:PLN03192 688 DDFS 691
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
308-498 |
3.39e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 54.12 E-value: 3.39e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 308 PLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARY----GHELLISTLMTNGADTARRGIHDMFPLHLAVLF-- 381
Cdd:PHA02878 40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKCSVFYTLVAIKDAFNNRNVEIFki 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 382 -------GFSDCCRKLLSSGQLYSIVSSLSNEHVLSAGFDINTPD-NLGRTCLHAAASGGNVECLNLLLSSGADLRRRDK 453
Cdd:PHA02878 120 iltnrykNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
|
170 180 190 200
....*....|....*....|....*....|....*....|....*
gi 1034579110 454 FGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAAS 498
Cdd:PHA02878 200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY 244
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
681-878 |
3.61e-07 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 54.32 E-value: 3.61e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 681 DVMDAYGQTPLM-LAIMNGHVDCVHLLLEKGSTADAadlrGRTALH---RGAVTGCEDCLAALLDHD----------AFV 746
Cdd:TIGR00870 46 NCPDRLGRSALFvAAIENENLELTELLLNLSCRGAV----GDTLLHaisLEYVDAVEAILLHLLAAFrksgplelanDQY 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 747 LCRDFKGRTPIHLASACGHTAVLRTLLQAALSTdPLDAGVD-----------YSGYSPMHWASYTGHEDCLELLLEHsPF 815
Cdd:TIGR00870 122 TSEFTPGITALHLAAHRQNYEIVKLLLERGASV-PARACGDffvksqgvdsfYHGESPLNAAACLGSPSIVALLSED-PA 199
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 816 SYLE----GNpfTPLHCAVINNQDST--TEM------LLGALGAKIVNSRDA------KGRTPLHAAAFADNVSGLRMLL 877
Cdd:TIGR00870 200 DILTadslGN--TLLHLLVMENEFKAeyEELscqmynFALSLLDKLRDSKELevilnhQGLTPLKLAAKEGRIVLFRLKL 277
|
.
gi 1034579110 878 Q 878
Cdd:TIGR00870 278 A 278
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
720-773 |
3.67e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 48.04 E-value: 3.67e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1034579110 720 GRTALHRGAVTGCEDCLAALLDHDAFVLCRDFKGRTPIHLASACGHTAVLRTLL 773
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
659-742 |
3.85e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 54.13 E-value: 3.85e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 659 AASGHTDSLHLLIDSGerADiTDVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAA 738
Cdd:PTZ00322 90 AASGDAVGARILLTGG--AD-PNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
....
gi 1034579110 739 LLDH 742
Cdd:PTZ00322 167 LSRH 170
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
86-283 |
4.35e-07 |
|
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: 54.12 E-value: 4.35e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 86 EKVLGLL----LAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRS--------------GRSALHHAV 147
Cdd:cd21882 2 EELLGLLeclrWYLTDSAYQRGATGKTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAI 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 148 HSGHLETVNLLLNKGASLNV--CDKKERQPLHWAAFLGHLEvlkllvargadlgckdrkgyglLHTAAASGQIEVVKYLL 225
Cdd:cd21882 82 ENRNLNLVRLLVENGADVSAraTGRFFRKSPGNLFYFGELP----------------------LSLAACTNQEEIVRLLL 139
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034579110 226 RMGAEIDEPNA---FGNTALHIACYLGQDAVAI---------ELVNAGANVNQ-------PNDKGFTPLHVAAVSTN 283
Cdd:cd21882 140 ENGAQPAALEAqdsLGNTVLHALVLQADNTPENsafvcqmynLLLSYGAHLDPtqqleeiPNHQGLTPLKLAAVEGK 216
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
205-258 |
5.37e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.27 E-value: 5.37e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1034579110 205 GYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELV 258
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
307-357 |
5.48e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.27 E-value: 5.48e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1034579110 307 SPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTL 357
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
586-636 |
5.87e-07 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 47.27 E-value: 5.87e-07
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1034579110 586 SPLHLAAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVL 636
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
614-773 |
6.25e-07 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 53.61 E-value: 6.25e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 614 DHKGRTALFLATERGSTECVEVLTAHGASALIKERKRKWTPlhaaaasghtdslhllidsgeradiTDVMDAY--GQTPL 691
Cdd:cd22194 138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFFNP-------------------------KYKHEGFyfGETPL 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 692 MLAIMNGHVDCVHLLLEKGSTADAA-DLRGRTALHrGAVTGCEDclaaLLDHDAFVL-----------------CRDFKG 753
Cdd:cd22194 193 ALAACTNQPEIVQLLMEKESTDITSqDSRGNTVLH-ALVTVAED----SKTQNDFVKrmydmillksenknletIRNNEG 267
|
170 180
....*....|....*....|
gi 1034579110 754 RTPIHLASACGHTAVLRTLL 773
Cdd:cd22194 268 LTPLQLAAKMGKAEILKYIL 287
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
179-342 |
7.28e-07 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 53.33 E-value: 7.28e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 179 AAFLGHLEVLKLLVARGADLGCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVaIELV 258
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKI-FRIL 610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 259 NAGANVNQPNDKGftPLHVAAVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCA---D 335
Cdd:PLN03192 611 YHFASISDPHAAG--DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAntdD 688
|
....*..
gi 1034579110 336 KFGNTPL 342
Cdd:PLN03192 689 DFSPTEL 695
|
|
| PHA02876 |
PHA02876 |
ankyrin repeat protein; Provisional |
839-996 |
7.83e-07 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165207 [Multi-domain] Cd Length: 682 Bit Score: 53.14 E-value: 7.83e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 839 EMLLGalGAKIVNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVE----------- 907
Cdd:PHA02876 162 EMLLE--GGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsnink 239
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 908 -----------------FLLYRGKADLTVLDENKNTALHLAC-SKGHEKCALMILAETQDlglINATNSALQMPLHIAAR 969
Cdd:PHA02876 240 ndlsllkairnedletsLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGAD---VNAKNIKGETPLYLMAK 316
|
170 180
....*....|....*....|....*...
gi 1034579110 970 NGLASV-VQALLSHGATVLAVDEEGHTP 996
Cdd:PHA02876 317 NGYDTEnIRTLIMLGADVNAADRLYITP 344
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
226-358 |
8.82e-07 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.98 E-value: 8.82e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 226 RMGAeIDEPNAFGNTALHiACYLGQDAVAielvnaGANVNQPNDKGFTP--LHVAAV------STNGALCLELLVNNGAD 297
Cdd:PTZ00322 36 RMAA-IQEEIARIDTHLE-ALEATENKDA------TPDHNLTTEEVIDPvvAHMLTVelcqlaASGDAVGARILLTGGAD 107
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034579110 298 VNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLM 358
Cdd:PTZ00322 108 PNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
414-462 |
1.24e-06 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 46.57 E-value: 1.24e-06
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1034579110 414 DINTPDNLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYA 462
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
37-165 |
1.41e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 52.56 E-value: 1.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 37 DQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLL--LAHSADVNARDKLWQTplhvaA 114
Cdd:PLN03192 555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAAGDLLCT-----A 629
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....
