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Conserved domains on  [gi|304434690|ref|NP_001182073|]
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serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit B isoform A [Homo sapiens]

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
SCOP:  4000366

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 6.61e-52

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 184.00  E-value: 6.61e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  54 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSV 133
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 134 NVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 213
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 214 ASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALcLELLV 293
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 304434690 294 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 343
Cdd:COG0666  240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
492-749 2.18e-36

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 2.18e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 492 NAHDNSEELERARELKEKEATLCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEESDSGATksPL 571
Cdd:COG0666   14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT--LL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 572 HLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLR 651
Cdd:COG0666   92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVK 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 652 LLLEI-ADnpeaVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSIL 730
Cdd:COG0666  171 LLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
                        250
                 ....*....|....*....
gi 304434690 731 CKDSRGRTPLHYAAARGHA 749
Cdd:COG0666  247 AKDKDGLTALLLAAAAGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
253-534 2.49e-33

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.46  E-value: 2.49e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 253 AVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI 332
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 333 DCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAA 412
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 413 AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAASDMDRNKTILGN 492
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 304434690 493 AHDNSEELERARELKEKEATLCLEFLLQNDANPSIRDKEGYN 534
Cdd:COG0666  241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
650-975 5.85e-32

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 5.85e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 650 LRLLLEIADNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSI 729
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 730 LCKDSRGRTPLHYAAARGHATWLSELLQmalSEEDCCFKDNQGYTPLHWACYNGNENCIEVLLEQKcfrkfignpftplh 809
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-------------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 810 cAIINdhgncaslllgaidssivsCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVD 889
Cdd:COG0666  144 -ADVN-------------------AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 890 ILVNsAQADLTVKDKDLNTPLHLACSKGHEKCALLILDKIQDeslINEKNNALQTPLHVAARNGLKVVVEELLAKGACVL 969
Cdd:COG0666  204 LLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279

                 ....*.
gi 304434690 970 AVDENA 975
Cdd:COG0666  280 AALLDL 285
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 4.29e-06

Ankyrin repeats (many copies);


:

Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 4.29e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 304434690   10 PPLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLI 61
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-343 6.61e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 184.00  E-value: 6.61e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  54 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSV 133
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 134 NVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 213
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 214 ASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALcLELLV 293
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 304434690 294 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 343
Cdd:COG0666  240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
22-310 5.91e-40

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 154.80  E-value: 5.91e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  22 EEIRMLIHKTEDVNTLDSEKRTPLHVaaFLG-----DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAV-QVLIK 95
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDViKLLIK 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  96 HSADVNARDKNWQTPLHVAAANKAVkcaeviipllssvnvsdrggrtalhhaalngHVEMVNLLLAKGANINAFDKKDRR 175
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 176 ALHwaAYMGH----LDVVALLINHGAEVTCKDKKGYTPLHAAASNGQIN--VVKHLLNLGVEIDEINVYGNTALHIACYN 249
Cdd:PHA03095 155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 304434690 250 G--QDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLELLvNNGADVNIQSKDGKSPL 310
Cdd:PHA03095 233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGNTPL 294
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
492-749 2.18e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 2.18e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 492 NAHDNSEELERARELKEKEATLCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEESDSGATksPL 571
Cdd:COG0666   14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT--LL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 572 HLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLR 651
Cdd:COG0666   92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVK 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 652 LLLEI-ADnpeaVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSIL 730
Cdd:COG0666  171 LLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
                        250
                 ....*....|....*....
gi 304434690 731 CKDSRGRTPLHYAAARGHA 749
Cdd:COG0666  247 AKDKDGLTALLLAAAAGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
253-534 2.49e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.46  E-value: 2.49e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 253 AVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI 332
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 333 DCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAA 412
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 413 AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAASDMDRNKTILGN 492
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 304434690 493 AHDNSEELERARELKEKEATLCLEFLLQNDANPSIRDKEGYN 534
Cdd:COG0666  241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
650-975 5.85e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 5.85e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 650 LRLLLEIADNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSI 729
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 730 LCKDSRGRTPLHYAAARGHATWLSELLQmalSEEDCCFKDNQGYTPLHWACYNGNENCIEVLLEQKcfrkfignpftplh 809
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-------------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 810 cAIINdhgncaslllgaidssivsCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVD 889
Cdd:COG0666  144 -ADVN-------------------AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 890 ILVNsAQADLTVKDKDLNTPLHLACSKGHEKCALLILDKIQDeslINEKNNALQTPLHVAARNGLKVVVEELLAKGACVL 969
Cdd:COG0666  204 LLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279

                 ....*.
gi 304434690 970 AVDENA 975
Cdd:COG0666  280 AALLDL 285
PHA03095 PHA03095
ankyrin-like protein; Provisional
212-475 6.39e-28

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 118.59  E-value: 6.39e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 212 AAASNGQINVVKHLLNLGVEIDEINVYGNTALH--IACYNGQDA-VVNELIDYGANVNQPNNNGFTPLHFAAASTHGALC 288
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 289 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGH---ELLiNTLITSGA 363
Cdd:PHA03095 100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGA 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 364 DTAKCGIHSMFPLHLAALNAHSD--CCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQ--SSGADFHKKDKCGR 439
Cdd:PHA03095 179 DVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPllIAGISINARNRYGQ 258
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 304434690 440 TPLHYAAANCHFHCIETLVTTGANVNETDDWGRTAL 475
Cdd:PHA03095 259 TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
355-664 8.71e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 102.80  E-value: 8.71e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 355 INTLITSGADTAKCGIHSMFPLHLAALNAHSDC---CRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVE-CIKLLQSSGAD 430
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGAD 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 431 FHKKDKCGRTPLH-YAA-ANCHFHCIETLVTTGANVNETDDWGRTALHyaaasdmdrnktILGNAHDNSEELerarelke 508
Cdd:PHA03095 110 VNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLA------------VLLKSRNANVEL-------- 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 509 keatlcLEFLLQNDANPSIRDKEGYNSIHYAAAYGH--RQCLELLLERTNSGFEESDSGATksPLHLAAYNGHHQALEV- 585
Cdd:PHA03095 170 ------LRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNT--PLHSMATGSSCKRSLVl 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 586 -LLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADNPEAVD 664
Cdd:PHA03095 242 pLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNTPLSLMVRNNNGRAVRAALAKNPSAETVA 320
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-269 2.35e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 2.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  177 LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNlGVEIDEINvYGNTALHIACYNGQDAVVN 256
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 304434690  257 ELIDYGANVNQPN 269
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
651-966 5.11e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 91.24  E-value: 5.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 651 RLLLEIADnpeaVDVKDAKGQTPLMLAVAYGH---IDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEE-CVQMLLEQE 726
Cdd:PHA03095  32 RLLAAGAD----VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 727 VSILCKDSRGRTPLH-YAA-ARGHATWLSELLQMALSEEDCcfkDNQGYTPLHwaCYNGNENC----IEVLLEQKCF--- 797
Cdd:PHA03095 108 ADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNAL---DLYGMTPLA--VLLKSRNAnvelLRLLIDAGADvya 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 798 RKFIGNpfTPLH--CAIINDHGNCASLLLGAIDSsiVSCRDDKGRTPLHAAAFADHVECLQL--LLRHSAPVNAVDNSGK 873
Cdd:PHA03095 183 VDDRFR--SLLHhhLQSFKPRARIVRELIRAGCD--PAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQ 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 874 TALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLACSKGHEKCALLILDKIQDESLINEKNNALQTPLHVAARNG 953
Cdd:PHA03095 259 TPLHYAAVFNNPRACRRLIA-LGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTASVAGGDIPSDA 337
                        330
                 ....*....|...
gi 304434690 954 LKVVVEELLAKGA 966
Cdd:PHA03095 338 TRLCVAKVVLRGA 350
Ank_2 pfam12796
Ankyrin repeats (3 copies);
376-468 1.58e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  376 LHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLqSSGADFHKKDKcGRTPLHYAAANCHFHCIE 455
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDN-GRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 304434690  456 TLVTTGANVNETD 468
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
604-700 4.14e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 4.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  604 LDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADnpeaVDVKDaKGQTPLMLAVAYGHI 683
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHL 74
                          90
                  ....*....|....*..
gi 304434690  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 7.39e-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: 7.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  74 WLTPLHRAVASRSEEAVQVLIK-HSADVNARDKNWQTPLHVAAANKAVKCAEVII---PLLssVNV---SD-RGGRTALH 145
Cdd:cd22192   17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaaPEL--VNEpmtSDlYQGETALH 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 146 HAALNGHVEMVNLLLAKGANIN------AFDKKDRRAL-----H---WAAYMGHLDVVALLINHGAEVTCKDKKGYTPLH 211
Cdd:cd22192   95 IAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 304434690 212 AAASNGQINVVKH----LLNLGVEIDEINVYgntalHIacyngqdavvnelidyganvnqPNNNGFTPLHFAAA 281
Cdd:cd22192  175 ILVLQPNKTFACQmydlILSYDKEDDLQPLD-----LV----------------------PNNQGLTPFKLAAK 221
Ank_2 pfam12796
Ankyrin repeats (3 copies);
843-931 1.53e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  843 LHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKdlnTPLHLACSKGHEKCA 922
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77

                  ....*....
gi 304434690  923 LLILDKIQD 931
Cdd:pfam12796  78 KLLLEKGAD 86
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
49-280 1.51e-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: 1.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690   49 AFLGDAEIIELLILSGARVNAK-------DNMWLTPLHRAVA-SRSEEAVQVLIKHSADVNARDknwqTPLHVAAANKAV 120
Cdd:TIGR00870  20 AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAISLEYVD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  121 KCAEVIIPLLSS---------VNVSDRG----GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRA----- 176
Cdd:TIGR00870  96 AVEAILLHLLAAfrksgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDsfyhg 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  177 ---LHWAAYMGHLDVVALLINHGAEVTCKDKKGytplhaaasngqiNVVKHLLNLGVEideiNVYGNTALHIACYngqda 253
Cdd:TIGR00870 176 espLNAAACLGSPSIVALLSEDPADILTADSLG-------------NTLLHLLVMENE----FKAEYEELSCQMY----- 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 304434690  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 3.89e-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: 3.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 567 TKSPLHLAAYNGHHQALEVLL-QSLVDLDIRDEKGRTALDLAAFKGHTECVEALInqgasifvkDNVTkrtplhasving 645
Cdd:cd22192   17 SESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLM---------EAAP------------ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 646 htlclrlllEIADNPEAVDVkdAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGcTALHRGI-------------- 711
Cdd:cd22192   76 ---------ELVNEPMTSDL--YQGETALHIAVVNQNLNLVRELIARGADVVSPRATG-TFFRPGPknliyygehplsfa 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 712 -MTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALSEE----DCCF---KDNQGYTPLHWACYNG 783
Cdd:cd22192  144 aCVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYDLILSYDkeddLQPLdlvPNNQGLTPFKLAAKEG 223

                 .
gi 304434690 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 1.32e-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: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 340 NTPLHVAARYGHELLINTLITS-GADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSG----FEIDTPDKF-GRTCLHAAA 413
Cdd:cd22192   18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelvNEPMTSDLYqGETALHIAV 97
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 304434690 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 3.67e-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: 3.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  569 SPLHLAAYNGHHQALEVLLQSLvdlDIRDEKGRTALdLAAFKGHTECVEALIN--------QGASIFVKDNVTKR----- 635
Cdd:TIGR00870  54 SALFVAAIENENLELTELLLNL---SCRGAVGDTLL-HAISLEYVDAVEAILLhllaafrkSGPLELANDQYTSEftpgi 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  636 TPLHASVINGHTLCLRLLLEIADNPEA----VDVKDAKGQT-------PLMLAVAYGHIDAVSLLLEKEANVDTVDILGC 704
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPAracgDFFVKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  705 TALHRGIMtgheECVQMLLEQEVSILCKDSrgrtplhyaaarghATWLSELLQMALSEEDCCfkDNQGYTPLHWACYNGN 784
Cdd:TIGR00870 210 TLLHLLVM----ENEFKAEYEELSCQMYNF--------------ALSLLDKLRDSKELEVIL--NHQGLTPLKLAAKEGR 269
                         250       260       270
                  ....*....|....*....|....*....|
gi 304434690  785 ENCIEVLLEQKCF-RKFIGNPFTPLHCAII 813
Cdd:TIGR00870 270 IVLFRLKLAIKYKqKKFVAWPNGQQLLSLY 299
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
140-168 3.93e-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: 3.93e-06
                           10        20
                   ....*....|....*....|....*....
gi 304434690   140 GRTALHHAALNGHVEMVNLLLAKGANINA 168
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 4.29e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 4.29e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 304434690   10 PPLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLI 61
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
720-926 6.91e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.08  E-value: 6.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  720 QMLLE-QEVSILCKDSRGRTPLHYAAARGHATWLSELLQmalseedccFKDNQGY---TPLHWACYNGNENCIEVLLEQK 795
Cdd:TIGR00870  35 RDLEEpKKLNINCPDRLGRSALFVAAIENENLELTELLL---------NLSCRGAvgdTLLHAISLEYVDAVEAILLHLL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  796 CFRKFIGNPF--------------TPLHCAIINDHGNCASLLL--GAIDSSIVSCRDDK----------GRTPLHAAAFA 849
Cdd:TIGR00870 106 AAFRKSGPLElandqytseftpgiTALHLAAHRQNYEIVKLLLerGASVPARACGDFFVksqgvdsfyhGESPLNAAACL 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  850 DHVECLQLLLRHSAPVNAVDNSGKTALMMA-------AENG------QAGAVDILvnsAQADLTVK-----DKDLNTPLH 911
Cdd:TIGR00870 186 GSPSIVALLSEDPADILTADSLGNTLLHLLvmenefkAEYEelscqmYNFALSLL---DKLRDSKElevilNHQGLTPLK 262
                         250
                  ....*....|....*
gi 304434690  912 LACSKGHEKCALLIL 926
Cdd:TIGR00870 263 LAAKEGRIVLFRLKL 277
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
774-964 1.82e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.47  E-value: 1.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 774 TPLHWACYNGNENCIEVLLEQK----CFRKFIGNpfTPLHCAIINDHGNCASLLLGAIDSSI---VSCRDDKGRTPLHAA 846
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCPscdlFQRGALGE--TALHVAALYDNLEAAVVLMEAAPELVnepMTSDLYQGETALHIA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 847 AFADHVECLQLLLRHSAPVNA-----------VDN---SGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHL 912
Cdd:cd22192   97 VVNQNLNLVRELIARGADVVSpratgtffrpgPKNliyYGEHPLSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVLHI 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 304434690 913 ACSKGHEKCA------LLILDKIQDE-SLINEKNNALQTPLHVAARNGLKVVVEELLAK 964
Cdd:cd22192  176 LVLQPNKTFAcqmydlILSYDKEDDLqPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
438-466 6.72e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 6.72e-04
                           10        20
                   ....*....|....*....|....*....
gi 304434690   438 GRTPLHYAAANCHFHCIETLVTTGANVNE 466
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
332-476 7.24e-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: 7.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  332 IDCVDKDGNTPLHVAARYG-HELLINTLITSGA-----DTAkcgihsmfpLHLAALNAH---SDCCRKLLSSGFEIDTPD 402
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISLEYVdavEAILLHLLAAFRKSGPLE 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  403 ----------KFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKC--------------GRTPLHYAAANCHFHCIETLV 458
Cdd:TIGR00870 116 landqytsefTPGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLS 195
                         170
                  ....*....|....*...
gi 304434690  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 ...
771-793 1.73e-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: 1.73e-03
                           10        20
                   ....*....|....*....|...
gi 304434690   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 3.90e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 3.90e-03
                           10        20
                   ....*....|....*....|....*....
gi 304434690   669 KGQTPLMLAVAYGHIDAVSLLLEKEANVD 697
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-343 6.61e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 184.00  E-value: 6.61e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  54 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSV 133
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 134 NVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 213
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 214 ASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALcLELLV 293
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 304434690 294 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 343
Cdd:COG0666  240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-307 3.75e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 176.30  E-value: 3.75e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  22 EEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVN 101
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 102 ARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAA 181
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 182 YMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDY 261
Cdd:COG0666  162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 304434690 262 GANVNQPNNNGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGK 307
Cdd:COG0666  242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
11-276 3.75e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 176.30  E-value: 3.75e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  11 PLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAV 90
Cdd:COG0666   24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  91 QVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFD 170
Cdd:COG0666  104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 171 KKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNG 250
Cdd:COG0666  184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
                        250       260
                 ....*....|....*....|....*.
gi 304434690 251 QDAVVNELIDYGANVNQPNNNGFTPL 276
Cdd:COG0666  264 AALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-243 3.71e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 156.27  E-value: 3.71e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690   8 DQPPLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSE 87
Cdd:COG0666   87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  88 EAVQVLIKHSADVNARDKNwqtplhvaaankavkcaeviipllssvnvsdrgGRTALHHAALNGHVEMVNLLLAKGANIN 167
Cdd:COG0666  167 EIVKLLLEAGADVNARDND---------------------------------GETPLHLAAENGHLEIVKLLLEAGADVN 213
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 304434690 168 AFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTAL 243
Cdd:COG0666  214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
22-310 5.91e-40

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 154.80  E-value: 5.91e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  22 EEIRMLIHKTEDVNTLDSEKRTPLHVaaFLG-----DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAV-QVLIK 95
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDViKLLIK 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  96 HSADVNARDKNWQTPLHVAAANKAVkcaeviipllssvnvsdrggrtalhhaalngHVEMVNLLLAKGANINAFDKKDRR 175
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 176 ALHwaAYMGH----LDVVALLINHGAEVTCKDKKGYTPLHAAASNGQIN--VVKHLLNLGVEIDEINVYGNTALHIACYN 249
Cdd:PHA03095 155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 304434690 250 G--QDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLELLvNNGADVNIQSKDGKSPL 310
Cdd:PHA03095 233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGNTPL 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
86-359 1.67e-39

