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Conserved domains on  [gi|300798249|ref|NP_001178804|]
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serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit C [Rattus norvegicus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-343 1.56e-47

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.68  E-value: 1.56e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   56 ILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNV 135
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  136 ADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAA 215
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  216 SGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGALcLELLVNN 295
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLLEA 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 300798249  296 GADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPL 343
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
289-622 1.01e-32

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.92  E-value: 1.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  289 LELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADTARR 368
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  369 GIHDMFPLHLAVLFGFSDCCRKLLSsgqlysivsslsnehvlsAGFDINTPDSLGRTCLHAAASGGNVECLNLLLSSGAD 448
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLE------------------AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  449 LRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAASDtyrraephtasshdaeedellkesrRKE 528
Cdd:COG0666   146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG-------------------------HLE 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  529 AffcLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNclEDVESTVPVSPLHLAAYNGHCEALKTLAETL 608
Cdd:COG0666   201 I---VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD--LNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
                         330
                  ....*....|....
gi 300798249  609 VNLDVRDHKGRTAL 622
Cdd:COG0666   276 LLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
668-998 1.29e-32

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.53  E-value: 1.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  668 LHLLIDSGERADITDVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFV 747
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  748 LCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDpldaGVDYSGYSPMHWASYTGHEDCLELLLEHspfsylegnpftpl 827
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN----ARDKDGETPLHLAAYNGNLEIVKLLLEA-------------- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  828 hcavinnqdsttemllgalGAKvVNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAV 907
Cdd:COG0666   143 -------------------GAD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  908 EFLLYRGkADLTVLDENKNTALHLACSKGHEKCALMILAEtqdLGLINATNSALQMPLHIAARNGLASVVQALLSRGATV 987
Cdd:COG0666   203 KLLLEAG-ADVNAKDNDGKTALDLAAENGNLEIVKLLLEA---GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
                         330
                  ....*....|.
gi 300798249  988 LAVDEEGHTPA 998
Cdd:COG0666   279 AAALLDLLTLL 289
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 2.81e-05

Ankyrin repeats (many copies);


:

Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 2.81e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 300798249    10 PPLVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLL 61
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
618-672 5.92e-04

Ankyrin repeats (many copies);


:

Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 5.92e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 300798249   618 GRTALFLATERGSTECVEVLTAHGASALIKERkRKWTPLHAAAASGHTDSLHLLI 672
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-343 1.56e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.68  E-value: 1.56e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   56 ILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNV 135
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  136 ADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAA 215
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  216 SGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGALcLELLVNN 295
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLLEA 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 300798249  296 GADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPL 343
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
20-317 1.11e-37

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 148.25  E-value: 1.11e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   20 DVEEVRSLLSQKENINVLDQERRTPLHA--AAYVGDVP-ILQLLLMSGANVNAKDTLWLTPLHRAAASRN-EKVLGLLLA 95
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLylHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   96 HSADVNARDKLWQTPLHVAaanratkcaealaplLSSLNVadrsgrsalhhavhsgHLETVNLLLNKGASLNVCDKKERQ 175
Cdd:PHA03095  106 AGADVNAKDKVGRTPLHVY---------------LSGFNI----------------NPKVIRLLLRKGADVNALDLYGMT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  176 PLHwaAFLGH----LEVLKLLVARGADLSCKDRKGYGLLHTAAASGQI--EVVKYLLRMGAEIDEPNAFGNTALHIACYL 249
Cdd:PHA03095  155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATG 232
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  250 G--QDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGALCLELLvNNGADVNYQSKEGKSPLHMAAIHG 317
Cdd:PHA03095  233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGNTPLSLMVRNN 301
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
289-622 1.01e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.92  E-value: 1.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  289 LELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADTARR 368
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  369 GIHDMFPLHLAVLFGFSDCCRKLLSsgqlysivsslsnehvlsAGFDINTPDSLGRTCLHAAASGGNVECLNLLLSSGAD 448
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLE------------------AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  449 LRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAASDtyrraephtasshdaeedellkesrRKE 528
Cdd:COG0666   146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG-------------------------HLE 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  529 AffcLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNclEDVESTVPVSPLHLAAYNGHCEALKTLAETL 608
Cdd:COG0666   201 I---VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD--LNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
                         330
                  ....*....|....
gi 300798249  609 VNLDVRDHKGRTAL 622
Cdd:COG0666   276 LLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
668-998 1.29e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.53  E-value: 1.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  668 LHLLIDSGERADITDVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFV 747
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  748 LCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDpldaGVDYSGYSPMHWASYTGHEDCLELLLEHspfsylegnpftpl 827
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN----ARDKDGETPLHLAAYNGNLEIVKLLLEA-------------- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  828 hcavinnqdsttemllgalGAKvVNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAV 907
Cdd:COG0666   143 -------------------GAD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  908 EFLLYRGkADLTVLDENKNTALHLACSKGHEKCALMILAEtqdLGLINATNSALQMPLHIAARNGLASVVQALLSRGATV 987
Cdd:COG0666   203 KLLLEAG-ADVNAKDNDGKTALDLAAENGNLEIVKLLLEA---GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
                         330
                  ....*....|.
gi 300798249  988 LAVDEEGHTPA 998
Cdd:COG0666   279 AAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
219-660 1.26e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 114.74  E-value: 1.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  219 IEVVKYLLRMGAEIDEPNAFGNTALH--IACYLGQDAVAIE-LVNAGANVNQPNDKGFTPLHVAAVSTNGALCLELLVNN 295
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKDIVRlLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  296 GADVNYQskegksplhmaaihgrftrsqiliqngseidcaDKFGNTPLHVaaryghellistlmtngadtarrgihdmfp 375
Cdd:PHA03095  107 GADVNAK---------------------------------DKVGRTPLHV------------------------------ 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  376 lHLAvlfgfSDCCRkllssgqlYSIVSSLsnehvLSAGFDINTPDSLGRTCLHA--AASGGNVECLNLLLSSGADLRRRD 453
Cdd:PHA03095  124 -YLS-----GFNIN--------PKVIRLL-----LRKGADVNALDLYGMTPLAVllKSRNANVELLRLLIDAGADVYAVD 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  454 KFGRTPLHYAAAN--GSYQCAVTLVTAGAGVNEADCKGCSPLHYAAASDTYRRAEphtasshdaeedellkesrrkeaff 531
Cdd:PHA03095  185 DRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSL------------------------- 239
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  532 cLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNCleDVESTVPVSPLHLAAYNGH----------CEAL 601
Cdd:PHA03095  240 -VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADI--NAVSSDGNTPLSLMVRNNNgravraalakNPSA 316
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 300798249  602 KTLAETLVNLDVRDHKGRTAlflaterGSTECVEVLTAHGASALIKERKRKwtpLHAAA 660
Cdd:PHA03095  317 ETVAATLNTASVAGGDIPSD-------ATRLCVAKVVLRGAFSLLPEPIRA---YHADF 365
PHA02876 PHA02876
ankyrin repeat protein; Provisional
604-985 1.05e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 94.74  E-value: 1.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  604 LAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKERKrKWTPLHAAAASGHTDSLHLLIDSGERADITDV 683
Cdd:PHA02876  164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD-DLSVLECAVDSKNIDTIKAIIDNRSNINKNDL 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  684 mdaygqtPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVT-GCEDCLAALLDHDAFVLCRDFKGRTPIHLAS 762
Cdd:PHA02876  243 -------SLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMA 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  763 ACGH-TAVLRTLLQAalstdpldaGVDYSGYSPMHwasytghedclelllehspfsylegnpFTPLHCAVINNQDSTTEM 841
Cdd:PHA02876  316 KNGYdTENIRTLIML---------GADVNAADRLY---------------------------ITPLHQASTLDRNKDIVI 359
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  842 LLGALGAKVvNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTA--AENGQTaAVEFLLYRGkADLT 919
Cdd:PHA02876  360 TLLELGANV-NARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlcGTNPYM-SVKTLIDRG-ANVN 436
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300798249  920 VLDENKNTALHLACSKgheKCALMILAETQDLGL-INATNSALQMPLHIAArnGLASVVQALLSRGA 985
Cdd:PHA02876  437 SKNKDLSTPLHYACKK---NCKLDVIEMLLDNGAdVNAINIQNQYPLLIAL--EYHGIVNILLHYGA 498
Ank_2 pfam12796
Ankyrin repeats (3 copies);
589-682 3.08e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 3.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   589 LHLAAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHgasALIKERKRKWTPLHAAAASGHTDSL 668
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 300798249   669 HLLIDSGERADITD 682
Cdd:pfam12796   78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
656-751 6.11e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.69  E-value: 6.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   656 LHAAAASGHTDSLHLLIDSGERADitdVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADaaDLRGRTALHRGAVTGCED 735
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADAN---LQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLE 75
                           90
                   ....*....|....*.
gi 300798249   736 CLAALLDHDAFVLCRD 751
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
376-486 1.33e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 1.33e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   376 LHLAVLFGFSDCCRKLLSSGqlysivsslsnehvlsagFDINTPDSLGRTCLHAAASGGNVECLNLLLSSgADLRRRDKf 455
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG------------------ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN- 60
                           90       100       110
                   ....*....|....*....|....*....|.
gi 300798249   456 GRTPLHYAAANGSYQCAVTLVTAGAGVNEAD 486
Cdd:pfam12796   61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
74-284 2.79e-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: 77.36  E-value: 2.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   74 WLTPLHRAAASRN-EKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEAL---APLLssLNVADRS----GRSALH 145
Cdd:cd22192    17 SESPLLLAAKENDvQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLmeaAPEL--VNEPMTSdlyqGETALH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  146 HAVHSGHLETVNLLLNKGASL---------------NVCDKKErQPLHWAAFLGHLEVLKLLVARGADLSCKDRkgygll 210
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVvspratgtffrpgpkNLIYYGE-HPLSFAACVGNEEIVRLLIEHGADIRAQDS------ 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  211 htaaasgqievvkyllrmgaeidepnaFGNTALHI---------ACYL---------GQDAVAIELVnaganvnqPNDKG 272
Cdd:cd22192   168 ---------------------------LGNTVLHIlvlqpnktfACQMydlilsydkEDDLQPLDLV--------PNNQG 212
                         250
                  ....*....|..
gi 300798249  273 FTPLHVAAVSTN 284
Cdd:cd22192   213 LTPFKLAAKEGN 224
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
48-284 8.31e-14

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 75.89  E-value: 8.31e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249    48 AAYVGDVPILQLLLMSGA--NVNAKDTLWLTPLHRAAA-SRNEKVLGLLLAHSADVNARDKLwqtpLHVAAANRATKCAE 124
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGDTL----LHAISLEYVDAVEA 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   125 ALAPLL-------SSLNVADRS------GRSALHHAVHSGHLETVNLLLNKGASLNV------CDKKERQ--------PL 177
Cdd:TIGR00870  100 ILLHLLaafrksgPLELANDQYtseftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVdsfyhgesPL 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   178 HWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHtaaasgqievvkyLLRMGAEidepNAFGNTALHIACY------LGQ 251
Cdd:TIGR00870  180 NAAACLGSPSIVALLSEDPADILTADSLGNTLLH-------------LLVMENE----FKAEYEELSCQMYnfalslLDK 242
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 300798249   252 --DAVAIELVnaganvnqPNDKGFTPLHVAAVSTN 284
Cdd:TIGR00870  243 lrDSKELEVI--------LNHQGLTPLKLAAKEGR 269
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
274-461 1.03e-10

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 65.80  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  274 TPLHVAAvSTNGALCLE-LLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSE-----IDCADKFGNTPLHVAA 347
Cdd:cd22192    19 SPLLLAA-KENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  348 RYGHELLISTLMTNGADTA---------RRGIHDMFplhlavLFGfsdccrkllssgqlysivsslsnEHVLSagFdint 418
Cdd:cd22192    98 VNQNLNLVRELIARGADVVspratgtffRPGPKNLI------YYG-----------------------EHPLS--F---- 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 300798249  419 pdslgrtclhaAASGGNVECLNLLLSSGADLRRRDKFGRTPLH 461
Cdd:cd22192   143 -----------AACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
587-760 2.53e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 54.63  E-value: 2.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  587 SPLHLAAYNGHCEALKTLAETlvnldvrdhkGRTALFlatERGstecvevltAHGASALikerkrkwtplHAAAASGHTD 666
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKC----------PSCDLF---QRG---------ALGETAL-----------HVAALYDNLE 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  667 SLHLLIDSGERAdITDVM--DAY-GQTPLMLAIMNGHVDCVHLLLEKGstADAADLR----------------GRTALHR 727
Cdd:cd22192    66 AAVVLMEAAPEL-VNEPMtsDLYqGETALHIAVVNQNLNLVRELIARG--ADVVSPRatgtffrpgpknliyyGEHPLSF 142
                         170       180       190
                  ....*....|....*....|....*....|...
gi 300798249  728 GAVTGCEDCLAALLDHDAFVLCRDFKGRTPIHL 760
Cdd:cd22192   143 AACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
682-879 6.56e-07

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 53.55  E-value: 6.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   682 DVMDAYGQTPLM-LAIMNGHVDCVHLLLEKGSTADAadlrGRTALH---RGAVTGCEDCLAALLDHD----------AFV 747
Cdd:TIGR00870   46 NCPDRLGRSALFvAAIENENLELTELLLNLSCRGAV----GDTLLHaisLEYVDAVEAILLHLLAAFrksgplelanDQY 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   748 LCRDFKGRTPIHLASACGHTAVLRTLLQAALSTdPLDAGVD-----------YSGYSPMHWASYTGHEDCLELLLEHsPF 816
Cdd:TIGR00870  122 TSEFTPGITALHLAAHRQNYEIVKLLLERGASV-PARACGDffvksqgvdsfYHGESPLNAAACLGSPSIVALLSED-PA 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   817 SYLE----GNpfTPLHCAVINNQDST--TEM------LLGALGAKVVNSRDA------KGRTPLHAAAFADNVSGLRMLL 878
Cdd:TIGR00870  200 DILTadslGN--TLLHLLVMENEFKAeyEELscqmynFALSLLDKLRDSKELevilnhQGLTPLKLAAKEGRIVLFRLKL 277

                   .
gi 300798249   879 Q 879
Cdd:TIGR00870  278 A 278
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 2.81e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 2.81e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 300798249    10 PPLVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLL 61
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
330-594 3.75e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.77  E-value: 3.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   330 SEIDCADKFGNTPLHVAARYG-HELLISTLMTNGA-----DTArrgihdmfpLHLAVLfGFSDCCRKLLSSgQLYSIVSS 403
Cdd:TIGR00870   43 LNINCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISL-EYVDAVEAILLH-LLAAFRKS 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   404 LSNEHVLSAGFDINTPDslgRTCLHAAASGGNVECLNLLLSSGADLRRRDK--------------FGRTPLHYAAANGSY 469
Cdd:TIGR00870  112 GPLELANDQYTSEFTPG---ITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSP 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   470 QCAVTLVTAGAGVNEADCKGCSPLHyAAASDTYRRAEPHTASSHdaeedellkesrrkeaffCLEFLLDNGA--DPSL-- 545
Cdd:TIGR00870  189 SIVALLSEDPADILTADSLGNTLLH-LLVMENEFKAEYEELSCQ------------------MYNFALSLLDklRDSKel 249
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 300798249   546 ---RDRQGYTAVHYAAAYGNRQNLELLLEMSFNCLEDVEStvPVSPLHLAAY 594
Cdd:TIGR00870  250 eviLNHQGLTPLKLAAKEGRIVLFRLKLAIKYKQKKFVAW--PNGQQLLSLY 299
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
12-97 4.88e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 4.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   12 LVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLG 91
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                  ....*.
gi 300798249   92 LLLAHS 97
Cdd:PTZ00322  166 LLSRHS 171
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
140-168 6.37e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.03  E-value: 6.37e-05
                            10        20
                    ....*....|....*....|....*....
gi 300798249    140 GRSALHHAVHSGHLETVNLLLNKGASLNV 168
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
687-716 1.77e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 1.77e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 300798249    687 YGQTPLMLAIMNGHVDCVHLLLEKGSTADA 716
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
423-449 4.68e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 4.68e-04
                            10        20
                    ....*....|....*....|....*..
gi 300798249    423 GRTCLHAAASGGNVECLNLLLSSGADL 449
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_4 pfam13637
Ankyrin repeats (many copies);
618-672 5.92e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 5.92e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 300798249   618 GRTALFLATERGSTECVEVLTAHGASALIKERkRKWTPLHAAAASGHTDSLHLLI 672
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
42-69 5.35e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 5.35e-03
                            10        20
                    ....*....|....*....|....*...
gi 300798249     42 RTPLHAAAYVGDVPILQLLLMSGANVNA 69
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-343 1.56e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.68  E-value: 1.56e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   56 ILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNV 135
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  136 ADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAA 215
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  216 SGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGALcLELLVNN 295
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLLEA 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 300798249  296 GADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPL 343
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
87-366 3.57e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.82  E-value: 3.57e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   87 EKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLLNKGASL 166
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  167 NVCDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIA 246
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  247 CYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGALcLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILI 326
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI-VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 300798249  327 QNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADTA 366
Cdd:COG0666   240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
21-301 5.52e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 164.36  E-value: 5.52e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   21 VEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADV 100
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  101 NARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWA 180
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  181 AFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVN 260
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 300798249  261 AGANVNQPNDKGFTPLHVAAVSTNGALCLELLVNNGADVNY 301
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
11-276 2.00e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 162.82  E-value: 2.00e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   11 PLVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVL 90
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   91 GLLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCD 170
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  171 KKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLG 250
Cdd:COG0666   184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
                         250       260
                  ....*....|....*....|....*.
gi 300798249  251 QDAVAIELVNAGANVNQPNDKGFTPL 276
Cdd:COG0666   264 AALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-243 3.88e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 3.88e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249    8 DQPPLVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNE 87
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   88 KVLGLLLAHSADVNARDKlwqtplhvaaanratkcaealapllsslnvadrSGRSALHHAVHSGHLETVNLLLNKGASLN 167
Cdd:COG0666   167 EIVKLLLEAGADVNARDN---------------------------------DGETPLHLAAENGHLEIVKLLLEAGADVN 213
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300798249  168 VCDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTAL 243
Cdd:COG0666   214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
20-317 1.11e-37

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 148.25  E-value: 1.11e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   20 DVEEVRSLLSQKENINVLDQERRTPLHA--AAYVGDVP-ILQLLLMSGANVNAKDTLWLTPLHRAAASRN-EKVLGLLLA 95
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLylHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   96 HSADVNARDKLWQTPLHVAaanratkcaealaplLSSLNVadrsgrsalhhavhsgHLETVNLLLNKGASLNVCDKKERQ 175
Cdd:PHA03095  106 AGADVNAKDKVGRTPLHVY---------------LSGFNI----------------NPKVIRLLLRKGADVNALDLYGMT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  176 PLHwaAFLGH----LEVLKLLVARGADLSCKDRKGYGLLHTAAASGQI--EVVKYLLRMGAEIDEPNAFGNTALHIACYL 249
Cdd:PHA03095  155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATG 232
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  250 G--QDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGALCLELLvNNGADVNYQSKEGKSPLHMAAIHG 317
Cdd:PHA03095  233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGNTPLSLMVRNN 301
PHA02876 PHA02876
ankyrin repeat protein; Provisional
56-417 5.55e-37

