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Conserved domains on  [gi|1958801668|ref|XP_038939221|]
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serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit B isoform X2 [Rattus norvegicus]

Protein Classification

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

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

CATH:  1.25.40.20
Gene Ontology:  GO:0005515
PubMed:  33435370|15152081|17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-343 1.81e-50

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.15  E-value: 1.81e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   54 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQSPVHVAAANKAVKCAEVIIPLLSSV 133
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  134 NVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 213
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  214 ASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLELLV 293
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958801668  294 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 343
Cdd:COG0666    240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
486-749 1.49e-36

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.09  E-value: 1.49e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  486 NKMILGNAHDNSEELERAREVKGKDAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNTGFEESDGG 565
Cdd:COG0666      8 LLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  566 AlkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVING 645
Cdd:COG0666     88 N--TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANG 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  646 HTLCLRLLLEI-ADnpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLE 724
Cdd:COG0666    165 NLEIVKLLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260
                   ....*....|....*....|....*
gi 1958801668  725 QEASILCKDSRGRTPLHYAAARGHA 749
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAA 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 1958801668  253 AVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI 332
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  333 DCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDTFGRTCLHAA 412
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  413 AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANINETDNWGRTALHYAAASDMDRNKMILGN 492
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1958801668  493 AHDNSEELERAREVKGKDAALCLEFLLQNDANPSIRDKEGYN 534
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
650-979 1.22e-31

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.84  E-value: 1.22e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  650 LRLLLEIADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLEQEASI 729
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  730 LCKDSRGRTPLHYAAARGHAtwlnELVQIALSE-EDCCLKDNQGYTPLHWACYNGNENCIEVLLEQKcfrkfignpftpl 808
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDL----EIVKLLLEAgADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG------------- 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  809 hcAIINghescaslllgaidssivsCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAV 888
Cdd:COG0666    144 --ADVN-------------------AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  889 DILVNsAQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIAARNGLKVVVEELLAKGACV 968
Cdd:COG0666    203 KLLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278

                          330
                   ....*....|.
gi 1958801668  969 LAVDENGHTPA 979
Cdd:COG0666    279 AAALLDLLTLL 289
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 2.34e-06

Ankyrin repeats (many copies);


:

Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 2.34e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958801668   10 PPLVQAIFSGDPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLI 61
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-343 1.81e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.15  E-value: 1.81e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   54 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQSPVHVAAANKAVKCAEVIIPLLSSV 133
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  134 NVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 213
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  214 ASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLELLV 293
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958801668  294 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 343
Cdd:COG0666    240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 86-359 2.27e-37

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 147.09  E-value: 2.27e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   86 SEEAVQVLIKHSADVNARDKNWQSPVHVAAANKAVKCAEVIIPLLSS---VNVSDRGGRTALHHAALNGH-MEMVNLLLA 161
Cdd:PHA03095    26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAgadVNAPERCGFTPLHLYLYNATtLDVIKLLIK 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  162 KGANINAFDKKDRRALHwaAYMG----HLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINV--VKHLLNLGVEIDEI 235
Cdd:PHA03095   106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  236 NVYGNTALHIACYNGQD--AVVNELIDYGANVNQPNNSGFTPLHFAAA-STHGALCLELLVNNGADVNIQSKDGKSPLHM 312
Cdd:PHA03095   184 DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1958801668  313 TAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLI 359
Cdd:PHA03095   264 AAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
486-749 1.49e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.09  E-value: 1.49e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  486 NKMILGNAHDNSEELERAREVKGKDAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNTGFEESDGG 565
Cdd:COG0666      8 LLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  566 AlkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVING 645
Cdd:COG0666     88 N--TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANG 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  646 HTLCLRLLLEI-ADnpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLE 724
Cdd:COG0666    165 NLEIVKLLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260
                   ....*....|....*....|....*
gi 1958801668  725 QEASILCKDSRGRTPLHYAAARGHA 749
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAA 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 1958801668  253 AVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI 332
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  333 DCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDTFGRTCLHAA 412
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  413 AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANINETDNWGRTALHYAAASDMDRNKMILGN 492
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1958801668  493 AHDNSEELERAREVKGKDAALCLEFLLQNDANPSIRDKEGYN 534
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
650-979 1.22e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.84  E-value: 1.22e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  650 LRLLLEIADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLEQEASI 729
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  730 LCKDSRGRTPLHYAAARGHAtwlnELVQIALSE-EDCCLKDNQGYTPLHWACYNGNENCIEVLLEQKcfrkfignpftpl 808
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDL----EIVKLLLEAgADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG------------- 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  809 hcAIINghescaslllgaidssivsCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAV 888
Cdd:COG0666    144 --ADVN-------------------AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  889 DILVNsAQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIAARNGLKVVVEELLAKGACV 968
Cdd:COG0666    203 KLLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278

                          330
                   ....*....|.
gi 1958801668  969 LAVDENGHTPA 979
Cdd:COG0666    279 AAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 212-475 6.87e-29

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 121.67  E-value: 6.87e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  212 AAASNGQINVVKHLLNLGVEIDEINVYGNTALH--IACYNGQDA-VVNELIDYGANVNQPNNSGFTPLHFAAASTHGALC 288
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  289 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGH---ELLiNTLITSGA 363
Cdd:PHA03095   100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGA 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  364 DTAKCGIHSMFPLHLAALNAHSD--CCRKLLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQ--SSGADFHKKDKCGR 439
Cdd:PHA03095   179 DVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPllIAGISINARNRYGQ 258

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1958801668  440 TPLHYAAA--NCHF--HCIKAlvttGANINETDNWGRTAL 475
Cdd:PHA03095   259 TPLHYAAVfnNPRAcrRLIAL----GADINAVSSDGNTPL 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
 355-664 5.02e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 100.87  E-value: 5.02e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  355 INTLITSGADTAKCGIHSMFPLHLAALNAHSDC---CRKLLSSGFEIDTPDTFGRTCLHAAAAGGNVE-CIKLLQSSGAD 430
Cdd:PHA03095    30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGAD 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  431 FHKKDKCGRTPLH-YAA-ANCHFHCIKALVTTGANINETDNWGRTALHyaaasdmdrnkmILGNAHDNSEELerarevkg 508
Cdd:PHA03095   110 VNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLA------------VLLKSRNANVEL-------- 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  509 kdaalcLEFLLQNDANPSIRDKEGYNSIHYAAAYGH--RQCLELLLERTNTGFEESDGGalKSPLHLAAYNGHHQALEV- 585
Cdd:PHA03095   170 ------LRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLG--NTPLHSMATGSSCKRSLVl 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  586 -LLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADNPEVVD 664
Cdd:PHA03095   242 pLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNTPLSLMVRNNNGRAVRAALAKNPSAETVA 320
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-269 3.39e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 3.39e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  177 LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNlGVEIDEINvYGNTALHIACYNGQDAVVN 256
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1958801668  257 ELIDYGANVNQPN 269
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
376-468 1.17e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 1.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  376 LHLAALNAHSDCCRKLLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLLqSSGADFHKKDKcGRTPLHYAAANCHFHCIK 455
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1958801668  456 ALVTTGANINETD 468
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
604-700 2.61e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 2.61e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  604 LYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADnpevVDVKDaKGQTPLMLAVAYGHI 683
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHL 74

                           90
                   ....*....|....*..
gi 1958801668  684 DAVSLLLEKEANVDAVD 700
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 651-1016 2.98e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 88.93  E-value: 2.98e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  651 RLLLEIADnpevVDVKDAKGQTPLMLAVAYGH---IDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEE-CVQMLLEQE 726
Cdd:PHA03095    32 RLLAAGAD----VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  727 ASILCKDSRGRTPLHyAAARGHATwlNELVQIALSEE--DCCLKDNQGYTPLHwaCYNGNENC-IEVLleqkcfrkfign 803
Cdd:PHA03095   108 ADVNAKDKVGRTPLH-VYLSGFNI--NPKVIRLLLRKgaDVNALDLYGMTPLA--VLLKSRNAnVELL------------ 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  804 pftplhcaiinghescaSLLLGAIdsSIVSCRDDKGRTTLH--AAAFGDHAECLQLLLRHDAQVNAVDNSGktalmmaae 881
Cdd:PHA03095   171 -----------------RLLIDAG--ADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLG--------- 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  882 ngqagavdilvnsaqadltvkdkdlNTPLHLAISKGHEKcALLILDKIQDESLINAKNSALQTPLHIAARNGLKVVVEEL 961
Cdd:PHA03095   223 -------------------------NTPLHSMATGSSCK-RSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRL 276

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801668  962 LAKGACVLAVDENGHTP-ALAcapnkdVADCLALILATMMTFSPSSTMTAVNFVYF 1016
Cdd:PHA03095   277 IALGADINAVSSDGNTPlSLM------VRNNNGRAVRAALAKNPSAETVAATLNTA 326
Ank_2 pfam12796
Ankyrin repeats (3 copies);
843-939 1.01e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 1.01e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  843 LHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKdlnTPLHLAISKGHEKCA 922
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77

                           90
                   ....*....|....*..
gi 1958801668  923 LLILDKIQDeslINAKN 939
Cdd:pfam12796   78 KLLLEKGAD---INVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 74-281 2.55e-15

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: 80.44  E-value: 2.55e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   74 WLTPLHRAVASRSEEAVQVLIK-HSADVNARDKNWQSPVHVAAANKAVKCAEVII---PLLssVNV---SD-RGGRTALH 145
Cdd:cd22192     17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaaPEL--VNEpmtSDlYQGETALH 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  146 HAALNGHMEMVNLLLAKGANIN------AFDKKDRRAL-----H---WAAYMGHLDVVALLINHGAEVTCKDKKGYTPLH 211
Cdd:cd22192     95 IAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801668  212 AAASNGQINVVKH----LLNLGVEIDEINVYgntalHIacyngqdavvnelidyganvnqPNNSGFTPLHFAAA 281
Cdd:cd22192    175 ILVLQPNKTFACQmydlILSYDKEDDLQPLD-----LV----------------------PNNQGLTPFKLAAK 221
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 538-757 3.48e-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: 67.35  E-value: 3.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  538 YAAAYGHRQCLELLLERTNTGFEESdgGAL-KSPLHLAAYNGHHQALEVLLQS---LVDLDIRDE--KGRTALYLAAFKG 611
Cdd:cd22192     23 LAAKENDVQAIKKLLKCPSCDLFQR--GALgETALHVAALYDNLEAAVVLMEAapeLVNEPMTSDlyQGETALHIAVVNQ 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  612 HTECVEALVNQGAsifvkDNVTKRTPLHASVINGHTLCLRllleiadnpevvdvkdakGQTPLMLAVAYGHIDAVSLLLE 691
Cdd:cd22192    101 NLNLVRELIARGA-----DVVSPRATGTFFRPGPKNLIYY------------------GEHPLSFAACVGNEEIVRLLIE 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801668  692 KEANVDAVDTVGCTALHRGIMTGHEECV-QM---LLEQEASI------LCKDSRGRTPLHYAAARGHATWLNELVQ 757
Cdd:cd22192    158 HGADIRAQDSLGNTVLHILVLQPNKTFAcQMydlILSYDKEDdlqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 49-280 3.52e-10

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: 64.33  E-value: 3.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   49 AFLGDAEIIELLILSGARVNAK-------DNMWLTPLHRAVA-SRSEEAVQVLIKHSADVNARDknwqSPVHVAAANKAV 120
Cdd:TIGR00870   20 AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAISLEYVD 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  121 KCAEVIIPLLSS---------VNVSDRG----GRTALHHAALNGHMEMVNLLLAKGANINA------FDKKDRRA----- 176
Cdd:TIGR00870   96 AVEAILLHLLAAfrksgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDsfyhg 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  177 ---LHWAAYMGHLDVVALLINHGAEVTCKDKKGytplhaaasngqiNVVKHLLNLGVEideiNVYGNTALHIACYngqda 253
Cdd:TIGR00870  176 espLNAAACLGSPSIVALLSEDPADILTADSLG-------------NTLLHLLVMENE----FKAEYEELSCQMY----- 233