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 153.26  E-value: 1.67e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  86 SEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSS---VNVSDRGGRTALHHAALNGHVE-MVNLLLA 161
Cdd:PHA03095  26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAgadVNAPERCGFTPLHLYLYNATTLdVIKLLIK 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 162 KGANINAFDKKDRRALHwaAYMG----HLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINV--VKHLLNLGVEIDEI 235
Cdd:PHA03095 106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 236 NVYGNTALHIACYNGQD--AVVNELIDYGANVNQPNNNGFTPLHFAAA-STHGALCLELLVNNGADVNIQSKDGKSPLHM 312
Cdd:PHA03095 184 DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 304434690 313 TAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLI 359
Cdd:PHA03095 264 AAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
153-507 7.29e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.64  E-value: 7.29e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 153 VEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEI 232
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 233 DEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALcLELLVNNGADVNIQskdgksplhm 312
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI-VKLLLEAGADVNAQ---------- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 313 tavhgrftrsqtliqnggeidcvDKDGNTPLHVAARYGHELLINTLITSGADtakcgihsmfplhlaalnahsdccrkll 392
Cdd:COG0666  150 -----------------------DNDGNTPLHLAAANGNLEIVKLLLEAGAD---------------------------- 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 393 ssgfeIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGR 472
Cdd:COG0666  179 -----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGL 253
                        330       340       350
                 ....*....|....*....|....*....|....*
gi 304434690 473 TALHYAAASDMDRNKTILGNAHDNSEELERARELK 507
Cdd:COG0666  254 TALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
PHA03100 PHA03100
ankyrin repeat protein; Provisional
55-301 5.07e-37

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 144.81  E-value: 5.07e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  55 EIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAV-----KCAEVIIPL 129
Cdd:PHA03100  16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEY 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 130 LSSVNVSDRGGRTALHHAALN--GHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGH--LDVVALLINHGAEVTCKDKk 205
Cdd:PHA03100  96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNR- 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 206 gytplhaaasngqinvVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHG 285
Cdd:PHA03100 175 ----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238
                        250
                 ....*....|....*.
gi 304434690 286 ALcLELLVNNGADVNI 301
Cdd:PHA03100 239 EI-FKLLLNNGPSIKT 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
492-749 2.18e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 2.18e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 492 NAHDNSEELERARELKEKEATLCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEESDSGATksPL 571
Cdd:COG0666   14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT--LL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 572 HLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLR 651
Cdd:COG0666   92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVK 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 652 LLLEI-ADnpeaVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSIL 730
Cdd:COG0666  171 LLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
                        250
                 ....*....|....*....
gi 304434690 731 CKDSRGRTPLHYAAARGHA 749
Cdd:COG0666  247 AKDKDGLTALLLAAAAGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
515-795 6.31e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.08  E-value: 6.31e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 515 LEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEESDSGATKSPLHLAAYNGHHQALEVLLQSLVDLD 594
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 595 IRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEI-ADnpeaVDVKDAKGQTP 673
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAgAD----VNAQDNDGNTP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 674 LMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLS 753
Cdd:COG0666  157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 304434690 754 ELLQMALSEEDccfKDNQGYTPLHWACYNGNENCIEVLLEQK 795
Cdd:COG0666  237 LLLEAGADLNA---KDKDGLTALLLAAAAGAALIVKLLLLAL 275
PHA02874 PHA02874
ankyrin repeat protein; Provisional
16-367 5.48e-34

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 136.25  E-value: 5.48e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  16 IFSGDPEEIRMLI-HKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLI 94
Cdd:PHA02874   9 IYSGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  95 KHSADVNArdknwqtplhvaaankavkcaeVIIPLLSSvnvsdrggrtalhhaalnghvEMVNLLLAKGANINAFDKKDR 174
Cdd:PHA02874  89 DNGVDTSI----------------------LPIPCIEK---------------------DMIKTILDCGIDVNIKDAELK 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 175 RALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAV 254
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 255 VNELIDYGANVNQPNNNGFTPLHfaAASTHGALCLELLVNNgADVNIQSKDGKSPLHMtAVHGRFTRS--QTLIQNGGEI 332
Cdd:PHA02874 206 IKLLIDHGNHIMNKCKNGFTPLH--NAIIHNRSAIELLINN-ASINDQDIDGSTPLHH-AINPPCDIDiiDILLYHKADI 281
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 304434690 333 DCVDKDGNTPLHVAARYGH------ELLINTLITSGADTAK 367
Cdd:PHA02874 282 SIKDNKGENPIDTAFKYINkdpvikDIIANAVLIKEADKLK 322
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
618-942 1.09e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.61  E-value: 1.09e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 618 ALINQGASIFVKDNVTKRTPLHASVINGHTLCLRLLLEIADNpeaVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVD 697
Cdd:COG0666    5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLA---LALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 698 TVDILGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQmalSEEDCCFKDNQGYTPLH 777
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE---AGADVNAQDNDGNTPLH 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 778 WACYNGNENCIEVLLEqkcfrkfignpftplHCAIINDhgncaslllgaidssivscRDDKGRTPLHAAAFADHVECLQL 857
Cdd:COG0666  159 LAAANGNLEIVKLLLE---------------AGADVNA-------------------RDNDGETPLHLAAENGHLEIVKL 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 858 LLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLACSKGHEKCALLILDKIQDESLINE 937
Cdd:COG0666  205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE-AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283

                 ....*
gi 304434690 938 KNNAL 942
Cdd:COG0666  284 DLLTL 288
PHA02876 PHA02876
ankyrin repeat protein; Provisional
26-364 1.92e-33

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 138.27  E-value: 1.92e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  26 MLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDK 105
Cdd:PHA02876 163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDL 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 106 NwqtpLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHV-EMVNLLLAKGANINAFDKKDRRALHWAAYMG 184
Cdd:PHA02876 243 S----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNG 318
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 185 H-LDVVALLINHGAEVTCKDKKGYTPLHAAAS-NGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYG 262
Cdd:PHA02876 319 YdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 263 ANVNQPNNNGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHG-RFTRSQTLIQNGGEIDCVDKDGNT 341
Cdd:PHA02876 399 ADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQY 478
                        330       340
                 ....*....|....*....|...
gi 304434690 342 PLHVAarYGHELLINTLITSGAD 364
Cdd:PHA02876 479 PLLIA--LEYHGIVNILLHYGAE 499
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
253-534 2.49e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.46  E-value: 2.49e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 253 AVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI 332
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 333 DCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAA 412
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 413 AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAASDMDRNKTILGN 492
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 304434690 493 AHDNSEELERARELKEKEATLCLEFLLQNDANPSIRDKEGYN 534
Cdd:COG0666  241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
325-669 5.52e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 5.52e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 325 LIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDKF 404
Cdd:COG0666    7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 405 GRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAASdmd 484
Cdd:COG0666   87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN--- 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 485 rnktilgnahdNSEELerarelkekeatlcLEFLLQNDANPSIRDKEGYnsihyaaayghrqclelllertnsgfeesds 564
Cdd:COG0666  164 -----------GNLEI--------------VKLLLEAGADVNARDNDGE------------------------------- 187
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 565 gatkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNVTKRTPLHASVIN 644
Cdd:COG0666  188 ----TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
                        330       340
                 ....*....|....*....|....*
gi 304434690 645 GHTLCLRLLLEIADNPEAVDVKDAK 669
Cdd:COG0666  264 AALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
650-975 5.85e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 5.85e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 650 LRLLLEIADNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSI 729
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 730 LCKDSRGRTPLHYAAARGHATWLSELLQmalSEEDCCFKDNQGYTPLHWACYNGNENCIEVLLEQKcfrkfignpftplh 809
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-------------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 810 cAIINdhgncaslllgaidssivsCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVD 889
Cdd:COG0666  144 -ADVN-------------------AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 890 ILVNsAQADLTVKDKDLNTPLHLACSKGHEKCALLILDKIQDeslINEKNNALQTPLHVAARNGLKVVVEELLAKGACVL 969
Cdd:COG0666  204 LLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279

                 ....*.
gi 304434690 970 AVDENA 975
Cdd:COG0666  280 AALLDL 285
PHA02876 PHA02876
ankyrin repeat protein; Provisional
56-385 1.03e-31

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 132.88  E-value: 1.03e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  56 IIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNV 135
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 136 SDrggrTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLD-VVALLINHGAEVTCKDKKGYTPLHAAA 214
Cdd:PHA02876 240 ND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMA 315
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 215 SNG-QINVVKHLLNLGVEIDEINVYGNTALHIACY--NGQDAVVNeLIDYGANVNQPNNNGFTPLHFAAAStHGALCLEL 291
Cdd:PHA02876 316 KNGyDTENIRTLIMLGADVNAADRLYITPLHQASTldRNKDIVIT-LLELGANVNARDYCDKTPIHYAAVR-NNVVIINT 393
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 292 LVNNGADVNIQSKDGKSPLHMtAVHGR--FTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHEL-LINTLITSGADTAKC 368
Cdd:PHA02876 394 LLDYGADIEALSQKIGTALHF-ALCGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAI 472
                        330
                 ....*....|....*..
gi 304434690 369 GIHSMFPLhLAALNAHS 385
Cdd:PHA02876 473 NIQNQYPL-LIALEYHG 488
PHA02876 PHA02876
ankyrin repeat protein; Provisional
123-465 1.21e-30

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 129.41  E-value: 1.21e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 123 AEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCK 202
Cdd:PHA02876 161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKN 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 203 DkkgyTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQ-DAVVNELIDYGANVNQPNNNGFTPLHFAAA 281
Cdd:PHA02876 241 D----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAK 316
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 282 STHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQ-TLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLIT 360
Cdd:PHA02876 317 NGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIViTLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 361 SGADtakcgihsmfplhLAALNahsdccrkllssgfeidtpDKFGrTCLHAAAAGGN-VECIKLLQSSGADFHKKDKCGR 439
Cdd:PHA02876 397 YGAD-------------IEALS-------------------QKIG-TALHFALCGTNpYMSVKTLIDRGANVNSKNKDLS 443
                        330       340
                 ....*....|....*....|....*..
gi 304434690 440 TPLHYAAA-NCHFHCIETLVTTGANVN 465
Cdd:PHA02876 444 TPLHYACKkNCKLDVIEMLLDNGADVN 470
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
474-740 5.34e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.83  E-value: 5.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 474 ALHYAAASDMDRNKTILGNAHDNSEELERARELKEKEATLCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLE 553
Cdd:COG0666   29 ALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 554 RTNSGFEESDSGATksPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvT 633
Cdd:COG0666  109 AGADVNARDKDGET--PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-D 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 634 KRTPLHASVINGHTLCLRLLLE-IADnpeaVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIM 712
Cdd:COG0666  186 GETPLHLAAENGHLEIVKLLLEaGAD----VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261
                        250       260
                 ....*....|....*....|....*...
gi 304434690 713 TGHEECVQMLLEQEVSILCKDSRGRTPL 740
Cdd:COG0666  262 AGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
12-265 2.26e-28

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 122.09  E-value: 2.26e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  12 LVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGD-AEIIELLILSGARVNAKDNMWLTPLH-RAVASRSEEA 89
Cdd:PHA02876 244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYlMAKNGYDTEN 323
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  90 VQVLIKHSADVNARDKNWQTPLHVAAANKAVKcaEVIIPLL---SSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANI 166
Cdd:PHA02876 324 IRTLIMLGADVNAADRLYITPLHQASTLDRNK--DIVITLLelgANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 167 NAFDKKDRRALHWAAY-MGHLDVVALLINHGAEVTCKDKKGYTPLH-AAASNGQINVVKHLLNLGVEIDEINVYGNTALH 244
Cdd:PHA02876 402 EALSQKIGTALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHyACKKNCKLDVIEMLLDNGADVNAINIQNQYPLL 481
                        250       260
                 ....*....|....*....|.
gi 304434690 245 IACynGQDAVVNELIDYGANV 265
Cdd:PHA02876 482 IAL--EYHGIVNILLHYGAEL 500
PHA03095 PHA03095
ankyrin-like protein; Provisional
212-475 6.39e-28

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 118.59  E-value: 6.39e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 212 AAASNGQINVVKHLLNLGVEIDEINVYGNTALH--IACYNGQDA-VVNELIDYGANVNQPNNNGFTPLHFAAASTHGALC 288
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 289 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGH---ELLiNTLITSGA 363
Cdd:PHA03095 100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGA 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 364 DTAKCGIHSMFPLHLAALNAHSD--CCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQ--SSGADFHKKDKCGR 439
Cdd:PHA03095 179 DVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPllIAGISINARNRYGQ 258
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 304434690 440 TPLHYAAANCHFHCIETLVTTGANVNETDDWGRTAL 475
Cdd:PHA03095 259 TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA03100 PHA03100
ankyrin repeat protein; Provisional
192-465 6.56e-28

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 117.84  E-value: 6.56e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 192 LINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIAC---YNGQDAV--VNELIDYGANVN 266
Cdd:PHA03100  21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikYNLTDVKeiVKLLLEYGANVN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 267 QPNNNGFTPLHFAAASTHGALCL-ELLVNNGADVNIQSKDGKSPLHMtavhgrFTRSqtliqnggeiDCVDKDgntplhv 345
Cdd:PHA03100 101 APDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHL------YLES----------NKIDLK------- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 346 aaryghelLINTLITSGAD-TAKCGIHSmfplhlaalnahsdccrkLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLL 424
Cdd:PHA03100 158 --------ILKLLIDKGVDiNAKNRVNY------------------LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYL 211
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 304434690 425 QSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVN 465
Cdd:PHA03100 212 LDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02878 PHA02878
ankyrin repeat protein; Provisional
75-346 1.77e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 114.21  E-value: 1.77e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  75 LTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVA--AANKavkcaEVIIPLLSSVNVSDRG-GRTALHHAALNG 151
Cdd:PHA02878  38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckEPNK-----LGMKEMIRSINKCSVFyTLVAIKDAFNNR 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 152 HVEMVNLLLakganINAFDKK---DRRALHWAAYMGHLD--VVALLINHGAEVTCKDK-KGYTPLHAAASNGQINVVKHL 225
Cdd:PHA02878 113 NVEIFKIIL-----TNRYKNIqtiDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELL 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 226 LNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLELLVNNGADVNIQSK- 304
Cdd:PHA02878 188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYi 267
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 304434690 305 DGKSPLHMTAVHGRFTRsqTLIQNGGEIDCVDKDGNTPLHVA 346
Cdd:PHA02878 268 LGLTALHSSIKSERKLK--LLLEYGADINSLNSYKLTPLSSA 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
28-238 9.74e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 111.30  E-value: 9.74e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  28 IHKTEDVNT-LDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLH-----RAVASRSEEAVQVLIKHSADVN 101
Cdd:PHA03100  21 IIMEDDLNDySYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 102 ARDKNWQTPLHVAAANKavKCAEVIIPLLSS----VNVSDRGGRTALHHAALNGHV--EMVNLLLAKGANINAFDK---- 171
Cdd:PHA03100 101 APDNNGITPLLYAISKK--SNSYSIVEYLLDnganVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRvnyl 178
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 304434690 172 ---------KDRR---ALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVY 238
Cdd:PHA03100 179 lsygvpiniKDVYgftPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA03095 PHA03095
ankyrin-like protein; Provisional
254-622 8.33e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 103.18  E-value: 8.33e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 254 VVNELIDYGANVNQPNNNGFTPLHFAAASTHGAL--CLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTR-SQTLIQNGG 330
Cdd:PHA03095  29 EVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDvIKLLIKAGA 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 331 EIDCVDKDGNTPLHVaaryghellintlitsgadtakcgihsmfplHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLH 410
Cdd:PHA03095 109 DVNAKDKVGRTPLHV-------------------------------YLSGFNINPKVIRLLLRKGADVNALDLYGMTPLA 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 411 A--AAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFH--CIETLVTTGANVNETDDWGRTALHYAAASDMDRN 486
Cdd:PHA03095 158 VllKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKR 237
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 487 KTILgnahdnseelerarelkekeatlcleFLLQNDANPSIRDKEGYnsihyaaayghrqclelllertnsgfeesdsga 566
Cdd:PHA03095 238 SLVL--------------------------PLLIAGISINARNRYGQ--------------------------------- 258
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 304434690 567 tkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQ 622
Cdd:PHA03095 259 --TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
PHA03095 PHA03095
ankyrin-like protein; Provisional
355-664 8.71e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 102.80  E-value: 8.71e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 355 INTLITSGADTAKCGIHSMFPLHLAALNAHSDC---CRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVE-CIKLLQSSGAD 430
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGAD 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 431 FHKKDKCGRTPLH-YAA-ANCHFHCIETLVTTGANVNETDDWGRTALHyaaasdmdrnktILGNAHDNSEELerarelke 508
Cdd:PHA03095 110 VNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLA------------VLLKSRNANVEL-------- 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 509 keatlcLEFLLQNDANPSIRDKEGYNSIHYAAAYGH--RQCLELLLERTNSGFEESDSGATksPLHLAAYNGHHQALEV- 585
Cdd:PHA03095 170 ------LRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNT--PLHSMATGSSCKRSLVl 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 586 -LLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADNPEAVD 664
Cdd:PHA03095 242 pLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNTPLSLMVRNNNGRAVRAALAKNPSAETVA 320
PHA02878 PHA02878
ankyrin repeat protein; Provisional
22-295 1.30e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 102.65  E-value: 1.30e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  22 EEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIK------ 95
Cdd:PHA02878  18 KYIEYIDHTENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcs 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  96 ------------HSADVNA-------RDKNWQTP--LHVAAANKAVKCAEVIIPLL----SSVNVSDR-GGRTALHHAAL 149
Cdd:PHA02878  98 vfytlvaikdafNNRNVEIfkiiltnRYKNIQTIdlVYIDKKSKDDIIEAEITKLLlsygADINMKDRhKGNTALHYATE 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 150 NGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASN-GQINVVKHLLNL 228
Cdd:PHA02878 178 NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEH 257
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 304434690 229 GVEID-EINVYGNTALHIACYNGQdaVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLELLVNN 295
Cdd:PHA02878 258 GVDVNaKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISN 323
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-269 2.35e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 2.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  177 LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNlGVEIDEINvYGNTALHIACYNGQDAVVN 256
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 304434690  257 ELIDYGANVNQPN 269
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
144-236 4.14e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 4.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  144 LHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHgAEVTCKDkKGYTPLHAAASNGQINVVK 223
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 304434690  224 HLLNLGVEIDEIN 236
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
218-598 7.16e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 98.60  E-value: 7.16e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 218 QINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHgALCLELLVNNGA 297
Cdd:PHA02876 157 ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN-IDTIKAIIDNRS 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 298 DVNiqsKDGKSPLHMTAvHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGH-ELLINTLITSGADTAKCGIHSMFPL 376
Cdd:PHA02876 236 NIN---KNDLSLLKAIR-NEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 377 HLAALNAH-SDCCRKLLSSGFEIDTPDKFGRTCLHAAAA-GGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCI 454
Cdd:PHA02876 312 YLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVII 391
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 455 ETLVTTGANVNETDDWGRTALHYA---------AASDMDRNKTILGNAHDNSEELERAreLKEKEATLCLEFLLQNDANP 525
Cdd:PHA02876 392 NTLLDYGADIEALSQKIGTALHFAlcgtnpymsVKTLIDRGANVNSKNKDLSTPLHYA--CKKNCKLDVIEMLLDNGADV 469
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 304434690 526 SIRDKEgyNSIHYAAAYGHRQCLELLLertNSGFEESDSGATKSPLHLAAYNGHHQALEVLLQSLVDLDIRDE 598
Cdd:PHA02876 470 NAINIQ--NQYPLLIALEYHGIVNILL---HYGAELRDSRVLHKSLNDNMFSFRYIIAHICIQDFIRHDIRNE 537
PHA03095 PHA03095
ankyrin-like protein; Provisional
24-235 1.68e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 95.86  E-value: 1.68e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  24 IRMLIHKTEDVNTLDSEKRTPLHV--AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASR--SEEAVQVLIKHSAD 99
Cdd:PHA03095 100 IKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGAD 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 100 VNARDKNWQTPLHVAAAN--KAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNL--LLAKGANINAFDKKDRR 175
Cdd:PHA03095 180 VYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQT 259
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 176 ALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEI 235
Cdd:PHA03095 260 PLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
PHA02875 PHA02875
ankyrin repeat protein; Provisional
48-266 2.40e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 94.67  E-value: 2.40e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  48 AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 127
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 128 PLLSSVN-VSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKG 206
Cdd:PHA02875  89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 304434690 207 YTPLHAAASNGQINVVKHLLNLGVEIDEINVYGN-TALHIACYNGQDAVVNELIDYGANVN 266
Cdd:PHA02875 169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02874 PHA02874
ankyrin repeat protein; Provisional
220-545 3.76e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 94.65  E-value: 3.76e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 220 NVVKHLLN-LGVEIDEINvygnTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLhFAAASTHGALCLELLVNNGAD 298
Cdd:PHA02874  19 KIIKNKGNcINISVDETT----TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPL-LTAIKIGAHDIIKLLIDNGVD 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 299 VNIqskdgkspLHMTAVHGRFTRsqTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHL 378
Cdd:PHA02874  94 TSI--------LPIPCIEKDMIK--TILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 379 AALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAanCHFHCIETLV 458
Cdd:PHA02874 164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI--IHNRSAIELL 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 459 TTGANVNETDDWGRTALHYAAASDMDRNktilgnahdnseelerarelkekeatlCLEFLLQNDANPSIRDKEGYNSIHY 538
Cdd:PHA02874 242 INNASINDQDIDGSTPLHHAINPPCDID---------------------------IIDILLYHKADISIKDNKGENPIDT 294

