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Conserved domains on  [gi|694897886|ref|XP_009442193|]
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serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit B isoform X2 [Pan troglodytes]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 13837771)

ankyrin repeat (ANK) domain-containing protein mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

CATH:  1.25.40.20
Gene Ontology:  GO:0005515
PubMed:  33435370|15152081|17176038

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-343 4.75e-52

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 184.77  E-value: 4.75e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   54 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSV 133
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  134 NVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 213
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  214 ASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALcLELLV 293
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 694897886  294 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 343
Cdd:COG0666   240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
492-749 2.27e-36

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 2.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  492 NAHENSEELERARELKEKEATLCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEESDSGATksPL 571
Cdd:COG0666    14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT--LL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  572 HLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLR 651
Cdd:COG0666    92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVK 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  652 LLLEI-ADnpeaVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSIL 730
Cdd:COG0666   171 LLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                         250
                  ....*....|....*....
gi 694897886  731 CKDSRGRTPLHYAAARGHA 749
Cdd:COG0666   247 AKDKDGLTALLLAAAAGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
253-534 1.59e-33

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.23  E-value: 1.59e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  253 AVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI 332
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  333 DCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAA 412
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  413 AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAASDMDRNKTILGN 492
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 694897886  493 AHENSEELERARELKEKEATLCLEFLLQNDANPSIRDKEGYN 534
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
650-979 1.03e-32

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.92  E-value: 1.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  650 LRLLLEIADNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSI 729
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  730 LCKDSRGRTPLHYAAARGHATWLSELLQmalSEEDCCFKDNQGYTPLHWACYNGNENCIEVLLEQKcfrkfignpftplh 809
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-------------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  810 cAIINdhgncaslllgaidssivsCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAADNSGKTALMMAAENGQAGAVD 889
Cdd:COG0666   144 -ADVN-------------------AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  890 ILVNsAQADLTVKDKDLNTPLHLACSKGHEKCALLILDKIQDeslINAKNNALQTPLHVAARNGLKVVVEELLAKGACVL 969
Cdd:COG0666   204 LLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279

                         330
                  ....*....|
gi 694897886  970 AVDENGHTPA 979
Cdd:COG0666   280 AALLDLLTLL 289
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 4.75e-06

Ankyrin repeats (many copies);


:

Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 4.75e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 694897886    10 PPLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLI 61
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-343 4.75e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 184.77  E-value: 4.75e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   54 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSV 133
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  134 NVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 213
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  214 ASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALcLELLV 293
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 694897886  294 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 343
Cdd:COG0666   240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 22-310 1.20e-39

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 154.03  E-value: 1.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   22 EEIRMLIHKTEDVNTLDSEKRTPLHVaaFLG-----DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAV-QVLIK 95
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDViKLLIK 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   96 HSADVNARDKNWQTPLHVAAANKAVkcaeviipllssvnvsdrggrtalhhaalngHVEMVNLLLAKGANINAFDKKDRR 175
Cdd:PHA03095  106 AGADVNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMT 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  176 ALHwaAYMGH----LDVVALLINHGAEVTCKDKKGYTPLHAAASNGQIN--VVKHLLNLGVEIDEINVYGNTALHIACYN 249
Cdd:PHA03095  155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694897886  250 G--QDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLELLvNNGADVNIQSKDGKSPL 310
Cdd:PHA03095  233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGNTPL 294
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
492-749 2.27e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 2.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  492 NAHENSEELERARELKEKEATLCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEESDSGATksPL 571
Cdd:COG0666    14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT--LL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  572 HLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLR 651
Cdd:COG0666    92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVK 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  652 LLLEI-ADnpeaVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSIL 730
Cdd:COG0666   171 LLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                         250
                  ....*....|....*....
gi 694897886  731 CKDSRGRTPLHYAAARGHA 749
Cdd:COG0666   247 AKDKDGLTALLLAAAAGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
253-534 1.59e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.23  E-value: 1.59e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  253 AVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI 332
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  333 DCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAA 412
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  413 AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAASDMDRNKTILGN 492
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 694897886  493 AHENSEELERARELKEKEATLCLEFLLQNDANPSIRDKEGYN 534
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
650-979 1.03e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.92  E-value: 1.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  650 LRLLLEIADNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSI 729
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  730 LCKDSRGRTPLHYAAARGHATWLSELLQmalSEEDCCFKDNQGYTPLHWACYNGNENCIEVLLEQKcfrkfignpftplh 809
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-------------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  810 cAIINdhgncaslllgaidssivsCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAADNSGKTALMMAAENGQAGAVD 889
Cdd:COG0666   144 -ADVN-------------------AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  890 ILVNsAQADLTVKDKDLNTPLHLACSKGHEKCALLILDKIQDeslINAKNNALQTPLHVAARNGLKVVVEELLAKGACVL 969
Cdd:COG0666   204 LLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279

                         330
                  ....*....|
gi 694897886  970 AVDENGHTPA 979
Cdd:COG0666   280 AALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 212-475 1.13e-27

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 118.20  E-value: 1.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  212 AAASNGQINVVKHLLNLGVEIDEINVYGNTALH--IACYNGQDA-VVNELIDYGANVNQPNNNGFTPLHFAAASTHGALC 288
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  289 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGH---ELLiNTLITSGA 363
Cdd:PHA03095  100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGA 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  364 DTAKCGIHSMFPLHLAALNAHSD--CCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQ--SSGADFHKKDKCGR 439
Cdd:PHA03095  179 DVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPllIAGISINARNRYGQ 258

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 694897886  440 TPLHYAAANCHFHCIETLVTTGANVNETDDWGRTAL 475
Cdd:PHA03095  259 TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
 355-664 2.13e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 102.03  E-value: 2.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  355 INTLITSGADTAKCGIHSMFPLHLAALNAHSDC---CRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVE-CIKLLQSSGAD 430
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGAD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  431 FHKKDKCGRTPLH-YAA-ANCHFHCIETLVTTGANVNETDDWGRTALHyaaasdmdrnktILgnahenseelerareLKE 508
Cdd:PHA03095  110 VNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLA------------VL---------------LKS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  509 KEATL-CLEFLLQNDANPSIRDKEGYNSIHYAAAYGH--RQCLELLLERTNSGFEESDSGATksPLHLAAYNGHHQALEV 585
Cdd:PHA03095  163 RNANVeLLRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNT--PLHSMATGSSCKRSLV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  586 --LLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADNPEAV 663
Cdd:PHA03095  241 lpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319


                  .
gi 694897886  664 D 664
Cdd:PHA03095  320 A 320
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-269 3.11e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 3.11e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   177 LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNlGVEIDEINvYGNTALHIACYNGQDAVVN 256
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 694897886   257 ELIDYGANVNQPN 269
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 651-966 1.57e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 90.08  E-value: 1.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  651 RLLLEIADnpeaVDVKDAKGQTPLMLAVAYGH---IDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEE-CVQMLLEQE 726
Cdd:PHA03095   32 RLLAAGAD----VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  727 VSILCKDSRGRTPLH-YAA-ARGHATWLSELLQMALSEEDCcfkDNQGYTPLHwaCYNGNENC----IEVLLEQKCF--- 797
Cdd:PHA03095  108 ADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNAL---DLYGMTPLA--VLLKSRNAnvelLRLLIDAGADvya 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  798 RKFIGNpfTPLH--CAIINDHGNCASLLLGAIDSsiVSCRDDKGRTPLHAAAFADHVECLQL--LLRHSAPVNAADNSGK 873
Cdd:PHA03095  183 VDDRFR--SLLHhhLQSFKPRARIVRELIRAGCD--PAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQ 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  874 TALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLACSKGHEKCALLILDKIQDESLINAKNNALQTPLHVAARNG 953
Cdd:PHA03095  259 TPLHYAAVFNNPRACRRLIA-LGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTASVAGGDIPSDA 337

                         330
                  ....*....|...
gi 694897886  954 LKVVVEELLAKGA 966
Cdd:PHA03095  338 TRLCVAKVVLRGA 350
Ank_2 pfam12796
Ankyrin repeats (3 copies);
376-468 1.91e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.91e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   376 LHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLqSSGADFHKKDKcGRTPLHYAAANCHFHCIE 455
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 694897886   456 TLVTTGANVNETD 468
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
604-700 5.31e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 5.31e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   604 LDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADnpeaVDVKDaKGQTPLMLAVAYGHI 683
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHL 74

                           90
                   ....*....|....*..
gi 694897886   684 DAVSLLLEKEANVDTVD 700
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 74-281 8.10e-17

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: 85.45  E-value: 8.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   74 WLTPLHRAVASRSEEAVQVLIK-HSADVNARDKNWQTPLHVAAANKAVKCAEVII---PLLssVNV---SD-RGGRTALH 145
Cdd:cd22192    17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaaPEL--VNEpmtSDlYQGETALH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  146 HAALNGHVEMVNLLLAKGANIN------AFDKKDRRAL-----H---WAAYMGHLDVVALLINHGAEVTCKDKKGYTPLH 211
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694897886  212 AAASNGQINVVKH----LLNLGVEIDEINVYgntalHIacyngqdavvnelidyganvnqPNNNGFTPLHFAAA 281
Cdd:cd22192   175 ILVLQPNKTFACQmydlILSYDKEDDLQPLD-----LV----------------------PNNQGLTPFKLAAK 221
Ank_2 pfam12796
Ankyrin repeats (3 copies);
843-939 1.97e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.97e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   843 LHAAAFADHVECLQLLLRHSAPVNAADNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKdlnTPLHLACSKGHEKCA 922
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77

                           90
                   ....*....|....*..
gi 694897886   923 LLILDKIQDeslINAKN 939
Cdd:pfam12796   78 KLLLEKGAD---INVKD 91
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 49-280 1.64e-11

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: 68.57  E-value: 1.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886    49 AFLGDAEIIELLILSGARVNAK-------DNMWLTPLHRAVA-SRSEEAVQVLIKHSADVNARDknwqTPLHVAAANKAV 120
Cdd:TIGR00870   20 AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAISLEYVD 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   121 KCAEVIIPLLSS---------VNVSDRG----GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRA----- 176
Cdd:TIGR00870   96 AVEAILLHLLAAfrksgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDsfyhg 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   177 ---LHWAAYMGHLDVVALLINHGAEVTCKDKKGytplhaaasngqiNVVKHLLNLGVEideiNVYGNTALHIACYngqda 253
Cdd:TIGR00870  176 espLNAAACLGSPSIVALLSEDPADILTADSLG-------------NTLLHLLVMENE----FKAEYEELSCQMY----- 233

                          250       260       270
                   ....*....|....*....|....*....|....
gi 694897886   254 vvNELIDYGANVNQ-------PNNNGFTPLHFAA 280
Cdd:TIGR00870  234 --NFALSLLDKLRDskeleviLNHQGLTPLKLAA 265
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 567-784 4.22e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 60.41  E-value: 4.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  567 TKSPLHLAAYNGHHQALEVLL-QSLVDLDIRDEKGRTALDLAAFKGHTECVEALInqgasifvkDNVTkrtplhasving 645
Cdd:cd22192    17 SESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLM---------EAAP------------ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  646 htlclrlllEIADNPEAVDVkdAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGcTALHRGI-------------- 711
Cdd:cd22192    76 ---------ELVNEPMTSDL--YQGETALHIAVVNQNLNLVRELIARGADVVSPRATG-TFFRPGPknliyygehplsfa 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  712 -MTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALSEE----DCCF---KDNQGYTPLHWACYNG 783
Cdd:cd22192   144 aCVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYDLILSYDkeddLQPLdlvPNNQGLTPFKLAAKEG 223


                  .
gi 694897886  784 N 784
Cdd:cd22192   224 N 224
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 340-476 1.43e-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: 58.87  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  340 NTPLHVAARYGHELLINTLITS-GADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSG----FEIDTPDKF-GRTCLHAAA 413
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelvNEPMTSDLYqGETALHIAV 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694897886  414 AGGNVECIKLLQSSGAD----------FHKKDKC----GRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALH 476
Cdd:cd22192    98 VNQNLNLVRELIARGADvvspratgtfFRPGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 569-813 3.98e-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: 3.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   569 SPLHLAAYNGHHQALEVLLQSLvdlDIRDEKGRTALdLAAFKGHTECVEALIN--------QGASIFVKDNVTKR----- 635
Cdd:TIGR00870   54 SALFVAAIENENLELTELLLNL---SCRGAVGDTLL-HAISLEYVDAVEAILLhllaafrkSGPLELANDQYTSEftpgi 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   636 TPLHASVINGHTLCLRLLLEIADNPEA----VDVKDAKGQT-------PLMLAVAYGHIDAVSLLLEKEANVDTVDILGC 704
Cdd:TIGR00870  130 TALHLAAHRQNYEIVKLLLERGASVPAracgDFFVKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   705 TALHRGIMtgheECVQMLLEQEVSILCKDSrgrtplhyaaarghATWLSELLQMALSEEDCCfkDNQGYTPLHWACYNGN 784
Cdd:TIGR00870  210 TLLHLLVM----ENEFKAEYEELSCQMYNF--------------ALSLLDKLRDSKELEVIL--NHQGLTPLKLAAKEGR 269

                          250       260       270
                   ....*....|....*....|....*....|
gi 694897886   785 ENCIEVLLEQKCF-RKFIGNPFTPLHCAII 813
Cdd:TIGR00870  270 IVLFRLKLAIKYKqKKFVAWPNGQQLLSLY 299
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 720-963 9.89e-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: 52.78  E-value: 9.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   720 QMLLE-QEVSILCKDSRGRTPLHYAAARGHATWLSELLQmalseedccFKDNQGY---TPLHWACYNGNENCIEVLLEQK 795
Cdd:TIGR00870   35 RDLEEpKKLNINCPDRLGRSALFVAAIENENLELTELLL---------NLSCRGAvgdTLLHAISLEYVDAVEAILLHLL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   796 CFRKFIGNPF--------------TPLHCAIINDHGNCASLLL--GAIDSSIVSCRDDK----------GRTPLHAAAFA 849
Cdd:TIGR00870  106 AAFRKSGPLElandqytseftpgiTALHLAAHRQNYEIVKLLLerGASVPARACGDFFVksqgvdsfyhGESPLNAAACL 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   850 DHVECLQLLLRHSAPVNAADNSGKTALMMAaengqagavdILVNSAQADltvkdkdlNTPLHLACSKGhekcALLILDKI 929
Cdd:TIGR00870  186 GSPSIVALLSEDPADILTADSLGNTLLHLL----------VMENEFKAE--------YEELSCQMYNF----ALSLLDKL 243

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 694897886   930 QD-ESLINAKNNALQTPLHVAARNGLKVVVEELLA 963
Cdd:TIGR00870  244 RDsKELEVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 774-964 2.78e-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: 2.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  774 TPLHWACYNGNENCIEVLLEQK----CFRKFIGNpfTPLHCAIINDHGNCASLLLGAIDSSI---VSCRDDKGRTPLHAA 846
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPscdlFQRGALGE--TALHVAALYDNLEAAVVLMEAAPELVnepMTSDLYQGETALHIA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  847 AFADHVECLQLLLRHSAPVNAADNS--------------GKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHL 912
Cdd:cd22192    97 VVNQNLNLVRELIARGADVVSPRATgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVLHI 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 694897886  913 ACSKGHEKCA------LLILDKIQDE-SLINAKNNALQTPLHVAARNGLKVVVEELLAK 964
Cdd:cd22192   176 LVLQPNKTFAcqmydlILSYDKEDDLqPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 140-168 4.65e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.12  E-value: 4.65e-06
                            10        20
                    ....*....|....*....|....*....
gi 694897886    140 GRTALHHAALNGHVEMVNLLLAKGANINA 168
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 4.75e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 4.75e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 694897886    10 PPLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLI 61
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 332-476 7.78e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.53  E-value: 7.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   332 IDCVDKDGNTPLHVAARYG-HELLINTLITSGA-----DTAkcgihsmfpLHLAALNAH---SDCCRKLLSSGFEIDTPD 402
Cdd:TIGR00870   45 INCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISLEYVdavEAILLHLLAAFRKSGPLE 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   403 ----------KFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKC--------------GRTPLHYAAANCHFHCIETLV 458
Cdd:TIGR00870  116 landqytsefTPGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLS 195

                          170
                   ....*....|....*...
gi 694897886   459 TTGANVNETDDWGRTALH 476
Cdd:TIGR00870  196 EDPADILTADSLGNTLLH 213
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 438-466 7.80e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 7.80e-04
                            10        20
                    ....*....|....*....|....*....
gi 694897886    438 GRTPLHYAAANCHFHCIETLVTTGANVNE 466
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 771-793 1.98e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 1.98e-03
                            10        20
                    ....*....|....*....|...
gi 694897886    771 QGYTPLHWACYNGNENCIEVLLE 793
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLD 23
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 669-697 4.62e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 4.62e-03
                            10        20
                    ....*....|....*....|....*....
gi 694897886    669 KGQTPLMLAVAYGHIDAVSLLLEKEANVD 697
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-343 4.75e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 184.77  E-value: 4.75e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   54 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSV 133
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  134 NVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 213
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  214 ASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALcLELLV 293
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 694897886  294 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 343
Cdd:COG0666   240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-307 2.75e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 176.68  E-value: 2.75e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   22 EEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVN 101
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  102 ARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAA 181
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  182 YMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDY 261
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 694897886  262 GANVNQPNNNGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGK 307
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
11-276 2.75e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 176.68  E-value: 2.75e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   11 PLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAV 90
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   91 QVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFD 170
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  171 KKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNG 250
Cdd:COG0666   184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263

                         250       260
                  ....*....|....*....|....*.
gi 694897886  251 QDAVVNELIDYGANVNQPNNNGFTPL 276
Cdd:COG0666   264 AALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-243 2.62e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 156.65  E-value: 2.62e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886    8 DQPPLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSE 87
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   88 EAVQVLIKHSADVNARDKNwqtplhvaaankavkcaeviipllssvnvsdrgGRTALHHAALNGHVEMVNLLLAKGANIN 167
Cdd:COG0666   167 EIVKLLLEAGADVNARDND---------------------------------GETPLHLAAENGHLEIVKLLLEAGADVN 213

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694897886  168 AFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTAL 243
Cdd:COG0666   214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 22-310 1.20e-39