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1958801668  254 vvNELIDYGANVNQ-------PNNSGFTPLHFAA 280
Cdd:TIGR00870  234 --NFALSLLDKLRDskeleviLNHQGLTPLKLAA 265
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 340-476 7.27e-10

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 63.11  E-value: 7.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  340 NTPLHVAARYGHELLINTLITS-GADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSG----FEIDTPDTF-GRTCLHAAA 413
Cdd:cd22192     18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelvNEPMTSDLYqGETALHIAV 97

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801668  414 AGGNVECIKLLQSSGAD----------FHKKDKC----GRTPLHYAAANCHFHCIKALVTTGANINETDNWGRTALH 476
Cdd:cd22192     98 VNQNLNLVRELIARGADvvspratgtfFRPGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 591-813 2.85e-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: 57.78  E-value: 2.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  591 VDLDIRDEKGRTALYLAAFKG-HTECVEALVNQGASIFVKDNVtkrtpLHASVINGH---TLCLRLLLEIA---DNPEVV 663
Cdd:TIGR00870   43 LNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTL-----LHAISLEYVdavEAILLHLLAAFrksGPLELA 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  664 DVKDA----KGQTPLMLAVAYGHIDAVSLLLEKEANVDAvdTVGCTALHRGIM----------------TGHEECVQMLL 723
Cdd:TIGR00870  118 NDQYTseftPGITALHLAAHRQNYEIVKLLLERGASVPA--RACGDFFVKSQGvdsfyhgesplnaaacLGSPSIVALLS 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  724 EQEASILCKDSRGRTPLHYAAARGHATWLNE-------------LVQIALSEEDCCLKDNQGYTPLHWACYNGNENCIEV 790
Cdd:TIGR00870  196 EDPADILTADSLGNTLLHLLVMENEFKAEYEelscqmynfalslLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRL 275

                          250       260
                   ....*....|....*....|....
gi 1958801668  791 LLEQKCF-RKFIGNPFTPLHCAII 813
Cdd:TIGR00870  276 KLAIKYKqKKFVAWPNGQQLLSLY 299
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 2.34e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 2.34e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958801668   10 PPLVQAIFSGDPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLI 61
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 140-168 5.03e-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: 5.03e-06
                            10        20
                    ....*....|....*....|....*....
gi 1958801668   140 GRTALHHAALNGHMEMVNLLLAKGANINA 168
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 720-964 1.65e-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: 48.86  E-value: 1.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  720 QMLLEQEasiLCKDSRGR-TPLHYAAARGHATWLNELvqiaLSEEDC--CLKDNQGYTPLHWACYNGNENCIEVLLEqkC 796
Cdd:cd22192      3 QMLDELH---LLQQKRISeSPLLLAAKENDVQAIKKL----LKCPSCdlFQRGALGETALHVAALYDNLEAAVVLME--A 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  797 FRKFIGNPFT--------PLHCAIINGHESCASLLL--GAidsSIVSCRDD-----KGRTTLhaAAFGDHAeclqlllrh 861
Cdd:cd22192     74 APELVNEPMTsdlyqgetALHIAVVNQNLNLVRELIarGA---DVVSPRATgtffrPGPKNL--IYYGEHP--------- 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  862 daqvnavdnsgktaLMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCA------LLILDKIQDE-SL 934
Cdd:cd22192    140 --------------LSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVLHILVLQPNKTFAcqmydlILSYDKEDDLqPL 204

                          250       260       270
                   ....*....|....*....|....*....|
gi 1958801668  935 INAKNSALQTPLHIAARNGLKVVVEELLAK 964
Cdd:cd22192    205 DLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 332-476 4.16e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.77  E-value: 4.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  332 IDCVDKDGNTPLHVAARYG-HELLINTLITSGA-----DTAkcgihsmfpLHLAALNAH---SDCCRKLLSSGFEIDTPD 402
Cdd:TIGR00870   45 INCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISLEYVdavEAILLHLLAAFRKSGPLE 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  403 ----------TFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKC--------------GRTPLHYAAANCHFHCIKALV 458
Cdd:TIGR00870  116 landqytsefTPGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLS 195

                          170
                   ....*....|....*...
gi 1958801668  459 TTGANINETDNWGRTALH 476
Cdd:TIGR00870  196 EDPADILTADSLGNTLLH 213
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 438-466 1.74e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 1.74e-04
                            10        20
                    ....*....|....*....|....*....
gi 1958801668   438 GRTPLHYAAANCHFHCIKALVTTGANINE 466
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 771-793 2.00e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 2.00e-03
                            10        20
                    ....*....|....*....|...
gi 1958801668   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 ...
 669-698 3.37e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 3.37e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1958801668   669 KGQTPLMLAVAYGHIDAVSLLLEKEANVDA 698
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-343 1.81e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.15  E-value: 1.81e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   54 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQSPVHVAAANKAVKCAEVIIPLLSSV 133
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  134 NVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 213
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  214 ASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLELLV 293
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958801668  294 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 343
Cdd:COG0666    240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-307 1.45e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.68  E-value: 1.45e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   22 EEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVN 101
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  102 ARDKNWQSPVHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAA 181
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  182 YMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDY 261
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1958801668  262 GANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGK 307
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
11-276 1.85e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.68  E-value: 1.85e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   11 PLVQAIFSGDPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAV 90
Cdd:COG0666     24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   91 QVLIKHSADVNARDKNWQSPVHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFD 170
Cdd:COG0666    104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  171 KKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNG 250
Cdd:COG0666    184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263

                          250       260
                   ....*....|....*....|....*.
gi 1958801668  251 QDAVVNELIDYGANVNQPNNSGFTPL 276
Cdd:COG0666    264 AALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-243 3.96e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 156.27  E-value: 3.96e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668    8 DQPPLVQAIFSGDPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSE 87
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   88 EAVQVLIKHSADVNARDKNwqspvhvaaankavkcaeviipllssvnvsdrgGRTALHHAALNGHMEMVNLLLAKGANIN 167
Cdd:COG0666    167 EIVKLLLEAGADVNARDND---------------------------------GETPLHLAAENGHLEIVKLLLEAGADVN 213