                 ....*..
gi 304434690 539 AAAYGHR 545
Cdd:PHA02874 295 AFKYINK 301
Ank_2 pfam12796
Ankyrin repeats (3 copies);
111-203 2.66e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 2.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  111 LHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKgANINAFDkKDRRALHWAAYMGHLDVVA 190
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 304434690  191 LLINHGAEVTCKD 203
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
389-664 4.31e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.88  E-value: 4.31e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 389 RKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHF--HCIET---LVTTGAN 463
Cdd:PHA03100  19 KYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltDVKEIvklLLEYGAN 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 464 VNETDDWGRTALHYAAASDMDRNKTIlgnahdnseelerarelkekeatlclEFLLQNDANPSIRDKEGYNSIHYAAAYG 543
Cdd:PHA03100  99 VNAPDNNGITPLLYAISKKSNSYSIV--------------------------EYLLDNGANVNIKNSDGENLLHLYLESN 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 544 HR--QCLELLLERTNsgfeesdsgatksplHLAAYNghhqALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALIN 621
Cdd:PHA03100 153 KIdlKILKLLIDKGV---------------DINAKN----RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLD 213
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|...
gi 304434690 622 QGASIFVKDNVTKrTPLHASVINGHTLCLRLLLEIADNPEAVD 664
Cdd:PHA03100 214 LGANPNLVNKYGD-TPLHIAILNNNKEIFKLLLNNGPSIKTII 255
PHA03095 PHA03095
ankyrin-like protein; Provisional
651-966 5.11e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 91.24  E-value: 5.11e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 651 RLLLEIADnpeaVDVKDAKGQTPLMLAVAYGH---IDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEE-CVQMLLEQE 726
Cdd:PHA03095  32 RLLAAGAD----VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 727 VSILCKDSRGRTPLH-YAA-ARGHATWLSELLQMALSEEDCcfkDNQGYTPLHwaCYNGNENC----IEVLLEQKCF--- 797
Cdd:PHA03095 108 ADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNAL---DLYGMTPLA--VLLKSRNAnvelLRLLIDAGADvya 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 798 RKFIGNpfTPLH--CAIINDHGNCASLLLGAIDSsiVSCRDDKGRTPLHAAAFADHVECLQL--LLRHSAPVNAVDNSGK 873
Cdd:PHA03095 183 VDDRFR--SLLHhhLQSFKPRARIVRELIRAGCD--PAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQ 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 874 TALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLACSKGHEKCALLILDKIQDESLINEKNNALQTPLHVAARNG 953
Cdd:PHA03095 259 TPLHYAAVFNNPRACRRLIA-LGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTASVAGGDIPSDA 337
                        330
                 ....*....|...
gi 304434690 954 LKVVVEELLAKGA 966
Cdd:PHA03095 338 TRLCVAKVVLRGA 350
Ank_2 pfam12796
Ankyrin repeats (3 copies);
210-302 6.27e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 6.27e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  210 LHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYgANVNqPNNNGFTPLHFAAASTHGAlCL 289
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLE-IV 77
                          90
                  ....*....|...
gi 304434690  290 ELLVNNGADVNIQ 302
Cdd:pfam12796  78 KLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
376-468 1.58e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  376 LHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLqSSGADFHKKDKcGRTPLHYAAANCHFHCIE 455
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDN-GRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 304434690  456 TLVTTGANVNETD 468
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
604-700 4.14e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 4.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  604 LDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADnpeaVDVKDaKGQTPLMLAVAYGHI 683
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHL 74
                          90
                  ....*....|....*..
gi 304434690  684 DAVSLLLEKEANVDTVD 700
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
45-170 1.22e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 1.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690   45 LHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHsADVNARDKnwqtplhvaaankavkcae 124
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN------------------- 60
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 304434690  125 viipllssvnvsdrgGRTALHHAALNGHVEMVNLLLAKGANINAFD 170
Cdd:pfam12796  61 ---------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
571-869 1.71e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 86.17  E-value: 1.71e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 571 LHLAAYNGHHQALEVLLQSLVD-LDIRDEKGRTALDLAAFKGHTECVEALINQGASI-FVKDNVTKrtPLHASVINGHTL 648
Cdd:PHA02874   5 LRMCIYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADInHINTKIPH--PLLTAIKIGAHD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 649 CLRLLLE--------------------IADNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALH 708
Cdd:PHA02874  83 IIKLLIDngvdtsilpipciekdmiktILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIH 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 709 RGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALSEEDCCfkdNQGYTPLHWACYNgNENCI 788
Cdd:PHA02874 163 IAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKC---KNGFTPLHNAIIH-NRSAI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 789 EVLLEQKCFRKFIGNPFTPLHCAIIN--DHGNCASLLLGAIDSSIvscRDDKGRTPLHAA-AFADHVECLQLLLRHSAPV 865
Cdd:PHA02874 239 ELLINNASINDQDIDGSTPLHHAINPpcDIDIIDILLYHKADISI---KDNKGENPIDTAfKYINKDPVIKDIIANAVLI 315

                 ....
gi 304434690 866 NAVD 869
Cdd:PHA02874 316 KEAD 319
PHA02875 PHA02875
ankyrin repeat protein; Provisional
254-465 2.00e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 85.81  E-value: 2.00e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 254 VVNELIDYGANVNQPNNNGFTPLHFAAaSTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI- 332
Cdd:PHA02875  17 IARRLLDIGINPNFEIYDGISPIKLAM-KFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAd 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 333 DCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAA 412
Cdd:PHA02875  96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 304434690 413 AAGGNVECIKLLQSSGA--DFHKKDKCgRTPLHYAAANCHFHCIETLVTTGANVN 465
Cdd:PHA02875 176 MAKGDIAICKMLLDSGAniDYFGKNGC-VAALCYAIENNKIDIVRLFIKRGADCN 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
571-664 6.38e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.69  E-value: 6.38e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  571 LHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQgasIFVKDNVTKRTPLHASVINGHTLCL 650
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 304434690  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 7.39e-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: 7.39e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  74 WLTPLHRAVASRSEEAVQVLIK-HSADVNARDKNWQTPLHVAAANKAVKCAEVII---PLLssVNV---SD-RGGRTALH 145
Cdd:cd22192   17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaaPEL--VNEpmtSDlYQGETALH 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 146 HAALNGHVEMVNLLLAKGANIN------AFDKKDRRAL-----H---WAAYMGHLDVVALLINHGAEVTCKDKKGYTPLH 211
Cdd:cd22192   95 IAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 304434690 212 AAASNGQINVVKH----LLNLGVEIDEINVYgntalHIacyngqdavvnelidyganvnqPNNNGFTPLHFAAA 281
Cdd:cd22192  175 ILVLQPNKTFACQmydlILSYDKEDDLQPLD-----LV----------------------PNNQGLTPFKLAAK 221
Ank_2 pfam12796
Ankyrin repeats (3 copies);
843-931 1.53e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.53e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  843 LHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKdlnTPLHLACSKGHEKCA 922
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77

                  ....*....
gi 304434690  923 LLILDKIQD 931
Cdd:pfam12796  78 KLLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
638-733 1.79e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.79e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  638 LHASVINGHTLCLRLLLEiadNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKeANVDTVDiLGCTALHRGIMTGHEE 717
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE---NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLE 75
                          90
                  ....*....|....*.
gi 304434690  718 CVQMLLEQEVSILCKD 733
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
12-104 2.42e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 2.42e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690   12 LVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLiLSGARVNAKDNMWlTPLHRAVASRSEEAVQ 91
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDNGR-TALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 304434690   92 VLIKHSADVNARD 104
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
20-170 4.74e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 82.24  E-value: 4.74e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  20 DPEEIRMLIHKTEDVNTLDSEK-RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSA 98
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 304434690  99 DVNARDKNWQTPLHVAAAnkAVKCAEVIIPLL---SSVNV-SDRGGRTALHHAALNGHVemVNLLLAKGANINAFD 170
Cdd:PHA02878 226 STDARDKCGNTPLHISVG--YCKDYDILKLLLehgVDVNAkSYILGLTALHSSIKSERK--LKLLLEYGADINSLN 297
PHA02878 PHA02878
ankyrin repeat protein; Provisional
233-550 5.46e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 81.85  E-value: 5.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 233 DEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLELL-VNNGADVNIQSKDGKSPLH 311
Cdd:PHA02878  31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIrSINKCSVFYTLVAIKDAFN 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 312 MTAVH-------GRFTRSQTLiqNGGEIDCVDKDGNTPLHVaaryghellINTLITSGADTAKCGIHSM-FPLHLAALNA 383
Cdd:PHA02878 111 NRNVEifkiiltNRYKNIQTI--DLVYIDKKSKDDIIEAEI---------TKLLLSYGADINMKDRHKGnTALHYATENK 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 384 HSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANC-HFHCIETLVTTGA 462
Cdd:PHA02878 180 DQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCkDYDILKLLLEHGV 259
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 463 NVN-ETDDWGRTALHYAAASDmDRNKTILG-----NAHDNSEELERARELKEKEATLCLEFL-----LQNDANPSIRDKE 531
Cdd:PHA02878 260 DVNaKSYILGLTALHSSIKSE-RKLKLLLEygadiNSLNSYKLTPLSSAVKQYLCINIGRILisnicLLKRIKPDIKNSE 338
                        330
                 ....*....|....*....
gi 304434690 532 GYnSIHYAAAYGHRQCLEL 550
Cdd:PHA02878 339 GF-IDNMDCITSNKRLNQI 356
Ank_2 pfam12796
Ankyrin repeats (3 copies);
776-869 6.67e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.00  E-value: 6.67e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  776 LHWACYNGNENCIEVLLEQKC-FRKFIGNPFTPLHCAIINDHGNCASLLLGAIDSSIvscrDDKGRTPLHAAAFADHVEC 854
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL----KDNGRTALHYAARSGHLEI 76
                          90
                  ....*....|....*
gi 304434690  855 LQLLLRHSAPVNAVD 869
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
707-796 1.29e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 1.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  707 LHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALSEEdccfkDNQGYTPLHWACYNGNEN 786
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAARSGHLE 75
                          90
                  ....*....|
gi 304434690  787 CIEVLLEQKC 796
Cdd:pfam12796  76 IVKLLLEKGA 85
PHA02798 PHA02798
ankyrin-like protein; Provisional
78-364 1.37e-15

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 80.65  E-value: 1.37e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  78 LHRAvaSRSEEAVQVLIKHSADVNARDKNWQTPLhvaaankavkCAeviipLLSsvNVSDrggrtalhhaaLNGHVEMVN 157
Cdd:PHA02798  44 LQRD--SPSTDIVKLFINLGANVNGLDNEYSTPL----------CT-----ILS--NIKD-----------YKHMLDIVK 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 158 LLLAKGANINAFDKKDRRALHWA---AYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNG---QINVVKHLLNLGVE 231
Cdd:PHA02798  94 ILIENGADINKKNSDGETPLYCLlsnGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVD 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 232 IDEI-NVYGNTALHiaCY-----NGQDA-VVNELIDYGANVNQPNNngftplhfAAASTHGALCLELLVNNG-------- 296
Cdd:PHA02798 174 INTHnNKEKYDTLH--CYfkyniDRIDAdILKLFVDNGFIINKENK--------SHKKKFMEYLNSLLYDNKrfkknild 243
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 304434690 297 ---ADVNIQSKD--GKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGAD 364
Cdd:PHA02798 244 fifSYIDINQVDelGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
PHA02876 PHA02876
ankyrin repeat protein; Provisional
584-966 1.50e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 81.26  E-value: 1.50e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 584 EVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGA--SIFVKDNVTkrtplhasvinghtlclrlLLEIADNPE 661
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGAdvNIIALDDLS-------------------VLECAVDSK 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 662 AVDVKDA---------KGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGH-EECVQMLLEQEVSILC 731
Cdd:PHA02876 223 NIDTIKAiidnrsninKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNA 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 732 KDSRGRTPLHYAAARGHATwlSELLQMALSEEDCCFKDNQGYTPLHWA-CYNGNENCIEVLLEqkcfrkfignpftplhc 810
Cdd:PHA02876 303 KNIKGETPLYLMAKNGYDT--ENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLE----------------- 363
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 811 aiindhgncasllLGAidssIVSCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMA-AENGQAGAVD 889
Cdd:PHA02876 364 -------------LGA----NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVK 426
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 890 ILVNSAqADLTVKDKDLNTPLHLACSKgheKCAL----LILDKIQDESLINEKNnalQTPLHVAArnGLKVVVEELLAKG 965
Cdd:PHA02876 427 TLIDRG-ANVNSKNKDLSTPLHYACKK---NCKLdvieMLLDNGADVNAINIQN---QYPLLIAL--EYHGIVNILLHYG 497

                 .
gi 304434690 966 A 966
Cdd:PHA02876 498 A 498
Ank_2 pfam12796
Ankyrin repeats (3 copies);
536-630 1.60e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 1.60e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  536 IHYAAAYGHRQCLELLLERTNSGFEESDSGATksPLHLAAYNGHHQALEVLLQSlVDLDIRDEkGRTALDLAAFKGHTEC 615
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRT--ALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEI 76
                          90
                  ....*....|....*
gi 304434690  616 VEALINQGASIFVKD 630
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
515-725 1.61e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.04  E-value: 1.61e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 515 LEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLerTNSGFEESDSGATKSPLHLAAYNGHHQALEVLLQS--LVD 592
Cdd:PHA02875  18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLM--KHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLgkFAD 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 593 lDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKdNVTKRTPLHASVINGHTLCLRLLLeiaDNPEAVDVKDAKGQT 672
Cdd:PHA02875  96 -DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP-NTDKFSPLHLAVMMGDIKGIELLI---DHKACLDIEDCCGCT 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 304434690 673 PLMLAVAYGHIDAVSLLLEKEANVDTVDILGC-TALHRGIMTGHEECVQMLLEQ 725
Cdd:PHA02875 171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKR 224
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
549-731 4.13e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 80.30  E-value: 4.13e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 549 ELLLERTnsgfEESDSGATKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFV 628
Cdd:PLN03192 511 DLLGDNG----GEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI 586
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 629 KDnVTKRTPLHASVINGHTLCLRLLLEIA--DNPEAvdvkdakGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTA 706
Cdd:PLN03192 587 RD-ANGNTALWNAISAKHHKIFRILYHFAsiSDPHA-------AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
                        170       180
                 ....*....|....*....|....*
gi 304434690 707 LHRGIMTGHEECVQMLLEQEVSILC 731
Cdd:PLN03192 659 LQVAMAEDHVDMVRLLIMNGADVDK 683
PHA03095 PHA03095
ankyrin-like protein; Provisional
17-168 6.48e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.53  E-value: 6.48e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  17 FSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVaaFLG----DAEIIELLILSGARVNAKDNMWLTPLHR-AVASRSEEAV- 90
Cdd:PHA03095 128 FNINPKVIRLLLRKGADVNALDLYGMTPLAV--LLKsrnaNVELLRLLIDAGADVYAVDDRFRSLLHHhLQSFKPRARIv 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  91 QVLIKHSADVNARDKNWQTPLHVAAANKAVKcAEVIIPLL---SSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANIN 167
Cdd:PHA03095 206 RELIRAGCDPAATDMLGNTPLHSMATGSSCK-RSLVLPLLiagISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284