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 154.03  E-value: 1.20e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   22 EEIRMLIHKTEDVNTLDSEKRTPLHVaaFLG-----DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAV-QVLIK 95
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDViKLLIK 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   96 HSADVNARDKNWQTPLHVAAANKAVkcaeviipllssvnvsdrggrtalhhaalngHVEMVNLLLAKGANINAFDKKDRR 175
Cdd:PHA03095  106 AGADVNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMT 154

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  176 ALHwaAYMGH----LDVVALLINHGAEVTCKDKKGYTPLHAAASNGQIN--VVKHLLNLGVEIDEINVYGNTALHIACYN 249
Cdd:PHA03095  155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694897886  250 G--QDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLELLvNNGADVNIQSKDGKSPL 310
Cdd:PHA03095  233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGNTPL 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
 86-359 3.29e-39

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 152.49  E-value: 3.29e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   86 SEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSS---VNVSDRGGRTALHHAALNGHVE-MVNLLLA 161
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAgadVNAPERCGFTPLHLYLYNATTLdVIKLLIK 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  162 KGANINAFDKKDRRALHwaAYMG----HLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINV--VKHLLNLGVEIDEI 235
Cdd:PHA03095  106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  236 NVYGNTALHIACYNGQD--AVVNELIDYGANVNQPNNNGFTPLHFAAA-STHGALCLELLVNNGADVNIQSKDGKSPLHM 312
Cdd:PHA03095  184 DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 694897886  313 TAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLI 359
Cdd:PHA03095  264 AAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
153-507 4.89e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.02  E-value: 4.89e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  153 VEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEI 232
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  233 DEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALcLELLVNNGADVNIQskdgksplhm 312
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI-VKLLLEAGADVNAQ---------- 149

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  313 tavhgrftrsqtliqnggeidcvDKDGNTPLHVAARYGHELLINTLITSGADtakcgihsmfplhlaalnahsdccrkll 392
Cdd:COG0666   150 -----------------------DNDGNTPLHLAAANGNLEIVKLLLEAGAD---------------------------- 178

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  393 ssgfeIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGR 472
Cdd:COG0666   179 -----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGL 253

                         330       340       350
                  ....*....|....*....|....*....|....*
gi 694897886  473 TALHYAAASDMDRNKTILGNAHENSEELERARELK 507
Cdd:COG0666   254 TALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 55-301 1.22e-36

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 144.04  E-value: 1.22e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   55 EIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAV-----KCAEVIIPL 129
Cdd:PHA03100   16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEY 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  130 LSSVNVSDRGGRTALHHAALN--GHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGH--LDVVALLINHGAEVTCKDKk 205
Cdd:PHA03100   96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNR- 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  206 gytplhaaasngqinvVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHG 285
Cdd:PHA03100  175 ----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238

                         250
                  ....*....|....*.
gi 694897886  286 ALcLELLVNNGADVNI 301
Cdd:PHA03100  239 EI-FKLLLNNGPSIKT 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
492-749 2.27e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 2.27e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  492 NAHENSEELERARELKEKEATLCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEESDSGATksPL 571
Cdd:COG0666    14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT--LL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  572 HLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLR 651
Cdd:COG0666    92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVK 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  652 LLLEI-ADnpeaVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSIL 730
Cdd:COG0666   171 LLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                         250
                  ....*....|....*....
gi 694897886  731 CKDSRGRTPLHYAAARGHA 749
Cdd:COG0666   247 AKDKDGLTALLLAAAAGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
515-795 4.23e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.85  E-value: 4.23e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  515 LEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEESDSGATKSPLHLAAYNGHHQALEVLLQSLVDLD 594
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  595 IRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEI-ADnpeaVDVKDAKGQTP 673
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAgAD----VNAQDNDGNTP 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  674 LMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLS 753
Cdd:COG0666   157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 694897886  754 ELLQMALSEEDccfKDNQGYTPLHWACYNGNENCIEVLLEQK 795
Cdd:COG0666   237 LLLEAGADLNA---KDKDGLTALLLAAAAGAALIVKLLLLAL 275
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 16-367 1.00e-33

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 135.48  E-value: 1.00e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   16 IFSGDPEEIRMLI-HKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLI 94
Cdd:PHA02874    9 IYSGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   95 KHSADVNArdknwqtplhvaaankavkcaeVIIPLLSSvnvsdrggrtalhhaalnghvEMVNLLLAKGANINAFDKKDR 174
Cdd:PHA02874   89 DNGVDTSI----------------------LPIPCIEK---------------------DMIKTILDCGIDVNIKDAELK 125

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  175 RALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAV 254
Cdd:PHA02874  126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  255 VNELIDYGANVNQPNNNGFTPLHfaAASTHGALCLELLVNNgADVNIQSKDGKSPLHMtAVHGRFTRS--QTLIQNGGEI 332
Cdd:PHA02874  206 IKLLIDHGNHIMNKCKNGFTPLH--NAIIHNRSAIELLINN-ASINDQDIDGSTPLHH-AINPPCDIDiiDILLYHKADI 281

                         330       340       350       360
                  ....*....|....*....|....*....|....*....|.
gi 694897886  333 DCVDKDGNTPLHVAARYGH------ELLINTLITSGADTAK 367
Cdd:PHA02874  282 SIKDNKGENPIDTAFKYINkdpvikDIIANAVLIKEADKLK 322
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
253-534 1.59e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.23  E-value: 1.59e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  253 AVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI 332
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  333 DCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAA 412
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  413 AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAASDMDRNKTILGN 492
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 694897886  493 AHENSEELERARELKEKEATLCLEFLLQNDANPSIRDKEGYN 534
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 26-364 2.88e-33

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 137.89  E-value: 2.88e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   26 MLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDK 105
Cdd:PHA02876  163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDL 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  106 NwqtpLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHV-EMVNLLLAKGANINAFDKKDRRALHWAAYMG 184
Cdd:PHA02876  243 S----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNG 318

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  185 H-LDVVALLINHGAEVTCKDKKGYTPLHAAAS-NGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYG 262
Cdd:PHA02876  319 YdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  263 ANVNQPNNNGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHG-RFTRSQTLIQNGGEIDCVDKDGNT 341
Cdd:PHA02876  399 ADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQY 478

                         330       340
                  ....*....|....*....|...
gi 694897886  342 PLHVAarYGHELLINTLITSGAD 364
Cdd:PHA02876  479 PLLIA--LEYHGIVNILLHYGAE 499
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
650-979 1.03e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.92  E-value: 1.03e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  650 LRLLLEIADNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSI 729
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  730 LCKDSRGRTPLHYAAARGHATWLSELLQmalSEEDCCFKDNQGYTPLHWACYNGNENCIEVLLEQKcfrkfignpftplh 809
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-------------- 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  810 cAIINdhgncaslllgaidssivsCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAADNSGKTALMMAAENGQAGAVD 889
Cdd:COG0666   144 -ADVN-------------------AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  890 ILVNsAQADLTVKDKDLNTPLHLACSKGHEKCALLILDKIQDeslINAKNNALQTPLHVAARNGLKVVVEELLAKGACVL 969
Cdd:COG0666   204 LLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279

                         330
                  ....*....|
gi 694897886  970 AVDENGHTPA 979
Cdd:COG0666   280 AALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
325-669 4.15e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.99  E-value: 4.15e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  325 LIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDKF 404
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  405 GRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAASdmd 484
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN--- 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  485 rnktilgnaheNSEELerarelkekeatlcLEFLLQNDANPSIRDKEGYnsihyaaayghrqclelllertnsgfeesds 564
Cdd:COG0666   164 -----------GNLEI--------------VKLLLEAGADVNARDNDGE------------------------------- 187

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  565 gatkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNVTKRTPLHASVIN 644
Cdd:COG0666   188 ----TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263

                         330       340
                  ....*....|....*....|....*
gi 694897886  645 GHTLCLRLLLEIADNPEAVDVKDAK 669
Cdd:COG0666   264 AALIVKLLLLALLLLAAALLDLLTL 288
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 56-385 1.57e-31

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 132.49  E-value: 1.57e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   56 IIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNV 135
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  136 SDrggrTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLD-VVALLINHGAEVTCKDKKGYTPLHAAA 214
Cdd:PHA02876  240 ND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMA 315

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  215 SNG-QINVVKHLLNLGVEIDEINVYGNTALHIACY--NGQDAVVNeLIDYGANVNQPNNNGFTPLHFAAAStHGALCLEL 291
Cdd:PHA02876  316 KNGyDTENIRTLIMLGADVNAADRLYITPLHQASTldRNKDIVIT-LLELGANVNARDYCDKTPIHYAAVR-NNVVIINT 393

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  292 LVNNGADVNIQSKDGKSPLHMtAVHGR--FTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHEL-LINTLITSGADTAKC 368
Cdd:PHA02876  394 LLDYGADIEALSQKIGTALHF-ALCGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAI 472

                         330
                  ....*....|....*..
gi 694897886  369 GIHSMFPLhLAALNAHS 385
Cdd:PHA02876  473 NIQNQYPL-LIALEYHG 488
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
683-997 8.52e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.14  E-value: 8.52e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  683 IDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALSE 762
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  763 EDccfKDNQGYTPLHWACYNGNENCIEVLLEQKcfrkfignpftplhcAIINDhgncaslllgaidssivscRDDKGRTP 842
Cdd:COG0666    81 NA---KDDGGNTLLHAAARNGDLEIVKLLLEAG---------------ADVNA-------------------RDKDGETP 123

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  843 LHAAAFADHVECLQLLLRHSAPVNAADNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLACSKGHEKCA 922
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLHLAAENGHLEIV 202

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694897886  923 LLILDKIQDeslINAKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVDENGHTPALACAPNKDVADCLALILA 997
Cdd:COG0666   203 KLLLEAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 123-465 1.87e-30

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 129.03  E-value: 1.87e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  123 AEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCK 202
Cdd:PHA02876  161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKN 240

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  203 DkkgyTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQ-DAVVNELIDYGANVNQPNNNGFTPLHFAAA 281
Cdd:PHA02876  241 D----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAK 316

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  282 STHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQ-TLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLIT 360
Cdd:PHA02876  317 NGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIViTLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  361 SGADtakcgihsmfplhLAALNahsdccrkllssgfeidtpDKFGrTCLHAAAAGGN-VECIKLLQSSGADFHKKDKCGR 439
Cdd:PHA02876  397 YGAD-------------IEALS-------------------QKIG-TALHFALCGTNpYMSVKTLIDRGANVNSKNKDLS 443

                         330       340
                  ....*....|....*....|....*..
gi 694897886  440 TPLHYAAA-NCHFHCIETLVTTGANVN 465
Cdd:PHA02876  444 TPLHYACKkNCKLDVIEMLLDNGADVN 470
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
515-740 5.50e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.83  E-value: 5.50e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  515 LEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEESDSGATksPLHLAAYNGHHQALEVLLQSLVDLD 594
Cdd:COG0666    70 ALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGET--PLHLAAYNGNLEIVKLLLEAGADVN 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  595 IRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLE-IADnpeaVDVKDAKGQTP 673
Cdd:COG0666   148 AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEaGAD----VNAKDNDGKTA 222

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694897886  674 LMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPL 740
Cdd:COG0666   223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 12-265 3.21e-28

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 122.09  E-value: 3.21e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   12 LVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGD-AEIIELLILSGARVNAKDNMWLTPLH-RAVASRSEEA 89
Cdd:PHA02876  244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYlMAKNGYDTEN 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   90 VQVLIKHSADVNARDKNWQTPLHVAAANKAVKcaEVIIPLL---SSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANI 166
Cdd:PHA02876  324 IRTLIMLGADVNAADRLYITPLHQASTLDRNK--DIVITLLelgANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  167 NAFDKKDRRALHWAAY-MGHLDVVALLINHGAEVTCKDKKGYTPLH-AAASNGQINVVKHLLNLGVEIDEINVYGNTALH 244
Cdd:PHA02876  402 EALSQKIGTALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHyACKKNCKLDVIEMLLDNGADVNAINIQNQYPLL 481

                         250       260
                  ....*....|....*....|.
gi 694897886  245 IACynGQDAVVNELIDYGANV 265
Cdd:PHA02876  482 IAL--EYHGIVNILLHYGAEL 500
PHA03095 PHA03095
ankyrin-like protein; Provisional
 212-475 1.13e-27

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 118.20  E-value: 1.13e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  212 AAASNGQINVVKHLLNLGVEIDEINVYGNTALH--IACYNGQDA-VVNELIDYGANVNQPNNNGFTPLHFAAASTHGALC 288
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  289 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGH---ELLiNTLITSGA 363
Cdd:PHA03095  100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGA 178

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  364 DTAKCGIHSMFPLHLAALNAHSD--CCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQ--SSGADFHKKDKCGR 439
Cdd:PHA03095  179 DVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPllIAGISINARNRYGQ 258

                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 694897886  440 TPLHYAAANCHFHCIETLVTTGANVNETDDWGRTAL 475
Cdd:PHA03095  259 TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 192-465 1.50e-27

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 116.69  E-value: 1.50e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  192 LINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIAC---YNGQDAV--VNELIDYGANVN 266
Cdd:PHA03100   21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikYNLTDVKeiVKLLLEYGANVN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  267 QPNNNGFTPLHFAAASTHGALCL-ELLVNNGADVNIQSKDGKSPLHMtavhgrFTRSqtliqnggeiDCVDKDgntplhv 345
Cdd:PHA03100  101 APDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHL------YLES----------NKIDLK------- 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  346 aaryghelLINTLITSGAD-TAKCGIHSmfplhlaalnahsdccrkLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLL 424
Cdd:PHA03100  158 --------ILKLLIDKGVDiNAKNRVNY------------------LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYL 211

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 694897886  425 QSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVN 465
Cdd:PHA03100  212 LDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 75-346 2.68e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 113.82  E-value: 2.68e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   75 LTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVA--AANKavkcaEVIIPLLSSVNVSDRG-GRTALHHAALNG 151
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckEPNK-----LGMKEMIRSINKCSVFyTLVAIKDAFNNR 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  152 HVEMVNLLLakganINAFDKK---DRRALHWAAYMGHLD--VVALLINHGAEVTCKDK-KGYTPLHAAASNGQINVVKHL 225
Cdd:PHA02878  113 NVEIFKIIL-----TNRYKNIqtiDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELL 187

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  226 LNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLELLVNNGADVNIQSK- 304
Cdd:PHA02878  188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYi 267

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 694897886  305 DGKSPLHMTAVHGRFTRsqTLIQNGGEIDCVDKDGNTPLHVA 346
Cdd:PHA02878  268 LGLTALHSSIKSERKLK--LLLEYGADINSLNSYKLTPLSSA 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 28-238 2.20e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 110.14  E-value: 2.20e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   28 IHKTEDVNT-LDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLH-----RAVASRSEEAVQVLIKHSADVN 101
Cdd:PHA03100   21 IIMEDDLNDySYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  102 ARDKNWQTPLHVAAANKavKCAEVIIPLLSS----VNVSDRGGRTALHHAALNGHV--EMVNLLLAKGANINAFDK---- 171
Cdd:PHA03100  101 APDNNGITPLLYAISKK--SNSYSIVEYLLDnganVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRvnyl 178

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694897886  172 ---------KDRR---ALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVY 238
Cdd:PHA03100  179 lsygvpiniKDVYgftPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA03095 PHA03095
ankyrin-like protein; Provisional
 254-622 1.63e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 102.41  E-value: 1.63e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  254 VVNELIDYGANVNQPNNNGFTPLHFAAASTHGAL--CLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTR-SQTLIQNGG 330
Cdd:PHA03095   29 EVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDvIKLLIKAGA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  331 EIDCVDKDGNTPLHVaaryghellintlitsgadtakcgihsmfplHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLH 410
Cdd:PHA03095  109 DVNAKDKVGRTPLHV-------------------------------YLSGFNINPKVIRLLLRKGADVNALDLYGMTPLA 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  411 A--AAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFH--CIETLVTTGANVNETDDWGRTALHYAAASDMDRN 486
Cdd:PHA03095  158 VllKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKR 237

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  487 KTILgnahenseelerarelkekeatlcleFLLQNDANPSIRDKEGYnsihyaaayghrqclelllertnsgfeesdsga 566
Cdd:PHA03095  238 SLVL--------------------------PLLIAGISINARNRYGQ--------------------------------- 258

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 694897886  567 tkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQ 622
Cdd:PHA03095  259 --TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 22-295 1.90e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 102.27  E-value: 1.90e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   22 EEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIK------ 95
Cdd:PHA02878   18 KYIEYIDHTENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcs 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   96 ------------HSADVNA-------RDKNWQTP--LHVAAANKAVKCAEVIIPLL----SSVNVSDR-GGRTALHHAAL 149
Cdd:PHA02878   98 vfytlvaikdafNNRNVEIfkiiltnRYKNIQTIdlVYIDKKSKDDIIEAEITKLLlsygADINMKDRhKGNTALHYATE 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  150 NGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASN-GQINVVKHLLNL 228
Cdd:PHA02878  178 NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEH 257

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694897886  229 GVEID-EINVYGNTALHIACYNGQdaVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLELLVNN 295
Cdd:PHA02878  258 GVDVNaKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISN 323
PHA03095 PHA03095
ankyrin-like protein; Provisional
 355-664 2.13e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 102.03  E-value: 2.13e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  355 INTLITSGADTAKCGIHSMFPLHLAALNAHSDC---CRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVE-CIKLLQSSGAD 430
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGAD 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  431 FHKKDKCGRTPLH-YAA-ANCHFHCIETLVTTGANVNETDDWGRTALHyaaasdmdrnktILgnahenseelerareLKE 508
Cdd:PHA03095  110 VNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLA------------VL---------------LKS 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  509 KEATL-CLEFLLQNDANPSIRDKEGYNSIHYAAAYGH--RQCLELLLERTNSGFEESDSGATksPLHLAAYNGHHQALEV 585
Cdd:PHA03095  163 RNANVeLLRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNT--PLHSMATGSSCKRSLV 240

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  586 --LLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADNPEAV 663
Cdd:PHA03095  241 lpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319


                  .
gi 694897886  664 D 664
Cdd:PHA03095  320 A 320
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 290-607 3.86e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 100.81  E-value: 3.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  290 ELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTakcg 369
Cdd:PHA02874   19 KIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDT---- 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  370 ihSMFPLHlaalNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANC 449
Cdd:PHA02874   95 --SILPIP----CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHN 168