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801668  168 AFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTAL 243
Cdd:COG0666    214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
154-505 3.55e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 3.55e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  154 EMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEID 233
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  234 EINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQskdgksplhmt 313
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI-VKLLLEAGADVNAQ----------- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  314 avhgrftrsqtliqnggeidcvDKDGNTPLHVAARYGHELLINTLITSGADtakcgihsmfplhlaalnahsdccrklls 393
Cdd:COG0666    150 ----------------------DNDGNTPLHLAAANGNLEIVKLLLEAGAD----------------------------- 178

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  394 sgfeIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANINETDNWGRT 473
Cdd:COG0666    179 ----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLT 254

                          330       340       350
                   ....*....|....*....|....*....|..
gi 1958801668  474 ALHYAAASDMDRNKMILGNAHDNSEELERARE 505
Cdd:COG0666    255 ALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
PHA03095 PHA03095
ankyrin-like protein; Provisional
 86-359 2.27e-37

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 147.09  E-value: 2.27e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   86 SEEAVQVLIKHSADVNARDKNWQSPVHVAAANKAVKCAEVIIPLLSS---VNVSDRGGRTALHHAALNGH-MEMVNLLLA 161
Cdd:PHA03095    26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAgadVNAPERCGFTPLHLYLYNATtLDVIKLLIK 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  162 KGANINAFDKKDRRALHwaAYMG----HLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINV--VKHLLNLGVEIDEI 235
Cdd:PHA03095   106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  236 NVYGNTALHIACYNGQD--AVVNELIDYGANVNQPNNSGFTPLHFAAA-STHGALCLELLVNNGADVNIQSKDGKSPLHM 312
Cdd:PHA03095   184 DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1958801668  313 TAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLI 359
Cdd:PHA03095   264 AAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA03095 PHA03095
ankyrin-like protein; Provisional
 22-310 5.65e-37

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 145.94  E-value: 5.65e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   22 EEIRLLIHKTEDVNALDSEKRTPLHVaaFLG-----DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAV-QVLIK 95
Cdd:PHA03095    28 EEVRRLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDViKLLIK 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   96 HSADVNARDKNWQSPVHVAAANKAVkcaeviipllssvnvsdrggrtalhhaalngHMEMVNLLLAKGANINAFDKKDRR 175
Cdd:PHA03095   106 AGADVNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMT 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  176 ALHwaAYMGH----LDVVALLINHGAEVTCKDKKGYTPLHAAASNGQIN--VVKHLLNLGVEIDEINVYGNTALHIACYN 249
Cdd:PHA03095   155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801668  250 G--QDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLvNNGADVNIQSKDGKSPL 310
Cdd:PHA03095   233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGNTPL 294
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
486-749 1.49e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.09  E-value: 1.49e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  486 NKMILGNAHDNSEELERAREVKGKDAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNTGFEESDGG 565
Cdd:COG0666      8 LLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  566 AlkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVING 645
Cdd:COG0666     88 N--TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANG 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  646 HTLCLRLLLEI-ADnpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLE 724
Cdd:COG0666    165 NLEIVKLLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260
                   ....*....|....*....|....*
gi 1958801668  725 QEASILCKDSRGRTPLHYAAARGHA 749
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAA 265
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 55-301 1.87e-35

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 140.19  E-value: 1.87e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   55 EIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQSPVHVAAANKAV-----KCAEVIIPL 129
Cdd:PHA03100    16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEY 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  130 LSSVNVSDRGGRTALHHAALN--GHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGH--LDVVALLINHGAEVTCKDKk 205
Cdd:PHA03100    96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNR- 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  206 gytplhaaasngqinvVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHG 285
Cdd:PHA03100   175 ----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238

                          250
                   ....*....|....*.
gi 1958801668  286 ALcLELLVNNGADVNI 301
Cdd:PHA03100   239 EI-FKLLLNNGPSIKT 253
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 23-266 1.26e-33

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 134.79  E-value: 1.26e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   23 EIRLLIHKTEDVN-ALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLH-----RAVASRSEEAVQVLIKH 96
Cdd:PHA03100    16 KNIKYIIMEDDLNdYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEY 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   97 SADVNARDKNWQSPVHVAAANKavKCAEVIIPLLSS----VNVSDRGGRTALHHAALNGH--MEMVNLLLAKGANINAfd 170
Cdd:PHA03100    96 GANVNAPDNNGITPLLYAISKK--SNSYSIVEYLLDnganVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINA-- 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  171 kKDRralhwaaymghldvVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNG 250
Cdd:PHA03100   172 -KNR--------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNN 236

                          250
                   ....*....|....*.
gi 1958801668  251 QDAVVNELIDYGANVN 266
Cdd:PHA03100   237 NKEIFKLLLNNGPSIK 252
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 1958801668  253 AVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI 332
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  333 DCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDTFGRTCLHAA 412
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  413 AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANINETDNWGRTALHYAAASDMDRNKMILGN 492
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1958801668  493 AHDNSEELERAREVKGKDAALCLEFLLQNDANPSIRDKEGYN 534
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 26-364 3.60e-33

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 137.50  E-value: 3.60e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   26 LLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDK 105
Cdd:PHA02876   163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDL 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  106 NWQSpvhvAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHM-EMVNLLLAKGANINAFDKKDRRALHWAAYMG 184
Cdd:PHA02876   243 SLLK----AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNG 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  185 H-LDVVALLINHGAEVTCKDKKGYTPLHAAAS-NGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYG 262
Cdd:PHA02876   319 YdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  263 ANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHG-RFTRSQTLIQNGGEIDCVDKDGNT 341
Cdd:PHA02876   399 ADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQY 478

                          330       340
                   ....*....|....*....|...
gi 1958801668  342 PLHVAarYGHELLINTLITSGAD 364
Cdd:PHA02876   479 PLLIA--LEYHGIVNILLHYGAE 499
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 16-367 6.28e-33