                 .
gi 304434690 168 A 168
Cdd:PHA03095 285 A 285
Ank_2 pfam12796
Ankyrin repeats (3 copies);
674-748 1.03e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.53  E-value: 1.03e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 304434690  674 LMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEvsILCKDSRGRTPLHYAAARGH 748
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--DVNLKDNGRTALHYAARSGH 73
PHA02874 PHA02874
ankyrin repeat protein; Provisional
290-631 1.12e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 77.70  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 290 ELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTakcg 369
Cdd:PHA02874  19 KIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDT---- 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 370 ihSMFPLHlaalNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANC 449
Cdd:PHA02874  95 --SILPIP----CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHN 168
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 450 HFHCIETLVTTGANVNETDDWGRTALHYAAAsdmdrnktilgnahdnseelerarelkekeatlclefllqndanpsird 529
Cdd:PHA02874 169 FFDIIKLLLEKGAYANVKDNNGESPLHNAAE------------------------------------------------- 199
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 530 kegynsihyaaaYGHRQCLELLLERTNSGFEESDSGATksPLHLAAYngHHQALEVLLQSLVDLDIRDEKGRTALDLA-A 608
Cdd:PHA02874 200 ------------YGDYACIKLLIDHGNHIMNKCKNGFT--PLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAiN 263
                        330       340
                 ....*....|....*....|...
gi 304434690 609 FKGHTECVEALINQGASIFVKDN 631
Cdd:PHA02874 264 PPCDIDIIDILLYHKADISIKDN 286
PHA02875 PHA02875
ankyrin repeat protein; Provisional
9-167 1.24e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 77.34  E-value: 1.24e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690   9 QPPLVQAIFSGDPEEIRMLIHKTEDVNTLDSEK-RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSE 87
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  88 EAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVN-VSDRGGRTALHHAALNGHVEMVNLLLAKGANI 166
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGADC 228

                 .
gi 304434690 167 N 167
Cdd:PHA02875 229 N 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
343-435 5.72e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.22  E-value: 5.72e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  343 LHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSgFEIDTPDKfGRTCLHAAAAGGNVECIK 422
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 304434690  423 LLQSSGADFHKKD 435
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
876-972 6.68e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.22  E-value: 6.68e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  876 LMMAAENGQAGAVDILVNSaQADLTVKDKDLNTPLHLACSKGHEKCALLILDKIQdeslINEKNNAlQTPLHVAARNGLK 955
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD----VNLKDNG-RTALHYAARSGHL 74
                          90
                  ....*....|....*..
gi 304434690  956 VVVEELLAKGACVLAVD 972
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
638-908 7.82e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 74.70  E-value: 7.82e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 638 LHASVINGHTLCLRLLLE--IADNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGH 715
Cdd:PHA03100   1 LYSYIVLTKSRIIKVKNIkyIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 716 E-----ECVQMLLEQEVSILCKDSRGRTPLHYAAAR--GHATWLSELLQMALSEEDccfKDNQGYTPLHWA--CYNGNEN 786
Cdd:PHA03100  81 NltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNI---KNSDGENLLHLYleSNKIDLK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 787 CIEVLLEqkcfrkfignpftplHCAIINDHGNCASLL-LGA-IDSsivscRDDKGRTPLHAAAFADHVECLQLLLRHSAP 864
Cdd:PHA03100 158 ILKLLID---------------KGVDINAKNRVNYLLsYGVpINI-----KDVYGFTPLHYAVYNNNPEFVKYLLDLGAN 217
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 304434690 865 VNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTV-------KDKDLNT 908
Cdd:PHA03100 218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIietllyfKDKDLNT 268
PHA02876 PHA02876
ankyrin repeat protein; Provisional
720-973 1.19e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 75.10  E-value: 1.19e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 720 QMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMAlseEDCCFKDNQGYTPLHWACYNGNENCIEVLLEQkcfRK 799
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYG---ADVNIIALDDLSVLECAVDSKNIDTIKAIIDN---RS 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 800 FIGNPFTPLHCAIINDHGNCASLLLGAIDSsiVSCRDDKGRTPLHAAAFADHVECL-QLLLRHSAPVNAVDNSGKTALMM 878
Cdd:PHA02876 236 NINKNDLSLLKAIRNEDLETSLLLYDAGFS--VNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYL 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 879 AAENGQAGAVDILVNSAQADLTVKDKDLNTPLHLACSKGHEKCALLILdkIQDESLINEKNNALQTPLHVAARNGLKVVV 958
Cdd:PHA02876 314 MAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITL--LELGANVNARDYCDKTPIHYAAVRNNVVII 391
                        250
                 ....*....|....*
gi 304434690 959 EELLAKGACVLAVDE 973
Cdd:PHA02876 392 NTLLDYGADIEALSQ 406
PHA03095 PHA03095
ankyrin-like protein; Provisional
683-974 1.20e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 74.68  E-value: 1.20e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 683 IDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEEC---VQMLLEQEVSILCKDSRGRTPLHYaaarghatwlseLLQMA 759
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHL------------YLYNA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 760 LSEE----------DCCFKDNQGYTPLHwACYNG---NENCIEVLLEQKcfrkfignpftplhcAIINDhgncaslllga 826
Cdd:PHA03095  95 TTLDvikllikagaDVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKG---------------ADVNA----------- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 827 idssivscRDDKGRTPLHA---AAFADhVECLQLLLRHSAPVNAVDNSGKTALMMAAEN--GQAGAVDILVnSAQADLTV 901
Cdd:PHA03095 148 --------LDLYGMTPLAVllkSRNAN-VELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELI-RAGCDPAA 217
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 304434690 902 KDKDLNTPLHLACSKGHEKcALLILDKIQDESLINEKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVDEN 974
Cdd:PHA03095 218 TDMLGNTPLHSMATGSSCK-RSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSD 289
PHA02798 PHA02798
ankyrin-like protein; Provisional
55-266 1.30e-13

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 74.49  E-value: 1.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  55 EIIELLILSGARVNAKDNMWLTPLHRAVASRSE-----EAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPL 129
Cdd:PHA02798  52 DIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFM 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 130 L---SSVNVSDRGGRTALHHAALNGH---VEMVNLLLAKGANINAFDKKDR-RALHwaAYMGH------LDVVALLINHG 196
Cdd:PHA02798 132 IengADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNNKEKyDTLH--CYFKYnidridADILKLFVDNG 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 197 ---------------------------------------AEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINV 237
Cdd:PHA02798 210 fiinkenkshkkkfmeylnsllydnkrfkknildfifsyIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITE 289
                        250       260
                 ....*....|....*....|....*....
gi 304434690 238 YGNTALHIACYNGQDAVVNELIDYGANVN 266
Cdd:PHA02798 290 LGNTCLFTAFENESKFIFNSILNKKPNKN 318
PHA02876 PHA02876
ankyrin repeat protein; Provisional
567-908 2.06e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 74.33  E-value: 2.06e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 567 TKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKD---------------- 630
Cdd:PHA02876 178 CITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDlsllkairnedletsl 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 631 ------------NVTKRTPLHASVingHTLCL-RLLLEIADNPEAVDVKDAKGQTPLMLAVAYGH-IDAVSLLLEKEANV 696
Cdd:PHA02876 258 llydagfsvnsiDDCKNTPLHHAS---QAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADV 334
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 697 DTVDILGCTALHRG-IMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALSEEDCCFKDNqgyTP 775
Cdd:PHA02876 335 NAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG---TA 411
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 776 LHWACYNgnencievlleqkcfrkfiGNPFTPLHCAIinDHGncaslllgaidsSIVSCRDDKGRTPLHAAAFAD-HVEC 854
Cdd:PHA02876 412 LHFALCG-------------------TNPYMSVKTLI--DRG------------ANVNSKNKDLSTPLHYACKKNcKLDV 458
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 304434690 855 LQLLLRHSAPVNAVDNSGKTALMMAAenGQAGAVDILVNSAQA--DLTVKDKDLNT 908
Cdd:PHA02876 459 IEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAElrDSRVLHKSLND 512
Ank_2 pfam12796
Ankyrin repeats (3 copies);
740-824 3.68e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.91  E-value: 3.68e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  740 LHYAAARGHATWLSELLQmalSEEDCCFKDNQGYTPLHWACYNGNENCIEVLLEQKCFRKFiGNPFTPLHCAIINDHGNC 819
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE---NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-DNGRTALHYAARSGHLEI 76

                  ....*
gi 304434690  820 ASLLL 824
Cdd:pfam12796  77 VKLLL 81
Ank_2 pfam12796
Ankyrin repeats (3 copies);
514-597 7.71e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.14  E-value: 7.71e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  514 CLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSgfEESDSGATksPLHLAAYNGHHQALEVLLQSLVDL 593
Cdd:pfam12796  12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRT--ALHYAARSGHLEIVKLLLEKGADI 87

                  ....
gi 304434690  594 DIRD 597
Cdd:pfam12796  88 NVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
48-201 9.55e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 72.59  E-value: 9.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  48 AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 127
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 304434690 128 PLLSSVNVSDRGgrTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTC 201
Cdd:PLN03192 612 HFASISDPHAAG--DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
PHA02878 PHA02878
ankyrin repeat protein; Provisional
309-610 1.78e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 70.68  E-value: 1.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 309 PLHMtAVHGR-FTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSgadTAKCGI-HSMFPLHLAALNAHSD 386
Cdd:PHA02878  40 PLHQ-AVEARnLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS---INKCSVfYTLVAIKDAFNNRNVE 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 387 CCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDK-CGRTPLHYAAANCHFHCIETLVTTGANVN 465
Cdd:PHA02878 116 IFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVN 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 466 ETDDWGRTALHYAAASdmdRNKTIlgnahdnseelerarelkekeatlcLEFLLQNDANPSIRDKEGYNSIHYAAAY-GH 544
Cdd:PHA02878 196 IPDKTNNSPLHHAVKH---YNKPI-------------------------VHILLENGASTDARDKCGNTPLHISVGYcKD 247
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 304434690 545 RQCLELLLERTNSGFEESdSGATKSPLHLAAYNghHQALEVLLQSLVDLDIRDEKGRTALDLAAFK 610
Cdd:PHA02878 248 YDILKLLLEHGVDVNAKS-YILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA02878 PHA02878
ankyrin repeat protein; Provisional
166-445 3.34e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.91  E-value: 3.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 166 INAFDKKDRRA----------LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEI 235
Cdd:PHA02878  20 IEYIDHTENYStsaslipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVF 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 236 NVYgnTALHIACYNGQDAVVNELIdyganVNQPNNNGFTPLHFAAASTHG----ALCLELLVNNGADVNIQSKD-GKSPL 310
Cdd:PHA02878 100 YTL--VAIKDAFNNRNVEIFKIIL-----TNRYKNIQTIDLVYIDKKSKDdiieAEITKLLLSYGADINMKDRHkGNTAL 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 311 HMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHS-DCCR 389
Cdd:PHA02878 173 HYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILK 252
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 304434690 390 KLLSSGFEIDTPDKF-GRTCLHAAAAGGNVecIKLLQSSGADFHKKDKCGRTPLHYA 445
Cdd:PHA02878 253 LLLEHGVDVNAKSYIlGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
Ank_4 pfam13637
Ankyrin repeats (many copies);
140-193 4.74e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.52  E-value: 4.74e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 304434690  140 GRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLI 193
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
391-743 4.89e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.09  E-value: 4.89e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 391 LLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNetddw 470
Cdd:PHA02876 164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN----- 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 471 grtalhyaaasdmdRNKTILGNAHDNsEELERArelkekeatlclefLLQNDANPSIRDKEGYNSihyaaayghrqclel 550
Cdd:PHA02876 239 --------------KNDLSLLKAIRN-EDLETS--------------LLLYDAGFSVNSIDDCKN--------------- 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 551 llertnsgfeesdsgatkSPLHLAAYNGHHQAL-EVLLQSLVDLDIRDEKGRTALDLAAFKGH-TECVEALINQGASIFV 628
Cdd:PHA02876 275 ------------------TPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNA 336
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 629 KDNVTKrTPLH-ASVINGHTLCLRLLLEIADNpeaVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTAL 707
Cdd:PHA02876 337 ADRLYI-TPLHqASTLDRNKDIVITLLELGAN---VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTAL 412
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 304434690 708 HRGIM-TGHEECVQMLLEQEVSILCKDSRGRTPLHYA 743
Cdd:PHA02876 413 HFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
Ank_4 pfam13637
Ankyrin repeats (many copies);
174-226 9.48e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.75  E-value: 9.48e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 304434690  174 RRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLL 226
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
310-402 1.24e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.67  E-value: 1.24e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  310 LHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGAdtAKCGIHSMFPLHLAALNAHSDCCR 389
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 304434690  390 KLLSSGFEIDTPD 402
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
276-364 1.46e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 1.46e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  276 LHFAAASTHgALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNgGEIDCVDkDGNTPLHVAARYGHELLI 355
Cdd:pfam12796   1 LHLAAKNGN-LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                  ....*....
gi 304434690  356 NTLITSGAD 364
Cdd:pfam12796  78 KLLLEKGAD 86
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
49-280 1.51e-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: 1.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690   49 AFLGDAEIIELLILSGARVNAK-------DNMWLTPLHRAVA-SRSEEAVQVLIKHSADVNARDknwqTPLHVAAANKAV 120
Cdd:TIGR00870  20 AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAISLEYVD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  121 KCAEVIIPLLSS---------VNVSDRG----GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRA----- 176
Cdd:TIGR00870  96 AVEAILLHLLAAfrksgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDsfyhg 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  177 ---LHWAAYMGHLDVVALLINHGAEVTCKDKKGytplhaaasngqiNVVKHLLNLGVEideiNVYGNTALHIACYngqda 253
Cdd:TIGR00870 176 espLNAAACLGSPSIVALLSEDPADILTADSLG-------------NTLLHLLVMENE----FKAEYEELSCQMY----- 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 304434690  254 vvNELIDYGANVNQ-------PNNNGFTPLHFAA 280
Cdd:TIGR00870 234 --NFALSLLDKLRDskeleviLNHQGLTPLKLAA 265
Ank_4 pfam13637
Ankyrin repeats (many copies);
405-458 1.86e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 1.86e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 304434690  405 GRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLV 458
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
183-374 2.32e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.97  E-value: 2.32e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 183 MGHLDVVALLINHGAEVTckDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYG 262
Cdd:PLN03192 504 LHDLNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 263 ANVNQPNNNGFTPLHFAAASTHGALcLELLVNNGADVNIQSkdGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTP 342
Cdd:PLN03192 582 CNVHIRDANGNTALWNAISAKHHKI-FRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
                        170       180       190
                 ....*....|....*....|....*....|..
gi 304434690 343 LHVAARYGHELLINTLITSGADTAKCGIHSMF 374
Cdd:PLN03192 659 LQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
PHA02859 PHA02859
ankyrin repeat protein; Provisional
150-275 5.17e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 63.30  E-value: 5.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 150 NGHVEMVNLLLAKGANINAFDKKDRRAL--HWAAYMGHL--DVVALLINHGAEVTCKDKKGYTPLHAAASNG--QINVVK 223
Cdd:PHA02859  63 KVNVEILKFLIENGADVNFKTRDNNLSAlhHYLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHMYMCNFnvRINVIK 142
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 304434690 224 HLLNLGVEIDEINVYGNTALH-IACYNGQDAVVNELIDYGANVNQPNNNGFTP 275
Cdd:PHA02859 143 LLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
PHA02878 PHA02878
ankyrin repeat protein; Provisional
441-678 5.24e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.06  E-value: 5.24e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 441 PLHYAAANCHFHCIETLVTTGANVNETDDWGRTALH--------------------------YAAASDMDRN------KT 488
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHiickepnklgmkemirsinkcsvfytLVAIKDAFNNrnveifKI 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 489 ILGNAHDNSEELErARELKEKEATLCLE-----FLLQNDANPSIRDKEGYNS-IHYAAAYGHRQCLELLLERtnsGFE-E 561
Cdd:PHA02878 120 ILTNRYKNIQTID-LVYIDKKSKDDIIEaeitkLLLSYGADINMKDRHKGNTaLHYATENKDQRLTELLLSY---GANvN 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 562 SDSGATKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLA-AFKGHTECVEALINQGASIFVKDNVTKRTPLHA 640
Cdd:PHA02878 196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILGLTALHS 275
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 304434690 641 SVINGHTlcLRLLLEIADNPEAVdvkDAKGQTPLMLAV 678
Cdd:PHA02878 276 SIKSERK--LKLLLEYGADINSL---NSYKLTPLSSAV 308
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
107-359 6.59e-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: 6.59e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 107 WQTPLHVAAANKAVKCaevIIPLL--SSVNVSDRG--GRTALHHAALNGHVEMVNLLLakganinafdkkdrralhwaay 182
Cdd:cd22192   17 SESPLLLAAKENDVQA---IKKLLkcPSCDLFQRGalGETALHVAALYDNLEAAVVLM---------------------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 183 mghlDVVALLINHgaEVTCkdkkgytplhaaasngqinvvkhllnlgveideiNVY-GNTALHIACYNGQDAVVNELIDY 261
Cdd:cd22192   72 ----EAAPELVNE--PMTS----------------------------------DLYqGETALHIAVVNQNLNLVRELIAR 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 262 GANVNQPNNNG--FT------------PLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI- 326
Cdd:cd22192  112 GADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEI-VRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYd 190
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 304434690 327 --------QNGGEIDCV-DKDGNTPLHVAARYGHELLINTLI 359
Cdd:cd22192  191 lilsydkeDDLQPLDLVpNNQGLTPFKLAAKEGNIVMFQHLV 232
PHA03100 PHA03100
ankyrin repeat protein; Provisional
616-795 6.65e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.46  E-value: 6.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 616 VEALINQGASIFVKDNvTKRTPLHASVINGHTLclRLLLEIAD----NPEAVDVKDAKGQTPLMLAVAY--GHIDAVSLL 689
Cdd:PHA03100  51 VKILLDNGADINSSTK-NNSTPLHYLSNIKYNL--TDVKEIVKllleYGANVNAPDNNGITPLLYAISKksNSYSIVEYL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 690 LEKEANVDTVDILGCTALH------------------RGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATW 751
Cdd:PHA03100 128 LDNGANVNIKNSDGENLLHlylesnkidlkilkllidKGVDINAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEF 207
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 304434690 752 LSELLQMALSEEDCcfkDNQGYTPLHWACYNGNENCIEVLLEQK 795
Cdd:PHA03100 208 VKYLLDLGANPNLV---NKYGDTPLHIAILNNNKEIFKLLLNNG 248
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
147-276 1.12e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 65.66  E-value: 1.12e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 147 AALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPL---------------- 210
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrily 611
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 211 --------HA-------AASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPN-NNGFT 274
Cdd:PLN03192 612 hfasisdpHAagdllctAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDDDFS 691