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  450 HFHCIETLVTTGANVNETDDWGRTALHYAAasdmdrnktilgnahenseelerarelkEKEATLCLEFLLQNDANPSIRD 529
Cdd:PHA02874  169 FFDIIKLLLEKGAYANVKDNNGESPLHNAA----------------------------EYGDYACIKLLIDHGNHIMNKC 220

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  530 KEGYNSIHYAAAYgHRQCLELLLerTNSGFEESD-SGATksPLHLA-AYNGHHQALEVLLQSLVDLDIRDEKGRTALDLA 607
Cdd:PHA02874  221 KNGFTPLHNAIIH-NRSAIELLI--NNASINDQDiDGST--PLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-269 3.11e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 3.11e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   177 LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNlGVEIDEINvYGNTALHIACYNGQDAVVN 256
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 694897886   257 ELIDYGANVNQPN 269
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
144-236 5.25e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 5.25e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   144 LHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHgAEVTCKDkKGYTPLHAAASNGQINVVK 223
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 694897886   224 HLLNLGVEIDEIN 236
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 24-235 2.56e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 95.48  E-value: 2.56e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   24 IRMLIHKTEDVNTLDSEKRTPLHV--AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASR--SEEAVQVLIKHSAD 99
Cdd:PHA03095  100 IKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGAD 179

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  100 VNARDKNWQTPLHVAAAN--KAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNL--LLAKGANINAFDKKDRR 175
Cdd:PHA03095  180 VYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQT 259

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  176 ALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEI 235
Cdd:PHA03095  260 PLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 48-266 3.50e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 94.29  E-value: 3.50e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   48 AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 127
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  128 PLLSSVN-VSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKG 206
Cdd:PHA02875   89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694897886  207 YTPLHAAASNGQINVVKHLLNLGVEIDEINVYGN-TALHIACYNGQDAVVNELIDYGANVN 266
Cdd:PHA02875  169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 220-545 5.58e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 93.87  E-value: 5.58e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  220 NVVKHLLN-LGVEIDEINvygnTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLhFAAASTHGALCLELLVNNGAD 298
Cdd:PHA02874   19 KIIKNKGNcINISVDETT----TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPL-LTAIKIGAHDIIKLLIDNGVD 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  299 VNIqskdgkspLHMTAVHGRFTRsqTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHL 378
Cdd:PHA02874   94 TSI--------LPIPCIEKDMIK--TILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  379 AALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAanCHFHCIETLV 458
Cdd:PHA02874  164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI--IHNRSAIELL 241

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  459 TTGANVNETDDWGRTALHYAAASDMDRNktilgnahenseelerarelkekeatlCLEFLLQNDANPSIRDKEGYNSIHY 538
Cdd:PHA02874  242 INNASINDQDIDGSTPLHHAINPPCDID---------------------------IIDILLYHKADISIKDNKGENPIDT 294


                  ....*..
gi 694897886  539 AAAYGHR 545
Cdd:PHA02874  295 AFKYINK 301
Ank_2 pfam12796
Ankyrin repeats (3 copies);
111-203 3.32e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.24  E-value: 3.32e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   111 LHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKgANINAFDkKDRRALHWAAYMGHLDVVA 190
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 694897886   191 LLINHGAEVTCKD 203
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
210-302 8.20e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.09  E-value: 8.20e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   210 LHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYgANVNqPNNNGFTPLHFAAASTHGAlCL 289
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLE-IV 77

                           90
                   ....*....|...
gi 694897886   290 ELLVNNGADVNIQ 302
Cdd:pfam12796   78 KLLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 389-664 8.29e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.11  E-value: 8.29e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  389 RKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHF--HCIET---LVTTGAN 463
Cdd:PHA03100   19 KYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltDVKEIvklLLEYGAN 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  464 VNETDDWGRTALHYAAASDMDRNKTIlgnahenseelerarelkekeatlclEFLLQNDANPSIRDKEGYNSIHYAAAYG 543
Cdd:PHA03100   99 VNAPDNNGITPLLYAISKKSNSYSIV--------------------------EYLLDNGANVNIKNSDGENLLHLYLESN 152

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  544 HR--QCLELLLERTNsgfeesdsgatksplHLAAYNghhqALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALIN 621
Cdd:PHA03100  153 KIdlKILKLLIDKGV---------------DINAKN----RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLD 213

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 694897886  622 QGASIFVKDNVTKrTPLHASVINGHTLCLRLLLEIADNPEAVD 664
Cdd:PHA03100  214 LGANPNLVNKYGD-TPLHIAILNNNKEIFKLLLNNGPSIKTII 255
PHA03095 PHA03095
ankyrin-like protein; Provisional
 651-966 1.57e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 90.08  E-value: 1.57e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  651 RLLLEIADnpeaVDVKDAKGQTPLMLAVAYGH---IDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEE-CVQMLLEQE 726
Cdd:PHA03095   32 RLLAAGAD----VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  727 VSILCKDSRGRTPLH-YAA-ARGHATWLSELLQMALSEEDCcfkDNQGYTPLHwaCYNGNENC----IEVLLEQKCF--- 797
Cdd:PHA03095  108 ADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNAL---DLYGMTPLA--VLLKSRNAnvelLRLLIDAGADvya 182

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  798 RKFIGNpfTPLH--CAIINDHGNCASLLLGAIDSsiVSCRDDKGRTPLHAAAFADHVECLQL--LLRHSAPVNAADNSGK 873
Cdd:PHA03095  183 VDDRFR--SLLHhhLQSFKPRARIVRELIRAGCD--PAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQ 258

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  874 TALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLACSKGHEKCALLILDKIQDESLINAKNNALQTPLHVAARNG 953
Cdd:PHA03095  259 TPLHYAAVFNNPRACRRLIA-LGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTASVAGGDIPSDA 337

                         330
                  ....*....|...
gi 694897886  954 LKVVVEELLAKGA 966
Cdd:PHA03095  338 TRLCVAKVVLRGA 350
Ank_2 pfam12796
Ankyrin repeats (3 copies);
376-468 1.91e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.91e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   376 LHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLqSSGADFHKKDKcGRTPLHYAAANCHFHCIE 455
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 694897886   456 TLVTTGANVNETD 468
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
604-700 5.31e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 5.31e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   604 LDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADnpeaVDVKDaKGQTPLMLAVAYGHI 683
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHL 74

                           90
                   ....*....|....*..
gi 694897886   684 DAVSLLLEKEANVDTVD 700
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
45-170 1.60e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 1.60e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886    45 LHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHsADVNARDKnwqtplhvaaankavkcae 124
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN------------------- 60

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 694897886   125 viipllssvnvsdrgGRTALHHAALNGHVEMVNLLLAKGANINAFD 170
Cdd:pfam12796   61 ---------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 571-869 2.43e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 85.79  E-value: 2.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  571 LHLAAYNGHHQALEVLLQSLVD-LDIRDEKGRTALDLAAFKGHTECVEALINQGASI-FVKDNVTKrtPLHASVINGHTL 648
Cdd:PHA02874    5 LRMCIYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADInHINTKIPH--PLLTAIKIGAHD 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  649 CLRLLLE--------------------IADNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALH 708
Cdd:PHA02874   83 IIKLLIDngvdtsilpipciekdmiktILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIH 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  709 RGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALSEEDCCfkdNQGYTPLHWACYNgNENCI 788
Cdd:PHA02874  163 IAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKC---KNGFTPLHNAIIH-NRSAI 238

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  789 EVLLEQKCFRKFIGNPFTPLHCAIIN--DHGNCASLLLGAIDSSIvscRDDKGRTPLHAA-AFADHVECLQLLLRHSAPV 865
Cdd:PHA02874  239 ELLINNASINDQDIDGSTPLHHAINPpcDIDIIDILLYHKADISI---KDNKGENPIDTAfKYINKDPVIKDIIANAVLI 315


                  ....
gi 694897886  866 NAAD 869
Cdd:PHA02874  316 KEAD 319
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 254-465 3.01e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 85.43  E-value: 3.01e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  254 VVNELIDYGANVNQPNNNGFTPLHFAAaSTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI- 332
Cdd:PHA02875   17 IARRLLDIGINPNFEIYDGISPIKLAM-KFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAd 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  333 DCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAA 412
Cdd:PHA02875   96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 694897886  413 AAGGNVECIKLLQSSGA--DFHKKDKCgRTPLHYAAANCHFHCIETLVTTGANVN 465
Cdd:PHA02875  176 MAKGDIAICKMLLDSGAniDYFGKNGC-VAALCYAIENNKIDIVRLFIKRGADCN 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
571-664 7.65e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.69  E-value: 7.65e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   571 LHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQgasIFVKDNVTKRTPLHASVINGHTLCL 650
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 694897886   651 RLLLEIADNPEAVD 664
Cdd:pfam12796   78 KLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 74-281 8.10e-17

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: 85.45  E-value: 8.10e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   74 WLTPLHRAVASRSEEAVQVLIK-HSADVNARDKNWQTPLHVAAANKAVKCAEVII---PLLssVNV---SD-RGGRTALH 145
Cdd:cd22192    17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaaPEL--VNEpmtSDlYQGETALH 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  146 HAALNGHVEMVNLLLAKGANIN------AFDKKDRRAL-----H---WAAYMGHLDVVALLINHGAEVTCKDKKGYTPLH 211
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694897886  212 AAASNGQINVVKH----LLNLGVEIDEINVYgntalHIacyngqdavvnelidyganvnqPNNNGFTPLHFAAA 281
Cdd:cd22192   175 ILVLQPNKTFACQmydlILSYDKEDDLQPLD-----LV----------------------PNNQGLTPFKLAAK 221
Ank_2 pfam12796
Ankyrin repeats (3 copies);
843-939 1.97e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.97e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   843 LHAAAFADHVECLQLLLRHSAPVNAADNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKdlnTPLHLACSKGHEKCA 922
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77

                           90
                   ....*....|....*..
gi 694897886   923 LLILDKIQDeslINAKN 939
Cdd:pfam12796   78 KLLLEKGAD---INVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 683-1016 2.07e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.15  E-value: 2.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  683 IDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEEC---VQMLLEQEVSILCKDSRGRTPLHYaaarghatwlseLLQMA 759
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHL------------YLYNA 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  760 LSEE----------DCCFKDNQGYTPLHwACYNG---NENCIEVLLEQKcfrkfignpftplhcAIINDhgncaslllga 826
Cdd:PHA03095   95 TTLDvikllikagaDVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKG---------------ADVNA----------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  827 idssivscRDDKGRTPLHA---AAFADhVECLQLLLRHSAPVNAADNSGKTALMMAAEN--GQAGAVDILVnSAQADLTV 901
Cdd:PHA03095  148 --------LDLYGMTPLAVllkSRNAN-VELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELI-RAGCDPAA 217

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  902 KDKDLNTPLHLACSKGHEKcALLILDKIQDESLINAKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVDENGHTP-AL 980
Cdd:PHA03095  218 TDMLGNTPLHSMATGSSCK-RSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPlSL 296

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 694897886  981 AcapnkdVADCLALILATMMPFSPSSTMMAVNFVCL 1016
Cdd:PHA03095  297 M------VRNNNGRAVRAALAKNPSAETVAATLNTA 326
Ank_2 pfam12796
Ankyrin repeats (3 copies);
638-733 2.25e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 2.25e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   638 LHASVINGHTLCLRLLLEiadNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKeANVDTVDiLGCTALHRGIMTGHEE 717
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLE---NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 694897886   718 CVQMLLEQEVSILCKD 733
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
12-104 3.02e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.77  E-value: 3.02e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886    12 LVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLiLSGARVNAKDNMWlTPLHRAVASRSEEAVQ 91
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDNGR-TALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 694897886    92 VLIKHSADVNARD 104
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 20-170 6.33e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 81.85  E-value: 6.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   20 DPEEIRMLIHKTEDVNTLDSEK-RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSA 98
Cdd:PHA02878  146 EAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694897886   99 DVNARDKNWQTPLHVAAAnkAVKCAEVIIPLL---SSVNV-SDRGGRTALHHAALNGHVemVNLLLAKGANINAFD 170
Cdd:PHA02878  226 STDARDKCGNTPLHISVG--YCKDYDILKLLLehgVDVNAkSYILGLTALHSSIKSERK--LKLLLEYGADINSLN 297
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 233-550 7.82e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 81.46  E-value: 7.82e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  233 DEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLELL-VNNGADVNIQSKDGKSPLH 311
Cdd:PHA02878   31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIrSINKCSVFYTLVAIKDAFN 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  312 MTAVH-------GRFTRSQTLiqNGGEIDCVDKDGNTPLHVaaryghellINTLITSGADTAKCGIHSM-FPLHLAALNA 383
Cdd:PHA02878  111 NRNVEifkiiltNRYKNIQTI--DLVYIDKKSKDDIIEAEI---------TKLLLSYGADINMKDRHKGnTALHYATENK 179

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  384 HSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANC-HFHCIETLVTTGA 462
Cdd:PHA02878  180 DQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCkDYDILKLLLEHGV 259

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  463 NVN-ETDDWGRTALHYAAASDMDRNKTILGNAHENSEELERARELKEKEAT-LCLE--------FLLQNDANPSIRDKEG 532
Cdd:PHA02878  260 DVNaKSYILGLTALHSSIKSERKLKLLLEYGADINSLNSYKLTPLSSAVKQyLCINigrilisnICLLKRIKPDIKNSEG 339

                         330
                  ....*....|....*...
gi 694897886  533 YnSIHYAAAYGHRQCLEL 550
Cdd:PHA02878  340 F-IDNMDCITSNKRLNQI 356
Ank_2 pfam12796
Ankyrin repeats (3 copies);
776-869 1.10e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 1.10e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   776 LHWACYNGNENCIEVLLEQKC-FRKFIGNPFTPLHCAIINDHGNCASLLLGAIDSSIvscrDDKGRTPLHAAAFADHVEC 854
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL----KDNGRTALHYAARSGHLEI 76

                           90
                   ....*....|....*
gi 694897886   855 LQLLLRHSAPVNAAD 869
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
707-796 1.56e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 1.56e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   707 LHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALSEEdccfkDNQGYTPLHWACYNGNEN 786
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAARSGHLE 75

                           90
                   ....*....|
gi 694897886   787 CIEVLLEQKC 796
Cdd:pfam12796   76 IVKLLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
536-630 1.98e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 1.98e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   536 IHYAAAYGHRQCLELLLERTNSGFEESDSGATksPLHLAAYNGHHQALEVLLQSlVDLDIRDEkGRTALDLAAFKGHTEC 615
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRT--ALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEI 76

                           90
                   ....*....|....*
gi 694897886   616 VEALINQGASIFVKD 630
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 584-966 2.18e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 80.88  E-value: 2.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  584 EVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGA--SIFVKDNVTkrtplhasvinghtlclrlLLEIADNPE 661
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGAdvNIIALDDLS-------------------VLECAVDSK 222

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  662 AVDVKDA---------KGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGH-EECVQMLLEQEVSILC 731
Cdd:PHA02876  223 NIDTIKAiidnrsninKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNA 302

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  732 KDSRGRTPLHYAAARGHATwlSELLQMALSEEDCCFKDNQGYTPLHWA-CYNGNENCIEVLLEqkcfrkfignpftplhc 810
Cdd:PHA02876  303 KNIKGETPLYLMAKNGYDT--ENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLE----------------- 363

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  811 aiindhgncasllLGAidssIVSCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAADNSGKTALMMA-AENGQAGAVD 889
Cdd:PHA02876  364 -------------LGA----NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVK 426

                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 694897886  890 ILVNSAqADLTVKDKDLNTPLHLACSKgheKCALLILDKIQDESL-INAKNNALQTPLHVAArnGLKVVVEELLAKGA 966
Cdd:PHA02876  427 TLIDRG-ANVNSKNKDLSTPLHYACKK---NCKLDVIEMLLDNGAdVNAINIQNQYPLLIAL--EYHGIVNILLHYGA 498
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 515-725 2.44e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 79.65  E-value: 2.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  515 LEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLerTNSGFEESDSGATKSPLHLAAYNGHHQALEVLLQS--LVD 592
Cdd:PHA02875   18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLM--KHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLgkFAD 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  593 lDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKdNVTKRTPLHASVINGHTLCLRLLLeiaDNPEAVDVKDAKGQT 672
Cdd:PHA02875   96 -DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP-NTDKFSPLHLAVMMGDIKGIELLI---DHKACLDIEDCCGCT 170

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 694897886  673 PLMLAVAYGHIDAVSLLLEKEANVDTVDILGC-TALHRGIMTGHEECVQMLLEQ 725
Cdd:PHA02875  171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKR 224
PHA02798 PHA02798
ankyrin-like protein; Provisional
 78-364 3.13e-15

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 79.88  E-value: 3.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   78 LHRAvaSRSEEAVQVLIKHSADVNARDKNWQTPLhvaaankavkCAeviipLLSsvNVSDrggrtalhhaaLNGHVEMVN 157
Cdd:PHA02798   44 LQRD--SPSTDIVKLFINLGANVNGLDNEYSTPL----------CT-----ILS--NIKD-----------YKHMLDIVK 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  158 LLLAKGANINAFDKKDRRALHWA---AYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNG---QINVVKHLLNLGVE 231
Cdd:PHA02798   94 ILIENGADINKKNSDGETPLYCLlsnGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVD 173

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  232 IDEI-NVYGNTALHiaCY-----NGQDA-VVNELIDYGANVNQPNNngftplhfAAASTHGALCLELLVNNG-------- 296
Cdd:PHA02798  174 INTHnNKEKYDTLH--CYfkyniDRIDAdILKLFVDNGFIINKENK--------SHKKKFMEYLNSLLYDNKrfkknild 243

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694897886  297 ---ADVNIQSKD--GKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGAD 364
Cdd:PHA02798  244 fifSYIDINQVDelGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 549-731 4.76e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 79.91  E-value: 4.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  549 ELLLERTnsgfEESDSGATKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFV 628
Cdd:PLN03192  511 DLLGDNG----GEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI 586

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  629 KDnVTKRTPLHASVINGHTLCLRLLLEIA--DNPEAvdvkdakGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTA 706
Cdd:PLN03192  587 RD-ANGNTALWNAISAKHHKIFRILYHFAsiSDPHA-------AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658