gi 1034579110 115 ANRATkcAEALAPLLS-SLNV--ADRSGRSALHHAVHSGHLETVNLLLNKGASL 165
Cdd:PLN03192 630 AKRND--LTAMKELLKqGLNVdsEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
844-910 |
1.45e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 52.21 E-value: 1.45e-06
10 20 30 40 50 60 70
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034579110 844 ALGAKIV-------NSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLL 910
Cdd:PTZ00322 95 AVGARILltggadpNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
324-485 |
1.70e-06 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 52.18 E-value: 1.70e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 324 LIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRKLLSsgqlysiVSSL 403
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYH-------FASI 616
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 404 SNEHvlsAGFDIntpdnlgrtcLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNE 483
Cdd:PLN03192 617 SDPH---AAGDL----------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
|
..
gi 1034579110 484 AD 485
Cdd:PLN03192 684 AN 685
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
782-1015 |
1.76e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 51.53 E-value: 1.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 782 LDAGVD-----YSGYSPMHWASYTGHEDCLELLLEHSPF-SYLEGNPFTPLHCAVINNQDSTTEMLLgALGAKIVNSRDA 855
Cdd:PHA02875 22 LDIGINpnfeiYDGISPIKLAMKFRDSEAIKLLMKHGAIpDVKYPDIESELHDAVEEGDVKAVEELL-DLGKFADDVFYK 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 856 KGRTPLHAAAFADNVSGLRMLLQHQAE--VNATDHTgrTALMTAAENGQTAAVEFLLYrgkadltvldenkntalHLACS 933
Cdd:PHA02875 101 DGMTPLHLATILKKLDIMKLLIARGADpdIPNTDKF--SPLHLAVMMGDIKGIELLID-----------------HKACL 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 934 KGHEKCALMilaetqdlglinatnsalqmPLHIAARNGLASVVQALLSHGATVLAVDEEGHTPALACAPNKDVADCLALI 1013
Cdd:PHA02875 162 DIEDCCGCT--------------------PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLF 221
|
..
gi 1034579110 1014 LS 1015
Cdd:PHA02875 222 IK 223
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
429-603 |
2.22e-06 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 51.55 E-value: 2.22e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 429 AASGGNVECLN-LLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAG-VNEADC----KGCSPLHYAAASDTY- 501
Cdd:cd22192 24 AAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVVNQNLn 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 502 -------RRAEPHTPsshdaeedeplkesRRKEAFF-------------------C------LEFLLDNGADPSLRDRQG 549
Cdd:cd22192 104 lvreliaRGADVVSP--------------RATGTFFrpgpknliyygehplsfaaCvgneeiVRLLIEHGADIRAQDSLG 169
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034579110 550 YTAVHYAAAYGNR----QNLELLLEMSFN----CLEDVESTIPVSPLHLAAYNGHCEALKTL 603
Cdd:cd22192 170 NTVLHILVLQPNKtfacQMYDLILSYDKEddlqPLDLVPNNQGLTPFKLAAKEGNIVMFQHL 231
|
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
122-226 |
2.24e-06 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 50.81 E-value: 2.24e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 122 AEALAPLLSSLNV--ADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKerQPLHWAAFLGHLEVLKLLVARGADLG 199
Cdd:PHA02791 11 SKQLKSFLSSKDAfkADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDS 88
|
90 100
....*....|....*....|....*..
gi 1034579110 200 CKDRKGYGLLHTAAASGQIEVVKYLLR 226
Cdd:PHA02791 89 QFDDKGNTALYYAVDSGNMQTVKLFVK 115
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
422-691 |
2.43e-06 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 51.42 E-value: 2.43e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 422 GRTCLHAAA---SGGNVECLNLLLSSGADLRRRDKF-----------GRTPLHYAAANGSYQCAVTLVTAGAGVNeadck 487
Cdd:cd21882 26 GKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVS----- 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 488 gcsplhyAAASDTYRRAEPHtPSSHDAEEDEPLKESRRKEAFfcLEFLLDNGADP---SLRDRQGYTAVHyaaaygnrqn 564
Cdd:cd21882 101 -------ARATGRFFRKSPG-NLFYFGELPLSLAACTNQEEI--VRLLLENGAQPaalEAQDSLGNTVLH---------- 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 565 leLLLEMSFNCLEDVESTIPVSPLhLAAYNGHCEALKTLAEtlvnldVRDHKGRTALFLATERGSTECVEVLTAHGASAL 644
Cdd:cd21882 161 --ALVLQADNTPENSAFVCQMYNL-LLSYGAHLDPTQQLEE------IPNHQGLTPLKLAAVEGKIVMFQHILQREFSGP 231
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034579110 645 IKERKRK---WT--PLHAAA-------ASGHTDSLHLLIDSGERADITDVMDaygQTPL 691
Cdd:cd21882 232 YQPLSRKfteWTygPVTSSLydlseidSWEKNSVLELIAFSKKREARHQMLV---QEPL 287
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
607-813 |
2.66e-06 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411977 [Multi-domain] Cd Length: 607 Bit Score: 51.33 E-value: 2.66e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 607 LVNLDVRD--HKGRTALFLATERGSTECVEVLTAHGASALIKERKRKWTPlhaaaASGHTDSLhllidsgeraditdvmd 684
Cdd:cd22193 64 FINAEYTDeyYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGRFFQP-----KYQGEGFY----------------- 121
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 685 aYGQTPLMLAIMNGHVDCVHLLLE---KGSTADAADLRGRTALHrGAVTGCEDclaaLLDHDAFV-------------LC 748
Cdd:cd22193 122 -FGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLH-ALVTVADN----TKENTKFVtrmydmilirgakLC 195
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 749 --------RDFKGRTPIHLASACGHTAVLRTLLQAALSTDP---LDAGVDYSGYSPMHWASY-------TGHEDCLELLL 810
Cdd:cd22193 196 ptveleeiRNNDGLTPLQLAAKMGKIEILKYILQREIKEPElrhLSRKFTDWAYGPVSSSLYdlsnvdtCEKNSVLEIIV 275
|
...
gi 1034579110 811 EHS 813
Cdd:cd22193 276 YNS 278
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
519-696 |
3.47e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 50.76 E-value: 3.47e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 519 PLKESRRKEAFFCLEFLLDNG--ADPSLRdRQGYTAVHYAAAYGNRQNLELLLEMSFNclEDVESTIPVSPLHLAAYNGH 596
Cdd:PHA02875 71 ELHDAVEEGDVKAVEELLDLGkfADDVFY-KDGMTPLHLATILKKLDIMKLLIARGAD--PDIPNTDKFSPLHLAVMMGD 147
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 597 CEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKERKRKWTPLHAAAASGHTDSLHLLIDSGER 676
Cdd:PHA02875 148 IKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
|
170 180
....*....|....*....|.