                 ..
gi 304434690 275 PL 276
Cdd:PLN03192 692 PT 693
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
743-912 2.29e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.89  E-value: 2.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 743 AAARGHATWLSELLQMALSEEdccFKDNQGYTPLHWACYNGNENCIEVLLEQKC---FRKFIGNpfTPLHCAIINDHGNC 819
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPD---IGDSKGRTPLHIAASKGYEDCVLVLLKHACnvhIRDANGN--TALWNAISAKHHKI 606
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 820 ASLLLGAIDSSIVSCRDDKgrtpLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILV-NSAQAD 898
Cdd:PLN03192 607 FRILYHFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLImNGADVD 682
                        170
                 ....*....|....
gi 304434690 899 LTVKDKDLnTPLHL 912
Cdd:PLN03192 683 KANTDDDF-SPTEL 695
Ank_4 pfam13637
Ankyrin repeats (many copies);
672-723 4.17e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 4.17e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 304434690  672 TPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLL 723
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
773-974 4.87e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 62.76  E-value: 4.87e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 773 YTPLHWACYNGNENCIEVLLEQKCF-RKFIGNPFTPLH-----CAIINDHGNCASLLL--GAIDSSIvscrDDKGRTPLH 844
Cdd:PHA03100  36 VLPLYLAKEARNIDVVKILLDNGADiNSSTKNNSTPLHylsniKYNLTDVKEIVKLLLeyGANVNAP----DNNGITPLL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 845 AAAFA--DHVECLQLLLRHSAPVNAVDNSGKTALMMAAENG------------------QAGAVDILVNSAqADLTVKDK 904
Cdd:PHA03100 112 YAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNkidlkilkllidkgvdinAKNRVNYLLSYG-VPINIKDV 190
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 905 DLNTPLHLACSKGHEKCALLILDKIQDESLINEKNNalqTPLHVAARNGLKVVVEELLAKGACVLAVDEN 974
Cdd:PHA03100 191 YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD---TPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02989 PHA02989
ankyrin repeat protein; Provisional
20-317 6.78e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 62.84  E-value: 6.78e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  20 DPEEIRMLIHKTEDVN-TLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMwLTPL-----HRAVAS-RSEEAVQV 92
Cdd:PHA02989  15 DKNALEFLLRTGFDVNeEYRGNSILLLYLKRKDVKIKIVKLLIDNGADVNYKGYI-ETPLcavlrNREITSnKIKKIVKL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  93 LIKHSADVNARDKNWQTPlhvaaankavkcaevIIPLLSSVNVSDrggrtalhhaalnghVEMVNLLLAKGANINafDKK 172
Cdd:PHA02989  94 LLKFGADINLKTFNGVSP---------------IVCFIYNSNINN---------------CDMLRFLLSKGINVN--DVK 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 173 DRRA---LH--WAAYMGHLDVVALLINHGAEV-TCKDKKGYTP----LHAAASNGQINVVKHLLNLGVEIDEINVYGNTA 242
Cdd:PHA02989 142 NSRGynlLHmyLESFSVKKDVIKILLSFGVNLfEKTSLYGLTPmniyLRNDIDVISIKVIKYLIKKGVNIETNNNGSESV 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 243 L------HIACYNGQDAVVNELIDYgANVNQPNNNGFTPLhFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVH 316
Cdd:PHA02989 222 LesfldnNKILSKKEFKVLNFILKY-IKINKKDKKGFNPL-LISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKH 299

                 .
gi 304434690 317 G 317
Cdd:PHA02989 300 G 300
PHA02946 PHA02946
ankyin-like protein; Provisional
207-553 6.79e-10

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 62.38  E-value: 6.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 207 YTPLHAAASNGQINVVKHLLNlgveidEINVYGNT-ALHIAC-YNGQDA-VVNELIDYGANVNQPNNNGFTPLHFAAAST 283
Cdd:PHA02946  10 YLSLYAKYNSKNLDVFRNMLQ------AIEPSGNYhILHAYCgIKGLDErFVEELLHRGYSPNETDDDGNYPLHIASKIN 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 284 HGALcLELLVNNGADVNIQSKDGKSPLHMTAvhgrftrsqtliqnGGEIDCVDKdgntpLHVAARYGHEllintlITSGA 363
Cdd:PHA02946  84 NNRI-VAMLLTHGADPNACDKQHKTPLYYLS--------------GTDDEVIER-----INLLVQYGAK------INNSV 137
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 364 DTAKCGihsmfPLhLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGN--VECIKLLQSSGADFHKKDKCGRTP 441
Cdd:PHA02946 138 DEEGCG-----PL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHDGNTP 211
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 442 LHYAAANCHFHC-IETLVTTGANVNETDDWGRTALHYAAASdmdrnktiLGNAHDNSEELERARELKEKEATLCLeFLLQ 520
Cdd:PHA02946 212 LHIVCSKTVKNVdIINLLLPSTDVNKQNKFGDSPLTLLIKT--------LSPAHLINKLLSTSNVITDQTVNICI-FYDR 282
                        330       340       350
                 ....*....|....*....|....*....|....*.
gi 304434690 521 NDANPSIRDK-EGYNSIHY--AAAYGHRQCLELLLE 553
Cdd:PHA02946 283 DDVLEIINDKgKQYDSTDFkmAVEVGSIRCVKYLLD 318
Ank_2 pfam12796
Ankyrin repeats (3 copies);
442-554 7.90e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 7.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  442 LHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAASdmdrnktilGNAHdnseelerarelkekeatlCLEFLLQN 521
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKN---------GHLE-------------------IVKLLLEH 52
                          90       100       110
                  ....*....|....*....|....*....|...
gi 304434690  522 dANPSIRDkEGYNSIHYAAAYGHRQCLELLLER 554
Cdd:pfam12796  53 -ADVNLKD-NGRTALHYAARSGHLEIVKLLLEK 83
Ank_4 pfam13637
Ankyrin repeats (many copies);
375-424 8.86e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 8.86e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 304434690  375 PLHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLL 424
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02878 PHA02878
ankyrin repeat protein; Provisional
3-114 1.39e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.82  E-value: 1.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690   3 VLKLTDQPPLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVA-AFLGDAEIIELLILSGARVNAKDNMW-LTPLHR 80
Cdd:PHA02878 196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILgLTALHS 275
                         90       100       110
                 ....*....|....*....|....*....|....
gi 304434690  81 AVasRSEEAVQVLIKHSADVNARDKNWQTPLHVA 114
Cdd:PHA02878 276 SI--KSERKLKLLLEYGADINSLNSYKLTPLSSA 307
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
144-226 1.44e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.84  E-value: 1.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 144 LHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVK 223
Cdd:PTZ00322  86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                 ...
gi 304434690 224 HLL 226
Cdd:PTZ00322 166 LLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
569-620 1.61e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 1.61e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 304434690  569 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALI 620
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
279-430 1.91e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.81  E-value: 1.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 279 AAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTL 358
Cdd:PLN03192 531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 304434690 359 --ITSGADTAKCGIhsmfPLHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGAD 430
Cdd:PLN03192 611 yhFASISDPHAAGD----LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
PHA02875 PHA02875
ankyrin repeat protein; Provisional
635-747 2.82e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 2.82e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 635 RTPLHASVINGHTLCLRLLLEIadNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTG 714
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLDL--GKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146
                         90       100       110
                 ....*....|....*....|....*....|...
gi 304434690 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 3.89e-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: 3.89e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 567 TKSPLHLAAYNGHHQALEVLL-QSLVDLDIRDEKGRTALDLAAFKGHTECVEALInqgasifvkDNVTkrtplhasving 645
Cdd:cd22192   17 SESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLM---------EAAP------------ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 646 htlclrlllEIADNPEAVDVkdAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGcTALHRGI-------------- 711
Cdd:cd22192   76 ---------ELVNEPMTSDL--YQGETALHIAVVNQNLNLVRELIARGADVVSPRATG-TFFRPGPknliyygehplsfa 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 712 -MTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALSEE----DCCF---KDNQGYTPLHWACYNG 783
Cdd:cd22192  144 aCVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYDLILSYDkeddLQPLdlvPNNQGLTPFKLAAKEG 223

                 .
gi 304434690 784 N 784
Cdd:cd22192  224 N 224
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
108-282 4.80e-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: 4.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 108 QTPLHVAAANKAVKCAEVIIPLLSSVNVSDRG--------------GRTALHHAALNGHVEMVNLLLAKGANINA----- 168
Cdd:cd21882   27 KTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAratgr 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 169 FDKKDRR--------ALHWAAYMGHLDVVALLINHGAE---VTCKDKKGYTPLHAAasngqinvvkhllnlgVEIDEiNV 237
Cdd:cd21882  107 FFRKSPGnlfyfgelPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHAL----------------VLQAD-NT 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 304434690 238 YGNTALHIACYNGqdavvneLIDYGANVNQ-------PNNNGFTPLHFAAAS 282
Cdd:cd21882  170 PENSAFVCQMYNL-------LLSYGAHLDPtqqleeiPNHQGLTPLKLAAVE 214
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
289-475 7.13e-09

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 59.93  E-value: 7.13e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 289 LELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRS--QTLIQNGGEIDCVDKDGNTPLH---VAARYGHELLINTLITSGA 363
Cdd:PHA02716 195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASviKKIIELGGDMDMKCVNGMSPIMtyiINIDNINPEITNIYIESLD 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 364 DTAKCGIHSMFPLHLA-ALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNV--ECIKLLQSSGADFHKKDKCGRT 440
Cdd:PHA02716 275 GNKVKNIPMILHSYITlARNIDISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIGNT 354
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 304434690 441 PLH-YAAANCHFH-------------CIETLVTTGANVNETDDWGRTAL 475
Cdd:PHA02716 355 VLHtYLSMLSVVNildpetdndirldVIQCLISLGADITAVNCLGYTPL 403
PHA02946 PHA02946
ankyin-like protein; Provisional
53-312 8.94e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 58.91  E-value: 8.94e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  53 DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKavkcAEVIipllss 132
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTD----DEVI------ 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 133 vnvsdrggrtalhhaalnghvEMVNLLLAKGANINafdkkdrralhwaaymghldvvallinhgaevTCKDKKGYTPLHA 212
Cdd:PHA02946 121 ---------------------ERINLLVQYGAKIN--------------------------------NSVDEEGCGPLLA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 213 AASNGQiNVVKHLLNLGVEIDEINVYGNTAL--HIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLE 290
Cdd:PHA02946 148 CTDPSE-RVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKNVDII 226
                        250       260
                 ....*....|....*....|..
gi 304434690 291 LLVNNGADVNIQSKDGKSPLHM 312
Cdd:PHA02946 227 NLLLPSTDVNKQNKFGDSPLTL 248
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
340-476 1.32e-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: 1.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 340 NTPLHVAARYGHELLINTLITS-GADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSG----FEIDTPDKF-GRTCLHAAA 413
Cdd:cd22192   18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelvNEPMTSDLYqGETALHIAV 97
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 304434690 414 AGGNVECIKLLQSSGAD----------FHKKDKC----GRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALH 476
Cdd:cd22192   98 VNQNLNLVRELIARGADvvspratgtfFRPGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
PHA02875 PHA02875
ankyrin repeat protein; Provisional
569-739 1.46e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 1.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 569 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGAsiFVKDNVTKR--TPLHASVINGH 646
Cdd:PHA02875  37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK--FADDVFYKDgmTPLHLATILKK 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 647 TLCLRLLLEIADNPeavDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQE 726
Cdd:PHA02875 115 LDIMKLLIARGADP---DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
                        170
                 ....*....|...
gi 304434690 727 VSIlckDSRGRTP 739
Cdd:PHA02875 192 ANI---DYFGKNG 201
PHA03095 PHA03095
ankyrin-like protein; Provisional
20-164 1.49e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.50  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  20 DPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGD--AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHS 97
Cdd:PHA03095 201 RARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 304434690  98 ADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRggrtALHHAALNGHV-------EMVNLLLAKGA 164
Cdd:PHA03095 281 ADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA----TLNTASVAGGDipsdatrLCVAKVVLRGA 350
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
411-626 1.83e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.34  E-value: 1.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 411 AAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAASDMDRNKTIL 490
Cdd:PLN03192 531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 491 gnahdnseelerarelkekeatlclefllqndanpsirdkegynsIHYAAAyghrqclelllertnsgfeeSDSGATKSP 570
Cdd:PLN03192 611 ---------------------------------------------YHFASI--------------------SDPHAAGDL 625
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 304434690 571 LHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASI 626
Cdd:PLN03192 626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PHA02874 PHA02874
ankyrin repeat protein; Provisional
11-147 1.83e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.05  E-value: 1.83e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  11 PLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVA-SRSeeA 89
Cdd:PHA02874 160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIhNRS--A 237
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 304434690  90 VQVLIkHSADVNARDKNWQTPLHVAAankAVKCAEVIIPLL----SSVNVSDRGGRTALHHA 147
Cdd:PHA02874 238 IELLI-NNASINDQDIDGSTPLHHAI---NPPCDIDIIDILlyhkADISIKDNKGENPIDTA 295
PHA02874 PHA02874
ankyrin repeat protein; Provisional
774-976 1.88e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.05  E-value: 1.88e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 774 TPLHWACYNGNENCIEVLLEQKCFRKFIG-NPFTPLHCAI-INDHGNCASLLLGAIDSSI-------------------- 831
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINtKIPHPLLTAIkIGAHDIIKLLIDNGVDTSIlpipciekdmiktildcgid 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 832 VSCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLH 911
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLH 195
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 304434690 912 LACSKGHEKCALLILDkiqDESLINEKNNALQTPLHVAARNGLKVVveELLAKGACVLAVDENAS 976
Cdd:PHA02874 196 NAAEYGDYACIKLLID---HGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGS 255
Ank_4 pfam13637
Ankyrin repeats (many copies);
438-480 1.93e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 1.93e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 304434690  438 GRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAA 480
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAAS 43
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
274-443 1.97e-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: 1.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 274 TPLhFAAASTHGALCLE-LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGE-----IDCVDKDGNTPLHVAA 347
Cdd:cd22192   19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 348 RYGHELLINTLITSGADTAK---CGihSMFplhlaALNAHSDCcrkllssgfeidtpdKFGRTCLHAAAAGGNVECIKLL 424
Cdd:cd22192   98 VNQNLNLVRELIARGADVVSpraTG--TFF-----RPGPKNLI---------------YYGEHPLSFAACVGNEEIVRLL 155
                        170
                 ....*....|....*....
gi 304434690 425 QSSGADFHKKDKCGRTPLH 443
Cdd:cd22192  156 IEHGADIRAQDSLGNTVLH 174
PHA02859 PHA02859
ankyrin repeat protein; Provisional
77-250 2.26e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 55.60  E-value: 2.26e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  77 PLHRAVASRSEEAVQVLIKHSADVNardKNWQTPLHVAAANKAV--KCAEVIIPLLSSVNVSDRG-GRTALHH-AALNGH 152
Cdd:PHA02859  24 PLFYYVEKDDIEGVKKWIKFVNDCN---DLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRDnNLSALHHyLSFNKN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 153 V--EMVNLLLAKGANINAFDKKDRRALHwaAYMGH----LDVVALLINHGAEVTCKDKKGYTPLHA-AASNGQINVVKHL 225
Cdd:PHA02859 101 VepEILKILIDSGSSITEEDEDGKNLLH--MYMCNfnvrINVIKLLIDSGVSFLNKDFDNNNILYSyILFHSDKKIFDFL 178
                        170       180
                 ....*....|....*....|....*
gi 304434690 226 LNLGVEIDEINVYGNTALHIACYNG 250
Cdd:PHA02859 179 TSLGIDINETNKSGYNCYDLIKFRN 203
Ank_4 pfam13637
Ankyrin repeats (many copies);
206-259 2.35e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 2.35e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 304434690  206 GYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELI 259
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
538-757 2.46e-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: 2.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 538 YAAAYGHRQCLELLL--ERTNSgFEESDSGATKspLHLAAYNGHHQALEVLLQS---LVDLDIRDE--KGRTALDLAAFK 610
Cdd:cd22192   23 LAAKENDVQAIKKLLkcPSCDL-FQRGALGETA--LHVAALYDNLEAAVVLMEAapeLVNEPMTSDlyQGETALHIAVVN 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 611 GHTECVEALINQGAsifvkDNVTKRTPLHASVINGHTLCLRllleiadnpeavdvkdakGQTPLMLAVAYGHIDAVSLLL 690
Cdd:cd22192  100 QNLNLVRELIARGA-----DVVSPRATGTFFRPGPKNLIYY------------------GEHPLSFAACVGNEEIVRLLI 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 304434690 691 EKEANVDTVDILGCTALHRGIMTGHEECV-QM---LLEQEVSI------LCKDSRGRTPLHYAAARGHATWLSELLQ 757
Cdd:cd22192  157 EHGADIRAQDSLGNTVLHILVLQPNKTFAcQMydlILSYDKEDdlqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
45-326 3.02e-08