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 133.17  E-value: 6.28e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   16 IFSGDPEEIRLLI-HKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLI 94
Cdd:PHA02874     9 IYSGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   95 KHSADVNArdknwqspvhvaaankavkcaeVIIPLLSSvnvsdrggrtalhhaalnghmEMVNLLLAKGANINAFDKKDR 174
Cdd:PHA02874    89 DNGVDTSI----------------------LPIPCIEK---------------------DMIKTILDCGIDVNIKDAELK 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  175 RALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAV 254
Cdd:PHA02874   126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  255 VNELIDYGANVNQPNNSGFTPLHfaAASTHGALCLELLVNNgADVNIQSKDGKSPLHMtAVHGRFTRS--QTLIQNGGEI 332
Cdd:PHA02874   206 IKLLIDHGNHIMNKCKNGFTPLH--NAIIHNRSAIELLINN-ASINDQDIDGSTPLHH-AINPPCDIDiiDILLYHKADI 281

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1958801668  333 DCVDKDGNTPLHVAARYGH------ELLINTLITSGADTAK 367
Cdd:PHA02874   282 SIKDNKGENPIDTAFKYINkdpvikDIIANAVLIKEADKLK 322
PHA03095 PHA03095
ankyrin-like protein; Provisional
 186-478 2.76e-32

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 132.07  E-value: 2.76e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  186 LDVVALLINHGAEVTCKDKKGYTPLHAAASNGQIN---VVKHLLNLGVEIDEINVYGNTALHI-ACYNGQDAVVNELIDY 261
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKA 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  262 GANVNQPNNSGFTPLH--FAAASTHgALCLELLVNNGADVNIQSKDGKSPLHMtavhgrFTRS--------QTLIQNGGE 331
Cdd:PHA03095   107 GADVNAKDKVGRTPLHvyLSGFNIN-PKVIRLLLRKGADVNALDLYGMTPLAV------LLKSrnanvellRLLIDAGAD 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  332 IDCVDKDGNTPLHVAARYGH--ELLINTLITSGADTAKCGIHSMFPLHLAAlnAHSDCCR----KLLSSGFEIDTPDTFG 405
Cdd:PHA03095   180 VYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNTPLHSMA--TGSSCKRslvlPLLIAGISINARNRYG 257

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801668  406 RTCLHAAAAGGN-VECIKLLQSsGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANINETDNwgrtALHYA 478
Cdd:PHA03095   258 QTPLHYAAVFNNpRACRRLIAL-GADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA----TLNTA 326
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
566-795 3.09e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.38  E-value: 3.09e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  566 ALKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVING 645
Cdd:COG0666     20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD-GGNTLLHAAARNG 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  646 HTLCLRLLLEIADNpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLEQ 725
Cdd:COG0666     99 DLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEA 175

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958801668  726 EASILCKDSRGRTPLHYAAARGHAtwlnELVQIALSEE-DCCLKDNQGYTPLHWACYNGNENCIEVLLEQK 795
Cdd:COG0666    176 GADVNARDNDGETPLHLAAENGHL----EIVKLLLEAGaDVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
650-979 1.22e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.84  E-value: 1.22e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  650 LRLLLEIADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLEQEASI 729
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  730 LCKDSRGRTPLHYAAARGHAtwlnELVQIALSE-EDCCLKDNQGYTPLHWACYNGNENCIEVLLEQKcfrkfignpftpl 808
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDL----EIVKLLLEAgADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG------------- 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  809 hcAIINghescaslllgaidssivsCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAV 888
Cdd:COG0666    144 --ADVN-------------------AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  889 DILVNsAQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIAARNGLKVVVEELLAKGACV 968
Cdd:COG0666    203 KLLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278

                          330
                   ....*....|.
gi 1958801668  969 LAVDENGHTPA 979
Cdd:COG0666    279 AAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
325-669 1.93e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.07  E-value: 1.93e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  325 LIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDTF 404
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  405 GRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANINETDNWGRTALHYAAASdmd 484
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN--- 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  485 rnkmilgnahdNSEELerarevkgkdaalcLEFLLQNDANPSIRDKEGYnsihyaaayghrqclelllertntgfeesdg 564
Cdd:COG0666    164 -----------GNLEI--------------VKLLLEAGADVNARDNDGE------------------------------- 187

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  565 galkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNVTKRTPLHASVIN 644
Cdd:COG0666    188 ----TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263

                          330       340
                   ....*....|....*....|....*
gi 1958801668  645 GHTLCLRLLLEIADNPEVVDVKDAK 669
Cdd:COG0666    264 AALIVKLLLLALLLLAAALLDLLTL 288
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 56-385 2.23e-31

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 131.72  E-value: 2.23e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   56 IIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQSPVHVAAANKAVKCAEVIIPLLSSVNV 135
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  136 SDrggrTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLD-VVALLINHGAEVTCKDKKGYTPLHAAA 214
Cdd:PHA02876   240 ND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMA 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  215 SNG-QINVVKHLLNLGVEIDEINVYGNTALHIACY--NGQDAVVNeLIDYGANVNQPNNSGFTPLHFAAAStHGALCLEL 291
Cdd:PHA02876   316 KNGyDTENIRTLIMLGADVNAADRLYITPLHQASTldRNKDIVIT-LLELGANVNARDYCDKTPIHYAAVR-NNVVIINT 393

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  292 LVNNGADVNIQSKDGKSPLHMtAVHGR--FTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHEL-LINTLITSGADTAKC 368
Cdd:PHA02876   394 LLDYGADIEALSQKIGTALHF-ALCGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAI 472