gi 1034579110 677 ADI-TDVMDAYGQTPLMLAIM 696
Cdd:PHA02875 228 CNImFMIEGEECTILDMICNM 248
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
862-982 |
3.90e-06 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 51.05 E-value: 3.90e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 862 HAAAFADNVsGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLLYRGkADLTVLDENKNTalhlacskghekcal 941
Cdd:PTZ00322 88 QLAASGDAV-GARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKT--------------- 150
|
90 100 110 120
....*....|....*....|....*....|....*....|.
gi 1034579110 942 milaetqdlglinatnsalqmPLHIAARNGLASVVQALLSH 982
Cdd:PTZ00322 151 ---------------------PLELAEENGFREVVQLLSRH 170
|
|
| PHA02878 |
PHA02878 |
ankyrin repeat protein; Provisional |
581-897 |
4.96e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222939 [Multi-domain] Cd Length: 477 Bit Score: 50.26 E-value: 4.96e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 581 STIPVSPLHLAAYNGHCEALKTLAETLVNLDVRDHKGRTALFLAtergsteCVEVlTAHGASALIKER-KRK-WTPLHAA 658
Cdd:PHA02878 34 SLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHII-------CKEP-NKLGMKEMIRSInKCSvFYTLVAI 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 659 AASGHTDSLH----LLIDSGERadITDVMDAYGQTPLMLAIMNGHVdcVHLLLEKGSTADAADL-RGRTALHRGAVTGCE 733
Cdd:PHA02878 106 KDAFNNRNVEifkiILTNRYKN--IQTIDLVYIDKKSKDDIIEAEI--TKLLLSYGADINMKDRhKGNTALHYATENKDQ 181
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 734 DCLAALLDHDAFVLCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAgvdySGYSPMHWA-SYTGHEDCLELLLEH 812
Cdd:PHA02878 182 RLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDK----CGNTPLHISvGYCKDYDILKLLLEH 257
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 813 SpfsylegnpftplhcAVINNQDSTtemllgalgakivnsrdaKGRTPLHAAAFADNVsgLRMLLQHQAEVNATDHTGRT 892
Cdd:PHA02878 258 G---------------VDVNAKSYI------------------LGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLT 302
|
....*
gi 1034579110 893 ALMTA 897
Cdd:PHA02878 303 PLSSA 307
|
|
| PHA02716 |
PHA02716 |
CPXV016; CPX019; EVM010; Provisional |
44-242 |
6.97e-06 |
|
CPXV016; CPX019; EVM010; Provisional
Pssm-ID: 165089 [Multi-domain] Cd Length: 764 Bit Score: 50.30 E-value: 6.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 44 LHAaaYVG----DVPILQLLLMSGANVNAKDTLWLTPLHRAAASRN--EKVLGLLLAHSADVNARDKLWQTPLHVAAANr 117
Cdd:PHA02716 181 LHA--YLGnmyvDIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMSPIMTYIIN- 257
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 118 atkcAEALAPLLSSLNVADRSGRSA------LHHAVHSGH---LETVNLLLNKGASLNVCDKKERQPLHwAAFLGH---L 185
Cdd:PHA02716 258 ----IDNINPEITNIYIESLDGNKVknipmiLHSYITLARnidISVVYSFLQPGVKLHYKDSAGRTCLH-QYILRHnisT 332
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034579110 186 EVLKLLVARGADLGCKDRKGYGLLHTAAA--------------SGQIEVVKYLLRMGAEIDEPNAFGNTAL 242
Cdd:PHA02716 333 DIIKLLHEYGNDLNEPDNIGNTVLHTYLSmlsvvnildpetdnDIRLDVIQCLISLGADITAVNCLGYTPL 403
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
56-316 |
7.76e-06 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 49.74 E-value: 7.76e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 56 LQLLLMSGANVNAK---DTLWLTPLHRAAASrnEKVLGLLLAHSADVNARDkLWQTPLHVAAANR--ATKCAEALAPLL- 129
Cdd:PHA02989 19 LEFLLRTGFDVNEEyrgNSILLLYLKRKDVK--IKIVKLLIDNGADVNYKG-YIETPLCAVLRNReiTSNKIKKIVKLLl 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 130 ---SSLNVADRSGRSALHHAVHSGHLETVN---LLLNKGASLN-VCDKKERQPLH--WAAFLGHLEVLKLLVARGADLgC 200
Cdd:PHA02989 96 kfgADINLKTFNGVSPIVCFIYNSNINNCDmlrFLLSKGINVNdVKNSRGYNLLHmyLESFSVKKDVIKILLSFGVNL-F 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 201 KDRKGYGL------LHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTAL------HIACYlGQDAVAIELVNAGANVNQPN 268
Cdd:PHA02989 175 EKTSLYGLtpmniyLRNDIDVISIKVIKYLIKKGVNIETNNNGSESVLesfldnNKILS-KKEFKVLNFILKYIKINKKD 253
|
250 260 270 280
....*....|....*....|....*....|....*....|....*...
gi 1034579110 269 DKGFTPLHVAAVSTNGALCLELLvNNGADVNYQSKEGKSPLHMAAIHG 316
Cdd:PHA02989 254 KKGFNPLLISAKVDNYEAFNYLL-KLGDDIYNVSKDGDTVLTYAIKHG 300
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
108-159 |
1.09e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.80 E-value: 1.09e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1034579110 108 TPLHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLL 159
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PLN03192 |
PLN03192 |
Voltage-dependent potassium channel; Provisional |
532-642 |
1.16e-05 |
|
Voltage-dependent potassium channel; Provisional
Pssm-ID: 215625 [Multi-domain] Cd Length: 823 Bit Score: 49.48 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 532 LEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNC-LEDVESTI----PVSPLH----------------- 589
Cdd:PLN03192 541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVhIRDANGNTalwnAISAKHhkifrilyhfasisdph 620
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 590 -------LAAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGAS 642
Cdd:PLN03192 621 aagdllcTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
215-359 |
1.16e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 47.51 E-value: 1.16e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 215 SGQIEVVKYLLRMgaeIDEPNAFGNTALHiACyLGQDAVAIE----LVNAGANVN-QPNDKGFTPLHvAAVSTNGAL--- 286
Cdd:PHA02859 31 KDDIEGVKKWIKF---VNDCNDLYETPIF-SC-LEKDKVNVEilkfLIENGADVNfKTRDNNLSALH-HYLSFNKNVepe 104
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034579110 287 CLELLVNNGADVNYQSKEGKSPLH--MAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMT 359
Cdd:PHA02859 105 ILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKKIFDFLT 179
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
546-774 |
1.19e-05 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 49.31 E-value: 1.19e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 546 DRQGYTAVHYAAAYGNRQNLELLLEmSFNCLEDVESTIpvspLHLAA--YNGHCEAL---------KTLAETLVNLDVRD 614
Cdd:TIGR00870 49 DRLGRSALFVAAIENENLELTELLL-NLSCRGAVGDTL----LHAISleYVDAVEAIllhllaafrKSGPLELANDQYTS 123
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 615 --HKGRTALFLATERGSTECVEVLTAHGASalikerkrkwtpLHAAA------ASGHTDSLHllidsgeraditdvmdaY 686
Cdd:TIGR00870 124 efTPGITALHLAAHRQNYEIVKLLLERGAS------------VPARAcgdffvKSQGVDSFY-----------------H 174
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 687 GQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALH------------RGAVTGCEDCLAALLDHdafvlCRD---- 750
Cdd:TIGR00870 175 GESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHllvmenefkaeyEELSCQMYNFALSLLDK-----LRDskel 249
|
250 260
....*....|....*....|....*....