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 57.61  E-value: 3.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  45 LHvaAFLG----DAEIIELLILSGARVNAKDNMWLTPLHRAV--ASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANK 118
Cdd:PHA02716 181 LH--AYLGnmyvDIDILEWLCNNGVNVNLQNNHLITPLHTYLitGNVCASVIKKIIELGGDMDMKCVNGMSPIMTYIINI 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 119 AVKCAEVI----------------------IPLLSSVNVS---------------DRGGRTALHHAAL--NGHVEMVNLL 159
Cdd:PHA02716 259 DNINPEITniyiesldgnkvknipmilhsyITLARNIDISvvysflqpgvklhykDSAGRTCLHQYILrhNISTDIIKLL 338
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 160 LAKGANINAFDKKDRRALHwaAYMG----------------HLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQ----- 218
Cdd:PHA02716 339 HEYGNDLNEPDNIGNTVLH--TYLSmlsvvnildpetdndiRLDVIQCLISLGADITAVNCLGYTPLTSYICTAQnymyy 416
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 219 -----------INVVKH--LLNLGVEIDE--------INVYG-NTALHIACYNGQDAVVNELIDYGANVNQPNNN----- 271
Cdd:PHA02716 417 diidclisdkvLNMVKHriLQDLLIRVDDtpciihhiIAKYNiPTDLYTDEYEPYDSTKIHDVYHCAIIERYNNAvcets 496
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 304434690 272 GFTPLHFAAASTHGAL----CLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI 326
Cdd:PHA02716 497 GMTPLHVSIISHTNANivmdSFVYLLSIQYNINIPTKNGVTPLMLTMRNNRLSGHQWYI 555
Ank_4 pfam13637
Ankyrin repeats (many copies);
109-160 3.38e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 3.38e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 304434690  109 TPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLL 160
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
569-813 3.67e-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: 3.67e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  569 SPLHLAAYNGHHQALEVLLQSLvdlDIRDEKGRTALdLAAFKGHTECVEALIN--------QGASIFVKDNVTKR----- 635
Cdd:TIGR00870  54 SALFVAAIENENLELTELLLNL---SCRGAVGDTLL-HAISLEYVDAVEAILLhllaafrkSGPLELANDQYTSEftpgi 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  636 TPLHASVINGHTLCLRLLLEIADNPEA----VDVKDAKGQT-------PLMLAVAYGHIDAVSLLLEKEANVDTVDILGC 704
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPAracgDFFVKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  705 TALHRGIMtgheECVQMLLEQEVSILCKDSrgrtplhyaaarghATWLSELLQMALSEEDCCfkDNQGYTPLHWACYNGN 784
Cdd:TIGR00870 210 TLLHLLVM----ENEFKAEYEELSCQMYNF--------------ALSLLDKLRDSKELEVIL--NHQGLTPLKLAAKEGR 269
                         250       260       270
                  ....*....|....*....|....*....|
gi 304434690  785 ENCIEVLLEQKCF-RKFIGNPFTPLHCAII 813
Cdd:TIGR00870 270 IVLFRLKLAIKYKqKKFVAWPNGQQLLSLY 299
Ank_4 pfam13637
Ankyrin repeats (many copies);
839-892 3.99e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 3.99e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 304434690  839 GRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILV 892
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
208-419 4.05e-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: 4.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 208 TPLHAAASNGQINVVKHLL-NLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGAN-VNQPNNN----GFTPLHFAAA 281
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSdlyqGETALHIAVV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 282 STHGALcLELLVNNGADVN---------IQSKD-----GKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVaa 347
Cdd:cd22192   99 NQNLNL-VRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI-- 175
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 304434690 348 ryghellintLITSGADTAKCgihSMFPLHLaALNAHSDccrkllssGFEIDT-PDKFGRTCLHAAAAGGNVE 419
Cdd:cd22192  176 ----------LVLQPNKTFAC---QMYDLIL-SYDKEDD--------LQPLDLvPNNQGLTPFKLAAKEGNIV 226
Ank_4 pfam13637
Ankyrin repeats (many copies);
74-127 4.11e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 4.11e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 304434690   74 WLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 127
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02859 PHA02859
ankyrin repeat protein; Provisional
209-368 4.40e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 54.44  E-value: 4.40e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 209 PLHAAASNGQINVVKHLLNLgveIDEINVYGNTALHiACYNGQDAVVNE---LIDYGANVN-QPNNNGFTPLHFAAASTH 284
Cdd:PHA02859  24 PLFYYVEKDDIEGVKKWIKF---VNDCNDLYETPIF-SCLEKDKVNVEIlkfLIENGADVNfKTRDNNLSALHHYLSFNK 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 285 GAL--CLELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLI-NTLI 359
Cdd:PHA02859 100 NVEpeILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKKIfDFLT 179

                 ....*....
gi 304434690 360 TSGADTAKC 368
Cdd:PHA02859 180 SLGIDINET 188
PHA02875 PHA02875
ankyrin repeat protein; Provisional
671-892 4.96e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.54  E-value: 4.96e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 671 QTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHAT 750
Cdd:PHA02875   3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 751 WLSELLQMALSEEDCCFKDnqGYTPLHWACYNGNENCIEVLLEQKCFRKFIG-NPFTPLHCAIINDHGNCASLLLGaiDS 829
Cdd:PHA02875  83 AVEELLDLGKFADDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNtDKFSPLHLAVMMGDIKGIELLID--HK 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 304434690 830 SIVSCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALM-MAAENGQAGAVDILV 892
Cdd:PHA02875 159 ACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFI 222
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
12-97 6.93e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 6.93e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  12 LVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQ 91
Cdd:PTZ00322  86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                 ....*.
gi 304434690  92 VLIKHS 97
Cdd:PTZ00322 166 LLSRHS 171
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
880-975 8.15e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 8.15e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 880 AENGQAGAVDILVNSAqADLTVKDKDLNTPLHLACSKGHEKCALLILDKIQDESLINEKNNalqTPLHVAARNGLKVVVE 959
Cdd:PTZ00322  90 AASGDAVGARILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK---TPLELAEENGFREVVQ 165
                         90
                 ....*....|....*.
gi 304434690 960 ELLAKGACVLAVDENA 975
Cdd:PTZ00322 166 LLSRHSQCHFELGANA 181
PHA02859 PHA02859
ankyrin repeat protein; Provisional
11-171 9.30e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 53.67  E-value: 9.30e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  11 PLVQAIFSGDPEEIRMLIHKTEDVNTLDsekRTPLH--VAAFLGDAEIIELLILSGARVNAK---DNmwLTPLHRAVA-- 83
Cdd:PHA02859  24 PLFYYVEKDDIEGVKKWIKFVNDCNDLY---ETPIFscLEKDKVNVEILKFLIENGADVNFKtrdNN--LSALHHYLSfn 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  84 -SRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAevIIPLLSSVNVS----DRGGRTALH-HAALNGHVEMVN 157
Cdd:PHA02859  99 kNVEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRIN--VIKLLIDSGVSflnkDFDNNNILYsYILFHSDKKIFD 176
                        170
                 ....*....|....
gi 304434690 158 LLLAKGANINAFDK 171
Cdd:PHA02859 177 FLTSLGIDINETNK 190
PHA02878 PHA02878
ankyrin repeat protein; Provisional
7-114 1.15e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.66  E-value: 1.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690   7 TDQPPLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVAS-R 85
Cdd:PHA02878 167 KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcK 246
                         90       100       110
                 ....*....|....*....|....*....|
gi 304434690  86 SEEAVQVLIKHSADVNARDKNWQ-TPLHVA 114
Cdd:PHA02878 247 DYDILKLLLEHGVDVNAKSYILGlTALHSS 276
PHA02878 PHA02878
ankyrin repeat protein; Provisional
692-972 1.53e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.27  E-value: 1.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 692 KEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALseedccfKDNQ 771
Cdd:PHA02878  26 TENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSIN-------KCSV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 772 GYT--PLHWACYNGNENCIEVLLeqkcFRKFIGNPFTPLH--CAIINDHGNCASL--LLGAIDSSIVSCRDDKGRTPLHA 845
Cdd:PHA02878  99 FYTlvAIKDAFNNRNVEIFKIIL----TNRYKNIQTIDLVyiDKKSKDDIIEAEItkLLLSYGADINMKDRHKGNTALHY 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 846 AAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLACSKGHEKCALLI 925
Cdd:PHA02878 175 ATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHISVGYCKDYDILKL 253
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 304434690 926 LdkIQDESLINEKNNALQ-TPLHVAARNGLKVVVeeLLAKGACVLAVD 972
Cdd:PHA02878 254 L--LEHGVDVNAKSYILGlTALHSSIKSERKLKL--LLEYGADINSLN 297
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
281-350 1.69e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 1.69e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 281 ASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYG 350
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
Ank_4 pfam13637
Ankyrin repeats (many copies);
239-293 1.82e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.82e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 304434690  239 GNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGAlCLELLV 293
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
705-748 1.82e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.82e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 304434690  705 TALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGH 748
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
Ank_5 pfam13857
Ankyrin repeats (many copies);
192-246 1.86e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 1.86e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 304434690  192 LINHG-AEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIA 246
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
69-198 3.37e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 3.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  69 AKDNMWLTPLHRAVasrSEEAVQVLIKHSADVNArdknwqtpLHVAAANKAVKcAEVIIPLLSSVNVSDRGGRTALHHAA 148
Cdd:PTZ00322  56 ATENKDATPDHNLT---TEEVIDPVVAHMLTVEL--------CQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIAC 123
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 304434690 149 LNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAE 198
Cdd:PTZ00322 124 ANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173
Ank_4 pfam13637
Ankyrin repeats (many copies);
42-94 3.52e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 3.52e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 304434690   42 RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLI 94
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
822-898 4.66e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 4.66e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 304434690 822 LLLGAIDSSivsCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILVNSAQAD 898
Cdd:PTZ00322 101 LLTGGADPN---CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCH 174
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
817-972 1.18e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 1.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 817 GNCA---SLLLGAIDSSIvscRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILVN 893
Cdd:PLN03192 536 GNAAlleELLKAKLDPDI---GDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYH 612
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 894 SAQADLTVKDKDLntpLHLACSKGHekcaLLILDKIQDESL-INEKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVD 972
Cdd:PLN03192 613 FASISDPHAAGDL---LCTAAKRND----LTAMKELLKQGLnVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
377-482 1.28e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 1.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 377 HLAALNAHSDccrKLLSSGFEIDTPDKFGRTCLHAA-------AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANC 449
Cdd:PTZ00322  50 HLEALEATEN---KDATPDHNLTTEEVIDPVVAHMLtvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANG 126
                         90       100       110
                 ....*....|....*....|....*....|...
gi 304434690 450 HFHCIETLVTTGANVNETDDWGRTALHYAAASD 482
Cdd:PTZ00322 127 HVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
189-261 1.44e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 1.44e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 304434690 189 VALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDY 261
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02878 PHA02878
ankyrin repeat protein; Provisional
569-795 1.93e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.42  E-value: 1.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 569 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKgrTALDLAAFKGHTECVEA-LINQGASIFVKDNVTKRTPLHASVINghT 647
Cdd:PHA02878  72 TPLHIICKEPNKLGMKEMIRSINKCSVFYTL--VAIKDAFNNRNVEIFKIiLTNRYKNIQTIDLVYIDKKSKDDIIE--A 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 648 LCLRLLLEIADNPEAVDvkDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEV 727
Cdd:PHA02878 148 EITKLLLSYGADINMKD--RHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 728 SILCKDSRGRTPLHYAAARGHATwlsELLQMALSEEDCCFKDN--QGYTPLHWACYngNENCIEVLLEQK 795
Cdd:PHA02878 226 STDARDKCGNTPLHISVGYCKDY---DILKLLLEHGVDVNAKSyiLGLTALHSSIK--SERKLKLLLEYG 290
PHA02874 PHA02874
ankyrin repeat protein; Provisional
672-949 2.61e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.12  E-value: 2.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 672 TPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEV--SILckdsrgrtPLHYAAARGHA 749
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVdtSIL--------PIPCIEKDMIK 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 750 TWLSellqmalSEEDCCFKDNQGYTPLHWACYNGNENCIEVLLEQKcfrkfignpftplhcaiindhgncaslllgaids 829
Cdd:PHA02874 109 TILD-------CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYG---------------------------------- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 830 SIVSCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTP 909
Cdd:PHA02874 148 ADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG-NHIMNKCKNGFTP 226
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 304434690 910 LHLACSKGHEKCALLIldkiqDESLINEKNNALQTPLHVA 949
Cdd:PHA02874 227 LHNAIIHNRSAIELLI-----NNASINDQDIDGSTPLHHA 261
Ank_4 pfam13637
Ankyrin repeats (many copies);
736-792 3.49e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 3.49e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 304434690  736 GRTPLHYAAARGHatwlSELLQMAL-SEEDCCFKDNQGYTPLHWACYNGNENCIEVLL 792
Cdd:pfam13637   1 ELTALHAAAASGH----LELLRLLLeKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
20-210 3.61e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 50.44  E-value: 3.61e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  20 DPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSE--EAVQVLIKHS 97
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEviERINLLVQYG 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  98 ADV-NARDKNWQTPLhVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAAL--NGHVEMVNLLLAKGANINAFDKKDR 174
Cdd:PHA02946 131 AKInNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMsdNPKASTISWMMKLGISPSKPDHDGN 209
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 304434690 175 RALH--WAAYMGHLDVVALLINhGAEVTCKDKKGYTPL 210
Cdd:PHA02946 210 TPLHivCSKTVKNVDIINLLLP-STDVNKQNKFGDSPL 246
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
140-168 3.93e-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: 3.93e-06
                           10        20
                   ....*....|....*....|....*....
gi 304434690   140 GRTALHHAALNGHVEMVNLLLAKGANINA 168
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
308-359 4.01e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 4.01e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 304434690  308 SPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLI 359
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 4.29e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 4.29e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 304434690   10 PPLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLI 61
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
687-879 4.54e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.26  E-value: 4.54e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 687 SLLLEKEANVDTVDILG-CTALHRGIMtgHEECVQMLLEQEVSILCKD-SRGRTPLHYAAARGHaTWLSELLQMALSEED 764
Cdd:PHA02878 119 IILTNRYKNIQTIDLVYiDKKSKDDII--EAEITKLLLSYGADINMKDrHKGNTALHYATENKD-QRLTELLLSYGANVN 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 765 CCFKDNQgyTPLHWACYNGNENCIEVLLEQKCF---RKFIGNpfTPLHCA-----------IINDHGNCASlllgaIDSS 830
Cdd:PHA02878 196 IPDKTNN--SPLHHAVKHYNKPIVHILLENGAStdaRDKCGN--TPLHISvgyckdydilkLLLEHGVDVN-----AKSY 266
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 304434690 831 IvscrddKGRTPLHAAAFADHVecLQLLLRHSAPVNAVDNSGKTALMMA 879
Cdd:PHA02878 267 I------LGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
391-510 5.88e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.25  E-value: 5.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 391 LLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPL-------HYAAANCHFHC---------- 453
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHHKIFRILYHFasisdphaag 623
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 454 --------------IETLVTTGANVNETDDWGRTALHYAAASD---------MDRNKTILGNAHDNSEELERARELKEKE 510
Cdd:PLN03192 624 dllctaakrndltaMKELLKQGLNVDSEDHQGATALQVAMAEDhvdmvrlliMNGADVDKANTDDDFSPTELRELLQKRE 703
Ank_5 pfam13857
Ankyrin repeats (many copies);
158-213 6.06e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 6.06e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 304434690  158 LLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 213
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
720-926 6.91e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.08  E-value: 6.91e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  720 QMLLE-QEVSILCKDSRGRTPLHYAAARGHATWLSELLQmalseedccFKDNQGY---TPLHWACYNGNENCIEVLLEQK 795
Cdd:TIGR00870  35 RDLEEpKKLNINCPDRLGRSALFVAAIENENLELTELLL---------NLSCRGAvgdTLLHAISLEYVDAVEAILLHLL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  796 CFRKFIGNPF--------------TPLHCAIINDHGNCASLLL--GAIDSSIVSCRDDK----------GRTPLHAAAFA 849
Cdd:TIGR00870 106 AAFRKSGPLElandqytseftpgiTALHLAAHRQNYEIVKLLLerGASVPARACGDFFVksqgvdsfyhGESPLNAAACL 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  850 DHVECLQLLLRHSAPVNAVDNSGKTALMMA-------AENG------QAGAVDILvnsAQADLTVK-----DKDLNTPLH 911
Cdd:TIGR00870 186 GSPSIVALLSEDPADILTADSLGNTLLHLLvmenefkAEYEelscqmYNFALSLL---DKLRDSKElevilNHQGLTPLK 262
                         250
                  ....*....|....*
gi 304434690  912 LACSKGHEKCALLIL 926
Cdd:TIGR00870 263 LAAKEGRIVLFRLKL 277
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
516-693 7.27e-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: 7.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 516 EFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEE---SDSGATKSPLHLAAYNGHHQALEVLLQSLVD 592
Cdd:cd22192   35 KLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtSDLYQGETALHIAVVNQNLNLVRELIARGAD 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 593 LD--------IRDEK------GRTALDLAAFKGHTECVEALINQGASIFVKDNVTKrTPLHASVINGHTL--C----LRL 652
Cdd:cd22192  115 VVspratgtfFRPGPknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN-TVLHILVLQPNKTfaCqmydLIL 193
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 304434690 653 LLEIADNPEAVD-VKDAKGQTPLMLAVAYGHIDAVSLLLEKE 693
Cdd:cd22192  194 SYDKEDDLQPLDlVPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
Ank_4 pfam13637
Ankyrin repeats (many copies);
600-654 8.71e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 8.71e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 304434690  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 9.60e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.05  E-value: 9.60e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 304434690  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 1.14e-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: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 140 GRTALHHAALN---GHVEMVNLLL---AKGANINAF------DK--KDRRALHWAAYMGHLDVVALLINHGAEVTC---- 201
Cdd:cd22196   47 GKTCLLKAMLNlhnGQNDTISLLLdiaEKTGNLKEFvnaaytDSyyKGQTALHIAIERRNMHLVELLVQNGADVHArasg 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 202 ------KDKKGY----TPLHAAASNGQINVVKHLLN---LGVEIDEINVYGNTALH----IAcYNGQD------AVVNEL 258
Cdd:cd22196  127 effkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLHalveVA-DNTPEntkfvtKMYNEI 205
                        170       180       190
                 ....*....|....*....|....*....|.
gi 304434690 259 IDYGANVNQ-------PNNNGFTPLHFAAAS 282
Cdd:cd22196  206 LILGAKIRPllkleeiTNKKGLTPLKLAAKT 236
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
543-780 1.18e-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: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 543 GHRQCLELLLerTNSGFEESDSGatKSPLHLAAYNGHHQALE---VLLQS---------LVDLDIRDE--KGRTALDLAA 608
Cdd:cd21882    6 GLLECLRWYL--TDSAYQRGATG--KTCLHKAALNLNDGVNEaimLLLEAapdsgnpkeLVNAPCTDEfyQGQTALHIAI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 609 FKGHTECVEALINQGASIFVKDNVT--KRTPLHASVINGHTLCL----------RLLLEIADNPEAVDVKDAKGQTPLml 676
Cdd:cd21882   82 ENRNLNLVRLLVENGADVSARATGRffRKSPGNLFYFGELPLSLaactnqeeivRLLLENGAQPAALEAQDSLGNTVL-- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 677 avaygHIdavslLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEqEVSilckDSRGRTPLHYAAARGHATWLSELL 756
Cdd:cd21882  160 -----HA-----LVLQADNTPENSAFVCQMYNLLLSYGAHLDPTQQLE-EIP----NHQGLTPLKLAAVEGKIVMFQHIL 224
                        250       260
                 ....*....|....*....|....
gi 304434690 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 1.38e-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: 1.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 213 AASNGqinVVKHLLNlgVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVN--------QP--NNNGF----TPLHF 278
Cdd:cd22194  120 AEENG---ILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffNPkyKHEGFyfgeTPLAL 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 279 AAASTHGALcLELLVNNGADvNIQSKD--GKSPLHMTAVHGRFTRSQT-----------LIQNGGEIDCV-DKDGNTPLH 344
Cdd:cd22194  195 AACTNQPEI-VQLLMEKEST-DITSQDsrGNTVLHALVTVAEDSKTQNdfvkrmydmilLKSENKNLETIrNNEGLTPLQ 272