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 149.44  E-value: 5.55e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   56 ILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVN--ARDKLwqTPLHVAAANRATKCAEALAPLLSSL 133
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNiiALDDL--SVLECAVDSKNIDTIKAIIDNRSNI 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  134 NVADRSgrsaLHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVL-KLLVARGADLSCKDRKGYGLLHT 212
Cdd:PHA02876  238 NKNDLS----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYL 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  213 AAASG-QIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDA-VAIELVNAGANVNQPNDKGFTPLHVAAVStNGALCLE 290
Cdd:PHA02876  314 MAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVR-NNVVIIN 392
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  291 LLVNNGADVNYQSKEGKSPLHMaAIHGR--FTRSQILIQNGSEIDCADKFGNTPLHVAARYGHEL-LISTLMTNGADTAR 367
Cdd:PHA02876  393 TLLDYGADIEALSQKIGTALHF-ALCGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNA 471
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|
gi 300798249  368 RGIHDMFPLHLAVlfGFSDCCRKLLSSGqlysivSSLSNEHVLSAGFDIN 417
Cdd:PHA02876  472 INIQNQYPLLIAL--EYHGIVNILLHYG------AELRDSRVLHKSLNDN 513
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
186-489 1.98e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.70  E-value: 1.98e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  186 LEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANV 265
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  266 NQPNDKGFTPLHvAAVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHV 345
Cdd:COG0666    81 NAKDDGGNTLLH-AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  346 AARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRKLlssgqlysivsslsnehvLSAGFDINTPDSLGRT 425
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL------------------LEAGADVNAKDNDGKT 221
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300798249  426 CLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKG 489
Cdd:COG0666   222 ALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
PHA02874 PHA02874
ankyrin repeat protein; Provisional
16-373 1.48e-33

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 135.09  E-value: 1.48e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   16 IFSRDVEEVRSLLSQKEN-INVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLL 94
Cdd:PHA02874    9 IYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   95 AHSADVNArdklwqtpLHVAAANRatkcaEALAPLLSS---LNVADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDK 171
Cdd:PHA02874   89 DNGVDTSI--------LPIPCIEK-----DMIKTILDCgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  172 KERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQ 251
Cdd:PHA02874  156 NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR 235
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  252 DAVAIELVNAGANVNQPNdkGFTPLHVAAVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAAIH-GRFTRSQILIQNGS 330
Cdd:PHA02874  236 SAIELLINNASINDQDID--GSTPLHHAINPPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKDIIANAV 313
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 300798249  331 EIDCADKFGNTPL--HVaaryghELLISTLMTNGADTARRGIHDM 373
Cdd:PHA02874  314 LIKEADKLKDSDFleHI------EIKDNKEFSDFIKECNEEIEDM 352
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
289-622 1.01e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.92  E-value: 1.01e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  289 LELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADTARR 368
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  369 GIHDMFPLHLAVLFGFSDCCRKLLSsgqlysivsslsnehvlsAGFDINTPDSLGRTCLHAAASGGNVECLNLLLSSGAD 448
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLE------------------AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  449 LRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAASDtyrraephtasshdaeedellkesrRKE 528
Cdd:COG0666   146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG-------------------------HLE 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  529 AffcLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNclEDVESTVPVSPLHLAAYNGHCEALKTLAETL 608
Cdd:COG0666   201 I---VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD--LNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
                         330
                  ....*....|....
gi 300798249  609 VNLDVRDHKGRTAL 622
Cdd:COG0666   276 LLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
668-998 1.29e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.53  E-value: 1.29e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  668 LHLLIDSGERADITDVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFV 747
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  748 LCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDpldaGVDYSGYSPMHWASYTGHEDCLELLLEHspfsylegnpftpl 827
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN----ARDKDGETPLHLAAYNGNLEIVKLLLEA-------------- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  828 hcavinnqdsttemllgalGAKvVNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAV 907
Cdd:COG0666   143 -------------------GAD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  908 EFLLYRGkADLTVLDENKNTALHLACSKGHEKCALMILAEtqdLGLINATNSALQMPLHIAARNGLASVVQALLSRGATV 987
Cdd:COG0666   203 KLLLEAG-ADVNAKDNDGKTALDLAAENGNLEIVKLLLEA---GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
                         330
                  ....*....|.
gi 300798249  988 LAVDEEGHTPA 998
Cdd:COG0666   279 AAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
773-1015 7.64e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.44  E-value: 7.64e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  773 LLQAALSTDPLDAGVDYSGYSPMHWASYTGHEDCLELLLEHSPFSYLEGNPFTPLHCAVINNQDSTTEMLLGALGAkVVN 852
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-DIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  853 SRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLLYRGkADLTVLDENKNTALHLA 932
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  933 CSKGHEKCALMILAETQDlglINATNSALQMPLHIAARNGLASVVQALLSRGATVLAVDEEGHTPALACAPNKDVADCLA 1012
Cdd:COG0666   161 AANGNLEIVKLLLEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237

                  ...
gi 300798249 1013 LIL 1015
Cdd:COG0666   238 LLE 240
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
706-1015 1.82e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 119.29  E-value: 1.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  706 LLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFVLCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDA 785
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  786 GvdysGYSPMHWASYTGHEDCLELLLEHspfsylegnpftplhcavinnqdsttemllgalGAKVvNSRDAKGRTPLHAA 865
Cdd:COG0666    86 G----GNTLLHAAARNGDLEIVKLLLEA---------------------------------GADV-NARDKDGETPLHLA 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  866 AFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLLYRGkADLTVLDENKNTALHLACSKGHEKCALMIL 945
Cdd:COG0666   128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENGHLEIVKLLL 206
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  946 AETQDlglINATNSALQMPLHIAARNGLASVVQALLSRGATVLAVDEEGHTPALACAPNKDVADCLALIL 1015
Cdd:COG0666   207 EAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
588-860 2.92e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.90  E-value: 2.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  588 PLHLAAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGAsALIKERKRKWTPLHAAAASGHTDS 667
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA-DINAKDDGGNTLLHAAARNGDLEI 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  668 LHLLIDSGerADItDVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFV 747
Cdd:COG0666   103 VKLLLEAG--ADV-NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  748 LCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAgvdySGYSPMHWASYTGHEDCLELLLEHSPFSYLEGNPFTPL 827
Cdd:COG0666   180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN----DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
                         250       260       270
                  ....*....|....*....|....*....|...
gi 300798249  828 HCAVINNQDSTTEMLLGALGAKVVNSRDAKGRT 860
Cdd:COG0666   256 LLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
PHA03100 PHA03100
ankyrin repeat protein; Provisional
21-301 1.02e-28

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 120.15  E-value: 1.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   21 VEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLH-----RAAASRNEKVLGLLLA 95
Cdd:PHA03100   15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   96 HSADVNARDKLWQTPLHVAAANratkcaealapllsslnvadrsgrsalhhavHSGHLETVNLLLNKGASLNVCDKKERQ 175
Cdd:PHA03100   95 YGANVNAPDNNGITPLLYAISK-------------------------------KSNSYSIVEYLLDNGANVNIKNSDGEN 143
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  176 PLHWAAFLGH--LEVLKLLVARGADLSCKDRkgygllhtaaasgqievVKYLLRMGAEIDEPNAFGNTALHIACYlgqdA 253
Cdd:PHA03100  144 LLHLYLESNKidLKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVY----N 202
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 300798249  254 VAIELVNA----GANVNQPNDKGFTPLHVAAVSTNGALcLELLVNNGADVNY 301
Cdd:PHA03100  203 NNPEFVKYlldlGANPNLVNKYGDTPLHIAILNNNKEI-FKLLLNNGPSIKT 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
512-758 1.09e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.98  E-value: 1.09e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  512 SHDAEEDELLKESRRKEAFFCLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNCleDVESTVPVSPLHL 591
Cdd:COG0666    49 LADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV--NARDKDGETPLHL 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  592 AAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKERKrKWTPLHAAAASGHTDSLHLL 671
Cdd:COG0666   127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLL 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  672 IDSGerADITDVmDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFVLCRD 751
Cdd:COG0666   206 LEAG--ADVNAK-DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282

                  ....*..
gi 300798249  752 FKGRTPI 758
Cdd:COG0666   283 LDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
656-956 3.95e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.44  E-value: 3.95e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  656 LHAAAASGHTDSLHLLIDSGERADITDVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCED 735
Cdd:COG0666    22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLE 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  736 CLAALLDHDAFVLCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAgvdySGYSPMHWASYTGHEDCLELLLEHsp 815
Cdd:COG0666   102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN----DGNTPLHLAAANGNLEIVKLLLEA-- 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  816 fsylegnpftplhcavinnqdsttemllgalGAKvVNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTAL 895
Cdd:COG0666   176 -------------------------------GAD-VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300798249  896 MTAAENGQTAAVEFLLYRGkADLTVLDENKNTALHLACSKGHEKCALMILAETQDLGLINA 956
Cdd:COG0666   224 DLAAENGNLEIVKLLLEAG-ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
410-725 1.72e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.51  E-value: 1.72e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  410 LSAGFDINTPDSLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKG 489
Cdd:COG0666    41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  490 CSPLHYAAASDtyrraepHTAsshdaeedellkesrrkeaffCLEFLLDNGADPSLRDRQGYTavhyaaaygnrqnlell 569
Cdd:COG0666   121 ETPLHLAAYNG-------NLE---------------------IVKLLLEAGADVNAQDNDGNT----------------- 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  570 lemsfncledvestvpvsPLHLAAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKEr 649
Cdd:COG0666   156 ------------------PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD- 216
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300798249  650 KRKWTPLHAAAASGHTDSLHLLIDSGERADITdvmDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTAL 725
Cdd:COG0666   217 NDGKTALDLAAENGNLEIVKLLLEAGADLNAK---DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
148-493 2.37e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 119.40  E-value: 2.37e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  148 VHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKYLLR 227
Cdd:PHA02876  153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIID 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  228 MGAEIDEP-----NAFGNTALHiacylgqdaVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGALCLELLVNNGADVNYQ 302
Cdd:PHA02876  233 NRSNINKNdlsllKAIRNEDLE---------TSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAK 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  303 SKEGKSPLHMAAIHGRFTRS-QILIQNGSEIDCADKFGNTPLHVAARYG-HELLISTLMTNGADTARRGIHDMFPLHLAV 380
Cdd:PHA02876  304 NIKGETPLYLMAKNGYDTENiRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAA 383
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  381 LfgfsdccrkllssGQLYSIVSSLsnehvLSAGFDINTPDSLGRTCLHAAASGGN-VECLNLLLSSGADLRRRDKFGRTP 459
Cdd:PHA02876  384 V-------------RNNVVIINTL-----LDYGADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTP 445
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 300798249  460 LHYAAANG-SYQCAVTLVTAGAGVNEADCKGCSPL 493
Cdd:PHA02876  446 LHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPL 480
PHA03095 PHA03095
ankyrin-like protein; Provisional
219-660 1.26e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 114.74  E-value: 1.26e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  219 IEVVKYLLRMGAEIDEPNAFGNTALH--IACYLGQDAVAIE-LVNAGANVNQPNDKGFTPLHVAAVSTNGALCLELLVNN 295
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKDIVRlLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  296 GADVNYQskegksplhmaaihgrftrsqiliqngseidcaDKFGNTPLHVaaryghellistlmtngadtarrgihdmfp 375
Cdd:PHA03095  107 GADVNAK---------------------------------DKVGRTPLHV------------------------------ 123
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  376 lHLAvlfgfSDCCRkllssgqlYSIVSSLsnehvLSAGFDINTPDSLGRTCLHA--AASGGNVECLNLLLSSGADLRRRD 453
Cdd:PHA03095  124 -YLS-----GFNIN--------PKVIRLL-----LRKGADVNALDLYGMTPLAVllKSRNANVELLRLLIDAGADVYAVD 184
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  454 KFGRTPLHYAAAN--GSYQCAVTLVTAGAGVNEADCKGCSPLHYAAASDTYRRAEphtasshdaeedellkesrrkeaff 531
Cdd:PHA03095  185 DRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSL------------------------- 239
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  532 cLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNCleDVESTVPVSPLHLAAYNGH----------CEAL 601
Cdd:PHA03095  240 -VLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADI--NAVSSDGNTPLSLMVRNNNgravraalakNPSA 316
                         410       420       430       440       450
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 300798249  602 KTLAETLVNLDVRDHKGRTAlflaterGSTECVEVLTAHGASALIKERKRKwtpLHAAA 660
Cdd:PHA03095  317 ETVAATLNTASVAGGDIPSD-------ATRLCVAKVVLRGAFSLLPEPIRA---YHADF 365
PHA02874 PHA02874
ankyrin repeat protein; Provisional
148-463 1.91e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 107.74  E-value: 1.91e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  148 VHSGHLETV-NLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKYLL 226
Cdd:PHA02874    9 IYSGDIEAIeKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  227 RMGAEidepnafgNTALHIACyLGQDAVAIeLVNAGANVNQPNDKGFTPLHVAaVSTNGALCLELLVNNGADVNYQSKEG 306
Cdd:PHA02874   89 DNGVD--------TSILPIPC-IEKDMIKT-ILDCGIDVNIKDAELKTFLHYA-IKKGDLESIKMLFEYGADVNIEDDNG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  307 KSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGfsd 386
Cdd:PHA02874  158 CYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN--- 234
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300798249  387 ccrkllssgqlYSIVSSLSNEHvlsagfDINTPDSLGRTCLHAAAS-GGNVECLNLLLSSGADLRRRDKFGRTPLHYA 463
Cdd:PHA02874  235 -----------RSAIELLINNA------SINDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA03100 PHA03100
ankyrin repeat protein; Provisional
15-204 3.41e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 103.59  E-value: 3.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   15 AIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAY--VGDVPILQLLLMSGANVNAKDTLWLTPLHRAAAS--RNEKVL 90
Cdd:PHA03100   80 YNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESnkIDLKIL 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   91 GLLLAHSADVNARDKLwqtplhvaaanratkcaEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCD 170
Cdd:PHA03100  160 KLLIDKGVDINAKNRV-----------------NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVN 222
                         170       180       190
                  ....*....|....*....|....*....|....
gi 300798249  171 KKERQPLHWAAFLGHLEVLKLLVARGADLSCKDR 204
Cdd:PHA03100  223 KYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02878 PHA02878
ankyrin repeat protein; Provisional
11-246 9.26e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 103.04  E-value: 9.26e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   11 PLVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLH-------------------------------AAAYVGDVPILQL 59
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHiickepnklgmkemirsinkcsvfytlvaikDAFNNRNVEIFKI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   60 LLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVNARDK-LWQTPLHVAAANRATKCAEALAPLLSSLNVADR 138
Cdd:PHA02878  120 ILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  139 SGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWA-AFLGHLEVLKLLVARGADLSCKDR-KGYGLLHTAAAS 216
Cdd:PHA02878  200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS 279
                         250       260       270
                  ....*....|....*....|....*....|
gi 300798249  217 GQieVVKYLLRMGAEIDEPNAFGNTALHIA 246
Cdd:PHA02878  280 ER--KLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02874 PHA02874
ankyrin repeat protein; Provisional
341-625 9.59e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 102.73  E-value: 9.59e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  341 TPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRKLLSSGQLYSI--VSSLSNEHV---LSAGFD 415
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIlpIPCIEKDMIktiLDCGID 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  416 INTPDSLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHY 495
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  496 AAASDTYRraephtasshdaeedellkesrrkeaffCLEFLLDNGADPSLRDRQGYTAVHYAAAYgNRQNLELLLEMSFN 575
Cdd:PHA02874  197 AAEYGDYA----------------------------CIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLINNASI 247
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 300798249  576 CLEDVESTvpvSPLHLA-AYNGHCEALKTLAETLVNLDVRDHKGRTALFLA 625
Cdd:PHA02874  248 NDQDIDGS---TPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02878 PHA02878
ankyrin repeat protein; Provisional
75-358 2.08e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 101.88  E-value: 2.08e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   75 LTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAaanratkCAE----ALAPLLSSLNVADRS-GRSALHHAVH 149
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHII-------CKEpnklGMKEMIRSINKCSVFyTLVAIKDAFN 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  150 SGHLETVN-LLLNKGASLNVCDKKERQPLHWAAFLgHLEVLKLLVARGADLSCKDR-KGYGLLHTAAASGQIEVVKYLLR 227
Cdd:PHA02878  111 NRNVEIFKiILTNRYKNIQTIDLVYIDKKSKDDII-EAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLS 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  228 MGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGALCLELLVNNGADVNYQSK-EG 306
Cdd:PHA02878  190 YGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYiLG 269
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 300798249  307 KSPLHMaAIHGRfTRSQILIQNGSEIDCADKFGNTPLHVAA--RYGHE---LLISTL 358
Cdd:PHA02878  270 LTALHS-SIKSE-RKLKLLLEYGADINSLNSYKLTPLSSAVkqYLCINigrILISNI 324
PHA02876 PHA02876
ankyrin repeat protein; Provisional
24-332 7.68e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 101.68  E-value: 7.68e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   24 VRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDtlwltpLHRAAASRNEKVLGLLLAHSA--DVN 101
Cdd:PHA02876  194 VNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND------LSLLKAIRNEDLETSLLLYDAgfSVN 267
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  102 ARDKLWQTPLHVAAanrATKCAEALAPLL----SSLNVADRSGRSALHHAVHSGH-LETVNLLLNKGASLNVCDKKERQP 176
Cdd:PHA02876  268 SIDDCKNTPLHHAS---QAPSLSRLVPKLlergADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITP 344
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  177 LHWAAFLG-HLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVA 255
Cdd:PHA02876  345 LHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMS 424
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300798249  256 IE-LVNAGANVNQPNDKGFTPLHVAAVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAAihGRFTRSQILIQNGSEI 332
Cdd:PHA02876  425 VKtLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
PHA03100 PHA03100
ankyrin repeat protein; Provisional
10-233 8.96e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 93.19  E-value: 8.96e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   10 PPLVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVG-----DVPILQLLLMSGANVNAKDTLWLTPLHRAAA- 83
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYGANVNAPDNNGITPLLYAISk 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   84 -SRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKcAEALAPLLSS---LNVADRsgrsalhhavhsghletVNLL 159
Cdd:PHA03100  117 kSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKID-LKILKLLIDKgvdINAKNR-----------------VNYL 178
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300798249  160 LNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEID 233
Cdd:PHA03100  179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02876 PHA02876
ankyrin repeat protein; Provisional
604-985 1.05e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 94.74  E-value: 1.05e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  604 LAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKERKrKWTPLHAAAASGHTDSLHLLIDSGERADITDV 683
Cdd:PHA02876  164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD-DLSVLECAVDSKNIDTIKAIIDNRSNINKNDL 242
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  684 mdaygqtPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVT-GCEDCLAALLDHDAFVLCRDFKGRTPIHLAS 762
Cdd:PHA02876  243 -------SLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMA 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  763 ACGH-TAVLRTLLQAalstdpldaGVDYSGYSPMHwasytghedclelllehspfsylegnpFTPLHCAVINNQDSTTEM 841
Cdd:PHA02876  316 KNGYdTENIRTLIML---------GADVNAADRLY---------------------------ITPLHQASTLDRNKDIVI 359
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  842 LLGALGAKVvNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTA--AENGQTaAVEFLLYRGkADLT 919
Cdd:PHA02876  360 TLLELGANV-NARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlcGTNPYM-SVKTLIDRG-ANVN 436
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300798249  920 VLDENKNTALHLACSKgheKCALMILAETQDLGL-INATNSALQMPLHIAArnGLASVVQALLSRGA 985
Cdd:PHA02876  437 SKNKDLSTPLHYACKK---NCKLDVIEMLLDNGAdVNAINIQNQYPLLIAL--EYHGIVNILLHYGA 498
PHA03100 PHA03100
ankyrin repeat protein; Provisional
186-466 1.28e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 92.81  E-value: 1.28e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  186 LEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIAC---YLGQDAVAIE--LVN 260
Cdd:PHA03100   15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikYNLTDVKEIVklLLE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  261 AGANVNQPNDKGFTPLHVAAVSTNGALCL-ELLVNNGADVNYQSKEGKSPLHMAA--IHGRFTRSQILIQNGSEIDCADK 337
Cdd:PHA03100   95 YGANVNAPDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNR 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  338 FgntplhvaaryghellistlmtngadtarrgihDMFplhlavlfgfsdccrkllssgqlysivsslsnehvLSAGFDIN 417
Cdd:PHA03100  175 V---------------------------------NYL-----------------------------------LSYGVPIN 186
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 300798249  418 TPDSLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAAN 466
Cdd:PHA03100  187 IKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILN 235
PHA02874 PHA02874
ankyrin repeat protein; Provisional
589-898 1.62e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 92.72  E-value: 1.62e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  589 LHLAAYNGHCEALKTLAETLVN-LDVRDHKGRTALFLATERGSTECVEVLTAHGASalIKERKRKW-TPLHAAAASGHTD 666
Cdd:PHA02874    5 LRMCIYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGAD--INHINTKIpHPLLTAIKIGAHD 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  667 SLHLLIDSGERADITDVMDAYGQTplmlaimnghvdcVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAF 746
Cdd:PHA02874   83 IIKLLIDNGVDTSILPIPCIEKDM-------------IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGAD 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  747 VLCRDFKGRTPIHLASACGHTAVLRTLLQ--AALSTDpldagvDYSGYSPMHWASYTGHEDCLELLLEH-SPFSYLEGNP 823
Cdd:PHA02874  150 VNIEDDNGCYPIHIAIKHNFFDIIKLLLEkgAYANVK------DNNGESPLHNAAEYGDYACIKLLIDHgNHIMNKCKNG 223
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300798249  824 FTPLHCAVINNQdSTTEMLlgaLGAKVVNSRDAKGRTPLH-AAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTA 898
Cdd:PHA02874  224 FTPLHNAIIHNR-SAIELL---INNASINDQDIDGSTPLHhAINPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02878 PHA02878
ankyrin repeat protein; Provisional
144-462 9.69e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 90.71  E-value: 9.69e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  144 LHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVArgadLSCKDRKGYGL--LHTAAASGQIEV 221
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR----SINKCSVFYTLvaIKDAFNNRNVEI 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  222 VKYLLrmgaeIDEPNAFGNTALHIACYLGQDAVaIE------LVNAGANVNQPN-DKGFTPLHVAAVSTNGALcLELLVN 294
Cdd:PHA02878  117 FKIIL-----TNRYKNIQTIDLVYIDKKSKDDI-IEaeitklLLSYGADINMKDrHKGNTALHYATENKDQRL-TELLLS 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  295 NGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHEL-LISTLMTNGAD-TARRGIHD 372
Cdd:PHA02878  190 YGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYdILKLLLEHGVDvNAKSYILG 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  373 MFPLHLAVlfgFSDCCRKLLssgqlysivsslsnehvLSAGFDINTPDSLGRTCLHAAA-SGGNVECLNLLLSSGADLRR 451
Cdd:PHA02878  270 LTALHSSI---KSERKLKLL-----------------LEYGADINSLNSYKLTPLSSAVkQYLCINIGRILISNICLLKR 329
                         330
                  ....*....|.
gi 300798249  452 RDKFGRTPLHY 462
Cdd:PHA02878  330 IKPDIKNSEGF 340
PHA02875 PHA02875
ankyrin repeat protein; Provisional
42-300 1.57e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 89.28  E-value: 1.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   42 RTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSA--DVNARDKlwqtplhvaaanra 119
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDI-------------- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  120 tkcaealapllsslnvadrsgRSALHHAVHSGHLETVNLLLNKGASLN-VCDKKERQPLHWAAFLGHLEVLKLLVARGAD 198
Cdd:PHA02875   69 ---------------------ESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGAD 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  199 LSCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHV 278
Cdd:PHA02875  128 PDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALC 207
                         250       260
                  ....*....|....*....|..
gi 300798249  279 AAVSTNGALCLELLVNNGADVN 300
Cdd:PHA02875  208 YAIENNKIDIVRLFIKRGADCN 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
589-682 3.08e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 3.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   589 LHLAAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHgasALIKERKRKWTPLHAAAASGHTDSL 668
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 300798249   669 HLLIDSGERADITD 682
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
247-563 3.77e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 88.48  E-value: 3.77e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  247 CYLGQDAVAIE--LVNAGANVNQPNDKGFTPLhVAAVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQI 324
Cdd:PHA02874    8 CIYSGDIEAIEkiIKNKGNCINISVDETTTPL-IDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKL 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  325 LIQNGSE-----------------IDCA------DKFGNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVL 381
Cdd:PHA02874   87 LIDNGVDtsilpipciekdmiktiLDCGidvnikDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  382 FGFSDCCRKLLSSGQLysivsslsnehvlsagfdINTPDSLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLH 461
Cdd:PHA02874  167 HNFFDIIKLLLEKGAY------------------ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLH 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  462 YAAANGsyQCAVTLVTAGAGVNEADCKGCSPLHYAAasdtyrraepHTASSHDAeedellkesrrkeaffcLEFLLDNGA 541
Cdd:PHA02874  229 NAIIHN--RSAIELLINNASINDQDIDGSTPLHHAI----------NPPCDIDI-----------------IDILLYHKA 279
                         330       340
                  ....*....|....*....|..
gi 300798249  542 DPSLRDRQGYTAVHYAAAYGNR 563
Cdd:PHA02874  280 DISIKDNKGENPIDTAFKYINK 301
PHA03095 PHA03095
ankyrin-like protein; Provisional
654-985 3.79e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 88.93  E-value: 3.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  654 TPLHAAAASGHTDSLHLLIDSGERADITDVM------------DAYGQTPLMLAIMNGHVDC---VHLLLEKGSTADAAD 718
Cdd:PHA03095    1 DEEDESVDIIMEAALYDYLLNASNVTVEEVRrllaagadvnfrGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPE 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  719 LRGRTALH---RGAVTgcEDCLAALLDHDAFVLCRDFKGRTPIH--LASACGHTAVLRTLLQAALSTDPLDAgvdySGYS 793
Cdd:PHA03095   81 RCGFTPLHlylYNATT--LDVIKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDL----YGMT 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  794 PMHwaSYTGHEDC----LELLLEH-SPFSYLEGNPFTPLHCAVINNQDSTTEM-LLGALGAKVvNSRDAKGRTPLHAAAF 867
Cdd:PHA03095  155 PLA--VLLKSRNAnvelLRLLIDAgADVYAVDDRFRSLLHHHLQSFKPRARIVrELIRAGCDP-AATDMLGNTPLHSMAT 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  868 ADNVSGLRM--LLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLLYRGkADLTVLDENKNTALHLACSKGHEKCALMIL 945
Cdd:PHA03095  232 GSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG-ADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 300798249  946 AETQDLGLINATNSALQMPLHIAARNGLASVVQALLSRGA 985
Cdd:PHA03095  311 AKNPSAETVAATLNTASVAGGDIPSDATRLCVAKVVLRGA 350
Ank_2 pfam12796
Ankyrin repeats (3 copies);
144-236 5.36e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 5.36e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   144 LHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARgADLSCKDrKGYGLLHTAAASGQIEVVK 223
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 300798249   224 YLLRMGAEIDEPN 236
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
519-929 6.91e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 88.97  E-value: 6.91e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  519 ELLKESRRKEAFFCLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLemSFNCLEDVESTVPVSPLHLAAYNGHC 598
Cdd:PHA02876  147 KLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLL--SYGADVNIIALDDLSVLECAVDSKNI 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  599 EALKTLAETLVNLDVRDhkgrTALFLATERGSTECVEVLTAHGASA-LIKERKRkwTPLHAAAasgHTDSLHLLIDS-GE 676
Cdd:PHA02876  225 DTIKAIIDNRSNINKND----LSLLKAIRNEDLETSLLLYDAGFSVnSIDDCKN--TPLHHAS---QAPSLSRLVPKlLE 295
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  677 RADITDVMDAYGQTPLMLAIMNGH-VDCVHLLLEKGSTADAADLRGRTALHRGA-VTGCEDCLAALLDHDAFVLCRDFKG 754
Cdd:PHA02876  296 RGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCD 375
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  755 RTPIHLASACGHTAVLRTLLQAALSTDPLDAGVDysgySPMHWASYTghedclelllehspfsyleGNPFTPLHCAVINN 834
Cdd:PHA02876  376 KTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG----TALHFALCG-------------------TNPYMSVKTLIDRG 432
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  835 QDsttemllgalgakvVNSRDAKGRTPLHAAAFAD-NVSGLRMLLQHQAEVNATDHTGRTALMTAAenGQTAAVEFLLYR 913
Cdd:PHA02876  433 AN--------------VNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHY 496
                         410
                  ....*....|....*...
gi 300798249  914 GKA--DLTVLDENKNTAL 929
Cdd:PHA02876  497 GAElrDSRVLHKSLNDNM 514
PHA03095 PHA03095
ankyrin-like protein; Provisional
599-907 3.58e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.85  E-value: 3.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  599 EALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEV---LTAHGASALIKERKrKWTPLHAAAASGHT-DSLHLLIDS 674
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERC-GFTPLHLYLYNATTlDVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  675 GerADITDVmDAYGQTPL--MLAIMNGHVDCVHLLLEKGSTADAADLRGRTALH-----RGAvtgCEDCLAALLDHDAFV 747
Cdd:PHA03095  107 G--ADVNAK-DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvllksRNA---NVELLRLLIDAGADV 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  748 LCRDFKGRTP--IHLASACGHTAVLRTLLqaALSTDPldAGVDYSGYSPMHwaSYTGHEDCLELLLehSPFsylegnpft 825
Cdd:PHA03095  181 YAVDDRFRSLlhHHLQSFKPRARIVRELI--RAGCDP--AATDMLGNTPLH--SMATGSSCKRSLV--LPL--------- 243
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  826 plhcaVINNQDsttemllgalgakvVNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTA 905
Cdd:PHA03095  244 -----LIAGIS--------------INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGR 304