gi 1034579110 751 -----FKGRTPIHLASACGHTAVLRTLLQ 774
Cdd:TIGR00870 250 evilnHQGLTPLKLAAKEGRIVLFRLKLA 278
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
273-325 |
1.24e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 43.42 E-value: 1.24e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|...
gi 1034579110 273 TPLHVAAVSTNGAlCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILI 325
Cdd:pfam13637 3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
257-312 |
1.26e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.49 E-value: 1.26e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034579110 257 LVNAG-ANVNQPNDKGFTPLHVAAvSTNGALCLELLVNNGADVNYQSKEGKSPLHMA 312
Cdd:pfam13857 1 LLEHGpIDLNRLDGEGYTPLHVAA-KYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
290-345 |
1.31e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.49 E-value: 1.31e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034579110 290 LLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVA 345
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
190-245 |
1.31e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 43.49 E-value: 1.31e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034579110 190 LLVARGADLGCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIA 245
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02874 |
PHA02874 |
ankyrin repeat protein; Provisional |
31-193 |
1.40e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165205 [Multi-domain] Cd Length: 434 Bit Score: 48.81 E-value: 1.40e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 31 SFLPSQDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAAsRNEKVLGLLlahsadVNARdklwqtpl 110
Cdd:PHA02874 181 AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII-HNRSAIELL------INNA-------- 245
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 111 hvaaanratkcaealapllsSLNVADRSGRSALHHAVH-SGHLETVNLLLNKGASLNVCDKKERQPLHWA-AFLGHLEVL 188
Cdd:PHA02874 246 --------------------SINDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTAfKYINKDPVI 305
|
....*
gi 1034579110 189 KLLVA 193
Cdd:PHA02874 306 KDIIA 310
|
|
| TRPV3 |
cd22194 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ... |
229-349 |
1.46e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411978 [Multi-domain] Cd Length: 680 Bit Score: 48.99 E-value: 1.46e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 229 AEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANVN--------QPNDK--GF----TPLHVAAVsTNGALCLELLVNN 294
Cdd:cd22194 132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffNPKYKheGFyfgeTPLALAAC-TNQPEIVQLLMEK 210
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034579110 295 GAD-VNYQSKEGKSPLHMAAIHGRFTRSQI--LIQNGSEI--DCADKF--------GNTPLHVAARYG 349
Cdd:cd22194 211 ESTdITSQDSRGNTVLHALVTVAEDSKTQNdfVKRMYDMIllKSENKNletirnneGLTPLQLAAKMG 278
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
16-125 |
1.47e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 49.13 E-value: 1.47e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 16 LGSLIAPLPRAHTPCSFLPSQDQERRTPLHAA-------AYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKV 88
Cdd:PTZ00322 51 LEALEATENKDATPDHNLTTEEVIDPVVAHMLtvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQV 130
|
90 100 110
....*....|....*....|....*....|....*..
gi 1034579110 89 LGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEAL 125
Cdd:PTZ00322 131 VRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
22-114 |
1.60e-05 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 48.92 E-value: 1.60e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 22 PLPRAHTPCSFLPSQDQerrTPLHAAAYVGDVPILQLLLMSGANVNAK------------DTLWLT--PLHRAAASRNEK 87
Cdd:TIGR00870 113 PLELANDQYTSEFTPGI---TALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqgvDSFYHGesPLNAAACLGSPS 189
|
90 100
....*....|....*....|....*..
gi 1034579110 88 VLGLLLAHSADVNARDKLWQTPLHVAA 114
Cdd:TIGR00870 190 IVALLSEDPADILTADSLGNTLLHLLV 216
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
408-466 |
2.36e-05 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 48.36 E-value: 2.36e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034579110 408 VLSAGFDINTPDNLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANG 466
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
236-344 |
3.17e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 47.95 E-value: 3.17e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 236 AFGNTALHIAC-YL--GQDAVAIELVNAGANVNQPND-----------KGFTPLHVAAVSTNgALCLELLVNNGADVNYQ 301
Cdd:cd21882 24 ATGKTCLHKAAlNLndGVNEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENRN-LNLVRLLVENGADVSAR 102
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034579110 302 SKE-------------GKSPLHMAAIHGRFTRSQILIQNGSEI---DCADKFGNTPLHV 344
Cdd:cd21882 103 ATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNTVLHA 161
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
890-944 |
3.25e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.26 E-value: 3.25e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1034579110 890 GRTALMTAAENGQTAAVEFLLYRGkADLTVLDENKNTALHLACSKGHEKCALMIL 944
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
516-569 |
3.42e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.26 E-value: 3.42e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1034579110 516 EDEPLKESRRKEAFFCLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLL 569
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
689-740 |
3.45e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 42.26 E-value: 3.45e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|..
gi 1034579110 689 TPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALL 740
Cdd:pfam13637 3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
608-774 |
3.53e-05 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 47.77 E-value: 3.53e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 608 VNLDVRDHKGRTALFLATERGST-ECVEVLTAHGASALIKErkrkwTPLHAAAASGHTD----SLHLLIDSGERADITDV 682
Cdd:TIGR00870 43 LNINCPDRLGRSALFVAAIENENlELTELLLNLSCRGAVGD-----TLLHAISLEYVDAveaiLLHLLAAFRKSGPLELA 117
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 683 MDAY------GQTPLMLAIMNGHVDCVHLLLEKGSTADAAdlrgrtalhrgavTGCEDCLAAlLDHDAFvlcrdFKGRTP 756
Cdd:TIGR00870 118 NDQYtseftpGITALHLAAHRQNYEIVKLLLERGASVPAR-------------ACGDFFVKS-QGVDSF-----YHGESP 178
|
170
....*....|....*...
gi 1034579110 757 IHLASACGHTAVLRTLLQ 774
Cdd:TIGR00870 179 LNAAACLGSPSIVALLSE 196
|
|
| PHA02859 |
PHA02859 |
ankyrin repeat protein; Provisional |
152-274 |
3.88e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165195 [Multi-domain] Cd Length: 209 Bit Score: 45.97 E-value: 3.88e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 152 LETVNLLLNKGASLNVCDKKER-QPLHWaaFLGH-----LEVLKLLVARGADLGCKDRKGYGLLHT--AAASGQIEVVKY 223
Cdd:PHA02859 66 VEILKFLIENGADVNFKTRDNNlSALHH--YLSFnknvePEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKL 143
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|..
gi 1034579110 224 LLRMGAEIDEPNAFGNTALH-IACYLGQDAVAIELVNAGANVNQPNDKGFTP 274
Cdd:PHA02859 144 LIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
790-842 |
4.77e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.88 E-value: 4.77e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1034579110 790 GYSPMHWASYTGHEDCLELLLEHS-PFSYLEGNPFTPLHCAVINNQDSTTEMLL 842
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGaDINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
753-810 |
4.87e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.88 E-value: 4.87e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1034579110 753 GRTPIHLASACGHTAVLRTLLQAALSTDPldagVDYSGYSPMHWASYTGHEDCLELLL 810
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINA----VDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV |
cd21882 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ... |
565-813 |
4.94e-05 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).