                 ....*.
gi 304434690 345 VAARYG 350
Cdd:cd22194  273 LAAKMG 278
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
211-314 1.63e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 1.63e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 211 HAAASNGQINVvKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALcLE 290
Cdd:PTZ00322  88 QLAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV-VQ 165
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 304434690 291 LLV-------NNGADVNIQSKDGK------SPLHMTA 314
Cdd:PTZ00322 166 LLSrhsqchfELGANAKPDSFTGKppsledSPISSHH 202
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
774-964 1.82e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.47  E-value: 1.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 774 TPLHWACYNGNENCIEVLLEQK----CFRKFIGNpfTPLHCAIINDHGNCASLLLGAIDSSI---VSCRDDKGRTPLHAA 846
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCPscdlFQRGALGE--TALHVAALYDNLEAAVVLMEAAPELVnepMTSDLYQGETALHIA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 847 AFADHVECLQLLLRHSAPVNA-----------VDN---SGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHL 912
Cdd:cd22192   97 VVNQNLNLVRELIARGADVVSpratgtffrpgPKNliyYGEHPLSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVLHI 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 304434690 913 ACSKGHEKCA------LLILDKIQDE-SLINEKNNALQTPLHVAARNGLKVVVEELLAK 964
Cdd:cd22192  176 LVLQPNKTFAcqmydlILSYDKEDDLqPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
532-587 1.93e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 1.93e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 304434690  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 2.19e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 42.24  E-value: 2.19e-05
                          10        20
                  ....*....|....*....|....*....
gi 304434690  140 GRTALHHAALNGHVEMVNLLLAKGANINA 168
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
93-147 2.83e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 2.83e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 304434690   93 LIKH-SADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHA 147
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
132-180 2.98e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 2.98e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 304434690  132 SVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWA 180
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
258-312 3.01e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.01e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 304434690  258 LIDYG-ANVNQPNNNGFTPLHFAAasTHGAL-CLELLVNNGADVNIQSKDGKSPLHM 312
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAA--KYGALeIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank_5 pfam13857
Ankyrin repeats (many copies);
29-81 3.03e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.03e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 304434690   29 HKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRA 81
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
635-690 3.28e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 3.28e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 304434690  635 RTPLHASVINGHTLCLRLLLEiadNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLL 690
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLE---KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
236-279 3.48e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.48e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 304434690  236 NVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFA 279
Cdd:pfam13857  13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02791 PHA02791
ankyrin-like protein; Provisional
750-945 3.74e-05

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 46.57  E-value: 3.74e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 750 TWLSELLQMALSEEDCCFKDNQGYTPLHWACYNGNENCIEVLLEQKCFRKFIGNPFtPLH-CAIINDHGNCASLLLGAID 828
Cdd:PHA02791   8 TWKSKQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF-PLHqAATLEDTKIVKILLFSGMD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 829 SSIVscrDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSG-KTALMMAAENGQAGAVDILVNSAQA--DLTVkdkd 905
Cdd:PHA02791  87 DSQF---DDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPStfDLAI---- 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 304434690 906 LNTPLHLACSKGHEKCALLILDKIQDeslINEKNNALQTP 945
Cdd:PHA02791 160 LLSCIHITIKNGHVDMMILLLDYMTS---TNTNNSLLFIP 196
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
46-117 3.83e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 3.83e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 304434690  46 HVAAFlGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAAN 117
Cdd:PTZ00322  88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
Ank_5 pfam13857
Ankyrin repeats (many copies);
857-913 3.92e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 3.92e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 304434690  857 LLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLA 913
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
238-266 4.22e-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: 41.42  E-value: 4.22e-05
                           10        20
                   ....*....|....*....|....*....
gi 304434690   238 YGNTALHIACYNGQDAVVNELIDYGANVN 266
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA03100 PHA03100
ankyrin repeat protein; Provisional
781-974 4.25e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.97  E-value: 4.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 781 YNGNENCIEVLLEQKCFRKFIGN------PFTPLHCAIindHGNCASLLLGAIDSSI-VSCRDDKGRTPLHAAAFADHV- 852
Cdd:PHA03100   6 VLTKSRIIKVKNIKYIIMEDDLNdysykkPVLPLYLAK---EARNIDVVKILLDNGAdINSSTKNNSTPLHYLSNIKYNl 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 853 ----ECLQLLLRHSAPVNAVDNSGKTALMMAAEN--GQAGAVDILVNSAqADLTVKDKDLNTPLHLACSKGHEK---CAL 923
Cdd:PHA03100  83 tdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDlkiLKL 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 304434690 924 LILDK------------IQDESLINEKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVDEN 974
Cdd:PHA03100 162 LIDKGvdinaknrvnylLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKY 224
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
838-870 4.31e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.51  E-value: 4.31e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 304434690  838 KGRTPLHAAA-FADHVECLQLLLRHSAPVNAVDN 870
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
423-478 4.96e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 4.96e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 304434690  423 LLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYA 478
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
806-859 5.69e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 5.69e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 304434690  806 TPLHCAIINDHGNCASLLLGAidSSIVSCRDDKGRTPLHAAAFADHVECLQLLL 859
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEK--GADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
772-824 5.86e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 5.86e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 304434690  772 GYTPLHWACYNGNENCIEVLLEQK-CFRKFIGNPFTPLHCAIINDHGNCASLLL 824
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGaDINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
344-438 7.57e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 7.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 344 HVAARyGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNVECIKL 423
Cdd:PTZ00322  88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
                         90
                 ....*....|....*
gi 304434690 424 LQSSGADFHKKDKCG 438
Cdd:PTZ00322 167 LSRHSQCHFELGANA 181
PHA02884 PHA02884
ankyrin repeat protein; Provisional
236-313 7.58e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 45.74  E-value: 7.58e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 236 NVYGNTALHIACYNGQDAVVNeLIDYGANVNQPNNNG-FTPLHFAAasTHGAL-CLELLVNNGADVNIQSKDGKSPLHMT 313
Cdd:PHA02884  68 NSKTNPLIYAIDCDNDDAAKL-LIRYGADVNRYAEEAkITPLYISV--LHGCLkCLEILLSYGADINIQTNDMVTPIELA 144
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
644-723 8.11e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 8.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 644 NGHTLCLRLLLEIADNPeavDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLL 723
Cdd:PTZ00322  92 SGDAVGARILLTGGADP---NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
606-690 8.39e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 8.39e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 606 LAAfKGHTECVEALINQGASIFVKDnVTKRTPLHASVINGHTLCLRLLLEIADNPEAVDvKDakGQTPLMLAVAYGHIDA 685
Cdd:PTZ00322  89 LAA-SGDAVGARILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLD-KD--GKTPLELAEENGFREV 163

                 ....*
gi 304434690 686 VSLLL 690
Cdd:PTZ00322 164 VQLLS 168
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
271-304 8.40e-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: 8.40e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 304434690  271 NGFTPLHFAAASTHGALCLELLVNNGADVNIQSK 304
Cdd:pfam00023   1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
238-270 9.36e-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: 9.36e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 304434690  238 YGNTALHIACY-NGQDAVVNELIDYGANVNQPNN 270
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
310-404 1.00e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 1.00e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 310 LHMTAVH-------GRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALN 382
Cdd:PTZ00322  79 AHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
                         90       100
                 ....*....|....*....|....*...
gi 304434690 383 AHSDCCRKLLS---SGFEIDT---PDKF 404
Cdd:PTZ00322 159 GFREVVQLLSRhsqCHFELGAnakPDSF 186
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
140-280 1.04e-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: 46.29  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 140 GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRR--------ALHWAAYMGHLDVVALLINHGAE-VTCKDK 204
Cdd:cd22194  141 GQTALNIAIERRQGDIVKLLIAKGADVNAhakgvfFNPKYKHegfyfgetPLALAACTNQPEIVQLLMEKESTdITSQDS 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 205 KGYTPLHAAA-----SNGQINVVKHLLnlgveiDEI-NVYGNTALhiacyngqdavvnELIdyganvnqPNNNGFTPLHF 278
Cdd:cd22194  221 RGNTVLHALVtvaedSKTQNDFVKRMY------DMIlLKSENKNL-------------ETI--------RNNEGLTPLQL 273

                 ..
gi 304434690 279 AA 280
Cdd:cd22194  274 AA 275
Ank_4 pfam13637
Ankyrin repeats (many copies);
514-552 1.83e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 1.83e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 304434690  514 CLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLL 552
Cdd:pfam13637  16 LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
613-882 1.85e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.21  E-value: 1.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 613 TECVEALINQGASIFVKDNvTKRTPLHA--SVINGHTLCLRLLLEIADNPEAVDVKDAKGQTPLMLAVAYGHIDA---VS 687
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDN-EYSTPLCTilSNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNleiLL 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 688 LLLEKEANVDTVDILGCTALHRGIMTGHE---ECVQMLLEQEVSIlckdsrgrtplhyaaaRGHATWlsellqmalseed 764
Cdd:PHA02798 130 FMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDI----------------NTHNNK------------- 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 765 ccfkdnQGYTPLHwaCY-NGNENCIEVLLEQ---------KCFRKFIGNPFTPLHCAIINDHGNCASLLLGAIDSSI-VS 833
Cdd:PHA02798 181 ------EKYDTLH--CYfKYNIDRIDADILKlfvdngfiiNKENKSHKKKFMEYLNSLLYDNKRFKKNILDFIFSYIdIN 252
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 304434690 834 CRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAEN 882
Cdd:PHA02798 253 QVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFEN 301
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
844-933 1.95e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 1.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 844 HAAAFADHVEcLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLACSKGHEKCAL 923
Cdd:PTZ00322  88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFREVVQ 165
                         90
                 ....*....|
gi 304434690 924 LILDKIQDES 933
Cdd:PTZ00322 166 LLSRHSQCHF 175
Ank_5 pfam13857
Ankyrin repeats (many copies);
656-708 2.06e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 2.06e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 304434690  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 2.07e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 2.07e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 304434690   205 KGYTPLHAAASNGQINVVKHLLNLGVEIDE 234
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
418-711 2.31e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.83  E-value: 2.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 418 VECIKLLQSSGADFHKKDKCGRTPL-----HYAAANCHFHCIETLVTTGANVNETDDWGRTALHyaaasdmdrnkTILGN 492
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLY-----------CLLSN 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 493 AHDNSEELerarelkekeatlcLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLlertnsgfeesdsgatksplh 572
Cdd:PHA02798 120 GYINNLEI--------------LLFMIENGADTTLLDKDGFTMLQVYLQSNHHIDIEII--------------------- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 573 laaynghhqalEVLLQSLVDLD-IRDEKGRTALDlAAFKGHTECVEA-----LINQGASIFVKDNVTKRTPLH--ASVI- 643
Cdd:PHA02798 165 -----------KLLLEKGVDINtHNNKEKYDTLH-CYFKYNIDRIDAdilklFVDNGFIINKENKSHKKKFMEylNSLLy 232
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 304434690 644 ---NGHTLCLRLLLEIADnpeaVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGI 711
Cdd:PHA02798 233 dnkRFKKNILDFIFSYID----INQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAF 299
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
385-554 2.38e-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: 45.13  E-value: 2.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 385 SDCCRKLLSSGFEidTPDKFGRTCLHAAAAGGNVECIKLLQSSGAD---------FHKKDK-----CGRTPLHYAAANCH 450
Cdd:cd22194  123 NGILDRFINAEYT--EEAYEGQTALNIAIERRQGDIVKLLIAKGADvnahakgvfFNPKYKhegfyFGETPLALAACTNQ 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 451 FHCIETLVTTGA-NVNETDDWGRTALH--YAAASDMDRNKTILGNAHDnseELERARELKEKEAtlclefllqndanpsI 527
Cdd:cd22194  201 PEIVQLLMEKEStDITSQDSRGNTVLHalVTVAEDSKTQNDFVKRMYD---MILLKSENKNLET---------------I 262
                        170       180
                 ....*....|....*....|....*..
gi 304434690 528 RDKEGYNSIHYAAAYGHRQCLELLLER 554
Cdd:cd22194  263 RNNEGLTPLQLAAKMGKAEILKYILSR 289
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
140-282 2.90e-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: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 140 GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRA--------LHWAAYMGHLDVVALLINHG---AEVTCK 202
Cdd:cd22193   76 GQTALHIAIERRQGDIVALLVENGADVHAhakgrfFQPKYQGEgfyfgelpLSLAACTNQPDIVQYLLENEhqpADIEAQ 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 203 DKKGYTPLHAAasngqinvvkhllnlgVEIDEiNVYGNTALHIACYNGqdavvneLIDYGANVNQP-------NNNGFTP 275
Cdd:cd22193  156 DSRGNTVLHAL----------------VTVAD-NTKENTKFVTRMYDM-------ILIRGAKLCPTveleeirNNDGLTP 211

                 ....*..
gi 304434690 276 LHFAAAS 282
Cdd:cd22193  212 LQLAAKM 218
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
405-558 3.87e-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: 44.46  E-value: 3.87e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 405 GRTCLHAAAAGGNVECIKLLQSSGADFH----------KKDKC---GRTPLHYAAANCHFHCIETLVTTG---ANVNETD 468
Cdd:cd22197   94 GHSALHIAIEKRSLQCVKLLVENGADVHaracgrffqkKQGTCfyfGELPLSLAACTKQWDVVNYLLENPhqpASLQAQD 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 469 DWGRTALH--YAAASDMDRNKTILGNAHDnseelerarELKEKEATLCLEFLLQndanpSIRDKEGYNSIHYAAAYGHRQ 546
Cdd:cd22197  174 SLGNTVLHalVMIADNSPENSALVIKMYD---------GLLQAGARLCPTVQLE-----EISNHEGLTPLKLAAKEGKIE 239
                        170
                 ....*....|..
gi 304434690 547 CLELLLERTNSG 558
Cdd:cd22197  240 IFRHILQREFSG 251
Ank_5 pfam13857
Ankyrin repeats (many copies);
688-743 3.91e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 3.91e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 304434690  688 LLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYA 743
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
569-607 3.91e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 3.91e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 304434690  569 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLA 607
Cdd:pfam13857  18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
838-953 4.40e-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: 4.40e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 838 KGRTPLHAAAFADHVECLQLLLRHSAPVNA---------VDNS-----GKTALMMAAENGQAGAVDILVNSAQADLTVKD 903
Cdd:cd22194  140 EGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQD 219
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 304434690 904 KDLNTPLHLAC-----SKGHEKCALLILDKI----QDESLINEKNNALQTPLHVAARNG 953
Cdd:cd22194  220 SRGNTVLHALVtvaedSKTQNDFVKRMYDMIllksENKNLETIRNNEGLTPLQLAAKMG 278
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
55-227 4.68e-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: 4.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  55 EIIELLI-----------LSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKN-WQTPLHvaaankavkc 122
Cdd:cd22194  111 EIVRILLafaeengildrFINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvFFNPKY---------- 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 123 aeviipllssvnvSDRG---GRTALHHAALNGHVEMVNLLLAKGANINAF-DKKDRRALHwAAYM------GHLDVV--- 189
Cdd:cd22194  181 -------------KHEGfyfGETPLALAACTNQPEIVQLLMEKESTDITSqDSRGNTVLH-ALVTvaedskTQNDFVkrm 246
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 304434690 190 --ALLINHGAEV--TCKDKKGYTPLHAAASNGQINVVKHLLN 227
Cdd:cd22194  247 ydMILLKSENKNleTIRNNEGLTPLQLAAKMGKAEILKYILS 288
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
201-347 4.77e-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: 4.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  201 CKDKKGYTPL-HAAASNGQINVVKHLLNLGVEIDEinvyGNTALHIACYNGQDAVvNELIDY-----GANVNQPNNN--- 271
Cdd:TIGR00870  47 CPDRLGRSALfVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLEYVDAV-EAILLHllaafRKSGPLELANdqy 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  272 ------GFTPLHFAAaSTHGALCLELLVNNGADVNIQSKDG---KSPLHMTAVHGRFTRS-----------QTLIQNGGE 331
Cdd:TIGR00870 122 tseftpGITALHLAA-HRQNYEIVKLLLERGASVPARACGDffvKSQGVDSFYHGESPLNaaaclgspsivALLSEDPAD 200
                         170
                  ....*....|....*.
gi 304434690  332 IDCVDKDGNTPLHVAA 347
Cdd:TIGR00870 201 ILTADSLGNTLLHLLV 216
Ank_4 pfam13637
Ankyrin repeats (many copies);
274-326 5.74e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 5.74e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 304434690  274 TPLHFAAASTHGAlCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI 326
Cdd:pfam13637   3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
874-968 5.89e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.85  E-value: 5.89e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 874 TALMMAAENGQAGAVDILVNSAQADLTVKDKDLNTPLHLACSKGHEKCALLILDkiQDESLINEK-NNAL---QTPLHVA 949
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPmTSDLyqgETALHIA 96
                         90
                 ....*....|....*....
gi 304434690 950 ARNGLKVVVEELLAKGACV 968
Cdd:cd22192   97 VVNQNLNLVRELIARGADV 115
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
438-469 6.00e-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: 6.00e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 304434690  438 GRTPLHYAAANC-HFHCIETLVTTGANVNETDD 469
Cdd:pfam00023   2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
238-266 6.16e-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: 6.16e-04
                          10        20
                  ....*....|....*....|....*....
gi 304434690  238 YGNTALHIACYNGQDAVVNELIDYGANVN 266
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
438-466 6.72e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 6.72e-04
                           10        20
                   ....*....|....*....|....*....
gi 304434690   438 GRTPLHYAAANCHFHCIETLVTTGANVNE 466
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
651-783 7.04e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.59  E-value: 7.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 651 RLLLEIADNPEAVDV--------KDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVD--------------ILGCTALH 708
Cdd:cd22194  114 RILLAFAEENGILDRfinaeyteEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykhegfYFGETPLA 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 709 RGIMTGHEECVQMLLEQE-VSILCKDSRGRTPLHYAA-----ARGHATWLSELLQMAL----SEEDCCFKDNQGYTPLHW 778
Cdd:cd22194  194 LAACTNQPEIVQLLMEKEsTDITSQDSRGNTVLHALVtvaedSKTQNDFVKRMYDMILlkseNKNLETIRNNEGLTPLQL 273