                  ..
gi 300798249  906 AV 907
Cdd:PHA03095  305 AV 306
Ank_2 pfam12796
Ankyrin repeats (3 copies);
111-203 3.65e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 3.65e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   111 LHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLLNKgASLNVCDKKeRQPLHWAAFLGHLEVLK 190
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 300798249   191 LLVARGADLSCKD 203
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-269 3.72e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 3.72e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   177 LHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKYLLRmGAEIDEPNaFGNTALHIACYLGQDAVAI 256
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 300798249   257 ELVNAGANVNQPN 269
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
11-198 4.26e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 85.04  E-value: 4.26e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   11 PLVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNakDTLW---LTPLHRAAASRNE 87
Cdd:PHA02875   38 PIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD--DVFYkdgMTPLHLATILKKL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   88 KVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLLNKGASLN 167
Cdd:PHA02875  116 DIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
                         170       180       190
                  ....*....|....*....|....*....|..
gi 300798249  168 VCDKK-ERQPLHWAAFLGHLEVLKLLVARGAD 198
Cdd:PHA02875  196 YFGKNgCVAALCYAIENNKIDIVRLFIKRGAD 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
656-751 6.11e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.69  E-value: 6.11e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   656 LHAAAASGHTDSLHLLIDSGERADitdVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADaaDLRGRTALHRGAVTGCED 735
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADAN---LQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLE 75
                           90
                   ....*....|....*.
gi 300798249   736 CLAALLDHDAFVLCRD 751
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
533-730 6.27e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 84.66  E-value: 6.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  533 LEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLleMSFNCLEDVESTVPVSPLHLAAYNGHCEALKTL--AETLVN 610
Cdd:PHA02875   18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLL--MKHGAIPDVKYPDIESELHDAVEEGDVKAVEELldLGKFAD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  611 lDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKERKRkWTPLHAAAASGHTDSLHLLIDsgERAdITDVMDAYGQT 690
Cdd:PHA02875   96 -DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDK-FSPLHLAVMMGDIKGIELLID--HKA-CLDIEDCCGCT 170
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 300798249  691 PLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAV 730
Cdd:PHA02875  171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAI 210
Ank_2 pfam12796
Ankyrin repeats (3 copies);
210-302 1.93e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.93e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   210 LHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNaGANVNqPNDKGFTPLHVAAVSTNGAlCL 289
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVN-LKDNGRTALHYAARSGHLE-IV 77
                           90
                   ....*....|...
gi 300798249   290 ELLVNNGADVNYQ 302
Cdd:pfam12796   78 KLLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
436-789 2.02e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.54  E-value: 2.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  436 VECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCA---VTLVTAGAGVNEADCKGCSPLHYAAasdtyrraephtasS 512
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGFTPLHLYL--------------Y 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  513 HDAEEDellkesrrkeaffCLEFLLDNGADPSLRDRQGYTAVHyaaaygnrqnlelllemsfncledvestvpvspLHLA 592
Cdd:PHA03095   93 NATTLD-------------VIKLLIKAGADVNAKDKVGRTPLH---------------------------------VYLS 126
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  593 AYNGHCEALKTLAETLVNLDVRDHKGRTAL--FLATERGSTECVEVLTAHGASALIKERKRKwTPLHAAAASGHTDS--L 668
Cdd:PHA03095  127 GFNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFR-SLLHHHLQSFKPRAriV 205
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  669 HLLIDSGERADITDVmdaYGQTPLMLAIMngHVDCVHL----LLEKGSTADAADLRGRTALHRGAVTG----CEDCLAAL 740
Cdd:PHA03095  206 RELIRAGCDPAATDM---LGNTPLHSMAT--GSSCKRSlvlpLLIAGISINARNRYGQTPLHYAAVFNnpraCRRLIALG 280
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 300798249  741 LDhdafVLCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAGVDY 789
Cdd:PHA03095  281 AD----INAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNT 325
Ank_2 pfam12796
Ankyrin repeats (3 copies);
862-955 5.26e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 5.26e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   862 LHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLLYRGKADltvLDENKNTALHLACSKGHEKCA 941
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN---LKDNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 300798249   942 LMILAETQDLGLIN 955
Cdd:pfam12796   78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
622-718 1.39e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 1.39e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   622 LFLATERGSTECVEVLTAHGASALIKErKRKWTPLHAAAASGHTDSLHLLIDSGeRADITDvmdaYGQTPLMLAIMNGHV 701
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD----NGRTALHYAARSGHL 74
                           90
                   ....*....|....*..
gi 300798249   702 DCVHLLLEKGSTADAAD 718
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
12-194 1.55e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 80.39  E-value: 1.55e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   12 LVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLG 91
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   92 LLLAHSADVNARDKLWQTPLHVAAA-NRATkcaealAPLL---SSLNVADRSGRSALHHAVH-SGHLETVNLLLNKGASL 166
Cdd:PHA02874  208 LLIDHGNHIMNKCKNGFTPLHNAIIhNRSA------IELLinnASINDQDIDGSTPLHHAINpPCDIDIIDILLYHKADI 281
                         170       180
                  ....*....|....*....|....*....
gi 300798249  167 NVCDKKERQPLHWA-AFLGHLEVLKLLVA 194
Cdd:PHA02874  282 SIKDNKGENPIDTAfKYINKDPVIKDIIA 310
Ank_2 pfam12796
Ankyrin repeats (3 copies);
12-104 3.25e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 3.25e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249    12 LVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLmSGANVNAKDTLWlTPLHRAAASRNEKVLG 91
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDNGR-TALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 300798249    92 LLLAHSADVNARD 104
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
740-993 4.02e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 80.11  E-value: 4.02e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  740 LLDHDAFVLCRDFKGRTPIHLASACGHTAVLRTLLQ--AALSTDPLDagvdysGYSPMHWASYTGHEDCLELLLEHSpfS 817
Cdd:PHA02876  164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSygADVNIIALD------DLSVLECAVDSKNIDTIKAIIDNR--S 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  818 YLEGNPFTPLHcaVINNQDSTTEMLLGALGAKVvNSRDAKGRTPLHAAAFADNVSGL-RMLLQHQAEVNATDHTGRTALM 896
Cdd:PHA02876  236 NINKNDLSLLK--AIRNEDLETSLLLYDAGFSV-NSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLY 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  897 TAAENG-QTAAVEFLLYRGkADLTVLDENKNTALHLACSKGHEKCALMILAEtqdLGL-INATNSALQMPLHIAARNGLA 974
Cdd:PHA02876  313 LMAKNGyDTENIRTLIMLG-ADVNAADRLYITPLHQASTLDRNKDIVITLLE---LGAnVNARDYCDKTPIHYAAVRNNV 388
                         250
                  ....*....|....*....
gi 300798249  975 SVVQALLSRGATVLAVDEE 993
Cdd:PHA02876  389 VIINTLLDYGADIEALSQK 407
PHA02876 PHA02876
ankyrin repeat protein; Provisional
8-199 1.02e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 78.95  E-value: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249    8 DQPPLVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVG-DVPILQLLLMSGANVNAKDTLWLTPLHRAAASRN 86
Cdd:PHA02876  308 ETPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNN 387
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   87 EKVLGLLLAHSADVNARDKLWQTPLHVA-AANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSG-HLETVNLLLNKGA 164
Cdd:PHA02876  388 VVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGA 467
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 300798249  165 SLNVCDKKERQPLHWAafLGHLEVLKLLVARGADL 199
Cdd:PHA02876  468 DVNAINIQNQYPLLIA--LEYHGIVNILLHYGAEL 500
Ank_2 pfam12796
Ankyrin repeats (3 copies);
376-486 1.33e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 1.33e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   376 LHLAVLFGFSDCCRKLLSSGqlysivsslsnehvlsagFDINTPDSLGRTCLHAAASGGNVECLNLLLSSgADLRRRDKf 455
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG------------------ADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN- 60
                           90       100       110
                   ....*....|....*....|....*....|.
gi 300798249   456 GRTPLHYAAANGSYQCAVTLVTAGAGVNEAD 486
Cdd:pfam12796   61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
397-718 1.34e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.40  E-value: 1.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  397 LYSIVS-------SLSNEHVLSAGFDINTPDSLGRT-CLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGS 468
Cdd:PHA03100    1 LYSYIVltksriiKVKNIKYIIMEDDLNDYSYKKPVlPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKY 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  469 YQCAVT-----LVTAGAGVNEADCKGCSPLHYAAasdtyrraephtasshdaeedellkeSRRKEAFFCLEFLLDNGADP 543
Cdd:PHA03100   81 NLTDVKeivklLLEYGANVNAPDNNGITPLLYAI--------------------------SKKSNSYSIVEYLLDNGANV 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  544 SLRDRQGYTAVHYAAAYgNRQNLELllemsfncledvestvpvsplhlaaynghceaLKTLAETLVNLDVRDHkgrtalf 623
Cdd:PHA03100  135 NIKNSDGENLLHLYLES-NKIDLKI--------------------------------LKLLIDKGVDINAKNR------- 174
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  624 latergstecVEVLTAHGASALIKErKRKWTPLHAAAASGHTDSLHLLIDSGerADITDVMDaYGQTPLMLAIMNGHVDC 703
Cdd:PHA03100  175 ----------VNYLLSYGVPINIKD-VYGFTPLHYAVYNNNPEFVKYLLDLG--ANPNLVNK-YGDTPLHIAILNNNKEI 240
                         330
                  ....*....|....*
gi 300798249  704 VHLLLEKGSTADAAD 718
Cdd:PHA03100  241 FKLLLNNGPSIKTII 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
427-547 1.56e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 1.56e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   427 LHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGvnEADCKGCSPLHYAAasdtyrrae 506
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAA--------- 69
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 300798249   507 phtasshdaeedellkESRRKEaffCLEFLLDNGADPSLRD 547
Cdd:pfam12796   70 ----------------RSGHLE---IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
692-775 1.59e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 1.59e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   692 LMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHdaFVLCRDFKGRTPIHLASACGHTAVLR 771
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDNGRTALHYAARSGHLEIVK 78

                   ....
gi 300798249   772 TLLQ 775
Cdd:pfam12796   79 LLLE 82
PHA02878 PHA02878
ankyrin repeat protein; Provisional
3-118 1.92e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 77.23  E-value: 1.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249    3 ILSITDQPPLVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLH-AAAYVGDVPILQLLLMSGANVNAKDT-LWLTPLHr 80
Cdd:PHA02878  196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHiSVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALH- 274
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 300798249   81 aAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANR 118
Cdd:PHA02878  275 -SSIKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQY 311
Ank_2 pfam12796
Ankyrin repeats (3 copies);
895-991 1.93e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.76  E-value: 1.93e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   895 LMTAAENGQTAAVEFLLYRGkADLTVLDENKNTALHLACSKGHEKCAlMILAETQDLGLINATNSalqmPLHIAARNGLA 974
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHLAAKNGHLEIV-KLLLEHADVNLKDNGRT----ALHYAARSGHL 74
                           90
                   ....*....|....*..
gi 300798249   975 SVVQALLSRGATVLAVD 991
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
45-137 2.54e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.37  E-value: 2.54e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249    45 LHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHsADVNARDKLWqTPLHVAAANRATKCAE 124
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 300798249   125 ALAPLLSSLNVAD 137
Cdd:pfam12796   79 LLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
74-284 2.79e-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: 77.36  E-value: 2.79e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   74 WLTPLHRAAASRN-EKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEAL---APLLssLNVADRS----GRSALH 145
Cdd:cd22192    17 SESPLLLAAKENDvQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLmeaAPEL--VNEPMTSdlyqGETALH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  146 HAVHSGHLETVNLLLNKGASL---------------NVCDKKErQPLHWAAFLGHLEVLKLLVARGADLSCKDRkgygll 210
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVvspratgtffrpgpkNLIYYGE-HPLSFAACVGNEEIVRLLIEHGADIRAQDS------ 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  211 htaaasgqievvkyllrmgaeidepnaFGNTALHI---------ACYL---------GQDAVAIELVnaganvnqPNDKG 272
Cdd:cd22192   168 ---------------------------LGNTVLHIlvlqpnktfACQMydlilsydkEDDLQPLDLV--------PNNQG 212
                         250
                  ....*....|..
gi 300798249  273 FTPLHVAAVSTN 284
Cdd:cd22192   213 LTPFKLAAKEGN 224
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
48-284 8.31e-14

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 75.89  E-value: 8.31e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249    48 AAYVGDVPILQLLLMSGA--NVNAKDTLWLTPLHRAAA-SRNEKVLGLLLAHSADVNARDKLwqtpLHVAAANRATKCAE 124
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGDTL----LHAISLEYVDAVEA 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   125 ALAPLL-------SSLNVADRS------GRSALHHAVHSGHLETVNLLLNKGASLNV------CDKKERQ--------PL 177
Cdd:TIGR00870  100 ILLHLLaafrksgPLELANDQYtseftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVdsfyhgesPL 179
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   178 HWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHtaaasgqievvkyLLRMGAEidepNAFGNTALHIACY------LGQ 251
Cdd:TIGR00870  180 NAAACLGSPSIVALLSEDPADILTADSLGNTLLH-------------LLVMENE----FKAEYEELSCQMYnfalslLDK 242
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 300798249   252 --DAVAIELVnaganvnqPNDKGFTPLHVAAVSTN 284
Cdd:TIGR00870  243 lrDSKELEVI--------LNHQGLTPLKLAAKEGR 269
PHA02875 PHA02875
ankyrin repeat protein; Provisional
141-408 1.38e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 74.26  E-value: 1.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  141 RSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIE 220
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  221 VVKYLLRMGAEIDEpnafgntalhiACYlgqdavaielvnaganvnqpnDKGFTPLHVAAVSTNGALcLELLVNNGADVN 300
Cdd:PHA02875   83 AVEELLDLGKFADD-----------VFY---------------------KDGMTPLHLATILKKLDI-MKLLIARGADPD 129
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  301 YQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADT---ARRGihDMFPLH 377
Cdd:PHA02875  130 IPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIdyfGKNG--CVAALC 207
                         250       260       270
                  ....*....|....*....|....*....|.
gi 300798249  378 LAVLFGFSDCCRKLLSSGQLYSIVSSLSNEH 408
Cdd:PHA02875  208 YAIENNKIDIVRLFIKRGADCNIMFMIEGEE 238
PHA02875 PHA02875
ankyrin repeat protein; Provisional
596-872 2.75e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 73.10  E-value: 2.75e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  596 GHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKERKRKwTPLHAAAASGHTDSLHLLIDSG 675
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIE-SELHDAVEEGDVKAVEELLDLG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  676 ERADitDVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFVLCRDFKGR 755
Cdd:PHA02875   92 KFAD--DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGC 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  756 TPIHLASACGHTAVLRTLLQAAlstdpldAGVDYSGYSP----MHWASYTGHEDCLELLLEHSP----FSYLEGNPFTPL 827
Cdd:PHA02875  170 TPLIIAMAKGDIAICKMLLDSG-------ANIDYFGKNGcvaaLCYAIENNKIDIVRLFIKRGAdcniMFMIEGEECTIL 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 300798249  828 HcaVINNQDSTTEM-LLGALGAKVVNSRDAKgrTPLHAAAFADNVS 872
Cdd:PHA02875  243 D--MICNMCTNLESeAIDALIADIAIRIHKK--TIRRDEGFKNNMS 284
PHA02876 PHA02876
ankyrin repeat protein; Provisional
441-761 5.00e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 73.17  E-value: 5.00e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  441 LLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAAS---DTYrRAEPHTASSHDAEE 517
Cdd:PHA02876  163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSkniDTI-KAIIDNRSNINKND 241
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  518 DELLKESRRKEAFFCLeFLLDNGadpslrdrqgytavhyaaaygnrqnlellleMSFNCLEDVESTvpvsPLHLAAYNGH 597
Cdd:PHA02876  242 LSLLKAIRNEDLETSL-LLYDAG-------------------------------FSVNSIDDCKNT----PLHHASQAPS 285
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  598 CEAL-KTLAETLVNLDVRDHKGRTALFLATERG-STECVEVLTAHGASALIKERKRKwTPLHAAAA-SGHTDSLHLLIDS 674
Cdd:PHA02876  286 LSRLvPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYI-TPLHQASTlDRNKDIVITLLEL 364
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  675 GERadiTDVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRgAVTGCEDCLA--ALLDHDAFVLCRDF 752
Cdd:PHA02876  365 GAN---VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHF-ALCGTNPYMSvkTLIDRGANVNSKNK 440

                  ....*....
gi 300798249  753 KGRTPIHLA 761
Cdd:PHA02876  441 DLSTPLHYA 449
PHA02878 PHA02878
ankyrin repeat protein; Provisional
233-477 5.13e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.61  E-value: 5.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  233 DEPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTN---------------------------- 284
Cdd:PHA02878   31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNklgmkemirsinkcsvfytlvaikdafn 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  285 -----------------------------------GALCLELLVNNGADVNYQSKE-GKSPLHMAAIHGRFTRSQILIQN 328
Cdd:PHA02878  111 nrnveifkiiltnrykniqtidlvyidkkskddiiEAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSY 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  329 GSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVlfgfsdccrkllSSGQLYSIVSSLsneh 408
Cdd:PHA02878  191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV------------GYCKDYDILKLL---- 254
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300798249  409 vLSAGFDINTPDS-LGRTCLHAAASGGNVecLNLLLSSGADLRRRDKFGRTPLHYAAANGS-YQCAVTLVT 477
Cdd:PHA02878  255 -LEHGVDVNAKSYiLGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAVKQYLcINIGRILIS 322
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
209-345 8.99e-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: 8.99e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  209 LLHTAAASGQIEVVKYLLRM-GAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGAN-VNQPND----KGFTPLHVAAVS 282
Cdd:cd22192    20 PLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVVN 99
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300798249  283 TNGALcLELLVNNGADVN-------YQSKEGKS-------PLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHV 345
Cdd:cd22192   100 QNLNL-VRELIARGADVVspratgtFFRPGPKNliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
PHA02875 PHA02875
ankyrin repeat protein; Provisional
9-168 1.01e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 71.56  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249    9 QPPLVQAIFSRDVEEVRSLLSQKENIN-VLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNE 87
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   88 KVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRSGR-SALHHAVHSGHLETVNLLLNKGASL 166
Cdd:PHA02875  149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADC 228

                  ..
gi 300798249  167 NV 168
Cdd:PHA02875  229 NI 230
PHA02874 PHA02874
ankyrin repeat protein; Provisional
536-761 1.44e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 71.15  E-value: 1.44e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  536 LLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNC-LEDVESTVPVsplHLAAYNGHCEALKTLAETLVNLDVR 614
Cdd:PHA02874  110 ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVnIEDDNGCYPI---HIAIKHNFFDIIKLLLEKGAYANVK 186
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  615 DHKGRTALFLATERGSTECVEVLTAHGASALIKeRKRKWTPLHAAAasghtdslhllidsgeraditdvmdAYGQTPLML 694
Cdd:PHA02874  187 DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK-CKNGFTPLHNAI-------------------------IHNRSAIEL 240
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300798249  695 AIMNghvdcvhlllekgSTADAADLRGRTALHRGAVTGCE-DCLAALLDHDAFVLCRDFKGRTPIHLA 761
Cdd:PHA02874  241 LINN-------------ASINDQDIDGSTPLHHAINPPCDiDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
310-395 1.66e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.37  E-value: 1.66e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   310 LHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGAdtARRGIHDMFPLHLAVLFGFSDCCR 389
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                   ....*.
gi 300798249   390 KLLSSG 395
Cdd:pfam12796   79 LLLEKG 84
Ank_2 pfam12796
Ankyrin repeats (3 copies);
276-364 1.90e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.98  E-value: 1.90e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   276 LHVAAVStNGALCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGsEIDCADKfGNTPLHVAARYGHELLI 355
Cdd:pfam12796    1 LHLAAKN-GNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIV 77

                   ....*....
gi 300798249   356 STLMTNGAD 364
Cdd:pfam12796   78 KLLLEKGAD 86
PHA03100 PHA03100
ankyrin repeat protein; Provisional
265-571 2.14e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.46  E-value: 2.14e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  265 VNQPNDKGFTPLHVAAVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAA-IHGRFTR----SQILIQNGSEIDCADKFG 339
Cdd:PHA03100   27 LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnIKYNLTDvkeiVKLLLEYGANVNAPDNNG 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  340 NTPLHVAA--RYGHELLISTLMTNGADT---ARRGIHdmfPLHLAVlfgfSDCCRKLlssgqlySIVSSLsnehvLSAGF 414
Cdd:PHA03100  107 ITPLLYAIskKSNSYSIVEYLLDNGANVnikNSDGEN---LLHLYL----ESNKIDL-------KILKLL-----IDKGV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  415 DINTPDSLgrtclhaaasggnveclNLLLSSGADlrrrdkfgrtplhyaaangsyqcavtlvtagagVNEADCKGCSPLH 494
Cdd:PHA03100  168 DINAKNRV-----------------NYLLSYGVP---------------------------------INIKDVYGFTPLH 197
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300798249  495 YAAasdtyrraephtasSHDAEEdellkesrrkeaFFclEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLE 571
Cdd:PHA03100  198 YAV--------------YNNNPE------------FV--KYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
Ank_2 pfam12796
Ankyrin repeats (3 copies);
555-647 2.40e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.98  E-value: 2.40e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   555 HYAAAYGNRQNLELLLEMSFNCleDVESTVPVSPLHLAAYNGHCEALKTLAETlVNLDVRDHkGRTALFLATERGSTECV 634
Cdd:pfam12796    2 HLAAKNGNLELVKLLLENGADA--NLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIV 77
                           90
                   ....*....|...
gi 300798249   635 EVLTAHGASALIK 647
Cdd:pfam12796   78 KLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
343-453 2.86e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.60  E-value: 2.86e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   343 LHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRKLLSSgqlysivsslsnehvlsagFDINTPDSl 422
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-------------------ADVNLKDN- 60
                           90       100       110
                   ....*....|....*....|....*....|.
gi 300798249   423 GRTCLHAAASGGNVECLNLLLSSGADLRRRD 453
Cdd:pfam12796   61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
522-789 3.13e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.08  E-value: 3.13e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  522 KESRRKEAffcLEFLLDNGADPSLRDRQGYTAVHYAAAYGNrqnlelllemsfncledVESTVPvsplhlaaynghcEAL 601
Cdd:PHA03100   43 KEARNIDV---VKILLDNGADINSSTKNNSTPLHYLSNIKY-----------------NLTDVK-------------EIV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  602 KTLAETLVNLDVRDHKGRTALFLA--TERGSTECVEVLTAHGASALIKeRKRKWTPLHAAAASGHTDS--LHLLIDSGer 677
Cdd:PHA03100   90 KLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIK-NSDGENLLHLYLESNKIDLkiLKLLIDKG-- 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  678 ADItDVMDAygqtplmlaimnghvdcVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFVLCRDFKGRTP 757
Cdd:PHA03100  167 VDI-NAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228
                         250       260       270
                  ....*....|....*....|....*....|..
gi 300798249  758 IHLASACGHTAVLRTLLQAALSTDPLDAGVDY 789
Cdd:PHA03100  229 LHIAILNNNKEIFKLLLNNGPSIKTIIETLLY 260
PHA02878 PHA02878
ankyrin repeat protein; Provisional
459-761 3.72e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.91  E-value: 3.72e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  459 PLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAAsdtyrraEPHTASShdaeeDELLKESrrkeaffcleflld 538
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICK-------EPNKLGM-----KEMIRSI-------------- 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  539 ngadpsLRDRQGYTAVHYAAAYGNRqNLELLLEMSFNCLeDVESTVPVSPLHLAAYNGHCEA--LKTLAETLVNLDVRD- 615
Cdd:PHA02878   94 ------NKCSVFYTLVAIKDAFNNR-NVEIFKIILTNRY-KNIQTIDLVYIDKKSKDDIIEAeiTKLLLSYGADINMKDr 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  616 HKGRTALFLATERGSTECVEVLTAHGASALIKERKRKwTPLHAAAASGHTDSLHLLIDSGERadiTDVMDAYGQTPLMLA 695
Cdd:PHA02878  166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNN-SPLHHAVKHYNKPIVHILLENGAS---TDARDKCGNTPLHIS 241
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  696 ImnGHV---DCVHLLLEKGSTADA-ADLRGRTALHRGAVTgcEDCLAALLDHDAFVLCRDFKGRTPIHLA 761
Cdd:PHA02878  242 V--GYCkdyDILKLLLEHGVDVNAkSYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
81-236 5.18e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 70.28  E-value: 5.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   81 AAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLL 160
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300798249  161 NKGASLNvcDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPN 236
Cdd:PLN03192  612 HFASISD--PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02878 PHA02878
ankyrin repeat protein; Provisional
342-592 8.97e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.75  E-value: 8.97e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  342 PLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAV----LFGFSDCCRKLLS---SGQLYSIVSSLSNEHV----- 409
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnKLGMKEMIRSINKcsvFYTLVAIKDAFNNRNVeifki 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  410 -LSAGFDINTPDSLGRTCLHAAASGGNVECLNLLLSSGADLRRRDK-FGRTPLHYAAANGSYQCAVTLVTAGAGVNEADC 487
Cdd:PHA02878  120 iLTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  488 KGCSPLHYAaasdtyrraephtasshdaeedelLKESRRKeaffCLEFLLDNGADPSLRDRQGYTAVHYAAAY-GNRQNL 566
Cdd:PHA02878  200 TNNSPLHHA------------------------VKHYNKP----IVHILLENGASTDARDKCGNTPLHISVGYcKDYDIL 251
                         250       260
                  ....*....|....*....|....*.
gi 300798249  567 ELLLEMSfNCLEDVESTVPVSPLHLA 592
Cdd:PHA02878  252 KLLLEHG-VDVNAKSYILGLTALHSS 276
Ank_2 pfam12796
Ankyrin repeats (3 copies);
795-888 9.22e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 9.22e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   795 MHWASYTGHEDCLELLLE-HSPFSYLEGNPFTPLHCAVINNQDSTTEMLLgalgAKVVNSRDAKGRTPLHAAAFADNVSG 873
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLEnGADANLQDKNGRTALHLAAKNGHLEIVKLLL----EHADVNLKDNGRTALHYAARSGHLEI 76
                           90
                   ....*....|....*
gi 300798249   874 LRMLLQHQAEVNATD 888
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
246-490 1.36e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 67.71  E-value: 1.36e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  246 ACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAaVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQIL 325
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLA-MKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  326 IQNGSEI-DCADKFGNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGfsdccrkllssgqlysivssl 404
Cdd:PHA02875   88 LDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG--------------------- 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  405 snehvlsagfDINTpdslgrtclhaaasggnvecLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNE 484
Cdd:PHA02875  147 ----------DIKG--------------------IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDY 196

                  ....*.
gi 300798249  485 ADCKGC 490
Cdd:PHA02875  197 FGKNGC 202
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
670-919 1.75e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 68.36  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  670 LLIDSGERaDITDVMDAygqtPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALLDHDAFVLC 749
Cdd:PLN03192  512 LLGDNGGE-HDDPNMAS----NLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI 586
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  750 RDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAGvdysgyspmhwasytghedclELLLEhspfsylegnpftplhc 829
Cdd:PLN03192  587 RDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG---------------------DLLCT----------------- 628
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  830 avinnqdsttemllgalgakvvnsrdakgrtplhaAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEF 909
Cdd:PLN03192  629 -----------------------------------AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRL 673
                         250
                  ....*....|
gi 300798249  910 LLYRGkADLT 919
Cdd:PLN03192  674 LIMNG-ADVD 682
Ank_2 pfam12796
Ankyrin repeats (3 copies);
532-615 2.83e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.90  E-value: 2.83e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   532 CLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNCLEDVESTvpvsPLHLAAYNGHCEALKTLAETLVNL 611
Cdd:pfam12796   12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT----ALHYAARSGHLEIVKLLLEKGADI 87

                   ....
gi 300798249   612 DVRD 615
Cdd:pfam12796   88 NVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
20-168 3.88e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.59  E-value: 3.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   20 DVEEVRSLLSQKENINVLDQERRTPLHA-AAYVGDVP-ILQLLLMSGANVNAKDTLWLTPLHRAAASRNEK--VLGLLLA 95
Cdd:PHA03095  166 NVELLRLLIDAGADVYAVDDRFRSLLHHhLQSFKPRArIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLI 245
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300798249   96 HSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLLNKGASLNV 168
Cdd:PHA03095  246 AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAET 318
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
113-276 5.88e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.82  E-value: 5.88e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  113 VAAANRATKCAEALAPLLSSL-------NVADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGH 185
Cdd:PLN03192  524 NMASNLLTVASTGNAALLEELlkakldpDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKH 603
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  186 LEVLKLL--VARGADlsckDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGA 263
Cdd:PLN03192  604 HKIFRILyhFASISD----PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
                         170
                  ....*....|....
gi 300798249  264 NVNQPN-DKGFTPL 276
Cdd:PLN03192  680 DVDKANtDDDFSPT 693
Ank_4 pfam13637
Ankyrin repeats (many copies);
423-476 6.65e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 6.65e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 300798249   423 GRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLV 476
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
274-461 1.03e-10

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 65.80  E-value: 1.03e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  274 TPLHVAAvSTNGALCLE-LLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSE-----IDCADKFGNTPLHVAA 347
Cdd:cd22192    19 SPLLLAA-KENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  348 RYGHELLISTLMTNGADTA---------RRGIHDMFplhlavLFGfsdccrkllssgqlysivsslsnEHVLSagFdint 418
Cdd:cd22192    98 VNQNLNLVRELIARGADVVspratgtffRPGPKNLI------YYG-----------------------EHPLS--F---- 142
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 300798249  419 pdslgrtclhaAASGGNVECLNLLLSSGADLRRRDKFGRTPLH 461
Cdd:cd22192   143 -----------AACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
PHA02946 PHA02946
ankyin-like protein; Provisional
257-460 1.64e-10