Pssm-ID: 411975 [Multi-domain] Cd Length: 600 Bit Score: 47.18 E-value: 4.94e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 565 LELLLEMSFNCLEDVESTIPV---SPLHLAAYNGHCEALKTLA------------ETLVNLDVRD--HKGRTALFLATER 627
Cdd:cd21882 4 LLGLLECLRWYLTDSAYQRGAtgkTCLHKAALNLNDGVNEAIMllleaapdsgnpKELVNAPCTDefYQGQTALHIAIEN 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 628 GSTECVEVLTAHGASAlikerkrkwtplhAAAASGH--TDSLHLLIdsgeraditdvmdAYGQTPLMLAIMNGHVDCVHL 705
Cdd:cd21882 84 RNLNLVRLLVENGADV-------------SARATGRffRKSPGNLF-------------YFGELPLSLAACTNQEEIVRL 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 706 LLEKG---STADAADLRGRTALH------------RGAVTGCEDCLAAL---LDH-DAFVLCRDFKGRTPIHLASACGHT 766
Cdd:cd21882 138 LLENGaqpAALEAQDSLGNTVLHalvlqadntpenSAFVCQMYNLLLSYgahLDPtQQLEEIPNHQGLTPLKLAAVEGKI 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034579110 767 AVLRTLLQAALST--DPLDAGVDYSGYSPMHWASY-------TGHEDCLELLLEHS 813
Cdd:cd21882 218 VMFQHILQREFSGpyQPLSRKFTEWTYGPVTSSLYdlseidsWEKNSVLELIAFSK 273
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
139-167 |
5.44e-05 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 41.03 E-value: 5.44e-05
10 20
....*....|....*....|....*....
gi 1034579110 139 GRSALHHAVHSGHLETVNLLLNKGASLNV 167
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
329-593 |
5.68e-05 |
|
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]
Pssm-ID: 273311 [Multi-domain] Cd Length: 743 Bit Score: 47.38 E-value: 5.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 329 SEIDCADKFGNTPLHVAARYG-HELLISTLMTNGA-----DTArrgihdmfpLHLAVLfGFSDCCRKLLSSgQLYSIVSS 402
Cdd:TIGR00870 43 LNINCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISL-EYVDAVEAILLH-LLAAFRKS 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 403 LSNEHVLSAGFDINTPDnlgRTCLHAAASGGNVECLNLLLSSGADLRRRDK--------------FGRTPLHYAAANGSY 468
Cdd:TIGR00870 112 GPLELANDQYTSEFTPG---ITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSP 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 469 QCAVTLVTAGAGVNEADCKGCSPLHyAAASDTYRRAEPHTPSSHdaeedeplkesrrkeaffCLEFLLDNGA--DPSL-- 544
Cdd:TIGR00870 189 SIVALLSEDPADILTADSLGNTLLH-LLVMENEFKAEYEELSCQ------------------MYNFALSLLDklRDSKel 249
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1034579110 545 ---RDRQGYTAVHYAAAYGNRQNLELLLEMSFNCLEDVEStiPVSPLHLAAY 593
Cdd:TIGR00870 250 eviLNHQGLTPLKLAAKEGRIVLFRLKLAIKYKQKKFVAW--PNGQQLLSLY 299
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
91-146 |
6.11e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 41.56 E-value: 6.11e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034579110 91 LLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHA 146
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA03100 |
PHA03100 |
ankyrin repeat protein; Provisional |
821-1006 |
7.39e-05 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222984 [Multi-domain] Cd Length: 422 Bit Score: 46.58 E-value: 7.39e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 821 NPFTPLHCAVINNQDSTTEMLLgALGAKIVNSRDaKGRTPLHAAAFA-----DNVSGLRMLLQHQAEVNATDHTGRTALM 895
Cdd:PHA03100 34 KPVLPLYLAKEARNIDVVKILL-DNGADINSSTK-NNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLL 111
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 896 TAAEN--GQTAAVEFLLYRGkADLTVLDENKNTALHLACSKGHEK---CALMIlaetqDLGL-INATNSalqmplhiaar 969
Cdd:PHA03100 112 YAISKksNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDlkiLKLLI-----DKGVdINAKNR----------- 174
|
170 180 190
....*....|....*....|....*....|....*....
gi 1034579110 970 nglasvVQALLSHGATVLAVDEEGHTPAL-AC-APNKDV 1006
Cdd:PHA03100 175 ------VNYLLSYGVPINIKDVYGFTPLHyAVyNNNPEF 207
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
270-303 |
8.49e-05 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 40.74 E-value: 8.49e-05
10 20 30
....*....|....*....|....*....|....
gi 1034579110 270 KGFTPLHVAAVSTNGALCLELLVNNGADVNYQSK 303
Cdd:pfam00023 1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
406-492 |
8.73e-05 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 46.20 E-value: 8.73e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 406 EHVLSAGFDINTPDNLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGS--YQCAVTLVTAGAGVNE 483
Cdd:PHA02946 56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINN 135
|
90
....*....|
gi 1034579110 484 A-DCKGCSPL 492
Cdd:PHA02946 136 SvDEEGCGPL 145
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
338-391 |
9.04e-05 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.11 E-value: 9.04e-05
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1034579110 338 GNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRKLL 391
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
374-442 |
1.01e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 41.11 E-value: 1.01e-04
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034579110 374 PLHLAVLFGFSDCCRKLLSSGqlysivsslsnehvlsagFDINTPDNLGRTCLHAAASGGNVECLNLLL 442
Cdd:pfam13637 4 ALHAAAASGHLELLRLLLEKG------------------ADINAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| PHA02875 |
PHA02875 |
ankyrin repeat protein; Provisional |
353-574 |
1.14e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165206 [Multi-domain] Cd Length: 413 Bit Score: 45.75 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 353 LISTLMTNGADTARR----GIHDMF-------PLHLAVLFGFSDCCRKLLSSGQLYsivsslsnehvlsagfDINTPDNl 421
Cdd:PHA02875 6 LCDAILFGELDIARRlldiGINPNFeiydgisPIKLAMKFRDSEAIKLLMKHGAIP----------------DVKYPDI- 68
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 422 gRTCLHAAASGGNVECLNLLLSSGA---DLRRRDkfGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAAS 498
Cdd:PHA02875 69 -ESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMM 145
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1034579110 499 DTYRRaephtpsshdaeedeplkesrrkeaffcLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFN 574
Cdd:PHA02875 146 GDIKG----------------------------IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
270-343 |
1.32e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411980 [Multi-domain] Cd Length: 649 Bit Score: 45.95 E-value: 1.32e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 270 KGFTPLHVAAVSTNGALcLELLVNNGADVN-------YQSKEGKS-------PLHMAAIHGRFTRSQILIQN---GSEID 332
Cdd:cd22196 93 KGQTALHIAIERRNMHL-VELLVQNGADVHarasgefFKKKKGGPgfyfgelPLSLAACTNQLDIVKFLLENphsPADIS 171
|
90
....*....|.