                         170       180
                  ....*....|....*....|....*
gi 694897886  707 LHRGIMTGHEECVQMLLEQEVSILC 731
Cdd:PLN03192  659 LQVAMAEDHVDMVRLLIMNGADVDK 683
PHA03095 PHA03095
ankyrin-like protein; Provisional
 17-168 1.02e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.14  E-value: 1.02e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   17 FSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVaaFLG----DAEIIELLILSGARVNAKDNMWLTPLHR-AVASRSEEAV- 90
Cdd:PHA03095  128 FNINPKVIRLLLRKGADVNALDLYGMTPLAV--LLKsrnaNVELLRLLIDAGADVYAVDDRFRSLLHHhLQSFKPRARIv 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   91 QVLIKHSADVNARDKNWQTPLHVAAANKAVKcAEVIIPLL---SSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANIN 167
Cdd:PHA03095  206 RELIRAGCDPAATDMLGNTPLHSMATGSSCK-RSLVLPLLiagISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284


                  .
gi 694897886  168 A 168
Cdd:PHA03095  285 A 285
Ank_2 pfam12796
Ankyrin repeats (3 copies);
674-748 1.25e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 1.25e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694897886   674 LMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEvsILCKDSRGRTPLHYAAARGH 748
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--DVNLKDNGRTALHYAARSGH 73
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 9-167 1.74e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.95  E-value: 1.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886    9 QPPLVQAIFSGDPEEIRMLIHKTEDVNTLDSEK-RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSE 87
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   88 EAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVN-VSDRGGRTALHHAALNGHVEMVNLLLAKGANI 166
Cdd:PHA02875  149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGADC 228


                  .
gi 694897886  167 N 167
Cdd:PHA02875  229 N 229
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 720-973 2.11e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.80  E-value: 2.11e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  720 QMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMAlseEDCCFKDNQGYTPLHWACYNGNENCIEVLLEQkcfRK 799
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYG---ADVNIIALDDLSVLECAVDSKNIDTIKAIIDN---RS 235

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  800 FIGNPFTPLHCAIINDHGNCASLLLGAIDSsiVSCRDDKGRTPLHAAAFADHVECL-QLLLRHSAPVNAADNSGKTALMM 878
Cdd:PHA02876  236 NINKNDLSLLKAIRNEDLETSLLLYDAGFS--VNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYL 313

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  879 AAENGQAGAVDILVNSAQADLTVKDKDLNTPLHLACSKGHEKCALLILdkIQDESLINAKNNALQTPLHVAARNGLKVVV 958
Cdd:PHA02876  314 MAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITL--LELGANVNARDYCDKTPIHYAAVRNNVVII 391

                         250
                  ....*....|....*
gi 694897886  959 EELLAKGACVLAVDE 973
Cdd:PHA02876  392 NTLLDYGADIEALSQ 406
Ank_2 pfam12796
Ankyrin repeats (3 copies);
343-435 7.05e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.22  E-value: 7.05e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   343 LHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSgFEIDTPDKfGRTCLHAAAAGGNVECIK 422
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 694897886   423 LLQSSGADFHKKD 435
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
876-972 9.27e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.83  E-value: 9.27e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   876 LMMAAENGQAGAVDILVNSaQADLTVKDKDLNTPLHLACSKGHEKCALLILDKIQdeslINAKNNAlQTPLHVAARNGLK 955
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD----VNLKDNG-RTALHYAARSGHL 74

                           90
                   ....*....|....*..
gi 694897886   956 VVVEELLAKGACVLAVD 972
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
PHA02798 PHA02798
ankyrin-like protein; Provisional
 55-266 2.67e-13

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 73.72  E-value: 2.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   55 EIIELLILSGARVNAKDNMWLTPLHRAVASRSE-----EAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPL 129
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFM 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  130 L---SSVNVSDRGGRTALHHAALNGH---VEMVNLLLAKGANINAFDKKDR-RALHwaAYMGH------LDVVALLINHG 196
Cdd:PHA02798  132 IengADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNNKEKyDTLH--CYFKYnidridADILKLFVDNG 209

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  197 ---------------------------------------AEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINV 237
Cdd:PHA02798  210 fiinkenkshkkkfmeylnsllydnkrfkknildfifsyIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITE 289

                         250       260
                  ....*....|....*....|....*....
gi 694897886  238 YGNTALHIACYNGQDAVVNELIDYGANVN 266
Cdd:PHA02798  290 LGNTCLFTAFENESKFIFNSILNKKPNKN 318
Ank_2 pfam12796
Ankyrin repeats (3 copies);
740-824 4.63e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.91  E-value: 4.63e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   740 LHYAAARGHATWLSELLQmalSEEDCCFKDNQGYTPLHWACYNGNENCIEVLLEQKCFRKFiGNPFTPLHCAIINDHGNC 819
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLE---NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-DNGRTALHYAARSGHLEI 76


                   ....*
gi 694897886   820 ASLLL 824
Cdd:pfam12796   77 VKLLL 81
Ank_2 pfam12796
Ankyrin repeats (3 copies);
514-597 9.06e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.14  E-value: 9.06e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   514 CLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSgfEESDSGATksPLHLAAYNGHHQALEVLLQSLVDL 593
Cdd:pfam12796   12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRT--ALHYAARSGHLEIVKLLLEKGADI 87


                   ....
gi 694897886   594 DIRD 597
Cdd:pfam12796   88 NVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 567-908 9.42e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 72.40  E-value: 9.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  567 TKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKD---------------- 630
Cdd:PHA02876  178 CITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDlsllkairnedletsl 257

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  631 ------------NVTKRTPLHASVingHTLCL-RLLLEIADNPEAVDVKDAKGQTPLMLAVAYGH-IDAVSLLLEKEANV 696
Cdd:PHA02876  258 llydagfsvnsiDDCKNTPLHHAS---QAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADV 334

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  697 DTVDILGCTALHRG-IMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALSEEDCCFKDNqgyTP 775
Cdd:PHA02876  335 NAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG---TA 411

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  776 LHWACYNgnencievlleqkcfrkfiGNPFTPLHCAIinDHGncaslllgaidsSIVSCRDDKGRTPLHAAAFAD-HVEC 854
Cdd:PHA02876  412 LHFALCG-------------------TNPYMSVKTLI--DRG------------ANVNSKNKDLSTPLHYACKKNcKLDV 458

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 694897886  855 LQLLLRHSAPVNAADNSGKTALMMAAenGQAGAVDILVNSAQA--DLTVKDKDLNT 908
Cdd:PHA02876  459 IEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAElrDSRVLHKSLND 512
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 638-908 9.96e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.62  E-value: 9.96e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  638 LHASVINGHTLCLRLLLE--IADNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGH 715
Cdd:PHA03100    1 LYSYIVLTKSRIIKVKNIkyIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKY 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  716 E-----ECVQMLLEQEVSILCKDSRGRTPLHYAAAR--GHATWLSELLQMALSEEDccfKDNQGYTPLHWA--CYNGNEN 786
Cdd:PHA03100   81 NltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNI---KNSDGENLLHLYleSNKIDLK 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  787 CIEVLLEqkcfrkfignpftplHCAIINDHGNCASLL-LGA-IDSsivscRDDKGRTPLHAAAFADHVECLQLLLRHSAP 864
Cdd:PHA03100  158 ILKLLID---------------KGVDINAKNRVNYLLsYGVpINI-----KDVYGFTPLHYAVYNNNPEFVKYLLDLGAN 217

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 694897886  865 VNAADNSGKTALMMAAENGQAGAVDILVNSAQADLTV-------KDKDLNT 908
Cdd:PHA03100  218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIietllyfKDKDLNT 268
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 48-201 1.10e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 72.21  E-value: 1.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   48 AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 127
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694897886  128 PLLSSVNVSDRGgrTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTC 201
Cdd:PLN03192  612 HFASISDPHAAG--DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 309-610 2.33e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 70.68  E-value: 2.33e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  309 PLHMtAVHGR-FTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSgadTAKCGI-HSMFPLHLAALNAHSD 386
Cdd:PHA02878   40 PLHQ-AVEARnLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS---INKCSVfYTLVAIKDAFNNRNVE 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  387 CCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDK-CGRTPLHYAAANCHFHCIETLVTTGANVN 465
Cdd:PHA02878  116 IFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVN 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  466 ETDDWGRTALHYAAASdmdRNKTIlgnahenseelerarelkekeatlcLEFLLQNDANPSIRDKEGYNSIHYAAAY-GH 544
Cdd:PHA02878  196 IPDKTNNSPLHHAVKH---YNKPI-------------------------VHILLENGASTDARDKCGNTPLHISVGYcKD 247

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694897886  545 RQCLELLLERTNSGFEESdSGATKSPLHLAAYNghHQALEVLLQSLVDLDIRDEKGRTALDLAAFK 610
Cdd:PHA02878  248 YDILKLLLEHGVDVNAKS-YILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 166-445 4.25e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.91  E-value: 4.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  166 INAFDKKDRRA----------LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEI 235
Cdd:PHA02878   20 IEYIDHTENYStsaslipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVF 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  236 NVYgnTALHIACYNGQDAVVNELIdyganVNQPNNNGFTPLHFAAASTHG----ALCLELLVNNGADVNIQSKD-GKSPL 310
Cdd:PHA02878  100 YTL--VAIKDAFNNRNVEIFKIIL-----TNRYKNIQTIDLVYIDKKSKDdiieAEITKLLLSYGADINMKDRHkGNTAL 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  311 HMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHS-DCCR 389
Cdd:PHA02878  173 HYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILK 252

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 694897886  390 KLLSSGFEIDTPDKF-GRTCLHAAAAGGNVecIKLLQSSGADFHKKDKCGRTPLHYA 445
Cdd:PHA02878  253 LLLEHGVDVNAKSYIlGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 391-743 4.93e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.09  E-value: 4.93e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  391 LLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNetddw 470
Cdd:PHA02876  164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN----- 238

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  471 grtalhyaaasdmdRNKTILGNAHENsEELERArelkekeatlclefLLQNDANPSIRDKEGYNSihyaaayghrqclel 550
Cdd:PHA02876  239 --------------KNDLSLLKAIRN-EDLETS--------------LLLYDAGFSVNSIDDCKN--------------- 274

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  551 llertnsgfeesdsgatkSPLHLAAYNGHHQAL-EVLLQSLVDLDIRDEKGRTALDLAAFKGH-TECVEALINQGASIFV 628
Cdd:PHA02876  275 ------------------TPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNA 336

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  629 KDNVTKrTPLH-ASVINGHTLCLRLLLEIADNpeaVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTAL 707
Cdd:PHA02876  337 ADRLYI-TPLHqASTLDRNKDIVITLLELGAN---VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTAL 412

                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 694897886  708 HRGIM-TGHEECVQMLLEQEVSILCKDSRGRTPLHYA 743
Cdd:PHA02876  413 HFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
Ank_4 pfam13637
Ankyrin repeats (many copies);
140-193 5.19e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.52  E-value: 5.19e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 694897886   140 GRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLI 193
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
174-226 1.05e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.75  E-value: 1.05e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 694897886   174 RRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLL 226
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 774-992 1.11e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.07  E-value: 1.11e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  774 TPLHWACYNGNENCIEVLLEQKCFRKFIG-NPFTPLHCAI-INDHGNCASLLLGAIDSSI-------------------- 831
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINtKIPHPLLTAIkIGAHDIIKLLIDNGVDTSIlpipciekdmiktildcgid 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  832 VSCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAADNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLH 911
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLH 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  912 LACSKGHEKCALLILDkiqDESLINAKNNALQTPLHVAARNGLKVVveELLAKGACVLAVDENGHTP---ALACAPNKDV 988
Cdd:PHA02874  196 NAAEYGDYACIKLLID---HGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPlhhAINPPCDIDI 270


                  ....
gi 694897886  989 ADCL 992
Cdd:PHA02874  271 IDIL 274
Ank_2 pfam12796
Ankyrin repeats (3 copies);
310-402 1.44e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.67  E-value: 1.44e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   310 LHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGAdtAKCGIHSMFPLHLAALNAHSDCCR 389
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 694897886   390 KLLSSGFEIDTPD 402
Cdd:pfam12796   79 LLLEKGADINVKD 91
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 49-280 1.64e-11

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: 68.57  E-value: 1.64e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886    49 AFLGDAEIIELLILSGARVNAK-------DNMWLTPLHRAVA-SRSEEAVQVLIKHSADVNARDknwqTPLHVAAANKAV 120
Cdd:TIGR00870   20 AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAISLEYVD 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   121 KCAEVIIPLLSS---------VNVSDRG----GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRA----- 176
Cdd:TIGR00870   96 AVEAILLHLLAAfrksgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDsfyhg 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   177 ---LHWAAYMGHLDVVALLINHGAEVTCKDKKGytplhaaasngqiNVVKHLLNLGVEideiNVYGNTALHIACYngqda 253
Cdd:TIGR00870  176 espLNAAACLGSPSIVALLSEDPADILTADSLG-------------NTLLHLLVMENE----FKAEYEELSCQMY----- 233

                          250       260       270
                   ....*....|....*....|....*....|....
gi 694897886   254 vvNELIDYGANVNQ-------PNNNGFTPLHFAA 280
Cdd:TIGR00870  234 --NFALSLLDKLRDskeleviLNHQGLTPLKLAA 265
Ank_2 pfam12796
Ankyrin repeats (3 copies);
276-364 1.86e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 1.86e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   276 LHFAAASTHgALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNgGEIDCVDkDGNTPLHVAARYGHELLI 355
Cdd:pfam12796    1 LHLAAKNGN-LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77


                   ....*....
gi 694897886   356 NTLITSGAD 364
Cdd:pfam12796   78 KLLLEKGAD 86
Ank_4 pfam13637
Ankyrin repeats (many copies);
405-458 2.06e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 2.06e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 694897886   405 GRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLV 458
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 183-374 2.66e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.97  E-value: 2.66e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  183 MGHLDVVALLINHGAEVTckDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYG 262
Cdd:PLN03192  504 LHDLNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  263 ANVNQPNNNGFTPLHFAAASTHGALcLELLVNNGADVNIQSkdGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTP 342
Cdd:PLN03192  582 CNVHIRDANGNTALWNAISAKHHKI-FRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658

                         170       180       190
                  ....*....|....*....|....*....|..
gi 694897886  343 LHVAARYGHELLINTLITSGADTAKCGIHSMF 374
Cdd:PLN03192  659 LQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 107-359 7.16e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 66.19  E-value: 7.16e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  107 WQTPLHVAAANKAVKCaevIIPLL--SSVNVSDRG--GRTALHHAALNGHVEMVNLLLakganinafdkkdrralhwaay 182
Cdd:cd22192    17 SESPLLLAAKENDVQA---IKKLLkcPSCDLFQRGalGETALHVAALYDNLEAAVVLM---------------------- 71

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  183 mghlDVVALLINHgaEVTCkdkkgytplhaaasngqinvvkhllnlgveideiNVY-GNTALHIACYNGQDAVVNELIDY 261
Cdd:cd22192    72 ----EAAPELVNE--PMTS----------------------------------DLYqGETALHIAVVNQNLNLVRELIAR 111

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  262 GANVNQPNNNG--FT------------PLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI- 326
Cdd:cd22192   112 GADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEI-VRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYd 190

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 694897886  327 --------QNGGEIDCV-DKDGNTPLHVAARYGHELLINTLI 359
Cdd:cd22192   191 lilsydkeDDLQPLDLVpNNQGLTPFKLAAKEGNIVMFQHLV 232
PHA02798 PHA02798
ankyrin-like protein; Provisional
 129-412 7.34e-11

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 66.01  E-value: 7.34e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  129 LLSSVNVSDRGGRTALHHAAL---NGHVEMVNLLLAKGANINAFDKKDRRAL-----HWAAYMGHLDVVALLINHGAEVT 200
Cdd:PHA02798   24 LIKSCNPNEIVNEYSIFQKYLqrdSPSTDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADIN 103

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  201 CKDKKGYTPLHAAASNGQIN---VVKHLLNLGVEIDEINVYGNTALHIACYNG---QDAVVNELIDYGANVNQPNNN-GF 273
Cdd:PHA02798  104 KKNSDGETPLYCLLSNGYINnleILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDINTHNNKeKY 183

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  274 TPLHFAAASTHGAL---CLELLVNNGADVNIQSKDGKSPLHMTAVhgrftrsqTLIQNGGEidcVDKDgntplhvaaryg 350
Cdd:PHA02798  184 DTLHCYFKYNIDRIdadILKLFVDNGFIINKENKSHKKKFMEYLN--------SLLYDNKR---FKKN------------ 240

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694897886  351 hellINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAA 412
Cdd:PHA02798  241 ----ILDFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 150-275 9.15e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 62.53  E-value: 9.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  150 NGHVEMVNLLLAKGANINAFDKKDRRAL--HWAAYMGHL--DVVALLINHGAEVTCKDKKGYTPLHAAASNG--QINVVK 223
Cdd:PHA02859   63 KVNVEILKFLIENGADVNFKTRDNNLSAlhHYLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHMYMCNFnvRINVIK 142

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 694897886  224 HLLNLGVEIDEINVYGNTALH-IACYNGQDAVVNELIDYGANVNQPNNNGFTP 275
Cdd:PHA02859  143 LLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 147-276 1.27e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 65.66  E-value: 1.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  147 AALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPL---------------- 210
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrily 611

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  211 --------HA-------AASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPN-NNGFT 274
Cdd:PLN03192  612 hfasisdpHAagdllctAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDDDFS 691


                  ..
gi 694897886  275 PL 276
Cdd:PLN03192  692 PT 693
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 441-678 1.56e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.90  E-value: 1.56e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  441 PLHYAAANCHFHCIETLVTTGANVNETDDWGRTALH--------------------------YAAASDMDRN------KT 488
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHiickepnklgmkemirsinkcsvfytLVAIKDAFNNrnveifKI 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  489 ILGNAHENSEELErARELKEKEATLCLE-----FLLQNDANPSIRDKEGYNS-IHYAAAYGHRQCLELLLERtnsGFE-E 561
Cdd:PHA02878  120 ILTNRYKNIQTID-LVYIDKKSKDDIIEaeitkLLLSYGADINMKDRHKGNTaLHYATENKDQRLTELLLSY---GANvN 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  562 SDSGATKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLA-AFKGHTECVEALINQGASIFVKDNVTKRTPLHA 640
Cdd:PHA02878  196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILGLTALHS 275