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 64.69  E-value: 1.64e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  257 ELVNAGANVNQPNDKGFTPLHVAAVSTNGALcLELLVNNGADVNYQSKEGKSPLHMAAIHGR--FTRSQILIQNGSEID- 333
Cdd:PHA02946   57 ELLHRGYSPNETDDDGNYPLHIASKINNNRI-VAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINn 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  334 CADKFGNTPLhVAARYGHELLISTLMTNGadtarrgihdmFPLHLAVLFGFSDCCRKLLSSGQLYSIVSSLsnehvLSAG 413
Cdd:PHA02946  136 SVDEEGCGPL-LACTDPSERVFKKIMSIG-----------FEARIVDKFGKNHIHRHLMSDNPKASTISWM-----MKLG 198
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 300798249  414 FDINTPDSLGRTCLHAAASG--GNVECLNLLLSSgADLRRRDKFGRTPL 460
Cdd:PHA02946  199 ISPSKPDHDGNTPLHIVCSKtvKNVDIINLLLPS-TDVNKQNKFGDSPL 246
Ank_4 pfam13637
Ankyrin repeats (many copies);
140-193 2.17e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.90  E-value: 2.17e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 300798249   140 GRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLV 193
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
429-570 3.10e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.50  E-value: 3.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  429 AAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPL--------------- 493
Cdd:PLN03192  531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifril 610
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300798249  494 -HYAAASDtyrraePHTASshdaeedELLKESRRKEAFFCLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLL 570
Cdd:PLN03192  611 yHFASISD------PHAAG-------DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
PHA02875 PHA02875
ankyrin repeat protein; Provisional
659-934 3.35e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.47  E-value: 3.35e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  659 AAASGHTDSLHLLIDSGERADITdVMDAYgqTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLA 738
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFE-IYDGI--SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  739 ALLDHDAF---VLCRDfkGRTPIHLASACGHTAVLRTLLqaALSTDPLDAGVDYsgYSPMHWASYTGHEDCLELLLEHSP 815
Cdd:PHA02875   86 ELLDLGKFaddVFYKD--GMTPLHLATILKKLDIMKLLI--ARGADPDIPNTDK--FSPLHLAVMMGDIKGIELLIDHKA 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  816 FSYLEgnpftplhcavinnqdsttemllgalgakvvnsrDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTAL 895
Cdd:PHA02875  160 CLDIE----------------------------------DCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 300798249  896 M-TAAENGQTAAVEFLLYRGkAD---LTVLDENKNTALHLACS 934
Cdd:PHA02875  206 LcYAIENNKIDIVRLFIKRG-ADcniMFMIEGEECTILDMICN 247
PHA02798 PHA02798
ankyrin-like protein; Provisional
51-346 4.73e-10

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 63.32  E-value: 4.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   51 VGDVPILQL--LLMSGANVN---AKDTLWLTPLHRAAASRneKVLGLLLAHSADVNARDKLWQTPLhvaaanratkCAea 125
Cdd:PHA02798   12 FSDNVKLSTvkLLIKSCNPNeivNEYSIFQKYLQRDSPST--DIVKLFINLGANVNGLDNEYSTPL----------CT-- 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  126 lapLLSslNVADrsgrsalhhavHSGHLETVNLLLNKGASLNVCDKKERQPLHWA---AFLGHLEVLKLLVARGADLSCK 202
Cdd:PHA02798   78 ---ILS--NIKD-----------YKHMLDIVKILIENGADINKKNSDGETPLYCLlsnGYINNLEILLFMIENGADTTLL 141
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  203 DRKGYGLLHTAAASG---QIEVVKYLLRMGAEIDE-PNAFGNTALHiaCYLGQDAVAIE------LVNAGANVNQPND-- 270
Cdd:PHA02798  142 DKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDINThNNKEKYDTLH--CYFKYNIDRIDadilklFVDNGFIINKENKsh 219
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300798249  271 -KGFTPLHVAAVSTNGALCLELL--VNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVA 346
Cdd:PHA02798  220 kKKFMEYLNSLLYDNKRFKKNILdfIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
Ank_4 pfam13637
Ankyrin repeats (many copies);
173-226 5.24e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 5.24e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 300798249   173 ERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKYLL 226
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
851-1011 9.12e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.29  E-value: 9.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  851 VNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLLYRGkADLTVLDENKNTALH 930
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLH 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  931 LACSKGHEKCALMILAETQDlgLINATNSALqMPLHIAARNGLASVvqALLSRGATVLAVDEEGHTP---ALACAPNKDV 1007
Cdd:PHA02874  196 NAAEYGDYACIKLLIDHGNH--IMNKCKNGF-TPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPlhhAINPPCDIDI 270

                  ....
gi 300798249 1008 ADCL 1011
Cdd:PHA02874  271 IDIL 274
PHA02946 PHA02946
ankyin-like protein; Provisional
132-312 9.53e-10

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 62.38  E-value: 9.53e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  132 SLNVADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGH--LEVLKLLVARGADLSCK-DRKGYG 208
Cdd:PHA02946   64 SPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNSvDEEGCG 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  209 LLhTAAASGQIEVVKYLLRMGAEIDEPNAFGNTalHIACYLGQD---AVAIE-LVNAGANVNQPNDKGFTPLHVAAVSTN 284
Cdd:PHA02946  144 PL-LACTDPSERVFKKIMSIGFEARIVDKFGKN--HIHRHLMSDnpkASTISwMMKLGISPSKPDHDGNTPLHIVCSKTV 220
                         170       180
                  ....*....|....*....|....*...
gi 300798249  285 GALCLELLVNNGADVNYQSKEGKSPLHM 312
Cdd:PHA02946  221 KNVDIINLLLPSTDVNKQNKFGDSPLTL 248
Ank_4 pfam13637
Ankyrin repeats (many copies);
653-708 3.05e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 3.05e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 300798249   653 WTPLHAAAASGHTDSLHLLIDSGerADItDVMDAYGQTPLMLAIMNGHVDCVHLLL 708
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKG--ADI-NAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
851-1007 3.23e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.42  E-value: 3.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  851 VNSRDAKGRTPLHA---AAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAV-EFLLYRGkADLTVLDENKN 926
Cdd:PHA03095   40 VNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDViKLLIKAG-ADVNAKDKVGR 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  927 TALHlACSKG---HEKCALMILAETQDlglINATNSALQMPLHIAARNGLASV--VQALLSRGATVLAVDEEG----HTP 997
Cdd:PHA03095  119 TPLH-VYLSGfniNPKVIRLLLRKGAD---VNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFrsllHHH 194
                         170
                  ....*....|
gi 300798249  998 ALACAPNKDV 1007
Cdd:PHA03095  195 LQSFKPRARI 204
PHA02875 PHA02875
ankyrin repeat protein; Provisional
339-576 6.75e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.23  E-value: 6.75e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  339 GNTPLHVAARYGHELLISTLMTNGA--DTARRGIHDmfPLHLAVLFGFSDCCRKLLSSGqlysivsSLSNEHVLSAGfdi 416
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIES--ELHDAVEEGDVKAVEELLDLG-------KFADDVFYKDG--- 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  417 NTPdslgrtcLHAAASGGNVECLNLLLSSGAD--LRRRDKFgrTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLH 494
Cdd:PHA02875  103 MTP-------LHLATILKKLDIMKLLIARGADpdIPNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLI 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  495 YAAAsdtyrraephtasshdaeedellkesrRKEAFFClEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNL-ELLLEMS 573
Cdd:PHA02875  174 IAMA---------------------------KGDIAIC-KMLLDSGANIDYFGKNGCVAALCYAIENNKIDIvRLFIKRG 225

                  ...
gi 300798249  574 FNC 576
Cdd:PHA02875  226 ADC 228
Ank_4 pfam13637
Ankyrin repeats (many copies);
858-911 9.87e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 9.87e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 300798249   858 GRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLL 911
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
592-719 1.00e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 59.50  E-value: 1.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  592 AAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKE---------------RKRKWTPL 656
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDangntalwnaisakhHKIFRILY 611
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300798249  657 HAAAASGHTDSLHLLIDSGERADIT------------DVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADL 719
Cdd:PLN03192  612 HFASISDPHAAGDLLCTAAKRNDLTamkellkqglnvDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANT 686
PHA02946 PHA02946
ankyin-like protein; Provisional
49-276 1.24e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 58.53  E-value: 1.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   49 AYVG----DVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKcae 124
Cdd:PHA02946   43 AYCGikglDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEV--- 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  125 alapllsslnvadrsgrsalhhavhsghLETVNLLLNKGASL-NVCDKKERQPLhWAAFLGHLEVLKLLVARGADLSCKD 203
Cdd:PHA02946  120 ----------------------------IERINLLVQYGAKInNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVD 170
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300798249  204 RKGYGLLHTAAASG--QIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAV-AIELVNAGANVNQPNDKGFTPL 276
Cdd:PHA02946  171 KFGKNHIHRHLMSDnpKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKNVdIINLLLPSTDVNKQNKFGDSPL 246
PHA02875 PHA02875
ankyrin repeat protein; Provisional
722-914 1.87e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  722 RTALHRGAVTGCEDCLAALLD---HDAFVLcrdFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAGVDysgySPMHWA 798
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDigiNPNFEI---YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIE----SELHDA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  799 SYTGHEDCLELLLEHSPFS----YLEGNpfTPLHCAVINNQDSTTEMLLGALGAKVVNSRDAKgrTPLHAAAFADNVSGL 874
Cdd:PHA02875   76 VEEGDVKAVEELLDLGKFAddvfYKDGM--TPLHLATILKKLDIMKLLIARGADPDIPNTDKF--SPLHLAVMMGDIKGI 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 300798249  875 RMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLLYRG 914
Cdd:PHA02875  152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
55-237 3.38e-08

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 3.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   55 PILQLLLMSGANVNAKDTLWLTPLHRAAASRNEkvLGLLLAHSADVNARDKLWQTPLHVAAANratkcaEALAP-LLSSL 133
Cdd:PTZ00322   11 SAFAAQLFFGTEGSRKRRAKPISFERMAAIQEE--IARIDTHLEALEATENKDATPDHNLTTE------EVIDPvVAHML 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  134 NVAdrsgrsaLHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTA 213
Cdd:PTZ00322   83 TVE-------LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
                         170       180
                  ....*....|....*....|....
gi 300798249  214 AASGQIEVVKYLLRMGAEIDEPNA 237
Cdd:PTZ00322  156 EENGFREVVQLLSRHSQCHFELGA 179
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
200-347 3.90e-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: 3.90e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   200 SCKDRKGYGLLHTAAASGQ-IEVVKYLLRMGAEIDEpnafGNTALHIACYLGQDAV----AIELVNAGANVNQP--ND-- 270
Cdd:TIGR00870   46 NCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAV----GDTLLHAISLEYVDAVeailLHLLAAFRKSGPLElaNDqy 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   271 -----KGFTPLHVAAVsTNGALCLELLVNNGADVNYQSK--------------EGKSPLHMAAIHGRFTRSQILIQNGSE 331
Cdd:TIGR00870  122 tseftPGITALHLAAH-RQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPAD 200
                          170
                   ....*....|....*.
gi 300798249   332 IDCADKFGNTPLHVAA 347
Cdd:TIGR00870  201 ILTADSLGNTLLHLLV 216
PHA02798 PHA02798
ankyrin-like protein; Provisional
153-448 3.93e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 57.15  E-value: 3.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  153 LETVNLLLNKGASLNVCDKKERQPL-----HWAAFLGHLEVLKLLVARGADLSCKDRKG----YGLLHTAAASgQIEVVK 223
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGetplYCLLSNGYIN-NLEILL 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  224 YLLRMGAEIDEPNAFGNTALHI----ACYLGQDAVAIeLVNAGANVNQPNDK-GFTPLHV---AAVSTNGALCLELLVNN 295
Cdd:PHA02798  130 FMIENGADTTLLDKDGFTMLQVylqsNHHIDIEIIKL-LLEKGVDINTHNNKeKYDTLHCyfkYNIDRIDADILKLFVDN 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  296 GADVNYQSKegksplhmaaihgrFTRSQILiqngseidcadkfgntplhvaaryghELLISTLMTNgadtaRRGIHDMFP 375
Cdd:PHA02798  209 GFIINKENK--------------SHKKKFM--------------------------EYLNSLLYDN-----KRFKKNILD 243
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300798249  376 LhlavLFGFSDCCRK-LLSSGQLYSIVSSLSN---EHVLSAGFDINTPDSLGRTCLHAAASGGNVECLNLLLSSGAD 448
Cdd:PHA02798  244 F----IFSYIDINQVdELGFNPLYYSVSHNNRkifEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
PHA02875 PHA02875
ankyrin repeat protein; Provisional
858-1020 5.98e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 5.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  858 GRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLLYRGKADLTVLDENKNTALHLACSKGH 937
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKK 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  938 EKCALMILAETQDLGLINATNSAlqmPLHIAARNGLASVVQALLSRGATVLAVDEEGHTPALACAPNKDVADCLALILST 1017
Cdd:PHA02875  115 LDIMKLLIARGADPDIPNTDKFS---PLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191

                  ...
gi 300798249 1018 MKP 1020
Cdd:PHA02875  192 ANI 194
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
337-494 7.00e-08

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.56  E-value: 7.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  337 KFGNTPLHVAARYGHELLISTLMT-NGADTARRGIHDMFPLHLAVLFGFSDCCRKLLSSgqlysiVSSLSNEHVLSAGFd 415
Cdd:cd22192    15 RISESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEA------APELVNEPMTSDLY- 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  416 intpdsLGRTCLHAAASGGNVECLNLLLSSGADL----------RRRDK----FGRTPLHYAAANGSYQCAVTLVTAGAG 481
Cdd:cd22192    88 ------QGETALHIAVVNQNLNLVRELIARGADVvspratgtffRPGPKnliyYGEHPLSFAACVGNEEIVRLLIEHGAD 161
                         170
                  ....*....|...
gi 300798249  482 VNEADCKGCSPLH 494
Cdd:cd22192   162 IRAQDSLGNTVLH 174
Ank_4 pfam13637
Ankyrin repeats (many copies);
41-94 8.27e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 8.27e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 300798249    41 RRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLL 94
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
740-992 9.31e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.83  E-value: 9.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  740 LLDHDAFVLCRDFKGRTPIHLASACGHTAVLRTLLQaaLSTDPlDAGVDYSgYSPMHWASYTGHE-----DCLELLLEH- 813
Cdd:PHA03100   21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLD--NGADI-NSSTKNN-STPLHYLSNIKYNltdvkEIVKLLLEYg 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  814 SPFSYLEGNPFTPLHCAVIN--NQDSTTEMLLgALGAKVvNSRDAKGRTPLHAAA--FADNVSGLRMLLQHQAEVNATDH 889
Cdd:PHA03100   97 ANVNAPDNNGITPLLYAISKksNSYSIVEYLL-DNGANV-NIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNR 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  890 tgrtalmtaaengqtaaVEFLLYRGkADLTVLDENKNTALHLACSKGHEKCALMILaetqDLGL-INATNSALQMPLHIA 968
Cdd:PHA03100  175 -----------------VNYLLSYG-VPINIKDVYGFTPLHYAVYNNNPEFVKYLL----DLGAnPNLVNKYGDTPLHIA 232
                         250       260
                  ....*....|....*....|....
gi 300798249  969 ARNGLASVVQALLSRGATVLAVDE 992
Cdd:PHA03100  233 ILNNNKEIFKLLLNNGPSIKTIIE 256
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
27-166 1.07e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 1.07e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   27 LLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLL--LAHSADVNARD 104
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHAAG 623
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300798249  105 KLWQTplhvaAANRATkcAEALAPLLS-SLNV--ADRSGRSALHHAVHSGHLETVNLLLNKGASL 166
Cdd:PLN03192  624 DLLCT-----AAKRND--LTAMKELLKqGLNVdsEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_4 pfam13637
Ankyrin repeats (many copies);
74-126 1.66e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 1.66e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 300798249    74 WLTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEAL 126
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02876 PHA02876
ankyrin repeat protein; Provisional
840-997 1.69e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.45  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  840 EMLLGalGAKVVNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVE----------- 908
Cdd:PHA02876  162 EMLLE--GGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsnink 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  909 -----------------FLLYRGKADLTVLDENKNTALHLAC-SKGHEKCALMILAETQDlglINATNSALQMPLHIAAR 970
Cdd:PHA02876  240 ndlsllkairnedletsLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGAD---VNAKNIKGETPLYLMAK 316
                         170       180
                  ....*....|....*....|....*...
gi 300798249  971 NGLASV-VQALLSRGATVLAVDEEGHTP 997
Cdd:PHA02876  317 NGYDTEnIRTLIMLGADVNAADRLYITP 344
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
428-501 1.90e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 1.90e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300798249  428 HAAASGGNVEcLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAASDT 501
Cdd:PTZ00322   88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF 160
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
587-760 2.53e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 54.63  E-value: 2.53e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  587 SPLHLAAYNGHCEALKTLAETlvnldvrdhkGRTALFlatERGstecvevltAHGASALikerkrkwtplHAAAASGHTD 666
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKC----------PSCDLF---QRG---------ALGETAL-----------HVAALYDNLE 65
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  667 SLHLLIDSGERAdITDVM--DAY-GQTPLMLAIMNGHVDCVHLLLEKGstADAADLR----------------GRTALHR 727
Cdd:cd22192    66 AAVVLMEAAPEL-VNEPMtsDLYqGETALHIAVVNQNLNLVRELIARG--ADVVSPRatgtffrpgpknliyyGEHPLSF 142
                         170       180       190
                  ....*....|....*....|....*....|...
gi 300798249  728 GAVTGCEDCLAALLDHDAFVLCRDFKGRTPIHL 760
Cdd:cd22192   143 AACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
PHA02878 PHA02878
ankyrin repeat protein; Provisional
842-997 2.67e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.50  E-value: 2.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  842 LLGALGAKVVNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLLYRGkADLTVL 921
Cdd:PHA02878  152 LLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDAR 230
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300798249  922 DENKNTALHLACSKGHEKCALMILAETQdlGLINATNSALQM-PLHIAARNglASVVQALLSRGATVLAVDEEGHTP 997
Cdd:PHA02878  231 DKCGNTPLHISVGYCKDYDILKLLLEHG--VDVNAKSYILGLtALHSSIKS--ERKLKLLLEYGADINSLNSYKLTP 303
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
723-814 3.17e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 3.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  723 TALHRGAVTGCEdcLAA---------LLDHDAFVLCRDFKGRTPIHLASACGHTAVLRTLLQaaLSTDPldAGVDYSGYS 793
Cdd:PTZ00322   77 VVAHMLTVELCQ--LAAsgdavgariLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLE--FGADP--TLLDKDGKT 150
                          90       100
                  ....*....|....*....|.
gi 300798249  794 PMHWASYTGHEDCLELLLEHS 814
Cdd:PTZ00322  151 PLELAEENGFREVVQLLSRHS 171
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
658-790 3.75e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 3.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  658 AAAASGHTDSLHLLIDSGERADITDvmdAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTAL------------ 725
Cdd:PLN03192  531 TVASTGNAALLEELLKAKLDPDIGD---SKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkif 607
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  726 ------------HRGAVTGCE-------DCLAALLDHDAFVLCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAG 786
Cdd:PLN03192  608 rilyhfasisdpHAAGDLLCTaakrndlTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687

                  ....
gi 300798249  787 VDYS 790
Cdd:PLN03192  688 DDFS 691
Ank_4 pfam13637
Ankyrin repeats (many copies);
721-774 4.09e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 4.09e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 300798249   721 GRTALHRGAVTGCEDCLAALLDHDAFVLCRDFKGRTPIHLASACGHTAVLRTLL 774
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
660-743 4.24e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 4.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  660 AASGHTDSLHLLIDSGerADiTDVMDAYGQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAA 739
Cdd:PTZ00322   90 AASGDAVGARILLTGG--AD-PNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                  ....
gi 300798249  740 LLDH 743
Cdd:PTZ00322  167 LSRH 170
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
87-284 4.59e-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: 53.73  E-value: 4.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   87 EKVLGLL----LAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRS--------------GRSALHHAV 148
Cdd:cd21882     2 EELLGLLeclrWYLTDSAYQRGATGKTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  149 HSGHLETVNLLLNKGASLNV--CDKKERQPLHWAAFLGHLEvlkllvargadlsckdrkgyglLHTAAASGQIEVVKYLL 226
Cdd:cd21882    82 ENRNLNLVRLLVENGADVSAraTGRFFRKSPGNLFYFGELP----------------------LSLAACTNQEEIVRLLL 139
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300798249  227 RMGAEIDEPNA---FGNTALHIACYLGQDAVAI---------ELVNAGANVNQ-------PNDKGFTPLHVAAVSTN 284
Cdd:cd21882   140 ENGAQPAALEAqdsLGNTVLHALVLQADNTPENsafvcqmynLLLSYGAHLDPtqqleeiPNHQGLTPLKLAAVEGK 216
Ank_4 pfam13637
Ankyrin repeats (many copies);
206-259 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 300798249   206 GYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELV 259
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
180-343 5.89e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 5.89e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  180 AAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVaIELV 259
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKI-FRIL 610
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  260 NAGANVNQPNDKGftPLHVAAVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCA---D 336
Cdd:PLN03192  611 YHFASISDPHAAG--DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAntdD 688