gi 1034579110 333 CADKFGNTPLH 343
Cdd:cd22196 172 ARDSMGNTVLH 182
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
446-495 |
1.37e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.79 E-value: 1.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|
gi 1034579110 446 ADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYA 495
Cdd:pfam13857 7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
213-313 |
1.40e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 46.04 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 213 AASGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGALcLELLV 292
Cdd:PTZ00322 90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV-VQLLS 168
|
90 100 110
....*....|....*....|....*....|....
gi 1034579110 293 -------NNGADVNYQSKEGK------SPLHMAA 313
Cdd:PTZ00322 169 rhsqchfELGANAKPDSFTGKppsledSPISSHH 202
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
686-715 |
1.47e-04 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 39.88 E-value: 1.47e-04
10 20 30
....*....|....*....|....*....|
gi 1034579110 686 YGQTPLMLAIMNGHVDCVHLLLEKGSTADA 715
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
310-398 |
1.59e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 45.66 E-value: 1.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 310 HMAAiHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRK 389
Cdd:PTZ00322 88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
|
....*....
gi 1034579110 390 LLSSGQLYS 398
Cdd:PTZ00322 167 LSRHSQCHF 175
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
851-1016 |
1.80e-04 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 45.43 E-value: 1.80e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 851 NSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTAL--MTAAENGQTAAVEFLLYRGKADLTVLDENKNTAL 928
Cdd:PHA02946 66 NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKINNSVDEEGCGPL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 929 hLACSKGHEKCALMILAETQDLGLINATNSAlQMPLHIAARNGLASVVQALLSHGATVLAVDEEGHTPA-LACAPNKDVA 1007
Cdd:PHA02946 146 -LACTDPSERVFKKIMSIGFEARIVDKFGKN-HIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLhIVCSKTVKNV 223
|
....*....
gi 1034579110 1008 DCLALILST 1016
Cdd:PHA02946 224 DIINLLLPS 232
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
139-170 |
2.01e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 39.58 E-value: 2.01e-04
10 20 30
....*....|....*....|....*....|...
gi 1034579110 139 GRSALHHAV-HSGHLETVNLLLNKGASLNVCDK 170
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
189-245 |
2.18e-04 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 45.27 E-value: 2.18e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034579110 189 KLLVARGADLGCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIA 245
Cdd:PTZ00322 99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
876-931 |
2.59e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 40.02 E-value: 2.59e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*..
gi 1034579110 876 LLQH-QAEVNATDHTGRTALMTAAENGQTAAVEFLLYRGkADLTVLDENKNTALHLA 931
Cdd:pfam13857 1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTALDLA 56
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
925-980 |
2.72e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 39.57 E-value: 2.72e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034579110 925 NTALHLACSKGHEKCALMILAETQDlglINATNSALQMPLHIAARNGLASVVQALL 980
Cdd:pfam13637 2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
42-161 |
2.88e-04 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.
Pssm-ID: 411976 [Multi-domain] Cd Length: 609 Bit Score: 45.00 E-value: 2.88e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 42 TPLHAAAYVGDVPILQLLLMSGANVN---AKDTLWLT-----------PLHRAAASRNEKVLGLLLAHSADVNARDKLWQ 107
Cdd:cd22192 91 TALHIAVVNQNLNLVRELIARGADVVsprATGTFFRPgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034579110 108 TPLHVAAANRATKCAEALAPLLSSLNVADRS----------GRSALHHAVHSGHLETVNLLLNK 161
Cdd:cd22192 171 TVLHILVLQPNKTFACQMYDLILSYDKEDDLqpldlvpnnqGLTPFKLAAKEGNIVMFQHLVQK 234
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
41-70 |
3.23e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 38.81 E-value: 3.23e-04
10 20 30
....*....|....*....|....*....|.
gi 1034579110 41 RTPLHAAAY-VGDVPILQLLLMSGANVNAKD 70
Cdd:pfam00023 3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
23-177 |
3.50e-04 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 44.27 E-value: 3.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 23 LPRAHTPcsflPSQDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKV--LGLLLAHSADV- 99
Cdd:PHA02946 59 LHRGYSP----NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAKIn 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 100 NARDKLWQTPLhVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGH--LETVNLLLNKGASLNVCDKKERQPLH 177
Cdd:PHA02946 135 NSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHDGNTPLH 213
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
157-212 |
3.73e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 39.25 E-value: 3.73e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*.
gi 1034579110 157 LLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLGCKDRKGYGLLHTA 212
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02946 |
PHA02946 |
ankyin-like protein; Provisional |
155-357 |
3.98e-04 |
|
ankyin-like protein; Provisional
Pssm-ID: 165256 [Multi-domain] Cd Length: 446 Bit Score: 44.27 E-value: 3.98e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 155 VNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLGCKDRKGYGLLHTAAASGQ--IEVVKYLLRMGAEID 232
Cdd:PHA02946 55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKIN 134
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 233 EPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTN-GALCLELLVNNGADVNYQSKEGKSPLHM 311
Cdd:PHA02946 135 NSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpKASTISWMMKLGISPSKPDHDGNTPLHI 214
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1034579110 312 AAIHGRFTRSQI-LIQNGSEIDCADKFGNTPLhvaaryghELLISTL 357
Cdd:PHA02946 215 VCSKTVKNVDIInLLLPSTDVNKQNKFGDSPL--------TLLIKTL 253
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
422-448 |
4.07e-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: 4.07e-04
|
| TRPV5-6 |
cd22192 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ... |
859-1030 |
5.23e-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: 43.85 E-value: 5.23e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 859 TPLHAAAFADNVSGL-RMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFL---------------LYRGKadltvlde 922
Cdd:cd22192 19 SPLLLAAKENDVQAIkKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLmeaapelvnepmtsdLYQGE-------- 90
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 923 nknTALHLACSKGHEKCALMILAETQDLGLINATNSAL-----------QMPLHIAARNGLASVVQALLSHGATVLAVDE 991
Cdd:cd22192 91 ---TALHIAVVNQNLNLVRELIARGADVVSPRATGTFFrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDS 167
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|.