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 694897886  641 SVINGHTlcLRLLLEIADNPEAVdvkDAKGQTPLMLAV 678
Cdd:PHA02878  276 SIKSERK--LKLLLEYGADINSL---NSYKLTPLSSAV 308
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 743-912 1.58e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 65.27  E-value: 1.58e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  743 AAARGHATWLSELLQMALSEEdccFKDNQGYTPLHWACYNGNENCIEVLLEQKC---FRKFIGNpfTPLHCAIINDHGNC 819
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPD---IGDSKGRTPLHIAASKGYEDCVLVLLKHACnvhIRDANGN--TALWNAISAKHHKI 606

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  820 ASLLLGAIDSSIVSCRDDKgrtpLHAAAFADHVECLQLLLRHSAPVNAADNSGKTALMMAAENGQAGAVDILV-NSAQAD 898
Cdd:PLN03192  607 FRILYHFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLImNGADVD 682

                         170
                  ....*....|....
gi 694897886  899 LTVKDKDLnTPLHL 912
Cdd:PLN03192  683 KANTDDDF-SPTEL 695
Ank_4 pfam13637
Ankyrin repeats (many copies);
672-723 4.66e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 4.66e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 694897886   672 TPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLL 723
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
442-554 9.65e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 9.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   442 LHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAASdmdrnktilGNAHenseelerarelkekeatlCLEFLLQN 521
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKN---------GHLE-------------------IVKLLLEH 52

                           90       100       110
                   ....*....|....*....|....*....|...
gi 694897886   522 dANPSIRDkEGYNSIHYAAAYGHRQCLELLLER 554
Cdd:pfam12796   53 -ADVNLKD-NGRTALHYAARSGHLEIVKLLLEK 83
Ank_4 pfam13637
Ankyrin repeats (many copies);
375-424 9.71e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 9.71e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 694897886   375 PLHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLL 424
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02946 PHA02946
ankyin-like protein; Provisional
 207-553 1.04e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 61.99  E-value: 1.04e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  207 YTPLHAAASNGQINVVKHLLNlgveidEINVYGNT-ALHIAC-YNGQDA-VVNELIDYGANVNQPNNNGFTPLHFAAAST 283
Cdd:PHA02946   10 YLSLYAKYNSKNLDVFRNMLQ------AIEPSGNYhILHAYCgIKGLDErFVEELLHRGYSPNETDDDGNYPLHIASKIN 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  284 HGALcLELLVNNGADVNIQSKDGKSPLHMTAvhgrftrsqtliqnGGEIDCVDKdgntpLHVAARYGHEllintlITSGA 363
Cdd:PHA02946   84 NNRI-VAMLLTHGADPNACDKQHKTPLYYLS--------------GTDDEVIER-----INLLVQYGAK------INNSV 137

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  364 DTAKCGihsmfPLhLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGN--VECIKLLQSSGADFHKKDKCGRTP 441
Cdd:PHA02946  138 DEEGCG-----PL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHDGNTP 211

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  442 LHYAAANCHFHC-IETLVTTGANVNETDDWGRTALHYAAASdmdrnktiLGNAHENSEELERARELKEKEATLCLeFLLQ 520
Cdd:PHA02946  212 LHIVCSKTVKNVdIINLLLPSTDVNKQNKFGDSPLTLLIKT--------LSPAHLINKLLSTSNVITDQTVNICI-FYDR 282

                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 694897886  521 NDANPSIRDK-EGYNSIHY--AAAYGHRQCLELLLE 553
Cdd:PHA02946  283 DDVLEIINDKgKQYDSTDFkmAVEVGSIRCVKYLLD 318
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 20-317 1.22e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 62.07  E-value: 1.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   20 DPEEIRMLIHKTEDVN-TLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMwLTPL-----HRAVAS-RSEEAVQV 92
Cdd:PHA02989   15 DKNALEFLLRTGFDVNeEYRGNSILLLYLKRKDVKIKIVKLLIDNGADVNYKGYI-ETPLcavlrNREITSnKIKKIVKL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   93 LIKHSADVNARDKNWQTPlhvaaankavkcaevIIPLLSSVNVSDrggrtalhhaalnghVEMVNLLLAKGANINafDKK 172
Cdd:PHA02989   94 LLKFGADINLKTFNGVSP---------------IVCFIYNSNINN---------------CDMLRFLLSKGINVN--DVK 141

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  173 DRRA---LH--WAAYMGHLDVVALLINHGAEV-TCKDKKGYTP----LHAAASNGQINVVKHLLNLGVEIDEINVYGNTA 242
Cdd:PHA02989  142 NSRGynlLHmyLESFSVKKDVIKILLSFGVNLfEKTSLYGLTPmniyLRNDIDVISIKVIKYLIKKGVNIETNNNGSESV 221

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  243 L------HIACYNGQDAVVNELIDYgANVNQPNNNGFTPLhFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVH 316
Cdd:PHA02989  222 LesfldnNKILSKKEFKVLNFILKY-IKINKKDKKGFNPL-LISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKH 299


                  .
gi 694897886  317 G 317
Cdd:PHA02989  300 G 300
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 769-968 1.37e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.82  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  769 DNQGYTPLHWACYNGNENCIEVLLEQKCFRKfIGNPFTPLHCAIINDHGNCASLLL-----GAIDSSIVSCRDDKGRTPL 843
Cdd:PHA02878   67 DHRDLTPLHIICKEPNKLGMKEMIRSINKCS-VFYTLVAIKDAFNNRNVEIFKIILtnrykNIQTIDLVYIDKKSKDDII 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  844 HAaafadhvECLQLLLRHSAPVNAAD-NSGKTALMMAAENGQAGAVDILVnSAQADLTVKDKDLNTPLHLACSKGHEKcA 922
Cdd:PHA02878  146 EA-------EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLL-SYGANVNIPDKTNNSPLHHAVKHYNKP-I 216

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 694897886  923 LLILdkIQDESLINAKNNALQTPLHVAARNGLKV-VVEELLAKGACV 968
Cdd:PHA02878  217 VHIL--LENGASTDARDKCGNTPLHISVGYCKDYdILKLLLEHGVDV 261
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 144-226 1.56e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.84  E-value: 1.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  144 LHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVK 223
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165


                  ...
gi 694897886  224 HLL 226
Cdd:PTZ00322  166 LLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
569-620 1.76e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 1.76e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 694897886   569 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALI 620
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 3-114 1.80e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.43  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886    3 VLKLTDQPPLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVA-AFLGDAEIIELLILSGARVNAKDNMW-LTPLHR 80
Cdd:PHA02878  196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILgLTALHS 275

                          90       100       110
                  ....*....|....*....|....*....|....
gi 694897886   81 AVasRSEEAVQVLIKHSADVNARDKNWQTPLHVA 114
Cdd:PHA02878  276 SI--KSERKLKLLLEYGADINSLNSYKLTPLSSA 307
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 279-430 2.13e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.81  E-value: 2.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  279 AAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTL 358
Cdd:PLN03192  531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694897886  359 --ITSGADTAKCGIhsmfPLHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGAD 430
Cdd:PLN03192  611 yhFASISDPHAAGD----LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 635-747 3.60e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.00  E-value: 3.60e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  635 RTPLHASVINGHTLCLRLLLEIadNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTG 714
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDL--GKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                          90       100       110
                  ....*....|....*....|....*....|...
gi 694897886  715 HEECVQMLLEQEVSILCKDSRGRTPLHYAAARG 747
Cdd:PHA02875  147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 567-784 4.22e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 60.41  E-value: 4.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  567 TKSPLHLAAYNGHHQALEVLL-QSLVDLDIRDEKGRTALDLAAFKGHTECVEALInqgasifvkDNVTkrtplhasving 645
Cdd:cd22192    17 SESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLM---------EAAP------------ 75

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  646 htlclrlllEIADNPEAVDVkdAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGcTALHRGI-------------- 711
Cdd:cd22192    76 ---------ELVNEPMTSDL--YQGETALHIAVVNQNLNLVRELIARGADVVSPRATG-TFFRPGPknliyygehplsfa 143

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  712 -MTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALSEE----DCCF---KDNQGYTPLHWACYNG 783
Cdd:cd22192   144 aCVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYDLILSYDkeddLQPLdlvPNNQGLTPFKLAAKEG 223


                  .
gi 694897886  784 N 784
Cdd:cd22192   224 N 224
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 692-978 4.63e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.89  E-value: 4.63e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  692 KEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALseedccfKDNQ 771
Cdd:PHA02878   26 TENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSIN-------KCSV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  772 GYT--PLHWACYNGNENCIEVLLeqkcFRKFIGNPFTPLH--CAIINDHGNCASL--LLGAIDSSIVSCRDDKGRTPLHA 845
Cdd:PHA02878   99 FYTlvAIKDAFNNRNVEIFKIIL----TNRYKNIQTIDLVyiDKKSKDDIIEAEItkLLLSYGADINMKDRHKGNTALHY 174

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  846 AAFADHVECLQLLLRHSAPVNAADNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLACSKGHEKCALLI 925
Cdd:PHA02878  175 ATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHISVGYCKDYDILKL 253

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 694897886  926 LdkIQDESLINAKNNALQ-TPLHVAARNGLKVVVeeLLAKGACVLAVDENGHTP 978
Cdd:PHA02878  254 L--LEHGVDVNAKSYILGlTALHSSIKSERKLKL--LLEYGADINSLNSYKLTP 303
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 108-282 5.20e-09

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: 60.28  E-value: 5.20e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  108 QTPLHVAAANKAVKCAEVIIPLLSSVNVSDRG--------------GRTALHHAALNGHVEMVNLLLAKGANINA----- 168
Cdd:cd21882    27 KTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAratgr 106

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  169 FDKKDRR--------ALHWAAYMGHLDVVALLINHGAE---VTCKDKKGYTPLHAAasngqinvvkhllnlgVEIDEiNV 237
Cdd:cd21882   107 FFRKSPGnlfyfgelPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHAL----------------VLQAD-NT 169

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 694897886  238 YGNTALHIACYNGqdavvneLIDYGANVNQ-------PNNNGFTPLHFAAAS 282
Cdd:cd21882   170 PENSAFVCQMYNL-------LLSYGAHLDPtqqleeiPNHQGLTPLKLAAVE 214
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 289-475 1.05e-08

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 59.54  E-value: 1.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  289 LELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRS--QTLIQNGGEIDCVDKDGNTPLH---VAARYGHELLINTLITSGA 363
Cdd:PHA02716  195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASviKKIIELGGDMDMKCVNGMSPIMtyiINIDNINPEITNIYIESLD 274

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  364 DTAKCGIHSMFPLHLA-ALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNV--ECIKLLQSSGADFHKKDKCGRT 440
Cdd:PHA02716  275 GNKVKNIPMILHSYITlARNIDISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIGNT 354

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 694897886  441 PLH-YAAANCHFH-------------CIETLVTTGANVNETDDWGRTAL 475
Cdd:PHA02716  355 VLHtYLSMLSVVNildpetdndirldVIQCLISLGADITAVNCLGYTPL 403
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 340-476 1.43e-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: 58.87  E-value: 1.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  340 NTPLHVAARYGHELLINTLITS-GADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSG----FEIDTPDKF-GRTCLHAAA 413
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelvNEPMTSDLYqGETALHIAV 97

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694897886  414 AGGNVECIKLLQSSGAD----------FHKKDKC----GRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALH 476
Cdd:cd22192    98 VNQNLNLVRELIARGADvvspratgtfFRPGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
PHA02946 PHA02946
ankyin-like protein; Provisional
 53-312 1.44e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 58.53  E-value: 1.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   53 DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKavkcAEVIipllss 132
Cdd:PHA02946   51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTD----DEVI------ 120

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  133 vnvsdrggrtalhhaalnghvEMVNLLLAKGANINafdkkdrralhwaaymghldvvallinhgaevTCKDKKGYTPLHA 212
Cdd:PHA02946  121 ---------------------ERINLLVQYGAKIN--------------------------------NSVDEEGCGPLLA 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  213 AASNGQiNVVKHLLNLGVEIDEINVYGNTAL--HIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLE 290
Cdd:PHA02946  148 CTDPSE-RVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKNVDII 226

                         250       260
                  ....*....|....*....|..
gi 694897886  291 LLVNNGADVNIQSKDGKSPLHM 312
Cdd:PHA02946  227 NLLLPSTDVNKQNKFGDSPLTL 248
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 569-739 1.96e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.69  E-value: 1.96e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  569 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGAsiFVKDNVTKR--TPLHASVINGH 646
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK--FADDVFYKDgmTPLHLATILKK 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  647 TLCLRLLLEIADNPeavDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQE 726
Cdd:PHA02875  115 LDIMKLLIARGADP---DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191

                         170
                  ....*....|...
gi 694897886  727 VSIlckDSRGRTP 739
Cdd:PHA02875  192 ANI---DYFGKNG 201
PHA03095 PHA03095
ankyrin-like protein; Provisional
 20-164 2.07e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.11  E-value: 2.07e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   20 DPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGD--AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHS 97
Cdd:PHA03095  201 RARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694897886   98 ADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRggrtALHHAALNGHV-------EMVNLLLAKGA 164
Cdd:PHA03095  281 ADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA----TLNTASVAGGDipsdatrLCVAKVVLRGA 350
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 411-626 2.12e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.34  E-value: 2.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  411 AAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAASDMDRNKTIL 490
Cdd:PLN03192  531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  491 gnahenseelerarelkekeatlclefllqndanpsirdkegynsIHYAAAyghrqclelllertnsgfeeSDSGATKSP 570
Cdd:PLN03192  611 ---------------------------------------------YHFASI--------------------SDPHAAGDL 625

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 694897886  571 LHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASI 626
Cdd:PLN03192  626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 274-443 2.13e-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: 58.10  E-value: 2.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  274 TPLhFAAASTHGALCLE-LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGE-----IDCVDKDGNTPLHVAA 347
Cdd:cd22192    19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  348 RYGHELLINTLITSGADTAK---CGihSMFplhlaALNAHSDCcrkllssgfeidtpdKFGRTCLHAAAAGGNVECIKLL 424
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSpraTG--TFF-----RPGPKNLI---------------YYGEHPLSFAACVGNEEIVRLL 155

                         170
                  ....*....|....*....
gi 694897886  425 QSSGADFHKKDKCGRTPLH 443
Cdd:cd22192   156 IEHGADIRAQDSLGNTVLH 174
Ank_4 pfam13637
Ankyrin repeats (many copies);
438-480 2.14e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 2.14e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 694897886   438 GRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAA 480
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAAS 43
Ank_4 pfam13637
Ankyrin repeats (many copies);
206-259 2.60e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 2.60e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 694897886   206 GYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELI 259
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 11-147 2.66e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.67  E-value: 2.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   11 PLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVA-SRSeeA 89
Cdd:PHA02874  160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIhNRS--A 237

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694897886   90 VQVLIkHSADVNARDKNWQTPLHVAAankAVKCAEVIIPLL----SSVNVSDRGGRTALHHA 147
Cdd:PHA02874  238 IELLI-NNASINDQDIDGSTPLHHAI---NPPCDIDIIDILlyhkADISIKDNKGENPIDTA 295
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 538-757 2.66e-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: 57.72  E-value: 2.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  538 YAAAYGHRQCLELLL--ERTNSgFEESDSGATKspLHLAAYNGHHQALEVLLQS---LVDLDIRDE--KGRTALDLAAFK 610
Cdd:cd22192    23 LAAKENDVQAIKKLLkcPSCDL-FQRGALGETA--LHVAALYDNLEAAVVLMEAapeLVNEPMTSDlyQGETALHIAVVN 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  611 GHTECVEALINQGAsifvkDNVTKRTPLHASVINGHTLCLRllleiadnpeavdvkdakGQTPLMLAVAYGHIDAVSLLL 690
Cdd:cd22192   100 QNLNLVRELIARGA-----DVVSPRATGTFFRPGPKNLIYY------------------GEHPLSFAACVGNEEIVRLLI 156

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694897886  691 EKEANVDTVDILGCTALHRGIMTGHEECV-QM---LLEQEVSI------LCKDSRGRTPLHYAAARGHATWLSELLQ 757
Cdd:cd22192   157 EHGADIRAQDSLGNTVLHILVLQPNKTFAcQMydlILSYDKEDdlqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
Ank_4 pfam13637
Ankyrin repeats (many copies);
109-160 3.74e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 3.74e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 694897886   109 TPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLL 160
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 569-813 3.98e-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: 3.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   569 SPLHLAAYNGHHQALEVLLQSLvdlDIRDEKGRTALdLAAFKGHTECVEALIN--------QGASIFVKDNVTKR----- 635
Cdd:TIGR00870   54 SALFVAAIENENLELTELLLNL---SCRGAVGDTLL-HAISLEYVDAVEAILLhllaafrkSGPLELANDQYTSEftpgi 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   636 TPLHASVINGHTLCLRLLLEIADNPEA----VDVKDAKGQT-------PLMLAVAYGHIDAVSLLLEKEANVDTVDILGC 704
Cdd:TIGR00870  130 TALHLAAHRQNYEIVKLLLERGASVPAracgDFFVKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   705 TALHRGIMtgheECVQMLLEQEVSILCKDSrgrtplhyaaarghATWLSELLQMALSEEDCCfkDNQGYTPLHWACYNGN 784
Cdd:TIGR00870  210 TLLHLLVM----ENEFKAEYEELSCQMYNF--------------ALSLLDKLRDSKELEVIL--NHQGLTPLKLAAKEGR 269

                          250       260       270
                   ....*....|....*....|....*....|
gi 694897886   785 ENCIEVLLEQKCF-RKFIGNPFTPLHCAII 813
Cdd:TIGR00870  270 IVLFRLKLAIKYKqKKFVAWPNGQQLLSLY 299
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 77-250 4.38e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 54.83  E-value: 4.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   77 PLHRAVASRSEEAVQVLIKHSADVNardKNWQTPLHVAAANKAV--KCAEVIIPLLSSVNVSDRG-GRTALHH-AALNGH 152
Cdd:PHA02859   24 PLFYYVEKDDIEGVKKWIKFVNDCN---DLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRDnNLSALHHyLSFNKN 100

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  153 V--EMVNLLLAKGANINAFDKKDRRALHwaAYMGH----LDVVALLINHGAEVTCKDKKGYTPLHA-AASNGQINVVKHL 225
Cdd:PHA02859  101 VepEILKILIDSGSSITEEDEDGKNLLH--MYMCNfnvrINVIKLLIDSGVSFLNKDFDNNNILYSyILFHSDKKIFDFL 178

                         170       180
                  ....*....|....*....|....*
gi 694897886  226 LNLGVEIDEINVYGNTALHIACYNG 250
Cdd:PHA02859  179 TSLGIDINETNKSGYNCYDLIKFRN 203
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 208-419 4.38e-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: 57.33  E-value: 4.38e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  208 TPLHAAASNGQINVVKHLL-NLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGAN-VNQPNNN----GFTPLHFAAA 281
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSdlyqGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  282 STHGALcLELLVNNGADVN---------IQSKD-----GKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVaa 347
Cdd:cd22192    99 NQNLNL-VRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI-- 175

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694897886  348 ryghellintLITSGADTAKCgihSMFPLHLaALNAHSDccrkllssGFEIDT-PDKFGRTCLHAAAAGGNVE 419
Cdd:cd22192   176 ----------LVLQPNKTFAC---QMYDLIL-SYDKEDD--------LQPLDLvPNNQGLTPFKLAAKEGNIV 226
Ank_4 pfam13637
Ankyrin repeats (many copies);
74-127 4.55e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 4.55e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 694897886    74 WLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 127
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 49-326 5.54e-08

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 56.84  E-value: 5.54e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   49 AFLG----DAEIIELLILSGARVNAKDNMWLTPLHRAV--ASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKC 122
Cdd:PHA02716  183 AYLGnmyvDIDILEWLCNNGVNVNLQNNHLITPLHTYLitGNVCASVIKKIIELGGDMDMKCVNGMSPIMTYIINIDNIN 262

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  123 AEVI----------------------IPLLSSVNVS---------------DRGGRTALHHAAL--NGHVEMVNLLLAKG 163
Cdd:PHA02716  263 PEITniyiesldgnkvknipmilhsyITLARNIDISvvysflqpgvklhykDSAGRTCLHQYILrhNISTDIIKLLHEYG 342

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  164 ANINAFDKKDRRALHwaAYMG----------------HLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQ--------- 218
Cdd:PHA02716  343 NDLNEPDNIGNTVLH--TYLSmlsvvnildpetdndiRLDVIQCLISLGADITAVNCLGYTPLTSYICTAQnymyydiid 420

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  219 -------INVVKH--LLNLGVEIDE--------INVYG-NTALHIACYNGQDAVVNELIDYGANVNQPNNN-----GFTP 275
Cdd:PHA02716  421 clisdkvLNMVKHriLQDLLIRVDDtpciihhiIAKYNiPTDLYTDEYEPYDSTKIHDVYHCAIIERYNNAvcetsGMTP 500

                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 694897886  276 LHFAAASTHGAL----CLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI 326
Cdd:PHA02716  501 LHVSIISHTNANivmdSFVYLLSIQYNINIPTKNGVTPLMLTMRNNRLSGHQWYI 555
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 781-985 5.64e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.60  E-value: 5.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  781 YNGNENCIEVLLEQKCFRKFIGN------PFTPLHCAIindHGNCASLLLGAIDSSI-VSCRDDKGRTPLHAAAFADHV- 852
Cdd:PHA03100    6 VLTKSRIIKVKNIKYIIMEDDLNdysykkPVLPLYLAK---EARNIDVVKILLDNGAdINSSTKNNSTPLHYLSNIKYNl 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  853 ----ECLQLLLRHSAPVNAADNSGKTALMMAAEN--GQAGAVDILVNSAqADLTVKDKDLNTPLHLACSKGHEK---CAL 923
Cdd:PHA03100   83 tdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDlkiLKL 161

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694897886  924 LILDK------------IQDESLINAKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVDENGHTPA-LACAPN 985
Cdd:PHA03100  162 LIDKGvdinaknrvnylLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLhIAILNN 236
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 12-97 7.49e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 7.49e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   12 LVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQ 91
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165


                  ....*.
gi 694897886   92 VLIKHS 97
Cdd:PTZ00322  166 LLSRHS 171
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 209-368 7.97e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 54.05  E-value: 7.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  209 PLHAAASNGQINVVKHLLNLgveIDEINVYGNTALHiACYNGQDAVVNE---LIDYGANVN-QPNNNGFTPLHFAAASTH 284
Cdd:PHA02859   24 PLFYYVEKDDIEGVKKWIKF---VNDCNDLYETPIF-SCLEKDKVNVEIlkfLIENGADVNfKTRDNNLSALHHYLSFNK 99

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  285 GAL--CLELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLI-NTLI 359
Cdd:PHA02859  100 NVEpeILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKKIfDFLT 179


                  ....*....
gi 694897886  360 TSGADTAKC 368
Cdd:PHA02859  180 SLGIDINET 188
Ank_4 pfam13637
Ankyrin repeats (many copies);
839-892 1.03e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 1.03e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 694897886   839 GRTPLHAAAFADHVECLQLLLRHSAPVNAADNSGKTALMMAAENGQAGAVDILV 892
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 7-114 1.45e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.27  E-value: 1.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886    7 TDQPPLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVAS-R 85
Cdd:PHA02878  167 KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcK 246

                          90       100       110
                  ....*....|....*....|....*....|
gi 694897886   86 SEEAVQVLIKHSADVNARDKNWQ-TPLHVA 114
Cdd:PHA02878  247 DYDILKLLLEHGVDVNAKSYILGlTALHSS 276
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 880-975 1.46e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 1.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  880 AENGQAGAVDILVNSAqADLTVKDKDLNTPLHLACSKGHEKCALLILDKIQDESLINAKNNalqTPLHVAARNGLKVVVE 959
Cdd:PTZ00322   90 AASGDAVGARILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK---TPLELAEENGFREVVQ 165

                          90
                  ....*....|....*.
gi 694897886  960 ELLAKGACVLAVDENG 975
Cdd:PTZ00322  166 LLSRHSQCHFELGANA 181
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 11-171 1.65e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 52.90  E-value: 1.65e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   11 PLVQAIFSGDPEEIRMLIHKTEDVNTLDsekRTPLH--VAAFLGDAEIIELLILSGARVNAK---DNmwLTPLHRAVA-- 83
Cdd:PHA02859   24 PLFYYVEKDDIEGVKKWIKFVNDCNDLY---ETPIFscLEKDKVNVEILKFLIENGADVNFKtrdNN--LSALHHYLSfn 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   84 -SRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAevIIPLLSSVNVS----DRGGRTALH-HAALNGHVEMVN 157
Cdd:PHA02859   99 kNVEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRIN--VIKLLIDSGVSflnkDFDNNNILYsYILFHSDKKIFD 176

                         170
                  ....*....|....
gi 694897886  158 LLLAKGANINAFDK 171
Cdd:PHA02859  177 FLTSLGIDINETNK 190
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 281-350 1.84e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 1.84e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  281 ASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYG 350
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
Ank_4 pfam13637
Ankyrin repeats (many copies);
705-748 2.02e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 2.02e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 694897886   705 TALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGH 748
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
Ank_4 pfam13637
Ankyrin repeats (many copies);
239-293 2.06e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 2.06e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 694897886   239 GNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGAlCLELLV 293
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
192-246 2.12e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 2.12e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 694897886   192 LINHG-AEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIA 246
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 672-978 2.32e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.58  E-value: 2.32e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  672 TPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEV--SILckdsrgrtPLHYAAARGHA 749
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVdtSIL--------PIPCIEKDMIK 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  750 TWLSellqmalSEEDCCFKDNQGYTPLHWACYNGNENCIEVLLEQKcfrkfignpftplhcaiindhgncaslllgaids 829
Cdd:PHA02874  109 TILD-------CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYG---------------------------------- 147

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  830 SIVSCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAADNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTP 909
Cdd:PHA02874  148 ADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG-NHIMNKCKNGFTP 226

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  910 LHLACSKGHEKCALLIldkiqDESLINAKNNALQTPLHVAARNGLKV-VVEELLAKGACVLAVDENGHTP 978
Cdd:PHA02874  227 LHNAIIHNRSAIELLI-----NNASINDQDIDGSTPLHHAINPPCDIdIIDILLYHKADISIKDNKGENP 291
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 671-892 2.36e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.23  E-value: 2.36e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  671 QTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHAT 750
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  751 WLSELLQMALSEEDCCFKDnqGYTPLHWACYNGNENCIEVLLEQKCFRKFIG-NPFTPLHCAIINDHGNCASLLLGaiDS 829
Cdd:PHA02875   83 AVEELLDLGKFADDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNtDKFSPLHLAVMMGDIKGIELLID--HK 158

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 694897886  830 SIVSCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAADNSGKTALM-MAAENGQAGAVDILV 892
Cdd:PHA02875  159 ACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFI 222
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 839-995 3.51e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.84  E-value: 3.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  839 GRTPLHAAAFADHVECLQLLLRHSAPVNAADNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKDLNTPLHLACSKGH 918
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKK 114

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694897886  919 EKCALLILDKIQDESLINAKNNalqTPLHVAARNGLKVVVEELLAKGACVLAVDENGHTPALACAPNKDVADCLALI 995
Cdd:PHA02875  115 LDIMKLLIARGADPDIPNTDKF---SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 69-198 3.64e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 3.64e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   69 AKDNMWLTPLHRAVasrSEEAVQVLIKHSADVNArdknwqtpLHVAAANKAVKcAEVIIPLLSSVNVSDRGGRTALHHAA 148
Cdd:PTZ00322   56 ATENKDATPDHNLT---TEEVIDPVVAHMLTVEL--------CQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIAC 123

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 694897886  149 LNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAE 198
Cdd:PTZ00322  124 ANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173
Ank_4 pfam13637
Ankyrin repeats (many copies);
42-94 3.93e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 3.93e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 694897886    42 RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLI 94
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 817-972 4.10e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.10  E-value: 4.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  817 GNCA---SLLLGAIDSSIvscRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAADNSGKTALMMAAENGQAGAVDILVN 893
Cdd:PLN03192  536 GNAAlleELLKAKLDPDI---GDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYH 612

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  894 SAQADLTVKDKDLntpLHLACSKGHekcaLLILDKIQDESL-INAKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVD 972
Cdd:PLN03192  613 FASISDPHAAGDL---LCTAAKRND----LTAMKELLKQGLnVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 822-898 8.13e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 8.13e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 694897886  822 LLLGAIDSSivsCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAADNSGKTALMMAAENGQAGAVDILVNSAQAD 898
Cdd:PTZ00322  101 LLTGGADPN---CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCH 174
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 720-963 9.89e-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: 52.78  E-value: 9.89e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   720 QMLLE-QEVSILCKDSRGRTPLHYAAARGHATWLSELLQmalseedccFKDNQGY---TPLHWACYNGNENCIEVLLEQK 795
Cdd:TIGR00870   35 RDLEEpKKLNINCPDRLGRSALFVAAIENENLELTELLL---------NLSCRGAvgdTLLHAISLEYVDAVEAILLHLL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   796 CFRKFIGNPF--------------TPLHCAIINDHGNCASLLL--GAIDSSIVSCRDDK----------GRTPLHAAAFA 849
Cdd:TIGR00870  106 AAFRKSGPLElandqytseftpgiTALHLAAHRQNYEIVKLLLerGASVPARACGDFFVksqgvdsfyhGESPLNAAACL 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   850 DHVECLQLLLRHSAPVNAADNSGKTALMMAaengqagavdILVNSAQADltvkdkdlNTPLHLACSKGhekcALLILDKI 929
Cdd:TIGR00870  186 GSPSIVALLSEDPADILTADSLGNTLLHLL----------VMENEFKAE--------YEELSCQMYNF----ALSLLDKL 243

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 694897886   930 QD-ESLINAKNNALQTPLHVAARNGLKVVVEELLA 963
Cdd:TIGR00870  244 RDsKELEVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 377-482 1.39e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  377 HLAALNAHSDccrKLLSSGFEIDTPDKFGRTCLHAA-------AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANC 449
Cdd:PTZ00322   50 HLEALEATEN---KDATPDHNLTTEEVIDPVVAHMLtvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANG 126

                          90       100       110
                  ....*....|....*....|....*....|...
gi 694897886  450 HFHCIETLVTTGANVNETDDWGRTALHYAAASD 482
Cdd:PTZ00322  127 HVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 189-261 1.56e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 1.56e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694897886  189 VALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDY 261
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 569-795 2.44e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.42  E-value: 2.44e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  569 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKgrTALDLAAFKGHTECVEA-LINQGASIFVKDNVTKRTPLHASVINghT 647
Cdd:PHA02878   72 TPLHIICKEPNKLGMKEMIRSINKCSVFYTL--VAIKDAFNNRNVEIFKIiLTNRYKNIQTIDLVYIDKKSKDDIIE--A 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  648 LCLRLLLEIADNPEAVDvkDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEV 727
Cdd:PHA02878  148 EITKLLLSYGADINMKD--RHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  728 SILCKDSRGRTPLHYAAARGHATwlsELLQMALSEEDCCFKDN--QGYTPLHWACYngNENCIEVLLEQK 795
Cdd:PHA02878  226 STDARDKCGNTPLHISVGYCKDY---DILKLLLEHGVDVNAKSyiLGLTALHSSIK--SERKLKLLLEYG 290
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 774-964 2.78e-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: 2.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  774 TPLHWACYNGNENCIEVLLEQK----CFRKFIGNpfTPLHCAIINDHGNCASLLLGAIDSSI---VSCRDDKGRTPLHAA 846
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPscdlFQRGALGE--TALHVAALYDNLEAAVVLMEAAPELVnepMTSDLYQGETALHIA 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  847 AFADHVECLQLLLRHSAPVNAADNS--------------GKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHL 912
Cdd:cd22192    97 VVNQNLNLVRELIARGADVVSPRATgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVLHI 175

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 694897886  913 ACSKGHEKCA------LLILDKIQDE-SLINAKNNALQTPLHVAARNGLKVVVEELLAK 964
Cdd:cd22192   176 LVLQPNKTFAcqmydlILSYDKEDDLqPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
736-792 3.87e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 3.87e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 694897886   736 GRTPLHYAAARGHatwlSELLQMAL-SEEDCCFKDNQGYTPLHWACYNGNENCIEVLL 792
Cdd:pfam13637    1 ELTALHAAAASGH----LELLRLLLeKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
308-359 4.44e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 4.44e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 694897886   308 SPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLI 359
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 140-168 4.65e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.12  E-value: 4.65e-06
                            10        20
                    ....*....|....*....|....*....
gi 694897886    140 GRTALHHAALNGHVEMVNLLLAKGANINA 168
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 4.75e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 4.75e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 694897886    10 PPLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLI 61
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 20-210 5.21e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 50.05  E-value: 5.21e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   20 DPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSE--EAVQVLIKHS 97
Cdd:PHA02946   51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEviERINLLVQYG 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   98 ADV-NARDKNWQTPLhVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAAL--NGHVEMVNLLLAKGANINAFDKKDR 174
Cdd:PHA02946  131 AKInNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMsdNPKASTISWMMKLGISPSKPDHDGN 209

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 694897886  175 RALH--WAAYMGHLDVVALLINhGAEVTCKDKKGYTPL 210
Cdd:PHA02946  210 TPLHivCSKTVKNVDIINLLLP-STDVNKQNKFGDSPL 246
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 493-693 6.78e-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: 50.01  E-value: 6.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  493 AHENSeeLERARELkekeatlclefLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEE---SDSGATKS 569
Cdd:cd22192    25 AKEND--VQAIKKL-----------LKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtSDLYQGET 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  570 PLHLAAYNGHHQALEVLLQSLVDLD--------IRDEK------GRTALDLAAFKGHTECVEALINQGASIFVKDNVTKr 635
Cdd:cd22192    92 ALHIAVVNQNLNLVRELIARGADVVspratgtfFRPGPknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN- 170

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 694897886  636 TPLHASVINGHTL--C----LRLLLEIADNPEAVD-VKDAKGQTPLMLAVAYGHIDAVSLLLEKE 693
Cdd:cd22192   171 TVLHILVLQPNKTfaCqmydLILSYDKEDDLQPLDlVPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
Ank_5 pfam13857
Ankyrin repeats (many copies);
158-213 6.91e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 6.91e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 694897886   158 LLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 213
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 391-510 9.54e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.87  E-value: 9.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  391 LLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPL-------HYAAANCHFHC---------- 453
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHHKIFRILYHFasisdphaag 623

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  454 --------------IETLVTTGANVNETDDWGRTALHYAAASD---------MDRNKTILGNAHENSEELERARELKEKE 510
Cdd:PLN03192  624 dllctaakrndltaMKELLKQGLNVDSEDHQGATALQVAMAEDhvdmvrlliMNGADVDKANTDDDFSPTELRELLQKRE 703
Ank_4 pfam13637
Ankyrin repeats (many copies);
600-654 9.64e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 9.64e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 694897886   600 GRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLL 654
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 140-171 1.02e-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: 43.05  E-value: 1.02e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 694897886   140 GRTALHHAAL-NGHVEMVNLLLAKGANINAFDK 171
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 140-282 1.23e-05

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 49.42  E-value: 1.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  140 GRTALHHAALN---GHVEMVNLLL---AKGANINAF------DK--KDRRALHWAAYMGHLDVVALLINHGAEVTC---- 201
Cdd:cd22196    47 GKTCLLKAMLNlhnGQNDTISLLLdiaEKTGNLKEFvnaaytDSyyKGQTALHIAIERRNMHLVELLVQNGADVHArasg 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  202 ------KDKKGY----TPLHAAASNGQINVVKHLLN---LGVEIDEINVYGNTALH----IAcYNGQD------AVVNEL 258
Cdd:cd22196   127 effkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLHalveVA-DNTPEntkfvtKMYNEI 205