                 ....*
gi 304434690 779 ACYNG 783
Cdd:cd22194  274 AAKMG 278
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
332-476 7.24e-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: 7.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  332 IDCVDKDGNTPLHVAARYG-HELLINTLITSGA-----DTAkcgihsmfpLHLAALNAH---SDCCRKLLSSGFEIDTPD 402
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISLEYVdavEAILLHLLAAFRKSGPLE 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  403 ----------KFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKC--------------GRTPLHYAAANCHFHCIETLV 458
Cdd:TIGR00870 116 landqytsefTPGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLS 195
                         170
                  ....*....|....*...
gi 304434690  459 TTGANVNETDDWGRTALH 476
Cdd:TIGR00870 196 EDPADILTADSLGNTLLH 213
Ank_5 pfam13857
Ankyrin repeats (many copies);
826-879 7.27e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 7.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 304434690  826 AIDSSIVSCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMA 879
Cdd:pfam13857   3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
140-280 7.33e-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: 7.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 140 GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRALhwaaYMGHLdvvallinhgaevtckdkkgytPLHAA 213
Cdd:cd22197   94 GHSALHIAIEKRSLQCVKLLVENGADVHAracgrfFQKKQGTCF----YFGEL----------------------PLSLA 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 214 ASNGQINVVKHLLNLGVE---IDEINVYGNTALHIACYNGQDAVVN---------ELIDYGANVNQ-------PNNNGFT 274
Cdd:cd22197  148 ACTKQWDVVNYLLENPHQpasLQAQDSLGNTVLHALVMIADNSPENsalvikmydGLLQAGARLCPtvqleeiSNHEGLT 227

                 ....*.
gi 304434690 275 PLHFAA 280
Cdd:cd22197  228 PLKLAA 233
Ank_5 pfam13857
Ankyrin repeats (many copies);
397-445 7.64e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 7.64e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 304434690  397 EIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYA 445
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
189-318 7.65e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 7.65e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 189 VALLINHGAEVTCKDKKGYTPLHAAASNGQIN-VVKHLLNlgVEIDEINVYGntalhiacyngqDAV-VNELIDYGANVN 266
Cdd:PTZ00322  44 IARIDTHLEALEATENKDATPDHNLTTEEVIDpVVAHMLT--VELCQLAASG------------DAVgARILLTGGADPN 109
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 304434690 267 QPNNNGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGR 318
Cdd:PTZ00322 110 CRDYDGRTPLHIACANGHVQV-VRVLLEFGADPTLLDKDGKTPLELAEENGF 160
PHA02989 PHA02989
ankyrin repeat protein; Provisional
214-478 7.70e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 43.19  E-value: 7.70e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 214 ASNGQINVVKHLLNLGVEIDEinVY-GNTAL--HIACYNGQDAVVNELIDYGANVNQpnnNGF--TPL-----HFAAAST 283
Cdd:PHA02989  11 SDTVDKNALEFLLRTGFDVNE--EYrGNSILllYLKRKDVKIKIVKLLIDNGADVNY---KGYieTPLcavlrNREITSN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 284 HGALCLELLVNNGADVNIQSKDGKSPLhMTAVHG---------RFtrsqtLIQNGGEIDCV-DKDGNTPLHVaarYGHEL 353
Cdd:PHA02989  86 KIKKIVKLLLKFGADINLKTFNGVSPI-VCFIYNsninncdmlRF-----LLSKGINVNDVkNSRGYNLLHM---YLESF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 354 LINT-----LITSGADT-AKCGIHSMFPLHLAALNAHS----DCCRKLLSSGFEIDTPDKFGRTCLHAAAAGGNV---EC 420
Cdd:PHA02989 157 SVKKdvikiLLSFGVNLfEKTSLYGLTPMNIYLRNDIDvisiKVIKYLIKKGVNIETNNNGSESVLESFLDNNKIlskKE 236
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 421 IKLLQS--SGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYA 478
Cdd:PHA02989 237 FKVLNFilKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
40-226 8.72e-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: 8.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  40 EKRTPLHVAAFLGDAEIIELLILSGARVNAKDN-------------MWLTPLHRAVASRSEEAVQVLIKHSAD---VNAR 103
Cdd:cd21882   72 QGQTALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQ 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 104 DKNWQTPLH--VAAANKAVKCAEVIIpllssvnvsdrggrtalhhaalnghvEMVNLLLAKGANINafdkkdrralhwaa 181
Cdd:cd21882  152 DSLGNTVLHalVLQADNTPENSAFVC--------------------------QMYNLLLSYGAHLD-------------- 191
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 304434690 182 ymgHLDVVALLINHgaevtckdkKGYTPLHAAASNGQINVVKHLL 226
Cdd:cd21882  192 ---PTQQLEEIPNH---------QGLTPLKLAAVEGKIVMFQHIL 224
Ank_5 pfam13857
Ankyrin repeats (many copies);
65-114 9.49e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 9.49e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 304434690   65 ARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVA 114
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
568-619 9.96e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 9.96e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 304434690 568 KSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEAL 619
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
205-234 1.01e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.01e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 304434690  205 KGYTPLHAAASNGQINVVKHLLNLGVEIDE 234
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
907-953 1.24e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.24e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 304434690  907 NTPLHLACSKGHEKCALLILDKIQDeslINEKNNALQTPLHVAARNG 953
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNG 45
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
675-767 1.28e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 1.28e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 675 MLAVAYGHIDA------VSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLE--QEVSILCKDsrGRTPLHYAAAR 746
Cdd:PTZ00322  81 MLTVELCQLAAsgdavgARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEfgADPTLLDKD--GKTPLELAEEN 158
                         90       100
                 ....*....|....*....|.
gi 304434690 747 GhatwLSELLQMALSEEDCCF 767
Cdd:PTZ00322 159 G----FREVVQLLSRHSQCHF 175
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
376-476 1.41e-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: 1.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 376 LHLAALNAHS---DCCRKLLSSGFEIDTPDKF-----------GRTCLHAAAAGGNVECIKLLQSSGADFH--------K 433
Cdd:cd21882   30 LHKAALNLNDgvnEAIMLLLEAAPDSGNPKELvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSaratgrffR 109
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 304434690 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 1.50e-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: 1.50e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 304434690   42 RTPLHVAA-FLGDAEIIELLILSGARVNAKDN 72
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02875 PHA02875
ankyrin repeat protein; Provisional
839-968 1.50e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.29  E-value: 1.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 839 GRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKDLNTPLHLACSKGH 918
Cdd:PHA02875  35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKK 114
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 304434690 919 EKCALLILDKIQDESLINEKNNalqTPLHVAARNGLKVVVEELLAKGACV 968
Cdd:PHA02875 115 LDIMKLLIARGADPDIPNTDKF---SPLHLAVMMGDIKGIELLIDHKACL 161
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
669-700 1.51e-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: 1.51e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 304434690  669 KGQTPLMLAVA-YGHIDAVSLLLEKEANVDTVD 700
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02795 PHA02795
ankyrin-like protein; Provisional
124-201 1.59e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 42.29  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 124 EVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMG--------HLDVVALLINH 195
Cdd:PHA02795 205 KLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHLKILEILLRE 284

                 ....*.
gi 304434690 196 GAEVTC 201
Cdd:PHA02795 285 PLSIDC 290
PHA02791 PHA02791
ankyrin-like protein; Provisional
144-275 1.72e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.57  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 144 LHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGY-TPLHAAASNGQINVV 222
Cdd:PHA02791  65 LHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIV 144
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 304434690 223 KHLLNLGVEIDEINVYgNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTP 275
Cdd:PHA02791 145 SYFLSEIPSTFDLAIL-LSCIHITIKNGHVDMMILLLDYMTSTNTNNSLLFIP 196
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
771-793 1.73e-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: 1.73e-03
                           10        20
                   ....*....|....*....|...
gi 304434690   771 QGYTPLHWACYNGNENCIEVLLE 793
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLD 23
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
176-204 2.05e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 2.05e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 304434690  176 ALHWAAYM-GHLDVVALLINHGAEVTCKDK 204
Cdd:pfam00023   5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02791 PHA02791
ankyrin-like protein; Provisional
40-237 2.25e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.18  E-value: 2.25e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  40 EKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKhsadvnardKNWQTPLHvaaanka 119
Cdd:PHA02791  60 ENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVK---------KNWRLMFY------- 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 120 vkcaeviipllssvnvSDRGGRTALHHAALNGHVEMVNLLLAKGAniNAFDKKDRRA-LHWAAYMGHLDVVALLINHGAE 198
Cdd:PHA02791 124 ----------------GKTGWKTSFYHAVMLNDVSIVSYFLSEIP--STFDLAILLScIHITIKNGHVDMMILLLDYMTS 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 304434690 199 VTCKDKKGYTP-LHAAASNGQINVVKHLLNLGVEIDEINV 237
Cdd:PHA02791 186 TNTNNSLLFIPdIKLAIDNKDLEMLQALFKYDINIYSVNL 225
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
838-867 2.25e-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: 2.25e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 304434690   838 KGRTPLHAAAFADHVECLQLLLRHSAPVNA 867
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
599-631 2.33e-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: 2.33e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 304434690  599 KGRTALDLAAFK-GHTECVEALINQGASIFVKDN 631
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
338-364 2.36e-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: 2.36e-03
                           10        20
                   ....*....|....*....|....*..
gi 304434690   338 DGNTPLHVAARYGHELLINTLITSGAD 364
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
405-433 2.39e-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: 2.39e-03
                           10        20
                   ....*....|....*....|....*....
gi 304434690   405 GRTCLHAAAAGGNVECIKLLQSSGADFHK 433
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
43-121 2.42e-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: 2.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690   43 TPLHVAAFLGDAEIIELLILSGARVNAKDN--MWLT------------PLHRAVASRSEEAVQVLIKHSADVNARDKNWQ 108
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPARACgdFFVKsqgvdsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209
                          90
                  ....*....|...
gi 304434690  109 TPLHVAAANKAVK 121
Cdd:TIGR00870 210 TLLHLLVMENEFK 222
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
669-698 2.54e-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: 2.54e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 304434690  669 KGQTPLMLAVAYGHIDAVSLLLEKEANVDT 698
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
363-554 2.57e-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: 41.70  E-value: 2.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 363 ADTAK-CGIHSMFPLHlaalNAHSDCCRKLLSSGFEIDTPDKF-----------GRTCLHAAAAGGNVECIKLLQSSGAD 430
Cdd:cd22193   26 SSTGKtCLMKALLNLN----PGTNDTIRILLDIAEKTDNLKRFinaeytdeyyeGQTALHIAIERRQGDIVALLVENGAD 101
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 431 ---------FHKKDK-----CGRTPLHYAAANCHFHCIETLVT---TGANVNETDDWGRTALHYAAasdmdrnkTILGNA 493
Cdd:cd22193  102 vhahakgrfFQPKYQgegfyFGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLHALV--------TVADNT 173
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 304434690 494 HDNSEELERA-RELKEKEATLCLEFLLQndanpSIRDKEGYNSIHYAAAYGHRQCLELLLER 554
Cdd:cd22193  174 KENTKFVTRMyDMILIRGAKLCPTVELE-----EIRNNDGLTPLQLAAKMGKIEILKYILQR 230
PHA02989 PHA02989
ankyrin repeat protein; Provisional
188-356 3.40e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 41.27  E-value: 3.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 188 VVALLINHGAEVTCKDKKGYTPLHAAASNGQIN---VVKHLLNLGVEIDEI-NVYGNTALHI---ACYNGQDaVVNELID 260
Cdd:PHA02989  90 IVKLLLKFGADINLKTFNGVSPIVCFIYNSNINncdMLRFLLSKGINVNDVkNSRGYNLLHMyleSFSVKKD-VIKILLS 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 261 YGANVNQPNN-NGFTPLHFAAASTHGALCLEL---LVNNGAD-------------------------------------- 298
Cdd:PHA02989 169 FGVNLFEKTSlYGLTPMNIYLRNDIDVISIKVikyLIKKGVNietnnngsesvlesfldnnkilskkefkvlnfilkyik 248
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 304434690 299 VNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLIN 356
Cdd:PHA02989 249 INKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLN 306
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
669-697 3.90e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 3.90e-03
                           10        20
                   ....*....|....*....|....*....
gi 304434690   669 KGQTPLMLAVAYGHIDAVSLLLEKEANVD 697
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
176-201 4.06e-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: 4.06e-03
                           10        20
                   ....*....|....*....|....*.
gi 304434690   176 ALHWAAYMGHLDVVALLINHGAEVTC 201
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
629-741 4.91e-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: 4.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 629 KDNVTKRTPLHASVIN---GHTLCLRLLLEIAD---------NPEAVDVKdAKGQTPLMLAVAYGHIDAVSLLLEKEANV 696
Cdd:cd22193   24 TESSTGKTCLMKALLNlnpGTNDTIRILLDIAEktdnlkrfiNAEYTDEY-YEGQTALHIAIERRQGDIVALLVENGADV 102
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 304434690 697 D--------------TVDILGCTALHRGIMTGHEECVQMLLE---QEVSILCKDSRGRTPLH 741
Cdd:cd22193  103 HahakgrffqpkyqgEGFYFGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLH 164
Ank_5 pfam13857
Ankyrin repeats (many copies);
291-346 5.32e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 5.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 304434690  291 LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVA 346
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02743 PHA02743
Viral ankyrin protein; Provisional
153-268 5.57e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 38.64  E-value: 5.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 153 VEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVV---ALLINHGAEVTCKDKK-GYTPLHAAASNGQINVVKHLL-N 227
Cdd:PHA02743  37 MEVAPFISGDGHLLHRYDHHGRQCTHMVAWYDRANAVmkiELLVNMGADINARELGtGNTLLHIAASTKNYELAEWLCrQ 116
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 304434690 228 LGVEIDEINVYGNTALHIAcYNGQDAVVNE-LIDYGANVNQP 268
Cdd:PHA02743 117 LGVNLGAINYQHETAYHIA-YKMRDRRMMEiLRANGAVCDDP 157
PHA02884 PHA02884
ankyrin repeat protein; Provisional
55-195 5.67e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.97  E-value: 5.67e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690  55 EIIELLILSGARVNAK----DNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQ-TPLHVAAANKAVKCAEVIIPL 129
Cdd:PHA02884  47 DIIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSY 126
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 304434690 130 LSSVNVSDRGGRTALHHAALNGHVEMVNLLlaKGANINAFDKKDRRalhwaaYMGHLDVVALLINH 195
Cdd:PHA02884 127 GADINIQTNDMVTPIELALMICNNFLAFMI--CDNEISNFYKHPKK------ILINFDILKILVSH 184
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
405-436 6.82e-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: 6.82e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 304434690  405 GRTCLHAAAA-GGNVECIKLLQSSGADFHKKDK 436
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
599-628 6.97e-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: 6.97e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 304434690   599 KGRTALDLAAFKGHTECVEALINQGASIFV 628
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
76-105 7.23e-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: 7.23e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 304434690   76 TPLHRAVASR-SEEAVQVLIKHSADVNARDK 105
Cdd:pfam00023   4 TPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
437-466 7.41e-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: 7.41e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 304434690  437 CGRTPLHYAAANCHFHCIETLVTTGANVNE 466
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02791 PHA02791
ankyrin-like protein; Provisional
499-698 7.53e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 39.64  E-value: 7.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 499 ELERARELKEKEATlclEFLLQNDANPSirDKEGYNSIHYAAAYGHRQCLELLLertnsgfeesDSGATKS------PLH 572
Cdd:PHA02791   2 DLSRINTWKSKQLK---SFLSSKDAFKA--DVHGHSALYYAIADNNVRLVCTLL----------NAGALKNllenefPLH 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 573 LAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNVTKRTPL-HASVINGHTLCLR 651
Cdd:PHA02791  67 QAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWKTSFyHAVMLNDVSIVSY 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 304434690 652 LLLEIadnPEAVDVkdAKGQTPLMLAVAYGHIDAVSLLLEKEANVDT 698
Cdd:PHA02791 147 FLSEI---PSTFDL--AILLSCIHITIKNGHVDMMILLLDYMTSTNT 188
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
239-350 9.65e-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: 39.78  E-value: 9.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 304434690 239 GNTALHIACYNGQDAVVNELIDYGANVN--------QPNNN------GFTPLHFAAASTHGALCLELLVNNGADVNIQSK 304
Cdd:cd22193   76 GQTALHIAIERRQGDIVALLVENGADVHahakgrffQPKYQgegfyfGELPLSLAACTNQPDIVQYLLENEHQPADIEAQ 155
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 304434690 305 D--GKSPLHMTAVHGRFTRSQT---------LIQNGGEI-------DCVDKDGNTPLHVAARYG 350
Cdd:cd22193  156 DsrGNTVLHALVTVADNTKENTkfvtrmydmILIRGAKLcptveleEIRNNDGLTPLQLAAKMG 219
 
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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