                          330
                   ....*....|....*..
gi 1958801668  369 GIHSMFPLhLAALNAHS 385
Cdd:PHA02876   473 NIQNQYPL-LIALEYHG 488
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
462-740 1.84e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.37  E-value: 1.84e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  462 ANINETDNWGRTALHYAAASDMDRNKMILGNAHDNSEELERAREVKGKDAALcLEFLLQNDANPSIRDKEGYNSIHYAAA 541
Cdd:COG0666     18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLV-ALLLLAAGADINAKDDGGNTLLHAAAR 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  542 YGHRQCLELLLER-TNTGFEESDGGalkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALV 620
Cdd:COG0666     97 NGDLEIVKLLLEAgADVNARDKDGE---TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  621 NQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLE-IADnpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAV 699
Cdd:COG0666    174 EAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEaGAD----VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1958801668  700 DTVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPL 740
Cdd:COG0666    249 DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 153-465 9.72e-30

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 126.72  E-value: 9.72e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  153 MEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEI 232
Cdd:PHA02876   158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  233 DE-----INVYGNTALHIACYngqdavvneLIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGK 307
Cdd:PHA02876   238 NKndlslLKAIRNEDLETSLL---------LYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGE 308

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  308 SPLHMTAVHGRFTRS-QTLIQNGGEIDCVDKDGNTPLHVAA---RYGHELLinTLITSGADTAKCGIHSMFPLHLAALNA 383
Cdd:PHA02876   309 TPLYLMAKNGYDTENiRTLIMLGADVNAADRLYITPLHQAStldRNKDIVI--TLLELGANVNARDYCDKTPIHYAAVRN 386

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  384 HSDCCRKLLSSGFEIDTPDTFGRTCLHAAAAGGN-VECIKLLQSSGADFHKKDKCGRTPLHYAAA-NCHFHCIKALVTTG 461
Cdd:PHA02876   387 NVVIINTLLDYGADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTPLHYACKkNCKLDVIEMLLDNG 466


                   ....
gi 1958801668  462 ANIN 465
Cdd:PHA02876   467 ADVN 470
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
752-997 1.08e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.06  E-value: 1.08e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  752 LNELVQIALSEEDCCLKDNQGYTPLHWACYNGNENCIEVLLEQKCFR-KFIGNPFTPLHCAIINGHESCASLLLGAIDSs 830
Cdd:COG0666     34 LLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADInAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD- 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  831 iVSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPL 910
Cdd:COG0666    113 -VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPL 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  911 HLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIAARNGLKVVVEELLAKGACVLAVDENGHTPALACAPNKDVAD 990
Cdd:COG0666    191 HLAAENGHLEIVKLLLEAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALI 267


                   ....*..
gi 1958801668  991 CLALILA 997
Cdd:COG0666    268 VKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
752-997 3.80e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.52  E-value: 3.80e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  752 LNELVQIALSEEDCCLKDNQGYTPLHWACYNGNENCIEVLLEQKCFRKFIGNPFTPLHCAIINGHESCASLLLGAIDSSI 831
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  832 VScRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLH 911
Cdd:COG0666     81 NA-KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE-AGADVNAQDNDGNTPLH 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  912 LAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIAARNGLKVVVEELLAKGACVLAVDENGHTPALACAPNKDVADC 991
Cdd:COG0666    159 LAAANGNLEIVKLLLEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235


                   ....*.
gi 1958801668  992 LALILA 997
Cdd:COG0666    236 KLLLEA 241
PHA03095 PHA03095
ankyrin-like protein; Provisional
 212-475 6.87e-29

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 121.67  E-value: 6.87e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  212 AAASNGQINVVKHLLNLGVEIDEINVYGNTALH--IACYNGQDA-VVNELIDYGANVNQPNNSGFTPLHFAAASTHGALC 288
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  289 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGH---ELLiNTLITSGA 363
Cdd:PHA03095   100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGA 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  364 DTAKCGIHSMFPLHLAALNAHSD--CCRKLLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQ--SSGADFHKKDKCGR 439
Cdd:PHA03095   179 DVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPllIAGISINARNRYGQ 258

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|
gi 1958801668  440 TPLHYAAA--NCHF--HCIKAlvttGANINETDNWGRTAL 475
Cdd:PHA03095   259 TPLHYAAVfnNPRAcrRLIAL----GADINAVSSDGNTPL 294
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 192-465 1.48e-27

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 116.69  E-value: 1.48e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  192 LINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIAC---YNGQDAV--VNELIDYGANVN 266
Cdd:PHA03100    21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikYNLTDVKeiVKLLLEYGANVN 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  267 QPNNSGFTPLHFAAASTHGALCL-ELLVNNGADVNIQSKDGKSPLHMtavhgrFTRSqtliqnggeiDCVDKDgntplhv 345
Cdd:PHA03100   101 APDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHL------YLES----------NKIDLK------- 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  346 aaryghelLINTLITSGAD-TAKCGIHSmfplhlaalnahsdccrkLLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLL 424
Cdd:PHA03100   158 --------ILKLLIDKGVDiNAKNRVNY------------------LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYL 211

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1958801668  425 QSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANIN 465
Cdd:PHA03100   212 LDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 12-265 3.64e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 118.63  E-value: 3.64e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   12 LVQAIFSGDPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGD-AEIIELLILSGARVNAKDNMWLTPLH-RAVASRSEEA 89
Cdd:PHA02876   244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYlMAKNGYDTEN 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   90 VQVLIKHSADVNARDKNWQSPVHVAAANKAVKcaEVIIPLL---SSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANI 166
Cdd:PHA02876   324 IRTLIMLGADVNAADRLYITPLHQASTLDRNK--DIVITLLelgANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  167 NAFDKKDRRALHWAAY-MGHLDVVALLINHGAEVTCKDKKGYTPLH-AAASNGQINVVKHLLNLGVEIDEINVYGNTALH 244
Cdd:PHA02876   402 EALSQKIGTALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHyACKKNCKLDVIEMLLDNGADVNAINIQNQYPLL 481

                          250       260
                   ....*....|....*....|.
gi 1958801668  245 IACynGQDAVVNELIDYGANV 265
Cdd:PHA02876   482 IAL--EYHGIVNILLHYGAEL 500
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 11-310 1.54e-25