                         170       180       190
                  ....*....|....*....|....*....|.
gi 694897886  259 IDYGANVNQ-------PNNNGFTPLHFAAAS 282
Cdd:cd22196   206 LILGAKIRPllkleeiTNKKGLTPLKLAAKT 236
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 543-780 1.27e-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: 49.11  E-value: 1.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  543 GHRQCLELLLerTNSGFEESDSGatKSPLHLAAYNGHHQALE---VLLQS---------LVDLDIRDE--KGRTALDLAA 608
Cdd:cd21882     6 GLLECLRWYL--TDSAYQRGATG--KTCLHKAALNLNDGVNEaimLLLEAapdsgnpkeLVNAPCTDEfyQGQTALHIAI 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  609 FKGHTECVEALINQGASIFVKDNVT--KRTPLHASVINGHTLCL----------RLLLEIADNPEAVDVKDAKGQTPLml 676
Cdd:cd21882    82 ENRNLNLVRLLVENGADVSARATGRffRKSPGNLFYFGELPLSLaactnqeeivRLLLENGAQPAALEAQDSLGNTVL-- 159

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  677 avaygHIdavslLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEqEVSilckDSRGRTPLHYAAARGHATWLSELL 756
Cdd:cd21882   160 -----HA-----LVLQADNTPENSAFVCQMYNLLLSYGAHLDPTQQLE-EIP----NHQGLTPLKLAAVEGKIVMFQHIL 224

                         250       260
                  ....*....|....*....|....
gi 694897886  757 QMALSEEdcCFKDNQGYTplHWAC 780
Cdd:cd21882   225 QREFSGP--YQPLSRKFT--EWTY 244
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 213-350 1.56e-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: 1.56e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  213 AASNGqinVVKHLLNlgVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVN--------QP--NNNGF----TPLHF 278
Cdd:cd22194   120 AEENG---ILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffNPkyKHEGFyfgeTPLAL 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  279 AAASTHGALcLELLVNNGADvNIQSKD--GKSPLHMTAVHGRFTRSQT-----------LIQNGGEIDCV-DKDGNTPLH 344
Cdd:cd22194   195 AACTNQPEI-VQLLMEKEST-DITSQDsrGNTVLHALVTVAEDSKTQNdfvkrmydmilLKSENKNLETIrNNEGLTPLQ 272


                  ....*.
gi 694897886  345 VAARYG 350
Cdd:cd22194   273 LAAKMG 278
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 211-314 1.79e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 1.79e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  211 HAAASNGQINVvKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALcLE 290
Cdd:PTZ00322   88 QLAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV-VQ 165

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 694897886  291 LLV-------NNGADVNIQSKDGK------SPLHMTA 314
Cdd:PTZ00322  166 LLSrhsqchfELGANAKPDSFTGKppsledSPISSHH 202
Ank_4 pfam13637
Ankyrin repeats (many copies);
532-587 2.13e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 2.13e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 694897886   532 GYNSIHYAAAYGHRQCLELLLERTNSGFEESDSGATksPLHLAAYNGHHQALEVLL 587
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGET--ALHFAASNGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 140-168 2.49e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.86  E-value: 2.49e-05
                           10        20
                   ....*....|....*....|....*....
gi 694897886   140 GRTALHHAALNGHVEMVNLLLAKGANINA 168
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
132-180 3.33e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.33e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 694897886   132 SVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWA 180
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
93-147 3.36e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.36e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 694897886    93 LIKH-SADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHA 147
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
258-312 3.43e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.43e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 694897886   258 LIDYG-ANVNQPNNNGFTPLHFAAasTHGAL-CLELLVNNGADVNIQSKDGKSPLHM 312
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAA--KYGALeIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank_5 pfam13857
Ankyrin repeats (many copies);
29-81 3.46e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.46e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 694897886    29 HKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRA 81
Cdd:pfam13857    4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
635-690 3.59e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 3.59e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 694897886   635 RTPLHASVINGHTLCLRLLLEiadNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLL 690
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLE---KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
236-279 3.78e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.78e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 694897886   236 NVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFA 279
Cdd:pfam13857   13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 46-117 4.12e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 4.12e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694897886   46 HVAAFlGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAAN 117
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
PHA02791 PHA02791
ankyrin-like protein; Provisional
 750-945 4.85e-05

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 46.57  E-value: 4.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  750 TWLSELLQMALSEEDCCFKDNQGYTPLHWACYNGNENCIEVLLEQKCFRKFIGNPFtPLH-CAIINDHGNCASLLLGAID 828
Cdd:PHA02791    8 TWKSKQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF-PLHqAATLEDTKIVKILLFSGMD 86

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  829 SSIVscrDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAADNSG-KTALMMAAENGQAGAVDILVNSAQA--DLTVkdkd 905
Cdd:PHA02791   87 DSQF---DDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPStfDLAI---- 159

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 694897886  906 LNTPLHLACSKGHEKCALLILDKIQDeslINAKNNALQTP 945
Cdd:PHA02791  160 LLSCIHITIKNGHVDMMILLLDYMTS---TNTNNSLLFIP 196
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 238-266 4.94e-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: 4.94e-05
                            10        20
                    ....*....|....*....|....*....
gi 694897886    238 YGNTALHIACYNGQDAVVNELIDYGANVN 266
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
857-913 5.38e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 5.38e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 694897886   857 LLLRHSAPVNAADNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLA 913
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
423-478 5.44e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 5.44e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 694897886   423 LLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYA 478
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
772-824 6.35e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 6.35e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 694897886   772 GYTPLHWACYNGNENCIEVLLEQK-CFRKFIGNPFTPLHCAIINDHGNCASLLL 824
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGaDINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
806-859 6.35e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 6.35e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 694897886   806 TPLHCAIINDHGNCASLLLGAidSSIVSCRDDKGRTPLHAAAFADHVECLQLLL 859
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEK--GADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 838-870 7.56e-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: 7.56e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 694897886   838 KGRTPLHAAA-FADHVECLQLLLRHSAPVNAADN 870
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 344-438 8.37e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 8.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  344 HVAARyGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKL 423
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                          90
                  ....*....|....*
gi 694897886  424 LQSSGADFHKKDKCG 438
Cdd:PTZ00322  167 LSRHSQCHFELGANA 181
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 644-723 8.73e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 8.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  644 NGHTLCLRLLLEIADNPeavDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLL 723
Cdd:PTZ00322   92 SGDAVGARILLTGGADP---NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 271-304 8.93e-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: 40.35  E-value: 8.93e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 694897886   271 NGFTPLHFAAASTHGALCLELLVNNGADVNIQSK 304
Cdd:pfam00023    1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 606-690 8.96e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 8.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  606 LAAfKGHTECVEALINQGASIFVKDnVTKRTPLHASVINGHTLCLRLLLEIADNPEAVDvKDakGQTPLMLAVAYGHIDA 685
Cdd:PTZ00322   89 LAA-SGDAVGARILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLD-KD--GKTPLELAEENGFREV 163


                  ....*
gi 694897886  686 VSLLL 690
Cdd:PTZ00322  164 VQLLS 168
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 238-270 9.95e-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: 40.35  E-value: 9.95e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 694897886   238 YGNTALHIACY-NGQDAVVNELIDYGANVNQPNN 270
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 310-404 1.10e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 1.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  310 LHMTAVH-------GRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALN 382
Cdd:PTZ00322   79 AHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158

                          90       100
                  ....*....|....*....|....*...
gi 694897886  383 AHSDCCRKLLS---SGFEIDT---PDKF 404
Cdd:PTZ00322  159 GFREVVQLLSRhsqCHFELGAnakPDSF 186
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 236-313 1.13e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 45.36  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  236 NVYGNTALHIACYNGQDAVVNeLIDYGANVNQPNNNG-FTPLHFAAasTHGAL-CLELLVNNGADVNIQSKDGKSPLHMT 313
Cdd:PHA02884   68 NSKTNPLIYAIDCDNDDAAKL-LIRYGADVNRYAEEAkITPLYISV--LHGCLkCLEILLSYGADINIQTNDMVTPIELA 144
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 140-280 1.25e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 45.90  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  140 GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRR--------ALHWAAYMGHLDVVALLINHGAE-VTCKDK 204
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNAhakgvfFNPKYKHegfyfgetPLALAACTNQPEIVQLLMEKESTdITSQDS 220

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  205 KGYTPLHAAA-----SNGQINVVKHLLnlgveiDEI-NVYGNTALhiacyngqdavvnELIdyganvnqPNNNGFTPLHF 278
Cdd:cd22194   221 RGNTVLHALVtvaedSKTQNDFVKRMY------DMIlLKSENKNL-------------ETI--------RNNEGLTPLQL 273


                  ..
gi 694897886  279 AA 280
Cdd:cd22194   274 AA 275
Ank_4 pfam13637
Ankyrin repeats (many copies);
514-552 2.01e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 2.01e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 694897886   514 CLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLL 552
Cdd:pfam13637   16 LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
656-708 2.22e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 2.22e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 694897886   656 IADNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALH 708
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 205-234 2.38e-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: 39.11  E-value: 2.38e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 694897886    205 KGYTPLHAAASNGQINVVKHLLNLGVEIDE 234
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 140-282 3.13e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 44.79  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  140 GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRA--------LHWAAYMGHLDVVALLINHG---AEVTCK 202
Cdd:cd22193    76 GQTALHIAIERRQGDIVALLVENGADVHAhakgrfFQPKYQGEgfyfgelpLSLAACTNQPDIVQYLLENEhqpADIEAQ 155

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  203 DKKGYTPLHAAasngqinvvkhllnlgVEIDEiNVYGNTALHIACYNGqdavvneLIDYGANVNQP-------NNNGFTP 275
Cdd:cd22193   156 DSRGNTVLHAL----------------VTVAD-NTKENTKFVTRMYDM-------ILIRGAKLCPTveleeirNNDGLTP 211


                  ....*..
gi 694897886  276 LHFAAAS 282
Cdd:cd22193   212 LQLAAKM 218
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 405-558 3.25e-04

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: 44.85  E-value: 3.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  405 GRTCLHAAAAGGNVECIKLLQSSGADFH----------KKDKC---GRTPLHYAAANCHFHCIETLVTTG---ANVNETD 468
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVENGADVHaracgrffqkKQGTCfyfGELPLSLAACTKQWDVVNYLLENPhqpASLQAQD 173

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  469 DWGRTALHYAAasdmdrnkTILGNAHENSEELERA-RELKEKEATLCLEFLLQndanpSIRDKEGYNSIHYAAAYGHRQC 547
Cdd:cd22197   174 SLGNTVLHALV--------MIADNSPENSALVIKMyDGLLQAGARLCPTVQLE-----EISNHEGLTPLKLAAKEGKIEI 240

                         170
                  ....*....|.
gi 694897886  548 LELLLERTNSG 558
Cdd:cd22197   241 FRHILQREFSG 251
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 214-360 3.48e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 44.52  E-value: 3.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  214 ASNGQINVVKHLLNLGVEIDEINVYGNTALH--IACYNGQDAVVNELIDYGANVNQPNNNGFTPLHfaaaSTHGALCLEL 291
Cdd:PHA02716  292 ARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLH----TYLSMLSVVN 367

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 694897886  292 LVNNGADVNIqskdgksplhmtavhgRFTRSQTLIQNGGEIDCVDKDGNTPLH----VAARYGHELLINTLIT 360
Cdd:PHA02716  368 ILDPETDNDI----------------RLDVIQCLISLGADITAVNCLGYTPLTsyicTAQNYMYYDIIDCLIS 424
PHA02798 PHA02798
ankyrin-like protein; Provisional
 418-711 4.09e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.06  E-value: 4.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  418 VECIKLLQSSGADFHKKDKCGRTPL-----HYAAANCHFHCIETLVTTGANVNETDDWGRTALHyaaasdmdrnkTILGN 492
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLY-----------CLLSN 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  493 AHENSEELerarelkekeatlcLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLlertnsgfeesdsgatksplh 572
Cdd:PHA02798  120 GYINNLEI--------------LLFMIENGADTTLLDKDGFTMLQVYLQSNHHIDIEII--------------------- 164

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  573 laaynghhqalEVLLQSLVDLD-IRDEKGRTALDlAAFKGHTECVEA-----LINQGASIFVKDNVTKRTPLH--ASVI- 643
Cdd:PHA02798  165 -----------KLLLEKGVDINtHNNKEKYDTLH-CYFKYNIDRIDAdilklFVDNGFIINKENKSHKKKFMEylNSLLy 232

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 694897886  644 ---NGHTLCLRLLLEIADnpeaVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGI 711
Cdd:PHA02798  233 dnkRFKKNILDFIFSYID----INQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAF 299
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 838-953 4.10e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 44.36  E-value: 4.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  838 KGRTPLHAAAFADHVECLQLLLRHSAPVNAADNS--------------GKTALMMAAENGQAGAVDILVNSAQADLTVKD 903
Cdd:cd22194   140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQD 219

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 694897886  904 KDLNTPLHLAC-----SKGHEKCALLILDKI----QDESLINAKNNALQTPLHVAARNG 953
Cdd:cd22194   220 SRGNTVLHALVtvaedSKTQNDFVKRMYDMIllksENKNLETIRNNEGLTPLQLAAKMG 278
Ank_5 pfam13857
Ankyrin repeats (many copies);
688-743 4.29e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 4.29e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 694897886   688 LLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYA 743
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
569-607 4.33e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 4.33e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 694897886   569 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLA 607
Cdd:pfam13857   18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 201-347 5.13e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.92  E-value: 5.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   201 CKDKKGYTPL-HAAASNGQINVVKHLLNLGVEIDEinvyGNTALHIACYNGQDAVvNELIDY-----GANVNQPNNN--- 271
Cdd:TIGR00870   47 CPDRLGRSALfVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLEYVDAV-EAILLHllaafRKSGPLELANdqy 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   272 ------GFTPLHFAAaSTHGALCLELLVNNGADVNIQSKDG---KSPLHMTAVHGRFTRS-----------QTLIQNGGE 331
Cdd:TIGR00870  122 tseftpGITALHLAA-HRQNYEIVKLLLERGASVPARACGDffvKSQGVDSFYHGESPLNaaaclgspsivALLSEDPAD 200

                          170
                   ....*....|....*.
gi 694897886   332 IDCVDKDGNTPLHVAA 347
Cdd:TIGR00870  201 ILTADSLGNTLLHLLV 216
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 844-937 5.15e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 5.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  844 HAAAFADHVEcLQLLLRHSAPVNAADNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLACSKGHEKCAL 923
Cdd:PTZ00322   88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFREVVQ 165

                          90
                  ....*....|....
gi 694897886  924 LILDKIQDESLINA 937
Cdd:PTZ00322  166 LLSRHSQCHFELGA 179
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 55-227 5.82e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.98  E-value: 5.82e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   55 EIIELLI-----------LSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKN-WQTPLHvaaankavkc 122
Cdd:cd22194   111 EIVRILLafaeengildrFINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvFFNPKY---------- 180

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  123 aeviipllssvnvSDRG---GRTALHHAALNGHVEMVNLLLAKGANINAF-DKKDRRALHwAAYM------GHLDVV--- 189
Cdd:cd22194   181 -------------KHEGfyfGETPLALAACTNQPEIVQLLMEKESTDITSqDSRGNTVLH-ALVTvaedskTQNDFVkrm 246

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 694897886  190 --ALLINHGAEV--TCKDKKGYTPLHAAASNGQINVVKHLLN 227
Cdd:cd22194   247 ydMILLKSENKNleTIRNNEGLTPLQLAAKMGKAEILKYILS 288
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 438-469 6.38e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 6.38e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 694897886   438 GRTPLHYAAANC-HFHCIETLVTTGANVNETDD 469
Cdd:pfam00023    2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
274-326 6.48e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 6.48e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 694897886   274 TPLHFAAASTHGAlCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI 326
Cdd:pfam13637    3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 238-266 7.08e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.01  E-value: 7.08e-04
                           10        20
                   ....*....|....*....|....*....
gi 694897886   238 YGNTALHIACYNGQDAVVNELIDYGANVN 266
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 332-476 7.78e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.53  E-value: 7.78e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   332 IDCVDKDGNTPLHVAARYG-HELLINTLITSGA-----DTAkcgihsmfpLHLAALNAH---SDCCRKLLSSGFEIDTPD 402
Cdd:TIGR00870   45 INCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISLEYVdavEAILLHLLAAFRKSGPLE 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   403 ----------KFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKC--------------GRTPLHYAAANCHFHCIETLV 458
Cdd:TIGR00870  116 landqytsefTPGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLS 195

                          170
                   ....*....|....*...
gi 694897886   459 TTGANVNETDDWGRTALH 476
Cdd:TIGR00870  196 EDPADILTADSLGNTLLH 213
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 438-466 7.80e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 7.80e-04
                            10        20
                    ....*....|....*....|....*....
gi 694897886    438 GRTPLHYAAANCHFHCIETLVTTGANVNE 466
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 189-318 8.23e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 8.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  189 VALLINHGAEVTCKDKKGYTPLHAAASNGQIN-VVKHLLNlgVEIDEINVYGntalhiacyngqDAV-VNELIDYGANVN 266
Cdd:PTZ00322   44 IARIDTHLEALEATENKDATPDHNLTTEEVIDpVVAHMLT--VELCQLAASG------------DAVgARILLTGGADPN 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 694897886  267 QPNNNGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGR 318
Cdd:PTZ00322  110 CRDYDGRTPLHIACANGHVQV-VRVLLEFGADPTLLDKDGKTPLELAEENGF 160
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 385-554 8.25e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.21  E-value: 8.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  385 SDCCRKLLSSGFEidTPDKFGRTCLHAAAAGGNVECIKLLQSSGAD---------FHKKDK-----CGRTPLHYAAANCH 450
Cdd:cd22194   123 NGILDRFINAEYT--EEAYEGQTALNIAIERRQGDIVKLLIAKGADvnahakgvfFNPKYKhegfyFGETPLALAACTNQ 200

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  451 FHCIETLVTTGA-NVNETDDWGRTALH--YAAASDMDRNKTILGNAHEnseELERARELKEKEAtlclefllqndanpsI 527
Cdd:cd22194   201 PEIVQLLMEKEStDITSQDSRGNTVLHalVTVAEDSKTQNDFVKRMYD---MILLKSENKNLET---------------I 262