                  ....*..
gi 300798249  337 KFGNTPL 343
Cdd:PLN03192  689 DFSPTEL 695
Ank_4 pfam13637
Ankyrin repeats (many copies);
308-358 5.99e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 5.99e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 300798249   308 SPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTL 358
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
615-774 6.26e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 53.61  E-value: 6.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  615 DHKGRTALFLATERGSTECVEVLTAHGASALIKERKRKWTPlhaaaasghtdslhllidsgeradiTDVMDAY--GQTPL 692
Cdd:cd22194   138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFFNP-------------------------KYKHEGFyfGETPL 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  693 MLAIMNGHVDCVHLLLEKGSTADAA-DLRGRTALHrGAVTGCEDclaaLLDHDAFVL-----------------CRDFKG 754
Cdd:cd22194   193 ALAACTNQPEIVQLLMEKESTDITSqDSRGNTVLH-ALVTVAED----SKTQNDFVKrmydmillksenknletIRNNEG 267
                         170       180
                  ....*....|....*....|
gi 300798249  755 RTPIHLASACGHTAVLRTLL 774
Cdd:cd22194   268 LTPLQLAAKMGKAEILKYIL 287
Ank_4 pfam13637
Ankyrin repeats (many copies);
587-637 6.54e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 6.54e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 300798249   587 SPLHLAAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVL 637
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
682-879 6.56e-07

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 53.55  E-value: 6.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   682 DVMDAYGQTPLM-LAIMNGHVDCVHLLLEKGSTADAadlrGRTALH---RGAVTGCEDCLAALLDHD----------AFV 747
Cdd:TIGR00870   46 NCPDRLGRSALFvAAIENENLELTELLLNLSCRGAV----GDTLLHaisLEYVDAVEAILLHLLAAFrksgplelanDQY 121
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   748 LCRDFKGRTPIHLASACGHTAVLRTLLQAALSTdPLDAGVD-----------YSGYSPMHWASYTGHEDCLELLLEHsPF 816
Cdd:TIGR00870  122 TSEFTPGITALHLAAHRQNYEIVKLLLERGASV-PARACGDffvksqgvdsfYHGESPLNAAACLGSPSIVALLSED-PA 199
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   817 SYLE----GNpfTPLHCAVINNQDST--TEM------LLGALGAKVVNSRDA------KGRTPLHAAAFADNVSGLRMLL 878
Cdd:TIGR00870  200 DILTadslGN--TLLHLLVMENEFKAeyEELscqmynFALSLLDKLRDSKELevilnhQGLTPLKLAAKEGRIVLFRLKL 277

                   .
gi 300798249   879 Q 879
Cdd:TIGR00870  278 A 278
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
869-1015 6.64e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 6.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  869 DNVSGLRMLLQHQAEVNA--------------TDHTGRTALMTAAENGQTAAVEFLLyRGKADLTVLDENKNTALHLACS 934
Cdd:PLN03192  489 DNVVILKNFLQHHKELHDlnvgdllgdnggehDDPNMASNLLTVASTGNAALLEELL-KAKLDPDIGDSKGRTPLHIAAS 567
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  935 KGHEKCALMILAETQDLGLINAT-NSAL---------------------QMP------LHIAARNGLASVVQALLSRGAT 986
Cdd:PLN03192  568 KGYEDCVLVLLKHACNVHIRDANgNTALwnaisakhhkifrilyhfasiSDPhaagdlLCTAAKRNDLTAMKELLKQGLN 647
                         170       180
                  ....*....|....*....|....*....
gi 300798249  987 VLAVDEEGHTpALACAPNKDVADCLALIL 1015
Cdd:PLN03192  648 VDSEDHQGAT-ALQVAMAEDHVDMVRLLI 675
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
186-471 8.74e-07

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 52.99  E-value: 8.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  186 LEVLKLLVARG-ADLSCKDRK-GYGLLHTaaasgqievvkYLLRMGAEIDepnafgntALHIACylgqdavaielvNAGA 263
Cdd:PHA02716  155 LDLIKYMVDVGiVNLNYVCKKtGYGILHA-----------YLGNMYVDID--------ILEWLC------------NNGV 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  264 NVNQPNDKGFTPLHVAAVSTN-GALCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDcADKFGNTP 342
Cdd:PHA02716  204 NVNLQNNHLITPLHTYLITGNvCASVIKKIIELGGDMDMKCVNGMSPIMTYIINIDNINPEITNIYIESLD-GNKVKNIP 282
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  343 --LHV---AARYGHELLISTLMTNGA-----DTARRGIhdmfpLHLAVLfgfsdccRKLLSSgqlySIVsSLSNEHvlsa 412
Cdd:PHA02716  283 miLHSyitLARNIDISVVYSFLQPGVklhykDSAGRTC-----LHQYIL-------RHNIST----DII-KLLHEY---- 341
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300798249  413 GFDINTPDSLGRTCLHAAAS--------------GGNVECLNLLLSSGADLRRRDKFGRTPLhyaaanGSYQC 471
Cdd:PHA02716  342 GNDLNEPDNIGNTVLHTYLSmlsvvnildpetdnDIRLDVIQCLISLGADITAVNCLGYTPL------TSYIC 408
PHA02791 PHA02791
ankyrin-like protein; Provisional
123-227 8.97e-07

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 51.97  E-value: 8.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  123 AEALAPLLSSLNV--ADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKerQPLHWAAFLGHLEVLKLLVARGADLS 200
Cdd:PHA02791   11 SKQLKSFLSSKDAfkADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDS 88
                          90       100
                  ....*....|....*....|....*..
gi 300798249  201 CKDRKGYGLLHTAAASGQIEVVKYLLR 227
Cdd:PHA02791   89 QFDDKGNTALYYAVDSGNMQTVKLFVK 115
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
227-359 9.95e-07

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 9.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  227 RMGAeIDEPNAFGNTALHiACYLGQDAVAielvnaGANVNQPNDKGFTP--LHVAAV------STNGALCLELLVNNGAD 298
Cdd:PTZ00322   36 RMAA-IQEEIARIDTHLE-ALEATENKDA------TPDHNLTTEEVIDPvvAHMLTVelcqlaASGDAVGARILLTGGAD 107
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300798249  299 VNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLM 359
Cdd:PTZ00322  108 PNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02874 PHA02874
ankyrin repeat protein; Provisional
825-997 1.21e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.27  E-value: 1.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  825 TPLHCAVINNQDSTTEMLLgALGAKVvNSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQT 904
Cdd:PHA02874  126 TFLHYAIKKGDLESIKMLF-EYGADV-NIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDY 203
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  905 AAVEFLLYRGkADLTVLDENKNTALHLACSKGHEKCALMILAETqdlglINATNSALQMPLHIAARNGLA-SVVQALLSR 983
Cdd:PHA02874  204 ACIKLLIDHG-NHIMNKCKNGFTPLHNAIIHNRSAIELLINNAS-----INDQDIDGSTPLHHAINPPCDiDIIDILLYH 277
                         170
                  ....*....|....
gi 300798249  984 GATVLAVDEEGHTP 997
Cdd:PHA02874  278 KADISIKDNKGENP 291
PHA02878 PHA02878
ankyrin repeat protein; Provisional
309-499 1.32e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.19  E-value: 1.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  309 PLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARY----GHELLISTLMTNGADTARRGIHDMFPLHLAVLF-- 382
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklGMKEMIRSINKCSVFYTLVAIKDAFNNRNVEIFki 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  383 -------GFSDCCRKLLSSGQLYSIVSSLSNEHVLSAGFDINTPD-SLGRTCLHAAASGGNVECLNLLLSSGADLRRRDK 454
Cdd:PHA02878  120 iltnrykNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 300798249  455 FGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAAS 499
Cdd:PHA02878  200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY 244
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
289-493 1.71e-06

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 52.22  E-value: 1.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  289 LELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQI--LIQNGSEIDCADKFGNTPlhvaaryghellISTLMTNgADTA 366
Cdd:PHA02716  195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASVIkkIIELGGDMDMKCVNGMSP------------IMTYIIN-IDNI 261
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  367 RRGIHDMFPLHLavlfgfsDCCRKLLSSGQLYSIVSSLSN------EHVLSAGFDINTPDSLGRTCLHA--AASGGNVEC 438
Cdd:PHA02716  262 NPEITNIYIESL-------DGNKVKNIPMILHSYITLARNidisvvYSFLQPGVKLHYKDSAGRTCLHQyiLRHNISTDI 334
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300798249  439 LNLLLSSGADLRRRDKFGRTPLHY------------AAANGSYQCAVT--LVTAGAGVNEADCKGCSPL 493
Cdd:PHA02716  335 IKLLHEYGNDLNEPDNIGNTVLHTylsmlsvvnildPETDNDIRLDVIqcLISLGADITAVNCLGYTPL 403
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
325-486 1.84e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.18  E-value: 1.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  325 LIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRKLLSsgqlysiVSSL 404
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYH-------FASI 616
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  405 SNEHvlsAGFDIntpdslgrtcLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNE 484
Cdd:PLN03192  617 SDPH---AAGDL----------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683

                  ..
gi 300798249  485 AD 486
Cdd:PLN03192  684 AN 685
Ank_5 pfam13857
Ankyrin repeats (many copies);
415-463 2.04e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 2.04e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 300798249   415 DINTPDSLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYA 463
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
845-911 2.13e-06

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 2.13e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300798249  845 ALGAKVV-------NSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLL 911
Cdd:PTZ00322   95 AVGARILltggadpNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
608-814 2.85e-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: 2.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  608 LVNLDVRD--HKGRTALFLATERGSTECVEVLTAHGASALIKERKRKWTPlhaaaASGHTDSLhllidsgeraditdvmd 685
Cdd:cd22193    64 FINAEYTDeyYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGRFFQP-----KYQGEGFY----------------- 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  686 aYGQTPLMLAIMNGHVDCVHLLLE---KGSTADAADLRGRTALHrGAVTGCEDclaaLLDHDAFV-------------LC 749
Cdd:cd22193   122 -FGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLH-ALVTVADN----TKENTKFVtrmydmilirgakLC 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  750 --------RDFKGRTPIHLASACGHTAVLRTLLQAALSTDP---LDAGVDYSGYSPMHWASY-------TGHEDCLELLL 811
Cdd:cd22193   196 ptveleeiRNNDGLTPLQLAAKMGKIEILKYILQREIKEPElrhLSRKFTDWAYGPVSSSLYdlsnvdtCEKNSVLEIIV 275

                  ...
gi 300798249  812 EHS 814
Cdd:cd22193   276 YNS 278
PHA02875 PHA02875
ankyrin repeat protein; Provisional
783-1016 3.10e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.76  E-value: 3.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  783 LDAGVD-----YSGYSPMHWASYTGHEDCLELLLEHSPF-SYLEGNPFTPLHCAVINNQDSTTEMLLgALGAKVVNSRDA 856
Cdd:PHA02875   22 LDIGINpnfeiYDGISPIKLAMKFRDSEAIKLLMKHGAIpDVKYPDIESELHDAVEEGDVKAVEELL-DLGKFADDVFYK 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  857 KGRTPLHAAAFADNVSGLRMLLQHQAE--VNATDHTgrTALMTAAENGQTAAVEFLLYrgkadltvldenkntalHLACS 934
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADpdIPNTDKF--SPLHLAVMMGDIKGIELLID-----------------HKACL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  935 KGHEKCALMilaetqdlglinatnsalqmPLHIAARNGLASVVQALLSRGATVLAVDEEGHTPALACAPNKDVADCLALI 1014
Cdd:PHA02875  162 DIEDCCGCT--------------------PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLF 221

                  ..
gi 300798249 1015 LS 1016
Cdd:PHA02875  222 IK 223
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
430-604 3.50e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.17  E-value: 3.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  430 AASGGNVECLN-LLLSSGADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAG-VNEADC----KGCSPLHYAAASDTY- 502
Cdd:cd22192    24 AAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVVNQNLn 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  503 -------RRAEPHTASSHDAeedeLLKESRRKEAFF---------C------LEFLLDNGADPSLRDRQGYTAVHYAAAY 560
Cdd:cd22192   104 lvreliaRGADVVSPRATGT----FFRPGPKNLIYYgehplsfaaCvgneeiVRLLIEHGADIRAQDSLGNTVLHILVLQ 179
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 300798249  561 GNR----QNLELLLEMSFN----CLEDVESTVPVSPLHLAAYNGHCEALKTL 604
Cdd:cd22192   180 PNKtfacQMYDLILSYDKEddlqPLDLVPNNQGLTPFKLAAKEGNIVMFQHL 231
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
421-692 4.14e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 50.65  E-value: 4.14e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  421 SLGRTCLHAAA---SGGNVECLNLLLSSGADLRRRDKF-----------GRTPLHYAAANGSYQCAVTLVTAGAGVNead 486
Cdd:cd21882    24 ATGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVS--- 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  487 ckgcsplhyAAASDTYRRAEPHTASsHDAEEDELLKESRRKEAFfcLEFLLDNGADP---SLRDRQGYTAVHyaaaygnr 563
Cdd:cd21882   101 ---------ARATGRFFRKSPGNLF-YFGELPLSLAACTNQEEI--VRLLLENGAQPaalEAQDSLGNTVLH-------- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  564 qnleLLLEMSFNcledvesTVPVSPLHLAAYNGHCEALKTLAETLVNLDVRDHKGRTALFLATERGSTECVEVLTAHGAS 643
Cdd:cd21882   161 ----ALVLQADN-------TPENSAFVCQMYNLLLSYGAHLDPTQQLEEIPNHQGLTPLKLAAVEGKIVMFQHILQREFS 229
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300798249  644 ALIKERKRK---WT--PLHAAA-------ASGHTDSLHLLIDSGERADITDVMDaygQTPL 692
Cdd:cd21882   230 GPYQPLSRKfteWTygPVTSSLydlseidSWEKNSVLELIAFSKKREARHQMLV---QEPL 287
PHA02878 PHA02878
ankyrin repeat protein; Provisional
740-898 4.40e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.65  E-value: 4.40e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  740 LLDHDAFVLCRD-FKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAGVDYsgysPMHWASYTGHEDCLELLLEHSPFS- 817
Cdd:PHA02878  153 LLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNS----PLHHAVKHYNKPIVHILLENGASTd 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  818 --YLEGNpfTPLHCAVINNQDSTTEMLLGALGAKVVNSRDAKGRTPLHAAAFADNVsgLRMLLQHQAEVNATDHTGRTAL 895
Cdd:PHA02878  229 arDKCGN--TPLHISVGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPL 304

                  ...
gi 300798249  896 MTA 898
Cdd:PHA02878  305 SSA 307
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
45-243 5.13e-06

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 50.68  E-value: 5.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   45 LHAaaYVG----DVPILQLLLMSGANVNAKDTLWLTPLHRAAASRN--EKVLGLLLAHSADVNARDKLWQTPLHVAAANr 118
Cdd:PHA02716  181 LHA--YLGnmyvDIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMSPIMTYIIN- 257
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  119 atkcAEALAPLLSSLNVADRSGRSA------LHHAVHSGH---LETVNLLLNKGASLNVCDKKERQPLHwAAFLGH---L 186
Cdd:PHA02716  258 ----IDNINPEITNIYIESLDGNKVknipmiLHSYITLARnidISVVYSFLQPGVKLHYKDSAGRTCLH-QYILRHnisT 332
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 300798249  187 EVLKLLVARGADLSCKDRKGYGLLHTAAA--------------SGQIEVVKYLLRMGAEIDEPNAFGNTAL 243
Cdd:PHA02716  333 DIIKLLHEYGNDLNEPDNIGNTVLHTYLSmlsvvnildpetdnDIRLDVIQCLISLGADITAVNCLGYTPL 403
PHA02875 PHA02875
ankyrin repeat protein; Provisional
533-697 6.89e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.60  E-value: 6.89e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  533 LEFLLDNG--ADPSLRdRQGYTAVHYAAAYGNRQNLELLLEMSFNclEDVESTVPVSPLHLAAYNGHCEALKTLAETLVN 610
Cdd:PHA02875   84 VEELLDLGkfADDVFY-KDGMTPLHLATILKKLDIMKLLIARGAD--PDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  611 LDVRDHKGRTALFLATERGSTECVEVLTAHGASALIKERKRKWTPLHAAAASGHTDSLHLLIDSGERADI-TDVMDAYGQ 689
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNImFMIEGEECT 240

                  ....*...
gi 300798249  690 TPLMLAIM 697
Cdd:PHA02875  241 ILDMICNM 248
PHA02989 PHA02989
ankyrin repeat protein; Provisional
57-317 7.77e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 49.74  E-value: 7.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   57 LQLLLMSGANVNAK---DTLWLTPLHRAAASrnEKVLGLLLAHSADVNARDkLWQTPLHVAAANR--ATKCAEALAPLL- 130
Cdd:PHA02989   19 LEFLLRTGFDVNEEyrgNSILLLYLKRKDVK--IKIVKLLIDNGADVNYKG-YIETPLCAVLRNReiTSNKIKKIVKLLl 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  131 ---SSLNVADRSGRSALHHAVHSGHLETVN---LLLNKGASLN-VCDKKERQPLH--WAAFLGHLEVLKLLVARGADLsC 201
Cdd:PHA02989   96 kfgADINLKTFNGVSPIVCFIYNSNINNCDmlrFLLSKGINVNdVKNSRGYNLLHmyLESFSVKKDVIKILLSFGVNL-F 174
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  202 KDRKGYGL------LHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTAL------HIACYlGQDAVAIELVNAGANVNQPN 269
Cdd:PHA02989  175 EKTSLYGLtpmniyLRNDIDVISIKVIKYLIKKGVNIETNNNGSESVLesfldnNKILS-KKEFKVLNFILKYIKINKKD 253
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 300798249  270 DKGFTPLHVAAVSTNGALCLELLvNNGADVNYQSKEGKSPLHMAAIHG 317
Cdd:PHA02989  254 KKGFNPLLISAKVDNYEAFNYLL-KLGDDIYNVSKDGDTVLTYAIKHG 300
PHA02859 PHA02859
ankyrin repeat protein; Provisional
216-360 1.17e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 47.51  E-value: 1.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  216 SGQIEVVKYLLRMgaeIDEPNAFGNTALHiACyLGQDAVAIE----LVNAGANVN-QPNDKGFTPLHvAAVSTNGAL--- 287
Cdd:PHA02859   31 KDDIEGVKKWIKF---VNDCNDLYETPIF-SC-LEKDKVNVEilkfLIENGADVNfKTRDNNLSALH-HYLSFNKNVepe 104
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300798249  288 CLELLVNNGADVNYQSKEGKSPLH--MAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMT 360
Cdd:PHA02859  105 ILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKKIFDFLT 179
Ank_4 pfam13637
Ankyrin repeats (many copies);
109-160 1.21e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 1.21e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 300798249   109 TPLHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGHLETVNLLL 160
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
547-775 1.33e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 49.31  E-value: 1.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   547 DRQGYTAVHYAAAYGNRQNLELLLEmSFNCLEDVESTVpvspLHLAA--YNGHCEAL---------KTLAETLVNLDVRD 615
Cdd:TIGR00870   49 DRLGRSALFVAAIENENLELTELLL-NLSCRGAVGDTL----LHAISleYVDAVEAIllhllaafrKSGPLELANDQYTS 123
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   616 --HKGRTALFLATERGSTECVEVLTAHGASalikerkrkwtpLHAAA------ASGHTDSLHllidsgeraditdvmdaY 687
Cdd:TIGR00870  124 efTPGITALHLAAHRQNYEIVKLLLERGAS------------VPARAcgdffvKSQGVDSFY-----------------H 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   688 GQTPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALH------------RGAVTGCEDCLAALLDHdafvlCRD---- 751
Cdd:TIGR00870  175 GESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHllvmenefkaeyEELSCQMYNFALSLLDK-----LRDskel 249
                          250       260
                   ....*....|....*....|....*....
gi 300798249   752 -----FKGRTPIHLASACGHTAVLRTLLQ 775
Cdd:TIGR00870  250 evilnHQGLTPLKLAAKEGRIVLFRLKLA 278
Ank_5 pfam13857
Ankyrin repeats (many copies);
291-346 1.36e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.36e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 300798249   291 LLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILIQNGSEIDCADKFGNTPLHVA 346
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
863-932 1.37e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 1.37e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  863 HAAAFADNVsGLRMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFLLYRGkADLTVLDENKNTALHLA 932
Cdd:PTZ00322   88 QLAASGDAV-GARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELA 155
Ank_5 pfam13857
Ankyrin repeats (many copies);
258-313 1.40e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.40e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 300798249   258 LVNAG-ANVNQPNDKGFTPLHVAAvSTNGALCLELLVNNGADVNYQSKEGKSPLHMA 313
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAA-KYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
274-326 1.43e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 1.43e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 300798249   274 TPLHVAAVSTNGAlCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQILI 326
Cdd:pfam13637    3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
230-350 1.46e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 48.99  E-value: 1.46e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  230 AEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANVN--------QPNDK--GF----TPLHVAAVsTNGALCLELLVNN 295
Cdd:cd22194   132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffNPKYKheGFyfgeTPLALAAC-TNQPEIVQLLMEK 210
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300798249  296 GAD-VNYQSKEGKSPLHMAAIHGRFTRSQI--LIQNGSEI--DCADKF--------GNTPLHVAARYG 350
Cdd:cd22194   211 ESTdITSQDSRGNTVLHALVTVAEDSKTQNdfVKRMYDMIllKSENKNletirnneGLTPLQLAAKMG 278
Ank_5 pfam13857
Ankyrin repeats (many copies);
191-246 2.09e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 2.09e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 300798249   191 LLVARGADLSCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIA 246
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02859 PHA02859
ankyrin repeat protein; Provisional
153-275 2.17e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 46.74  E-value: 2.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  153 LETVNLLLNKGASLNVCDKKER-QPLHWaaFLGH-----LEVLKLLVARGADLSCKDRKGYGLLHT--AAASGQIEVVKY 224
Cdd:PHA02859   66 VEILKFLIENGADVNFKTRDNNlSALHH--YLSFnknvePEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKL 143
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 300798249  225 LLRMGAEIDEPNAFGNTALH-IACYLGQDAVAIELVNAGANVNQPNDKGFTP 275
Cdd:PHA02859  144 LIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
409-467 2.26e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 2.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 300798249  409 VLSAGFDINTPDSLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANG 467
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 2.81e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 2.81e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 300798249    10 PPLVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLL 61
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
533-692 2.82e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.33  E-value: 2.82e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  533 LEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFNC-LEDVESTvpvSPLHLAAYNGHCEALKTLAETLVNL 611
Cdd:PLN03192  541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVhIRDANGN---TALWNAISAKHHKIFRILYHFASIS 617
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  612 DvrDHKGRTALFLATERGSTECVEVLTAHGASALIKERKRKwTPLHAAAASGHTDSLHLLIDSGERADITDVMDAYGQTP 691
Cdd:PLN03192  618 D--PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGA-TALQVAMAEDHVDMVRLLIMNGADVDKANTDDDFSPTE 694