gi 1034579110 992 EGHTP--ALACAPNKDVAdCLA--LILSTMKP--------FPPKDAVSPFS 1030
Cdd:cd22192 168 LGNTVlhILVLQPNKTFA-CQMydLILSYDKEddlqpldlVPNNQGLTPFK 217
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
617-671 |
5.36e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.79 E-value: 5.36e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1034579110 617 GRTALFLATERGSTECVEVLTAHGASALIKERkRKWTPLHAAAASGHTDSLHLLI 671
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
26-80 |
5.37e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.87 E-value: 5.37e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1034579110 26 AHTPCSfLPSQDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRA 80
Cdd:pfam13857 3 EHGPID-LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| PHA02989 |
PHA02989 |
ankyrin repeat protein; Provisional |
218-495 |
6.94e-04 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 222954 [Multi-domain] Cd Length: 494 Bit Score: 43.58 E-value: 6.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 218 IEVVKYLLRMGAEIDEPNAfGNTALHIacYLGQDAVAIE----LVNAGANVNQpndKGF--TPLhvAAVSTNGALC---- 287
Cdd:PHA02989 16 KNALEFLLRTGFDVNEEYR-GNSILLL--YLKRKDVKIKivklLIDNGADVNY---KGYieTPL--CAVLRNREITsnki 87
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 288 ---LELLVNNGADVNYQSKEGKSPLhMAAIHGrftrsqiliqngSEIDCADkfgntplhvaaryghelLISTLMTNGADT 364
Cdd:PHA02989 88 kkiVKLLLKFGADINLKTFNGVSPI-VCFIYN------------SNINNCD-----------------MLRFLLSKGINV 137
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 365 ARRGIHDMFPLHLAVLFGFS---DCCRKLLSSG-------QLY-------------SIVSSLSNEHVLSAGFDINTPDNL 421
Cdd:PHA02989 138 NDVKNSRGYNLLHMYLESFSvkkDVIKILLSFGvnlfektSLYgltpmniylrndiDVISIKVIKYLIKKGVNIETNNNG 217
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 422 GRTCL------HAAASGGNVECLNLLLSSgADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYA 495
Cdd:PHA02989 218 SESVLesfldnNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
422-453 |
7.98e-04 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 38.04 E-value: 7.98e-04
10 20 30
....*....|....*....|....*....|...
gi 1034579110 422 GRTCLHAAA-SGGNVECLNLLLSSGADLRRRDK 453
Cdd:pfam00023 2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
949-996 |
8.53e-04 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 38.48 E-value: 8.53e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*...
gi 1034579110 949 DLGLINATNSALQMPLHIAARNGLASVVQALLSHGATVLAVDEEGHTP 996
Cdd:pfam13857 5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
686-715 |
1.11e-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: 37.24 E-value: 1.11e-03
10 20 30
....*....|....*....|....*....|
gi 1034579110 686 YGQTPLMLAIMNGHVDCVHLLLEKGSTADA 715
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
824-877 |
1.13e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 38.02 E-value: 1.13e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1034579110 824 TPLHCAVINNQDSTTEMLLgALGAKIvNSRDAKGRTPLHAAAFADNVSGLRMLL 877
Cdd:pfam13637 3 TALHAAAASGHLELLRLLL-EKGADI-NAVDGNGETALHFAASNGNVEVLKLLL 54
|
|
| TRPV1-4 |
cd22193 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ... |
270-343 |
1.72e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411977 [Multi-domain] Cd Length: 607 Bit Score: 42.48 E-value: 1.72e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 270 KGFTPLHVAAVSTNGAlCLELLVNNGADVNYQSKE--------------GKSPLHMAAIHGRFTRSQILIQNG---SEID 332
Cdd:cd22193 75 EGQTALHIAIERRQGD-IVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEhqpADIE 153
|
90
....*....|.
gi 1034579110 333 CADKFGNTPLH 343
Cdd:cd22193 154 AQDSRGNTVLH 164
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
961-1028 |
1.94e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 42.19 E-value: 1.94e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034579110 961 QMPLHIAARNGLASVVQALLSHGATVLAVDEEGHTPaLACAPNKDVADCLALILSTMKPFPPKDAVSP 1028
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP-LELAEENGFREVVQLLSRHSQCHFELGANAK 182
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
139-167 |
1.94e-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: 36.85 E-value: 1.94e-03
10 20
....*....|....*....|....*....
gi 1034579110 139 GRSALHHAVHSGHLETVNLLLNKGASLNV 167
Cdd:pfam13606 2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
686-717 |
2.01e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.88 E-value: 2.01e-03
10 20 30
....*....|....*....|....*....|...
gi 1034579110 686 YGQTPLMLAI-MNGHVDCVHLLLEKGSTADAAD 717
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
238-292 |
2.15e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.25 E-value: 2.15e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1034579110 238 GNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGAlCLELLV 292
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
455-505 |
2.19e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 37.25 E-value: 2.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|.
gi 1034579110 455 GRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAASDTYRRAE 505
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
909-967 |
2.19e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 37.33 E-value: 2.19e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*....
gi 1034579110 909 LLYRGKADLTVLDENKNTALHLACSKGHEKCALMILAETQDlglINATNSALQMPLHIA 967
Cdd:pfam13857 1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD---LNLKDEEGLTALDLA 56
|
|
| trp |
TIGR00870 |
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ... |
802-931 |
2.21e-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: 41.99 E-value: 2.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 802 HEDCLELLLEHSPFSYLEGnpfTPLHCAVINNQDSTTEMLL-------GALGAKIVNSRDA----KGRTPLHAAAFADNV 870
Cdd:TIGR00870 65 NLELTELLLNLSCRGAVGD---TLLHAISLEYVDAVEAILLhllaafrKSGPLELANDQYTseftPGITALHLAAHRQNY 141
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034579110 871 SGLRMLLQHQAEVNA---------TDHT-----GRTALMTAAENGQTAAVEFLLYRGkADLTVLDENKNTALHLA 931
Cdd:TIGR00870 142 EIVKLLLERGASVPAracgdffvkSQGVdsfyhGESPLNAAACLGSPSIVALLSEDP-ADILTADSLGNTLLHLL 215
|
|
| Ank_3 |
pfam13606 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
204-233 |
2.30e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.
Pssm-ID: 463933 [Multi-domain] Cd Length: 30 Bit Score: 36.47 E-value: 2.30e-03
10 20 30
....*....|....*....|....*....|
gi 1034579110 204 KGYGLLHTAAASGQIEVVKYLLRMGAEIDE 233
Cdd:pfam13606 1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
455-483 |
3.47e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 36.03 E-value: 3.47e-03
10 20
....*....|....*....|....*....
gi 1034579110 455 GRTPLHYAAANGSYQCAVTLVTAGAGVNE 483
Cdd:smart00248 2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
35-96 |
3.49e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 41.42 E-value: 3.49e-03
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034579110 35 SQDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHS 96
Cdd:PTZ00322 110 CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHS 171
|
|
| Ank_4 |
pfam13637 |
Ankyrin repeats (many copies); |
549-603 |
3.62e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 372654 [Multi-domain] Cd Length: 54 Bit Score: 36.48 E-value: 3.62e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1034579110 549 GYTAVHYAAAYGNRQNLELLLEMSFNCLEDVESTIPvsPLHLAAYNGHCEALKTL 603
Cdd:pfam13637 1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGET--ALHFAASNGNVEVLKLL 53
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
856-888 |
3.85e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 36.11 E-value: 3.85e-03
10 20 30
....*....|....*....|....*....|....