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 113.62  E-value: 1.54e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   11 PLVQAIFSGDPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDnmwlTPLHRAVASRSEEAV 90
Cdd:PHA02876   181 PIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND----LSLLKAIRNEDLETS 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   91 QVLIKHSADVNARDKNWQSPVHVAAanKAVKCAEVIIPLL---SSVNVSDRGGRTALHHAALNGH-MEMVNLLLAKGANI 166
Cdd:PHA02876   257 LLLYDAGFSVNSIDDCKNTPLHHAS--QAPSLSRLVPKLLergADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADV 334

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  167 NAFDKKDRRALHWAAYMG-HLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHI 245
Cdd:PHA02876   335 NAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHF 414

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801668  246 ACYNGQDAV-VNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPL 310
Cdd:PHA02876   415 ALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIEMLLDNGADVNAINIQNQYPL 480
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 75-346 4.72e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 109.97  E-value: 4.72e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   75 LTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQSPVHVA--AANKavkcaEVIIPLLSSVNVSDRG-GRTALHHAALNG 151
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckEPNK-----LGMKEMIRSINKCSVFyTLVAIKDAFNNR 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  152 HMEMVNLLLakganINAFDKK---DRRALHWAAYMGHLD--VVALLINHGAEVTCKDK-KGYTPLHAAASNGQINVVKHL 225
Cdd:PHA02878   113 NVEIFKIIL-----TNRYKNIqtiDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELL 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  226 LNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSK- 304
Cdd:PHA02878   188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYi 267

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1958801668  305 DGKSPLHMTAVHGRFTRsqTLIQNGGEIDCVDKDGNTPLHVA 346
Cdd:PHA02878   268 LGLTALHSSIKSERKLK--LLLEYGADINSLNSYKLTPLSSA 307
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 290-607 5.98e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 103.12  E-value: 5.98e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  290 ELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTakcg 369
Cdd:PHA02874    19 KIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDT---- 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  370 ihSMFPLHlaalNAHSDCCRKLLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANC 449
Cdd:PHA02874    95 --SILPIP----CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHN 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  450 HFHCIKALVTTGANINETDNWGRTALHYAaasdmdrnkmilgnahdnseelerareVKGKDAAlCLEFLLQNDANPSIRD 529
Cdd:PHA02874   169 FFDIIKLLLEKGAYANVKDNNGESPLHNA---------------------------AEYGDYA-CIKLLIDHGNHIMNKC 220

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958801668  530 KEGYNSIHYAAAYgHRQCLELLLERTNTGFEESDGgalKSPLHLA-AYNGHHQALEVLLQSLVDLDIRDEKGRTALYLA 607
Cdd:PHA02874   221 KNGFTPLHNAIIH-NRSAIELLINNASINDQDIDG---STPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 22-295 1.40e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 102.65  E-value: 1.40e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   22 EEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIK------ 95
Cdd:PHA02878    18 KYIEYIDHTENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcs 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   96 ------------HSADV--------NARDKNWQSP-VHVAAANKAVKCAEVIIPLL----SSVNVSDR-GGRTALHHAAL 149
Cdd:PHA02878    98 vfytlvaikdafNNRNVeifkiiltNRYKNIQTIDlVYIDKKSKDDIIEAEITKLLlsygADINMKDRhKGNTALHYATE 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  150 NGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASN-GQINVVKHLLNL 228
Cdd:PHA02878   178 NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEH 257

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801668  229 GVEID-EINVYGNTALHIACYNGQdaVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNN 295
Cdd:PHA02878   258 GVDVNaKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISN 323
PHA03095 PHA03095
ankyrin-like protein; Provisional
 355-664 5.02e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 100.87  E-value: 5.02e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  355 INTLITSGADTAKCGIHSMFPLHLAALNAHSDC---CRKLLSSGFEIDTPDTFGRTCLHAAAAGGNVE-CIKLLQSSGAD 430
Cdd:PHA03095    30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGAD 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  431 FHKKDKCGRTPLH-YAA-ANCHFHCIKALVTTGANINETDNWGRTALHyaaasdmdrnkmILGNAHDNSEELerarevkg 508
Cdd:PHA03095   110 VNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLA------------VLLKSRNANVEL-------- 169

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  509 kdaalcLEFLLQNDANPSIRDKEGYNSIHYAAAYGH--RQCLELLLERTNTGFEESDGGalKSPLHLAAYNGHHQALEV- 585
Cdd:PHA03095   170 ------LRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLG--NTPLHSMATGSSCKRSLVl 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  586 -LLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADNPEVVD 664
Cdd:PHA03095   242 pLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNTPLSLMVRNNNGRAVRAALAKNPSAETVA 320
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-269 3.39e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 3.39e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  177 LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNlGVEIDEINvYGNTALHIACYNGQDAVVN 256
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1958801668  257 ELIDYGANVNQPN 269
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 218-495 6.32e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 98.60  E-value: 6.32e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  218 QINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAAS----THGALC----- 288
Cdd:PHA02876   157 ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSknidTIKAIIdnrsn 236

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  289 ----------------LE---LLVNNGADVNIQSKDGKSPLHMTAVHGRFTR-SQTLIQNGGEIDCVDKDGNTPLHVAAR 348
Cdd:PHA02876   237 inkndlsllkairnedLEtslLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRlVPKLLERGADVNAKNIKGETPLYLMAK 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  349 YGHELL-INTLITSGADTAKCGIHSMFPLHLAA-LNAHSDCCRKLLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQS 426
Cdd:PHA02876   317 NGYDTEnIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958801668  427 SGADFHKKDKCGRTPLHYAAANCH-FHCIKALVTTGANINETDNWGRTALHYAAASD--MDRNKMILGNAHD 495
Cdd:PHA02876   397 YGADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNckLDVIEMLLDNGAD 468
Ank_2 pfam12796
Ankyrin repeats (3 copies);
144-236 9.51e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 9.51e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  144 LHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHgAEVTCKDkKGYTPLHAAASNGQINVVK 223
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1958801668  224 HLLNLGVEIDEIN 236
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 24-235 2.58e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 95.48  E-value: 2.58e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   24 IRLLIHKTEDVNALDSEKRTPLHV--AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASR--SEEAVQVLIKHSAD 99
Cdd:PHA03095   100 IKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGAD 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  100 VNARDKNWQSPVHVAAAN--KAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNL--LLAKGANINAFDKKDRR 175
Cdd:PHA03095   180 VYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQT 259