                         170       180
                  ....*....|....*....|....*..
gi 694897886  528 RDKEGYNSIHYAAAYGHRQCLELLLER 554
Cdd:cd22194   263 RNNEGLTPLQLAAKMGKAEILKYILSR 289
Ank_5 pfam13857
Ankyrin repeats (many copies);
397-445 8.29e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 8.29e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 694897886   397 EIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYA 445
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 140-280 8.59e-04

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: 43.30  E-value: 8.59e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  140 GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRALhwaaYMGHLdvvallinhgaevtckdkkgytPLHAA 213
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVENGADVHAracgrfFQKKQGTCF----YFGEL----------------------PLSLA 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  214 ASNGQINVVKHLLNLGVE---IDEINVYGNTALHIACYNGQDAVVN---------ELIDYGANVNQ-------PNNNGFT 274
Cdd:cd22197   148 ACTKQWDVVNYLLENPHQpasLQAQDSLGNTVLHALVMIADNSPENsalvikmydGLLQAGARLCPtvqleeiSNHEGLT 227


                  ....*.
gi 694897886  275 PLHFAA 280
Cdd:cd22197   228 PLKLAA 233
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 651-783 8.98e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.21  E-value: 8.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  651 RLLLEIADNPEAVDV--------KDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVD--------------ILGCTALH 708
Cdd:cd22194   114 RILLAFAEENGILDRfinaeyteEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykhegfYFGETPLA 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  709 RGIMTGHEECVQMLLEQE-VSILCKDSRGRTPLHYAA-----ARGHATWLSELLQMAL----SEEDCCFKDNQGYTPLHW 778
Cdd:cd22194   194 LAACTNQPEIVQLLMEKEsTDITSQDSRGNTVLHALVtvaedSKTQNDFVKRMYDMILlkseNKNLETIRNNEGLTPLQL 273


                  ....*
gi 694897886  779 ACYNG 783
Cdd:cd22194   274 AAKMG 278
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 40-226 9.38e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 43.33  E-value: 9.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   40 EKRTPLHVAAFLGDAEIIELLILSGARVNAKDN-------------MWLTPLHRAVASRSEEAVQVLIKHSAD---VNAR 103
Cdd:cd21882    72 QGQTALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQ 151

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  104 DKNWQTPLH--VAAANKAVKCAEVIIpllssvnvsdrggrtalhhaalnghvEMVNLLLAKGANINafdkkdrralhwaa 181
Cdd:cd21882   152 DSLGNTVLHalVLQADNTPENSAFVC--------------------------QMYNLLLSYGAHLD-------------- 191

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 694897886  182 ymgHLDVVALLINHgaevtckdkKGYTPLHAAASNGQINVVKHLL 226
Cdd:cd21882   192 ---PTQQLEEIPNH---------QGLTPLKLAAVEGKIVMFQHIL 224
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 568-619 1.06e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 1.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 694897886  568 KSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEAL 619
Cdd:PTZ00322  116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 214-517 1.06e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 42.81  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  214 ASNGQINVVKHLLNLGVEIDEinVY-GNTAL--HIACYNGQDAVVNELIDYGANVNQpnnNGF--TPL-----HFAAAST 283
Cdd:PHA02989   11 SDTVDKNALEFLLRTGFDVNE--EYrGNSILllYLKRKDVKIKIVKLLIDNGADVNY---KGYieTPLcavlrNREITSN 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  284 HGALCLELLVNNGADVNIQSKDGKSPLhMTAVHG---------RFtrsqtLIQNGGEIDCV-DKDGNTPLHVaarYGHEL 353
Cdd:PHA02989   86 KIKKIVKLLLKFGADINLKTFNGVSPI-VCFIYNsninncdmlRF-----LLSKGINVNDVkNSRGYNLLHM---YLESF 156

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  354 LINT-----LITSGADT-AKCGIHSMFPLHLAALNAHS----DCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNV---EC 420
Cdd:PHA02989  157 SVKKdvikiLLSFGVNLfEKTSLYGLTPMNIYLRNDIDvisiKVIKYLIKKGVNIETNNNGSESVLESFLDNNKIlskKE 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  421 IKLLQS--SGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAasdmdrnktilgnAHENSE 498
Cdd:PHA02989  237 FKVLNFilKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAI-------------KHGNID 303

                         330
                  ....*....|....*....
gi 694897886  499 ELERARELKEKEATLCLEF 517
Cdd:PHA02989  304 MLNRILQLKPGKYLIKKTF 322
Ank_5 pfam13857
Ankyrin repeats (many copies);
65-114 1.07e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.07e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 694897886    65 ARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVA 114
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 205-234 1.15e-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: 1.15e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 694897886   205 KGYTPLHAAASNGQINVVKHLLNLGVEIDE 234
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
907-953 1.18e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 1.18e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 694897886   907 NTPLHLACSKGHEKCALLILDKIQDeslINAKNNALQTPLHVAARNG 953
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNG 45
PHA02798 PHA02798
ankyrin-like protein; Provisional
 613-882 1.27e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.51  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  613 TECVEALINQGASIFVKDNvTKRTPLHA--SVINGHTLCLRLLLEIADNPEAVDVKDAKGQTPLMLAVAYGHIDA---VS 687
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDN-EYSTPLCTilSNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNleiLL 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  688 LLLEKEANVDTVDILGCTALHRGIMTGHE---ECVQMLLEQEVSIlckdsrgrtplhyaaaRGHATWlsellqmalseed 764
Cdd:PHA02798  130 FMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDI----------------NTHNNK------------- 180

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  765 ccfkdnQGYTPLHwaCY-NGNENCIEVLLEQ---------KCFRKFIGNPFTPLHCAIINDHGNCASLLLGAIDSSI-VS 833
Cdd:PHA02798  181 ------EKYDTLH--CYfKYNIDRIDADILKlfvdngfiiNKENKSHKKKFMEYLNSLLYDNKRFKKNILDFIFSYIdIN 252

                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 694897886  834 CRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAADNSGKTALMMAAEN 882
Cdd:PHA02798  253 QVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFEN 301
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 675-767 1.36e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  675 MLAVAYGHIDA------VSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLE--QEVSILCKDsrGRTPLHYAAAR 746
Cdd:PTZ00322   81 MLTVELCQLAAsgdavgARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEfgADPTLLDKD--GKTPLELAEEN 158

                          90       100
                  ....*....|....*....|.
gi 694897886  747 GhatwLSELLQMALSEEDCCF 767
Cdd:PTZ00322  159 G----FREVVQLLSRHSQCHF 175
Ank_5 pfam13857
Ankyrin repeats (many copies);
826-879 1.51e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 1.51e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 694897886   826 AIDSSIVSCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAADNSGKTALMMA 879
Cdd:pfam13857    3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 376-476 1.51e-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: 42.56  E-value: 1.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  376 LHLAALNAHS---DCCRKLLSSGFEIDTPDKF-----------GRTCLHAAAAGGNVECIKLLQSSGADFH--------K 433
Cdd:cd21882    30 LHKAALNLNDgvnEAIMLLLEAAPDSGNPKELvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSaratgrffR 109

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 694897886  434 KDKC-----GRTPLHYAAANCHFHCIETLVTTG---ANVNETDDWGRTALH 476
Cdd:cd21882   110 KSPGnlfyfGELPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLH 160
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 42-72 1.59e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 1.59e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 694897886    42 RTPLHVAA-FLGDAEIIELLILSGARVNAKDN 72
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 669-700 1.61e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 1.61e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 694897886   669 KGQTPLMLAVA-YGHIDAVSLLLEKEANVDTVD 700
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 874-968 1.87e-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: 42.31  E-value: 1.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  874 TALMMAAENGQAGAVDILVNSAQADLTVKDKDLNTPLHLACSKGHEKCALLILDkiQDESLIN-AKNNAL---QTPLHVA 949
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNePMTSDLyqgETALHIA 96

                          90
                  ....*....|....*....
gi 694897886  950 ARNGLKVVVEELLAKGACV 968
Cdd:cd22192    97 VVNQNLNLVRELIARGADV 115
PHA02795 PHA02795
ankyrin-like protein; Provisional
 124-201 1.98e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 41.90  E-value: 1.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  124 EVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMG--------HLDVVALLINH 195
Cdd:PHA02795  205 KLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHLKILEILLRE 284


                  ....*.
gi 694897886  196 GAEVTC 201
Cdd:PHA02795  285 PLSIDC 290
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 771-793 1.98e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 1.98e-03
                            10        20
                    ....*....|....*....|...
gi 694897886    771 QGYTPLHWACYNGNENCIEVLLE 793
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLD 23
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 363-554 2.14e-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: 42.09  E-value: 2.14e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  363 ADTAK-CGIHSMFPLHlaalNAHSDCCRKLLSSGFEIDTPDKF-----------GRTCLHAAAAGGNVECIKLLQSSGAD 430
Cdd:cd22193    26 SSTGKtCLMKALLNLN----PGTNDTIRILLDIAEKTDNLKRFinaeytdeyyeGQTALHIAIERRQGDIVALLVENGAD 101

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  431 ---------FHKKDK-----CGRTPLHYAAANCHFHCIETLVT---TGANVNETDDWGRTALHYAAasdmdrnkTILGNA 493
Cdd:cd22193   102 vhahakgrfFQPKYQgegfyFGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLHALV--------TVADNT 173

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694897886  494 HENSEELERA-RELKEKEATLCLEFLLQndanpSIRDKEGYNSIHYAAAYGHRQCLELLLER 554
Cdd:cd22193   174 KENTKFVTRMyDMILIRGAKLCPTVELE-----EIRNNDGLTPLQLAAKMGKIEILKYILQR 230
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 176-204 2.18e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 2.18e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 694897886   176 ALHWAAYM-GHLDVVALLINHGAEVTCKDK 204
Cdd:pfam00023    5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02791 PHA02791
ankyrin-like protein; Provisional
 144-275 2.28e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.18  E-value: 2.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  144 LHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGY-TPLHAAASNGQINVV 222
Cdd:PHA02791   65 LHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIV 144

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 694897886  223 KHLLNLGVEIDEINVYgNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTP 275
Cdd:PHA02791  145 SYFLSEIPSTFDLAIL-LSCIHITIKNGHVDMMILLLDYMTSTNTNNSLLFIP 196
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 599-631 2.48e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 2.48e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 694897886   599 KGRTALDLAAFK-GHTECVEALINQGASIFVKDN 631
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 43-121 2.61e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.99  E-value: 2.61e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886    43 TPLHVAAFLGDAEIIELLILSGARVNAKDN--MWLT------------PLHRAVASRSEEAVQVLIKHSADVNARDKNWQ 108
Cdd:TIGR00870  130 TALHLAAHRQNYEIVKLLLERGASVPARACgdFFVKsqgvdsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209

                           90
                   ....*....|...
gi 694897886   109 TPLHVAAANKAVK 121
Cdd:TIGR00870  210 TLLHLLVMENEFK 222
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 838-867 2.61e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 2.61e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 694897886    838 KGRTPLHAAAFADHVECLQLLLRHSAPVNA 867
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 405-433 2.69e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 2.69e-03
                            10        20
                    ....*....|....*....|....*....
gi 694897886    405 GRTCLHAAAAGGNVECIKLLQSSGADFHK 433
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 338-364 2.69e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 2.69e-03
                            10        20
                    ....*....|....*....|....*..
gi 694897886    338 DGNTPLHVAARYGHELLINTLITSGAD 364
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 669-698 2.80e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.08  E-value: 2.80e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 694897886   669 KGQTPLMLAVAYGHIDAVSLLLEKEANVDT 698
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02791 PHA02791
ankyrin-like protein; Provisional
 40-237 3.28e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.80  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   40 EKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKhsadvnardKNWQTPLHvaaanka 119
Cdd:PHA02791   60 ENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVK---------KNWRLMFY------- 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  120 vkcaeviipllssvnvSDRGGRTALHHAALNGHVEMVNLLLAKGAniNAFDKKDRRA-LHWAAYMGHLDVVALLINHGAE 198
Cdd:PHA02791  124 ----------------GKTGWKTSFYHAVMLNDVSIVSYFLSEIP--STFDLAILLScIHITIKNGHVDMMILLLDYMTS 185

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 694897886  199 VTCKDKKGYTP-LHAAASNGQINVVKHLLNLGVEIDEINV 237
Cdd:PHA02791  186 TNTNNSLLFIPdIKLAIDNKDLEMLQALFKYDINIYSVNL 225
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 850-985 3.93e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.20  E-value: 3.93e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  850 DHVECLQLLLRHSAPVNAADNSGKTALMMAAENGQAGAVDILVnSAQADLTVKDKDLNTPLHLACSKGH----------- 918
Cdd:PHA02876  156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLL-SYGADVNIIALDDLSVLECAVDSKNidtikaiidnr 234

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  919 ---EKCALLILDKIQDESL------------INAKNNALQTPLHVAARN-GLKVVVEELLAKGACVLAVDENGHTPALAC 982
Cdd:PHA02876  235 sniNKNDLSLLKAIRNEDLetslllydagfsVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLM 314


                  ...
gi 694897886  983 APN 985
Cdd:PHA02876  315 AKN 317
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 176-201 4.58e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 4.58e-03
                            10        20
                    ....*....|....*....|....*.
gi 694897886    176 ALHWAAYMGHLDVVALLINHGAEVTC 201
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 669-697 4.62e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 4.62e-03
                            10        20
                    ....*....|....*....|....*....
gi 694897886    669 KGQTPLMLAVAYGHIDAVSLLLEKEANVD 697
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 188-356 4.69e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 40.88  E-value: 4.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  188 VVALLINHGAEVTCKDKKGYTPLHAAASNGQIN---VVKHLLNLGVEIDEI-NVYGNTALHI---ACYNGQDaVVNELID 260
Cdd:PHA02989   90 IVKLLLKFGADINLKTFNGVSPIVCFIYNSNINncdMLRFLLSKGINVNDVkNSRGYNLLHMyleSFSVKKD-VIKILLS 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  261 YGANVNQPNN-NGFTPLHFAAASTHGALCLEL---LVNNGAD-------------------------------------- 298
Cdd:PHA02989  169 FGVNLFEKTSlYGLTPMNIYLRNDIDVISIKVikyLIKKGVNietnnngsesvlesfldnnkilskkefkvlnfilkyik 248

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 694897886  299 VNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLIN 356
Cdd:PHA02989  249 INKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLN 306
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 629-741 5.28e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.55  E-value: 5.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  629 KDNVTKRTPLHASVIN---GHTLCLRLLLEIAD---------NPEAVDVKdAKGQTPLMLAVAYGHIDAVSLLLEKEANV 696
Cdd:cd22193    24 TESSTGKTCLMKALLNlnpGTNDTIRILLDIAEktdnlkrfiNAEYTDEY-YEGQTALHIAIERRQGDIVALLVENGADV 102

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 694897886  697 D--------------TVDILGCTALHRGIMTGHEECVQMLLE---QEVSILCKDSRGRTPLH 741
Cdd:cd22193   103 HahakgrffqpkyqgEGFYFGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLH 164
Ank_5 pfam13857
Ankyrin repeats (many copies);
291-346 5.77e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 5.77e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 694897886   291 LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVA 346
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 840-997 6.09e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.36  E-value: 6.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  840 RTPLHAAAFADHVECLQLLLRHSAPVN-AADNSGKTALMMAAENGQAGAVDILVnSAQADLTVKDKDLNTPLHLACSKGH 918
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLI-ARGADPDIPNTDKFSPLHLAVMMGD 147

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 694897886  919 EKCALLILDKiqdESLINAKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVDENGHTPALACAPNKDVADCLALILA 997
Cdd:PHA02875  148 IKGIELLIDH---KACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIK 223
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 153-268 6.30e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 38.64  E-value: 6.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  153 VEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVV---ALLINHGAEVTCKDKK-GYTPLHAAASNGQINVVKHLL-N 227
Cdd:PHA02743   37 MEVAPFISGDGHLLHRYDHHGRQCTHMVAWYDRANAVmkiELLVNMGADINARELGtGNTLLHIAASTKNYELAEWLCrQ 116

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 694897886  228 LGVEIDEINVYGNTALHIAcYNGQDAVVNE-LIDYGANVNQP 268
Cdd:PHA02743  117 LGVNLGAINYQHETAYHIA-YKMRDRRMMEiLRANGAVCDDP 157
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 839-987 6.36e-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: 6.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  839 GRTPLHAAAFADHVECLQLLLRhSAP--VNAADNS----GKTALMMAAENGQAGAVDIL------VNSAQADLTV---KD 903
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLME-AAPelVNEPMTSdlyqGETALHIAVVNQNLNLVRELiargadVVSPRATGTFfrpGP 129

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886  904 KDL----NTPLHLACSKGHEKCALLILD-----KIQDeSLINaknnalqTPLHVAARNGLKVVVEELLakgACVLAVDEN 974
Cdd:cd22192   130 KNLiyygEHPLSFAACVGNEEIVRLLIEhgadiRAQD-SLGN-------TVLHILVLQPNKTFACQMY---DLILSYDKE 198

                         170
                  ....*....|...
gi 694897886  975 GHTPALACAPNKD 987
Cdd:cd22192   199 DDLQPLDLVPNNQ 211
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 405-436 7.25e-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: 7.25e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 694897886   405 GRTCLHAAAA-GGNVECIKLLQSSGADFHKKDK 436
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 76-105 7.69e-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: 7.69e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 694897886    76 TPLHRAVASR-SEEAVQVLIKHSADVNARDK 105
Cdd:pfam00023    4 TPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 599-628 7.86e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 7.86e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 694897886    599 KGRTALDLAAFKGHTECVEALINQGASIFV 628
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 437-466 8.19e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 8.19e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 694897886   437 CGRTPLHYAAANCHFHCIETLVTTGANVNE 466
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 55-195 8.87e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.58  E-value: 8.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 694897886   55 EIIELLILSGARVNAK----DNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQ-TPLHVAAANKAVKCAEVIIPL 129
Cdd:PHA02884   47 DIIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSY 126

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 694897886  130 LSSVNVSDRGGRTALHHAALNGHVEMVNLLlaKGANINAFDKKDRRalhwaaYMGHLDVVALLINH 195
Cdd:PHA02884  127 GADINIQTNDMVTPIELALMICNNFLAFMI--CDNEISNFYKHPKK------ILINFDILKILVSH 184
Ank_5 pfam13857
Ankyrin repeats (many copies);
934-978 9.83e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 9.83e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 694897886   934 LINAKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVDENGHTP 978
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
 
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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