                  .
gi 300798249  692 L 692
Cdd:PLN03192  695 L 695
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
237-345 3.28e-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: 3.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  237 AFGNTALHIAC-YL--GQDAVAIELVNAGANVNQPND-----------KGFTPLHVAAVSTNgALCLELLVNNGADVNYQ 302
Cdd:cd21882    24 ATGKTCLHKAAlNLndGVNEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENRN-LNLVRLLVENGADVSAR 102
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 300798249  303 SKE-------------GKSPLHMAAIHGRFTRSQILIQNGSEI---DCADKFGNTPLHV 345
Cdd:cd21882   103 ATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNTVLHA 161
Ank_4 pfam13637
Ankyrin repeats (many copies);
891-945 3.49e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 3.49e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 300798249   891 GRTALMTAAENGQTAAVEFLLYRGkADLTVLDENKNTALHLACSKGHEKCALMIL 945
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
609-775 3.53e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.77  E-value: 3.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   609 VNLDVRDHKGRTALFLATERGST-ECVEVLTAHGASALIKErkrkwTPLHAAAASGHTD----SLHLLIDSGERADITDV 683
Cdd:TIGR00870   43 LNINCPDRLGRSALFVAAIENENlELTELLLNLSCRGAVGD-----TLLHAISLEYVDAveaiLLHLLAAFRKSGPLELA 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   684 MDAY------GQTPLMLAIMNGHVDCVHLLLEKGSTADAAdlrgrtalhrgavTGCEDCLAAlLDHDAFvlcrdFKGRTP 757
Cdd:TIGR00870  118 NDQYtseftpGITALHLAAHRQNYEIVKLLLERGASVPAR-------------ACGDFFVKS-QGVDSF-----YHGESP 178
                          170
                   ....*....|....*...
gi 300798249   758 IHLASACGHTAVLRTLLQ 775
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSE 196
Ank_4 pfam13637
Ankyrin repeats (many copies);
690-741 3.74e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 3.74e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 300798249   690 TPLMLAIMNGHVDCVHLLLEKGSTADAADLRGRTALHRGAVTGCEDCLAALL 741
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
330-594 3.75e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.77  E-value: 3.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   330 SEIDCADKFGNTPLHVAARYG-HELLISTLMTNGA-----DTArrgihdmfpLHLAVLfGFSDCCRKLLSSgQLYSIVSS 403
Cdd:TIGR00870   43 LNINCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISL-EYVDAVEAILLH-LLAAFRKS 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   404 LSNEHVLSAGFDINTPDslgRTCLHAAASGGNVECLNLLLSSGADLRRRDK--------------FGRTPLHYAAANGSY 469
Cdd:TIGR00870  112 GPLELANDQYTSEFTPG---ITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSP 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   470 QCAVTLVTAGAGVNEADCKGCSPLHyAAASDTYRRAEPHTASSHdaeedellkesrrkeaffCLEFLLDNGA--DPSL-- 545
Cdd:TIGR00870  189 SIVALLSEDPADILTADSLGNTLLH-LLVMENEFKAEYEELSCQ------------------MYNFALSLLDklRDSKel 249
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 300798249   546 ---RDRQGYTAVHYAAAYGNRQNLELLLEMSFNCLEDVEStvPVSPLHLAAY 594
Cdd:TIGR00870  250 eviLNHQGLTPLKLAAKEGRIVLFRLKLAIKYKQKKFVAW--PNGQQLLSLY 299
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
43-115 4.15e-05

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.77  E-value: 4.15e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249    43 TPLHAAAYVGDVPILQLLLMSGANVNAK------------DTLWLT--PLHRAAASRNEKVLGLLLAHSADVNARDKLWQ 108
Cdd:TIGR00870  130 TALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqgvDSFYHGesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209

                   ....*..
gi 300798249   109 TPLHVAA 115
Cdd:TIGR00870  210 TLLHLLV 216
PHA02946 PHA02946
ankyin-like protein; Provisional
13-178 4.24e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 47.36  E-value: 4.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   13 VQAIFSRDVEEvrsLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKV--L 90
Cdd:PHA02946   47 IKGLDERFVEE---LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerI 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   91 GLLLAHSADV-NARDKLWQTPLhVAAANRATKCAEALAPLLSSLNVADRSGRSALHHAVHSGH--LETVNLLLNKGASLN 167
Cdd:PHA02946  124 NLLVQYGAKInNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPS 202
                         170
                  ....*....|.
gi 300798249  168 VCDKKERQPLH 178
Cdd:PHA02946  203 KPDHDGNTPLH 213
Ank_4 pfam13637
Ankyrin repeats (many copies);
530-570 4.24e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 4.24e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 300798249   530 FFCLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLL 570
Cdd:pfam13637   14 LELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
52-126 4.51e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 4.51e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300798249   52 GDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATKCAEAL 126
Cdd:PTZ00322   93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
566-814 4.62e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 47.57  E-value: 4.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  566 LELLLEMSFNCLEDVESTVPV---SPLHLAAYNGHCEALKTLA------------ETLVNLDVRD--HKGRTALFLATER 628
Cdd:cd21882     4 LLGLLECLRWYLTDSAYQRGAtgkTCLHKAALNLNDGVNEAIMllleaapdsgnpKELVNAPCTDefYQGQTALHIAIEN 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  629 GSTECVEVLTAHGASAlikerkrkwtplhAAAASGH--TDSLHLLIdsgeraditdvmdAYGQTPLMLAIMNGHVDCVHL 706
Cdd:cd21882    84 RNLNLVRLLVENGADV-------------SARATGRffRKSPGNLF-------------YFGELPLSLAACTNQEEIVRL 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  707 LLEKG---STADAADLRGRTALH------------RGAVTGCEDCLAAL---LDH-DAFVLCRDFKGRTPIHLASACGHT 767
Cdd:cd21882   138 LLENGaqpAALEAQDSLGNTVLHalvlqadntpenSAFVCQMYNLLLSYgahLDPtQQLEEIPNHQGLTPLKLAAVEGKI 217
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 300798249  768 AVLRTLLQAALST--DPLDAGVDYSGYSPMHWASY-------TGHEDCLELLLEHS 814
Cdd:cd21882   218 VMFQHILQREFSGpyQPLSRKFTEWTYGPVTSSLYdlseidsWEKNSVLELIAFSK 273
Ank_5 pfam13857
Ankyrin repeats (many copies);
32-81 4.64e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 4.64e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 300798249    32 ENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRA 81
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
12-97 4.88e-05

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 4.88e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   12 LVQAIFSRDVEEVRSLLSQKENINVLDQERRTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLG 91
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                  ....*.
gi 300798249   92 LLLAHS 97
Cdd:PTZ00322  166 LLSRHS 171
Ank_4 pfam13637
Ankyrin repeats (many copies);
791-843 5.17e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 5.17e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 300798249   791 GYSPMHWASYTGHEDCLELLLEHS-PFSYLEGNPFTPLHCAVINNQDSTTEMLL 843
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGaDINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
754-811 5.43e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 5.43e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 300798249   754 GRTPIHLASACGHTAVLRTLLQAALSTDPldagVDYSGYSPMHWASYTGHEDCLELLL 811
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINA----VDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
407-637 5.53e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.97  E-value: 5.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  407 EHVLSAGFDINTPDSLGRTCLHAAASGGNVECLNLLLSSGADLRRRDKFGRTPLHYAAANGS--YQCAVTLVTAGAGVNE 484
Cdd:PHA02946   56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINN 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  485 A-DCKGCSPLhyAAASDTYRRAEPHTAS-----------SHDAEEDELLKESRRKEAffcLEFLLDNGADPSLRDRQGYT 552
Cdd:PHA02946  136 SvDEEGCGPL--LACTDPSERVFKKIMSigfearivdkfGKNHIHRHLMSDNPKAST---ISWMMKLGISPSKPDHDGNT 210
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  553 AVHYAAA--YGNRQNLELLLEMS----FNCLEDVESTV---PVSPLHLaaYNGHCEALKTLAETLVN----------LDV 613
Cdd:PHA02946  211 PLHIVCSktVKNVDIINLLLPSTdvnkQNKFGDSPLTLlikTLSPAHL--INKLLSTSNVITDQTVNicifydrddvLEI 288
                         250       260
                  ....*....|....*....|....*...
gi 300798249  614 RDHKGR----TALFLATERGSTECVEVL 637
Cdd:PHA02946  289 INDKGKqydsTDFKMAVEVGSIRCVKYL 316
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
140-168 6.37e-05

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.03  E-value: 6.37e-05
                            10        20
                    ....*....|....*....|....*....
gi 300798249    140 GRSALHHAVHSGHLETVNLLLNKGASLNV 168
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
92-147 6.61e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 6.61e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 300798249    92 LLLAHSADVNARDKLWQTPLHVAAANRATKCAEALAPLLSSLNVADRSGRSALHHA 147
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
354-575 8.29e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.14  E-value: 8.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  354 LISTLMTNGADTARR----GIHDMF-------PLHLAVLFGFSDCCRKLLSSGQLYsivsslsnehvlsagfDINTPDSl 422
Cdd:PHA02875    6 LCDAILFGELDIARRlldiGINPNFeiydgisPIKLAMKFRDSEAIKLLMKHGAIP----------------DVKYPDI- 68
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  423 gRTCLHAAASGGNVECLNLLLSSGA---DLRRRDkfGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAAS 499
Cdd:PHA02875   69 -ESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMM 145
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 300798249  500 DTYRRaephtasshdaeedellkesrrkeaffcLEFLLDNGADPSLRDRQGYTAVHYAAAYGNRQNLELLLEMSFN 575
Cdd:PHA02875  146 GDIKG----------------------------IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
271-304 8.84e-05

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 8.84e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 300798249   271 KGFTPLHVAAVSTNGALCLELLVNNGADVNYQSK 304
Cdd:pfam00023    1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
339-392 9.88e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 9.88e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 300798249   339 GNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRKLL 392
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
375-443 1.28e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 1.28e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 300798249   375 PLHLAVLFGFSDCCRKLLSSGqlysivsslsnehvlsagFDINTPDSLGRTCLHAAASGGNVECLNLLL 443
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKG------------------ADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
271-344 1.32e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 45.95  E-value: 1.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  271 KGFTPLHVAAVSTNGALcLELLVNNGADVN-------YQSKEGKS-------PLHMAAIHGRFTRSQILIQN---GSEID 333
Cdd:cd22196    93 KGQTALHIAIERRNMHL-VELLVQNGADVHarasgefFKKKKGGPgfyfgelPLSLAACTNQLDIVKFLLENphsPADIS 171
                          90
                  ....*....|.
gi 300798249  334 CADKFGNTPLH 344
Cdd:cd22196   172 ARDSMGNTVLH 182
Ank_5 pfam13857
Ankyrin repeats (many copies);
447-496 1.50e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 1.50e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 300798249   447 ADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYA 496
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
214-314 1.61e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 1.61e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  214 AASGQIEVVKYLLRMGAEIDEPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGALcLELLV 293
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV-VQLLS 168
                          90       100       110
                  ....*....|....*....|....*....|....
gi 300798249  294 -------NNGADVNYQSKEGK------SPLHMAA 314
Cdd:PTZ00322  169 rhsqchfELGANAKPDSFTGKppsledSPISSHH 202
PHA02946 PHA02946
ankyin-like protein; Provisional
852-1017 1.65e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.43  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  852 NSRDAKGRTPLHAAAFADNVSGLRMLLQHQAEVNATDHTGRTAL--MTAAENGQTAAVEFLLYRGKADLTVLDENKNTAL 929
Cdd:PHA02946   66 NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyyLSGTDDEVIERINLLVQYGAKINNSVDEEGCGPL 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  930 hLACSKGHEKCALMILAETQDLGLINATNSAlQMPLHIAARNGLASVVQALLSRGATVLAVDEEGHTPA-LACAPNKDVA 1008
Cdd:PHA02946  146 -LACTDPSERVFKKIMSIGFEARIVDKFGKN-HIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLhIVCSKTVKNV 223

                  ....*....
gi 300798249 1009 DCLALILST 1017
Cdd:PHA02946  224 DIINLLLPS 232
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
311-399 1.75e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 1.75e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  311 HMAAiHGRFTRSQILIQNGSEIDCADKFGNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRK 390
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                  ....*....
gi 300798249  391 LLSSGQLYS 399
Cdd:PTZ00322  167 LSRHSQCHF 175
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
687-716 1.77e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 1.77e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 300798249    687 YGQTPLMLAIMNGHVDCVHLLLEKGSTADA 716
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
190-246 1.78e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 1.78e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 300798249  190 KLLVARGADLSCKDRKGYGLLHTAAASGQIEVVKYLLRMGAEIDEPNAFGNTALHIA 246
Cdd:PTZ00322   99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
140-171 2.06e-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: 2.06e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 300798249   140 GRSALHHAV-HSGHLETVNLLLNKGASLNVCDK 171
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
893-987 2.25e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.39  E-value: 2.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  893 TALMTAAENGQTAAVEFLLYRGKADL---TVLDEnknTALHLACSKGHEKCALMILAEtqDLGLIN-ATNSAL---QMPL 965
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLfqrGALGE---TALHVAALYDNLEAAVVLMEA--APELVNePMTSDLyqgETAL 93
                          90       100
                  ....*....|....*....|..
gi 300798249  966 HIAARNGLASVVQALLSRGATV 987
Cdd:cd22192    94 HIAVVNQNLNLVRELIARGADV 115
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
899-982 2.62e-04

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 2.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  899 AENGQTAAVEFLLyRGKADLTVLDENKNTALHLACSKGHEKCALMILAETQDLGLINATNSAlqmPLHIAARNGLASVVQ 978
Cdd:PTZ00322   90 AASGDAVGARILL-TGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKT---PLELAEENGFREVVQ 165

                  ....
gi 300798249  979 ALLS 982
Cdd:PTZ00322  166 LLSR 169
Ank_5 pfam13857
Ankyrin repeats (many copies);
877-932 2.75e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 2.75e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 300798249   877 LLQH-QAEVNATDHTGRTALMTAAENGQTAAVEFLLYRGkADLTVLDENKNTALHLA 932
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
43-162 2.88e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.00  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   43 TPLHAAAYVGDVPILQLLLMSGANVN---AKDTLWLT-----------PLHRAAASRNEKVLGLLLAHSADVNARDKLWQ 108
Cdd:cd22192    91 TALHIAVVNQNLNLVRELIARGADVVsprATGTFFRPgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 300798249  109 TPLHVAAANRATKCAEALAPLLSSLNVADRS----------GRSALHHAVHSGHLETVNLLLNK 162
Cdd:cd22192   171 TVLHILVLQPNKTFACQMYDLILSYDKEDDLqpldlvpnnqGLTPFKLAAKEGNIVMFQHLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
926-981 2.92e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 2.92e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 300798249   926 NTALHLACSKGHEKCALMILAETQDlglINATNSALQMPLHIAARNGLASVVQALL 981
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
156-358 3.10e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 44.66  E-value: 3.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  156 VNLLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTAAASGQ--IEVVKYLLRMGAEID 233
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKIN 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  234 EPNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTN-GALCLELLVNNGADVNYQSKEGKSPLHM 312
Cdd:PHA02946  135 NSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpKASTISWMMKLGISPSKPDHDGNTPLHI 214
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 300798249  313 AAIHGRFTRSQI-LIQNGSEIDCADKFGNTPLhvaaryghELLISTL 358
Cdd:PHA02946  215 VCSKTVKNVDIInLLLPSTDVNKQNKFGDSPL--------TLLIKTL 253
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
42-71 3.30e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 3.30e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 300798249    42 RTPLHAAAY-VGDVPILQLLLMSGANVNAKD 71
Cdd:pfam00023    3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02791 PHA02791
ankyrin-like protein; Provisional
12-167 4.04e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 43.49  E-value: 4.04e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   12 LVQAIFSRDVEEVRSLLSQKENINVLDQErrTPLHAAAYVGDVPILQLLLMSGANVNAKDTLWLTPLHRAAASRNEKVLG 91
Cdd:PHA02791   34 LYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVK 111
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300798249   92 LLLAHSADVNARDKL-WQTPL-HVAAANRATKCAEALAPLLSSLNVADRsgRSALHHAVHSGHLETVNLLLNKGASLN 167
Cdd:PHA02791  112 LFVKKNWRLMFYGKTgWKTSFyHAVMLNDVSIVSYFLSEIPSTFDLAIL--LSCIHITIKNGHVDMMILLLDYMTSTN 187
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
423-449 4.68e-04