gi 1034579110 856 KGRTPLHAAA-FADNVSGLRMLLQHQAEVNATDH 888
Cdd:pfam00023 1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| PHA02884 |
PHA02884 |
ankyrin repeat protein; Provisional |
208-312 |
4.03e-03 |
|
ankyrin repeat protein; Provisional
Pssm-ID: 165212 [Multi-domain] Cd Length: 300 Bit Score: 40.74 E-value: 4.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 208 LLHTAAASGQIEVVKYLLRMGAEIDEP-----NAFGNTALHIACYLGQDAvAIELVNAGANVNQ-PNDKGFTPLHVAAVS 281
Cdd:PHA02884 36 ILYSSIKFHYTDIIDAILKLGADPEAPfplseNSKTNPLIYAIDCDNDDA-AKLLIRYGADVNRyAEEAKITPLYISVLH 114
|
90 100 110
....*....|....*....|....*....|.
gi 1034579110 282 TNGAlCLELLVNNGADVNYQSKEGKSPLHMA 312
Cdd:PHA02884 115 GCLK-CLEILLSYGADINIQTNDMVTPIELA 144
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
557-639 |
4.10e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 41.04 E-value: 4.10e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 557 AAYGNRQNLELLLE--MSFNCLEDVESTipvsPLHLAAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVE 634
Cdd:PTZ00322 90 AASGDAVGARILLTggADPNCRDYDGRT----PLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165
|
....*
gi 1034579110 635 VLTAH 639
Cdd:PTZ00322 166 LLSRH 170
|
|
| PTZ00322 |
PTZ00322 |
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional |
653-707 |
4.14e-03 |
|
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
Pssm-ID: 140343 [Multi-domain] Cd Length: 664 Bit Score: 41.04 E-value: 4.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*
gi 1034579110 653 TPLHAAAASGHTDSLHLLIDSGerADITdVMDAYGQTPLMLAIMNGHVDCVHLLL 707
Cdd:PTZ00322 117 TPLHIACANGHVQVVRVLLEFG--ADPT-LLDKDGKTPLELAEENGFREVVQLLS 168
|
|
| TRPV1 |
cd22196 |
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ... |
608-725 |
4.38e-03 |
|
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.
Pssm-ID: 411980 [Multi-domain] Cd Length: 649 Bit Score: 40.94 E-value: 4.38e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 608 VNLDVRD--HKGRTALFLATERGSTECVEVLTAHGASalikerkrkwtpLHAAAasghtdslhllidSGERADITDVMDA 685
Cdd:cd22196 83 VNAAYTDsyYKGQTALHIAIERRNMHLVELLVQNGAD------------VHARA-------------SGEFFKKKKGGPG 137
|
90 100 110 120
....*....|....*....|....*....|....*....|....*
gi 1034579110 686 --YGQTPLMLAIMNGHVDCVHLLLE---KGSTADAADLRGRTALH 725
Cdd:cd22196 138 fyFGELPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLH 182
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
790-814 |
4.44e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.64 E-value: 4.44e-03
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
41-68 |
4.66e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 35.64 E-value: 4.66e-03
|
| PHA02791 |
PHA02791 |
ankyrin-like protein; Provisional |
39-166 |
5.03e-03 |
|
ankyrin-like protein; Provisional
Pssm-ID: 165154 [Multi-domain] Cd Length: 284 Bit Score: 40.03 E-value: 5.03e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034579110 39 ERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVNARDKL-WQTPL-HVAAAN 116
Cdd:PHA02791 60 ENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTgWKTSFyHAVMLN 139
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|
gi 1034579110 117 RATKCAEALAPLLSSLNVADRsgRSALHHAVHSGHLETVNLLLNKGASLN 166
Cdd:PHA02791 140 DVSIVSYFLSEIPSTFDLAIL--LSCIHITIKNGHVDMMILLLDYMTSTN 187
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
131-179 |
5.07e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 36.17 E-value: 5.07e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*....
gi 1034579110 131 SLNVADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWA 179
Cdd:pfam13857 8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
175-203 |
5.44e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 35.34 E-value: 5.44e-03
10 20 30
....*....|....*....|....*....|
gi 1034579110 175 PLHWAA-FLGHLEVLKLLVARGADLGCKDR 203
Cdd:pfam00023 5 PLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
75-104 |
6.43e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 35.34 E-value: 6.43e-03
10 20 30
....*....|....*....|....*....|.
gi 1034579110 75 TPLHRAAASR-NEKVLGLLLAHSADVNARDK 104
Cdd:pfam00023 4 TPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
|
|
| Ank_5 |
pfam13857 |
Ankyrin repeats (many copies); |
234-278 |
7.16e-03 |
|
Ankyrin repeats (many copies);
Pssm-ID: 433530 [Multi-domain] Cd Length: 56 Bit Score: 35.79 E-value: 7.16e-03
10 20 30 40
....*....|....*....|....*....|....*....|....*
gi 1034579110 234 PNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVA 278
Cdd:pfam13857 12 LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
|
|
| Ank |
pfam00023 |
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ... |
238-269 |
8.06e-03 |
|
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.
Pssm-ID: 459634 [Multi-domain] Cd Length: 34 Bit Score: 34.96 E-value: 8.06e-03
10 20 30
....*....|....*....|....*....|...
gi 1034579110 238 GNTALHIACY-LGQDAVAIELVNAGANVNQPND 269
Cdd:pfam00023 2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
338-363 |
8.33e-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: 8.33e-03
|
| Ank_2 |
pfam12796 |
Ankyrin repeats (3 copies); |
964-1017 |
8.68e-03 |
|
Ankyrin repeats (3 copies);
Pssm-ID: 463710 [Multi-domain] Cd Length: 91 Bit Score: 36.63 E-value: 8.68e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1034579110 964 LHIAARNGLASVVQALLSHGATVLAVDEEGHTPALACApNKDVADCLALILSTM 1017
Cdd:pfam12796 1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAA-KNGHLEIVKLLLEHA 53
|
|
| PHA02736 |
PHA02736 |
Viral ankyrin protein; Provisional |
422-471 |
9.14e-03 |
|
Viral ankyrin protein; Provisional
Pssm-ID: 165103 [Multi-domain] Cd Length: 154 Bit Score: 37.93 E-value: 9.14e-03
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....
gi 1034579110 422 GRTCLHAAASGGNV---ECLNLLLSSGADLRRRD-KFGRTPLHYAAANGSYQCA 471
Cdd:PHA02736 55 GKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKErVFGNTPLHIAVYTQNYELA 108
|
|
| ANK |
smart00248 |
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ... |
856-885 |
9.28e-03 |
|
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.
Pssm-ID: 197603 [Multi-domain] Cd Length: 30 Bit Score: 34.87 E-value: 9.28e-03
10 20 30
....*....|....*....|....*....|
gi 1034579110 856 KGRTPLHAAAFADNVSGLRMLLQHQAEVNA 885
Cdd:smart00248 1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
|
|
| |