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 4.68e-04
                            10        20
                    ....*....|....*....|....*..
gi 300798249    423 GRTCLHAAASGGNVECLNLLLSSGADL 449
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_4 pfam13637
Ankyrin repeats (many copies);
618-672 5.92e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 5.92e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 300798249   618 GRTALFLATERGSTECVEVLTAHGASALIKERkRKWTPLHAAAASGHTDSLHLLI 672
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
158-213 5.99e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 5.99e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 300798249   158 LLLNKGASLNVCDKKERQPLHWAAFLGHLEVLKLLVARGADLSCKDRKGYGLLHTA 213
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
860-1031 8.44e-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: 43.46  E-value: 8.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  860 TPLHAAAFADNVSGL-RMLLQHQAEVNATDHTGRTALMTAAENGQTAAVEFL---------------LYRGKadltvlde 923
Cdd:cd22192    19 SPLLLAAKENDVQAIkKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLmeaapelvnepmtsdLYQGE-------- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  924 nknTALHLACSKGHEKCALMILAETQDLGLINATNSAL-----------QMPLHIAARNGLASVVQALLSRGATVLAVDE 992
Cdd:cd22192    91 ---TALHIAVVNQNLNLVRELIARGADVVSPRATGTFFrpgpknliyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDS 167
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 300798249  993 EGHTP--ALACAPNKDVAdCLA--LILSTMKP--------FPPKDAVSPFS 1031
Cdd:cd22192   168 LGNTVlhILVLQPNKTFA-CQMydLILSYDKEddlqpldlVPNNQGLTPFK 217
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
423-454 8.47e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.65  E-value: 8.47e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 300798249   423 GRTCLHAAA-SGGNVECLNLLLSSGADLRRRDK 454
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
950-997 1.02e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.02e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 300798249   950 DLGLINATNSALQMPLHIAARNGLASVVQALLSRGATVLAVDEEGHTP 997
Cdd:pfam13857    5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
486-640 1.09e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 1.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  486 DCKGCSPLHYAAASDTY--------RRAEPHTASSHDAEEDELLKESRRKEAFFCLEFLL---------DNGADPSLRDR 548
Cdd:PTZ00322    2 SFLVCSVASSAFAAQLFfgtegsrkRRAKPISFERMAAIQEEIARIDTHLEALEATENKDatpdhnlttEEVIDPVVAHM 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  549 QGYTAVHYAAAyGNRQNLELLLE--MSFNCLEDVESTvpvsPLHLAAYNGHCEALKTLAETLVNLDVRDHKGRTALFLAT 626
Cdd:PTZ00322   82 LTVELCQLAAS-GDAVGARILLTggADPNCRDYDGRT----PLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAE 156
                         170
                  ....*....|....
gi 300798249  627 ERGSTECVEVLTAH 640
Cdd:PTZ00322  157 ENGFREVVQLLSRH 170
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
687-716 1.11e-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 300798249   687 YGQTPLMLAIMNGHVDCVHLLLEKGSTADA 716
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
271-344 1.78e-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: 1.78e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  271 KGFTPLHVAAVSTNGAlCLELLVNNGADVNYQSKE--------------GKSPLHMAAIHGRFTRSQILIQNG---SEID 333
Cdd:cd22193    75 EGQTALHIAIERRQGD-IVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEhqpADIE 153
                          90
                  ....*....|.
gi 300798249  334 CADKFGNTPLH 344
Cdd:cd22193   154 AQDSRGNTVLH 164
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
140-168 1.95e-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: 1.95e-03
                           10        20
                   ....*....|....*....|....*....
gi 300798249   140 GRSALHHAVHSGHLETVNLLLNKGASLNV 168
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02989 PHA02989
ankyrin repeat protein; Provisional
219-496 2.00e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 42.04  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  219 IEVVKYLLRMGAEIDEPNAfGNTALHIacYLGQDAVAIE----LVNAGANVNQpndKGF--TPLhvAAVSTNGALC---- 288
Cdd:PHA02989   16 KNALEFLLRTGFDVNEEYR-GNSILLL--YLKRKDVKIKivklLIDNGADVNY---KGYieTPL--CAVLRNREITsnki 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  289 ---LELLVNNGADVNYQSKEGKSPLhMAAIHGrftrsqiliqngSEIDCADkfgntplhvaaryghelLISTLMTNGADT 365
Cdd:PHA02989   88 kkiVKLLLKFGADINLKTFNGVSPI-VCFIYN------------SNINNCD-----------------MLRFLLSKGINV 137
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  366 ARRGIHDMFPLHLAVLFGFS---DCCRKLLSSG-------QLY-------------SIVSSLSNEHVLSAGFDINTPDSL 422
Cdd:PHA02989  138 NDVKNSRGYNLLHMYLESFSvkkDVIKILLSFGvnlfektSLYgltpmniylrndiDVISIKVIKYLIKKGVNIETNNNG 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  423 GRTCL------HAAASGGNVECLNLLLSSgADLRRRDKFGRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYA 496
Cdd:PHA02989  218 SESVLesfldnNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296
Ank_4 pfam13637
Ankyrin repeats (many copies);
825-878 2.03e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 2.03e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 300798249   825 TPLHCAVINNQDSTTEMLLGALgaKVVNSRDAKGRTPLHAAAFADNVSGLRMLL 878
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKG--ADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
687-718 2.05e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 2.05e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 300798249   687 YGQTPLMLAI-MNGHVDCVHLLLEKGSTADAAD 718
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
205-234 2.35e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 2.35e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 300798249   205 KGYGLLHTAAASGQIEVVKYLLRMGAEIDE 234
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
239-293 2.42e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 2.42e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 300798249   239 GNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVAAVSTNGAlCLELLV 293
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
910-968 2.42e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 2.42e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 300798249   910 LLYRGKADLTVLDENKNTALHLACSKGHEKCALMILAETQDlglINATNSALQMPLHIA 968
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD---LNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
456-506 2.49e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 2.49e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 300798249   456 GRTPLHYAAANGSYQCAVTLVTAGAGVNEADCKGCSPLHYAAASDTYRRAE 506
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
306-467 3.22e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 41.40  E-value: 3.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  306 GKSPLHMAAIH---GRFTRSQILIQNGSEID---------CADKF--GNTPLHVAARYGHELLISTLMTNGADTARRGIH 371
Cdd:cd21882    26 GKTCLHKAALNlndGVNEAIMLLLEAAPDSGnpkelvnapCTDEFyqGQTALHIAIENRNLNLVRLLVENGADVSARATG 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  372 DMFPLHLAVLFGFSDCCRKLLSSGQLYSIVSSL-SNEHVLSagfDINTPDSLGRTCLHAAASGGN---------VECLNL 441
Cdd:cd21882   106 RFFRKSPGNLFYFGELPLSLAACTNQEEIVRLLlENGAQPA---ALEAQDSLGNTVLHALVLQADntpensafvCQMYNL 182
                         170       180       190
                  ....*....|....*....|....*....|...
gi 300798249  442 LLSSGADLRRRDKF-------GRTPLHYAAANG 467
Cdd:cd21882   183 LLSYGAHLDPTQQLeeipnhqGLTPLKLAAVEG 215
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
962-1029 3.35e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 3.35e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300798249  962 QMPLHIAARNGLASVVQALLSRGATVLAVDEEGHTPaLACAPNKDVADCLALILSTMKPFPPKDAVSP 1029
Cdd:PTZ00322  116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTP-LELAEENGFREVVQLLSRHSQCHFELGANAK 182
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
334-467 3.38e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 41.38  E-value: 3.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  334 CADKF--GNTPLHVAARYGHELLISTLMTNGADTARRGIHDMFPLHLAVLFGFSDCCRKLLSSGQLYSIVSS-LSNEHVL 410
Cdd:cd22197    87 CTDEYyrGHSALHIAIEKRSLQCVKLLVENGADVHARACGRFFQKKQGTCFYFGELPLSLAACTKQWDVVNYlLENPHQP 166
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300798249  411 SAgfdINTPDSLGRTCLHAAA-----SGGNVECL----NLLLSSGADLRRRDKF-------GRTPLHYAAANG 467
Cdd:cd22197   167 AS---LQAQDSLGNTVLHALVmiadnSPENSALVikmyDGLLQAGARLCPTVQLeeisnheGLTPLKLAAKEG 236
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
176-204 3.67e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 3.67e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 300798249   176 PLHWAA-FLGHLEVLKLLVARGADLSCKDR 204
Cdd:pfam00023    5 PLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
803-932 3.68e-03

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.22  E-value: 3.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   803 HEDCLELLLEHSPFSYLEGnpfTPLHCAVINNQDSTTEMLL-------GALGAKVVNSRDA----KGRTPLHAAAFADNV 871
Cdd:TIGR00870   65 NLELTELLLNLSCRGAVGD---TLLHAISLEYVDAVEAILLhllaafrKSGPLELANDQYTseftPGITALHLAAHRQNY 141
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 300798249   872 SGLRMLLQHQAEVNA---------TDHT-----GRTALMTAAENGQTAAVEFLLYRGkADLTVLDENKNTALHLA 932
Cdd:TIGR00870  142 EIVKLLLERGASVPAracgdffvkSQGVdsfyhGESPLNAAACLGSPSIVALLSEDP-ADILTADSLGNTLLHLL 215
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
456-484 3.95e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 3.95e-03
                            10        20
                    ....*....|....*....|....*....
gi 300798249    456 GRTPLHYAAANGSYQCAVTLVTAGAGVNE 484
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02884 PHA02884
ankyrin repeat protein; Provisional
209-313 4.04e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.74  E-value: 4.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  209 LLHTAAASGQIEVVKYLLRMGAEIDEP-----NAFGNTALHIACYLGQDAvAIELVNAGANVNQ-PNDKGFTPLHVAAVS 282
Cdd:PHA02884   36 ILYSSIKFHYTDIIDAILKLGADPEAPfplseNSKTNPLIYAIDCDNDDA-AKLLIRYGADVNRyAEEAKITPLYISVLH 114
                          90       100       110
                  ....*....|....*....|....*....|.
gi 300798249  283 TNGAlCLELLVNNGADVNYQSKEGKSPLHMA 313
Cdd:PHA02884  115 GCLK-CLEILLSYGADINIQTNDMVTPIELA 144
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
857-889 4.05e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 4.05e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 300798249   857 KGRTPLHAAA-FADNVSGLRMLLQHQAEVNATDH 889
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
609-726 4.38e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 40.94  E-value: 4.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  609 VNLDVRD--HKGRTALFLATERGSTECVEVLTAHGASalikerkrkwtpLHAAAasghtdslhllidSGERADITDVMDA 686
Cdd:cd22196    83 VNAAYTDsyYKGQTALHIAIERRNMHLVELLVQNGAD------------VHARA-------------SGEFFKKKKGGPG 137
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 300798249  687 --YGQTPLMLAIMNGHVDCVHLLLE---KGSTADAADLRGRTALH 726
Cdd:cd22196   138 fyFGELPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLH 182
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
654-708 4.55e-03

6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.04  E-value: 4.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 300798249  654 TPLHAAAASGHTDSLHLLIDSGerADITdVMDAYGQTPLMLAIMNGHVDCVHLLL 708
Cdd:PTZ00322  117 TPLHIACANGHVQVVRVLLEFG--ADPT-LLDKDGKTPLELAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
550-604 4.55e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 4.55e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 300798249   550 GYTAVHYAAAYGNRQNLELLLEMSFNCLEDVESTVPvsPLHLAAYNGHCEALKTL 604
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGET--ALHFAASNGNVEVLKLL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
791-815 5.00e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 5.00e-03
                            10        20
                    ....*....|....*....|....*
gi 300798249    791 GYSPMHWASYTGHEDCLELLLEHSP 815
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGA 26
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
42-69 5.35e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 5.35e-03
                            10        20
                    ....*....|....*....|....*...
gi 300798249     42 RTPLHAAAYVGDVPILQLLLMSGANVNA 69
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
132-180 5.39e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 5.39e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 300798249   132 SLNVADRSGRSALHHAVHSGHLETVNLLLNKGASLNVCDKKERQPLHWA 180
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
139-280 6.32e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 40.56  E-value: 6.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  139 SGRSALHHA---VHSGHLETVNLLLN---KGASLN------VCDK--KERQPLHWAAFLGHLEVLKLLVARGADLSC--- 201
Cdd:cd22196    46 TGKTCLLKAmlnLHNGQNDTISLLLDiaeKTGNLKefvnaaYTDSyyKGQTALHIAIERRNMHLVELLVQNGADVHAras 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  202 -------KDRKGYGL----LHTAAASGQIEVVKYLLR---MGAEIDEPNAFGNTALHIACYLGQDAVA---------IEL 258
Cdd:cd22196   126 geffkkkKGGPGFYFgelpLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLHALVEVADNTPEntkfvtkmyNEI 205
                         170       180
                  ....*....|....*....|....*....
gi 300798249  259 VNAGANVNQ-------PNDKGFTPLHVAA 280
Cdd:cd22196   206 LILGAKIRPllkleeiTNKKGLTPLKLAA 234
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
76-105 6.63e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 6.63e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 300798249    76 TPLHRAAASR-NEKVLGLLLAHSADVNARDK 105
Cdd:pfam00023    4 TPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
PHA02859 PHA02859
ankyrin repeat protein; Provisional
11-171 6.71e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.03  E-value: 6.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   11 PLVQAIFSRDVEEVRSLLSQKENINVLDQerrTPLHAA---AYVgDVPILQLLLMSGANVNAKDTLW-LTPLHRAAA--- 83
Cdd:PHA02859   24 PLFYYVEKDDIEGVKKWIKFVNDCNDLYE---TPIFSClekDKV-NVEILKFLIENGADVNFKTRDNnLSALHHYLSfnk 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249   84 SRNEKVLGLLLAHSADVNARDKLWQTPLHVAAANRATK--CAEALAPLLSSLNVADRSGRSALHHAV--HSGHlETVNLL 159
Cdd:PHA02859  100 NVEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRinVIKLLIDSGVSFLNKDFDNNNILYSYIlfHSDK-KIFDFL 178
                         170
                  ....*....|..
gi 300798249  160 LNKGASLNVCDK 171
Cdd:PHA02859  179 TSLGIDINETNK 190
PHA02741 PHA02741
hypothetical protein; Provisional
186-325 7.34e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 38.49  E-value: 7.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  186 LEVLKLLVARGADLSCKDRKGYGLLHTAAASGQIEV------------VKYLLRMgaeidePNAFGNTALHIACYLGQDA 253
Cdd:PHA02741    1 MESPHFMTCLEEMIAEKNSEGENFFHEAARCGCFDIiarftpfirgdcHAAALNA------TDDAGQMCIHIAAEKHEAQ 74
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 300798249  254 VAIE----LVNAGANVN-QPNDKGFTPLHVAAVSTNGALCLELLVNNGADVNYQSKEGKSPLHMAAIHGRFTRSQIL 325
Cdd:PHA02741   75 LAAEiidhLIELGADINaQEMLEGDTALHLAAHRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAIDNEDVAMMQIL 151
Ank_5 pfam13857
Ankyrin repeats (many copies);
235-279 7.60e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 7.60e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 300798249   235 PNAFGNTALHIACYLGQDAVAIELVNAGANVNQPNDKGFTPLHVA 279
Cdd:pfam13857   12 LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
793-931 7.70e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and TRPV6 (TRPV5/6) are two homologous members within the vanilloid subfamily of the transient receptor potential (TRP) family. TRPV5 and TRPV6 show only 30-40% homology with other members of the TRP family and have unique properties that differentiates them from other TRP channels. They mediate calcium uptake in epithelia and their expression is dramatically increased in numerous types of cancer. The structure of TRPV5/6 shows the typical topology features of all TRP family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6, which is predicted to form the Ca2+ pore, and large intracellular N- and C-terminal domains. The N-terminal domain of TRPV5/6 contains three ankyrin repeats. This structural element is present in several proteins and plays a role in protein-protein interactions. The N- and C-terminal tails of TRPV5/6 each contain an internal PDZ motif which can function as part of a molecular scaffold via interaction with PDZ-domain containing proteins. A major difference between the properties of TRPV5 and TRPV6 is in their tissue distribution: TRPV5 is predominantly expressed in the distal convoluted tubules (DCT) and connecting tubules (CNT) of the kidney, with limited expression in extrarenal tissues. In contrast, TRPV6 has a broader expression pattern such as expression in the intestine, kidney, placenta, epididymis, exocrine tissues, and a few other tissues.


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.38  E-value: 7.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  793 SPMHWASYTGHEDCLELLLEHSPFSYLEGNPF--TPLHCAVINNQDSTTEMLLGA---LGAKVVNSRDAKGRTPLHAAAF 867
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALgeTALHVAALYDNLEAAVVLMEAapeLVNEPMTSDLYQGETALHIAVV 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 300798249  868 ADNVSGLRMLLQHQAEVN---ATD-----------HTGRTALMTAAENGQTAAVEFLLYRGkADLTVLDENKNTALHL 931
Cdd:cd22192    99 NQNLNLVRELIARGADVVsprATGtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVLHI 175
PHA02989 PHA02989
ankyrin repeat protein; Provisional
218-467 8.23e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 40.11  E-value: 8.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  218 QIEVVKYLLRMGAEIdepNAFGNTALHIACYLGQDAVA--------IELVNAGANVNQPNDKGFTPLHVAAVSTNGALC- 288
Cdd:PHA02989   49 KIKIVKLLIDNGADV---NYKGYIETPLCAVLRNREITsnkikkivKLLLKFGADINLKTFNGVSPIVCFIYNSNINNCd 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  289 -LELLVNNGADVN-YQSKEGKSPLHMAaIHGRFTRS---QILIQNGSEI-DCADKFGNTPLHVAARYGHEL----LISTL 358
Cdd:PHA02989  126 mLRFLLSKGINVNdVKNSRGYNLLHMY-LESFSVKKdviKILLSFGVNLfEKTSLYGLTPMNIYLRNDIDVisikVIKYL 204
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  359 MTNGADtarrgIHDMFPLHLAVLFGFSDCcRKLLSSGQ---LYSIVSSLSnehvlsagfdINTPDSLGRTCLHAAASGGN 435
Cdd:PHA02989  205 IKKGVN-----IETNNNGSESVLESFLDN-NKILSKKEfkvLNFILKYIK----------INKKDKKGFNPLLISAKVDN 268
                         250       260       270
                  ....*....|....*....|....*....|..
gi 300798249  436 VECLNLLLSSGADLRRRDKFGRTPLHYAAANG 467
Cdd:PHA02989  269 YEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHG 300
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
239-270 8.39e-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: 8.39e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 300798249   239 GNTALHIACY-LGQDAVAIELVNAGANVNQPND 270
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA02736 PHA02736
Viral ankyrin protein; Provisional
423-472 9.23e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.93  E-value: 9.23e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 300798249  423 GRTCLHAAASGGNV---ECLNLLLSSGADLRRRD-KFGRTPLHYAAANGSYQCA 472
Cdd:PHA02736   55 GKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKErVFGNTPLHIAVYTQNYELA 108
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
339-364 9.29e-03

ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four consecutive copies. They are involved in protein-protein interactions. The core of the repeat seems to be an helix-loop-helix structure.


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 9.29e-03
                            10        20
                    ....*....|....*....|....*.
gi 300798249    339 GNTPLHVAARYGHELLISTLMTNGAD 364
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
721-913 9.61e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 39.86  E-value: 9.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  721 GRTALHRGAV---TGCEDCLAALLDHD-----------AFVLCRDFKGRTPIHLASACGHTAVLRTLLQAALSTDPLDAG 786
Cdd:cd21882    26 GKTCLHKAALnlnDGVNEAIMLLLEAApdsgnpkelvnAPCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARATG 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 300798249  787 ---------VDYSGYSPMHWASYTGHEDCLELLLEHspfsylegnpftPLHCAVINNQDSTTEMLLGALGAKVVNSRDak 857
Cdd:cd21882   106 rffrkspgnLFYFGELPLSLAACTNQEEIVRLLLEN------------GAQPAALEAQDSLGNTVLHALVLQADNTPE-- 171
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 300798249  858 grtplhAAAFAdnVSGLRMLLQHQAEVNAT-------DHTGRTALMTAAENGQTAAVEFLLYR 913
Cdd:cd21882   172 ------NSAFV--CQMYNLLLSYGAHLDPTqqleeipNHQGLTPLKLAAVEGKIVMFQHILQR 226
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
176-201 9.76e-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: 9.76e-03
                            10        20
                    ....*....|....*....|....*.
gi 300798249    176 PLHWAAFLGHLEVLKLLVARGADLSC 201
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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