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  176 ALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEI 235
Cdd:PHA03095   260 PLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 48-266 6.73e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 93.52  E-value: 6.73e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   48 AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQSPVHVAAANKAVKCAEVII 127
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  128 PLLSSVN-VSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKG 206
Cdd:PHA02875    89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958801668  207 YTPLHAAASNGQINVVKHLLNLGVEIDEINVYGN-TALHIACYNGQDAVVNELIDYGANVN 266
Cdd:PHA02875   169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 220-545 7.94e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 93.49  E-value: 7.94e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  220 NVVKHLLN-LGVEIDEINvygnTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLhFAAASTHGALCLELLVNNGAD 298
Cdd:PHA02874    19 KIIKNKGNcINISVDETT----TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPL-LTAIKIGAHDIIKLLIDNGVD 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  299 VNIqskdgkspLHMTAVHGRFTRsqTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHL 378
Cdd:PHA02874    94 TSI--------LPIPCIEKDMIK--TILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  379 AALNAHSDCCRKLLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAanCHFHCIKALV 458
Cdd:PHA02874   164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI--IHNRSAIELL 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  459 TTGANINETDNWGRTALHYAAASDMDRNkmilgnahdnseelerarevkgkdaalCLEFLLQNDANPSIRDKEGYNSIHY 538
Cdd:PHA02874   242 INNASINDQDIDGSTPLHHAINPPCDID---------------------------IIDILLYHKADISIKDNKGENPIDT 294


                   ....*..
gi 1958801668  539 AAAYGHR 545
Cdd:PHA02874   295 AFKYINK 301
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 389-664 9.67e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.11  E-value: 9.67e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  389 RKLLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCH-----FHCIKALVTTGAN 463
Cdd:PHA03100    19 KYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGAN 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  464 INETDNWGRTALHYAAASDMDRNKMIlgnahdnseelerarevkgkdaalclEFLLQNDANPSIRDKEGYNSIHYAAAYG 543
Cdd:PHA03100    99 VNAPDNNGITPLLYAISKKSNSYSIV--------------------------EYLLDNGANVNIKNSDGENLLHLYLESN 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  544 HR--QCLELLLERTNtgfeesdggalksplHLAAYNghhqALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVN 621
Cdd:PHA03100   153 KIdlKILKLLIDKGV---------------DINAKN----RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLD 213

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1958801668  622 QGASIFVKDNVTKrTPLHASVINGHTLCLRLLLEIADNPEVVD 664
Cdd:PHA03100   214 LGANPNLVNKYGD-TPLHIAILNNNKEIFKLLLNNGPSIKTII 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
376-468 1.17e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 1.17e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  376 LHLAALNAHSDCCRKLLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLLqSSGADFHKKDKcGRTPLHYAAANCHFHCIK 455
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1958801668  456 ALVTTGANINETD 468
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
604-700 2.61e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 2.61e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  604 LYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADnpevVDVKDaKGQTPLMLAVAYGHI 683
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHL 74

                           90
                   ....*....|....*..
gi 1958801668  684 DAVSLLLEKEANVDAVD 700
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 651-1016 2.98e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 88.93  E-value: 2.98e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  651 RLLLEIADnpevVDVKDAKGQTPLMLAVAYGH---IDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEE-CVQMLLEQE 726
Cdd:PHA03095    32 RLLAAGAD----VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  727 ASILCKDSRGRTPLHyAAARGHATwlNELVQIALSEE--DCCLKDNQGYTPLHwaCYNGNENC-IEVLleqkcfrkfign 803
Cdd:PHA03095   108 ADVNAKDKVGRTPLH-VYLSGFNI--NPKVIRLLLRKgaDVNALDLYGMTPLA--VLLKSRNAnVELL------------ 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  804 pftplhcaiinghescaSLLLGAIdsSIVSCRDDKGRTTLH--AAAFGDHAECLQLLLRHDAQVNAVDNSGktalmmaae 881
Cdd:PHA03095   171 -----------------RLLIDAG--ADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLG--------- 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  882 ngqagavdilvnsaqadltvkdkdlNTPLHLAISKGHEKcALLILDKIQDESLINAKNSALQTPLHIAARNGLKVVVEEL 961
Cdd:PHA03095   223 -------------------------NTPLHSMATGSSCK-RSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRL 276

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801668  962 LAKGACVLAVDENGHTP-ALAcapnkdVADCLALILATMMTFSPSSTMTAVNFVYF 1016
Cdd:PHA03095   277 IALGADINAVSSDGNTPlSLM------VRNNNGRAVRAALAKNPSAETVAATLNTA 326
Ank_2 pfam12796
Ankyrin repeats (3 copies);
112-203 3.08e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 3.08e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  112 HVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKgANINAFDkKDRRALHWAAYMGHLDVVAL 191
Cdd:pfam12796    2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|..
gi 1958801668  192 LINHGAEVTCKD 203
Cdd:pfam12796   80 LLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
571-664 5.52e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 5.52e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  571 LHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQgasIFVKDNVTKRTPLHASVINGHTLCL 650
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 1958801668  651 RLLLEIADNPEVVD 664
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 182-696 9.99e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 88.58  E-value: 9.99e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  182 YMGHLDVVALLIN-----HGAEvTCKDKK-GYTPLHAAASNGQINVVKHLLNLGVEIDEINVYG-NTALHIACY--NGQD 252
Cdd:PHA02876    12 RGNCIDILSAIDNydlhkHGAN-QCENESiPFTAIHQALQLRQIDIVEEIIQQNPELIYITDHKcHSTLHTICIipNVMD 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  253 AVVNELIDYGANVNQPNNSGFTPLHfaaasTHGALCLELLVN--NGADVNIqSKDGKSPLHMTAVHGRFTR-----SQTL 325
Cdd:PHA02876    91 IVISLTLDCDIILDIKYASIILNKH-----KLDEACIHILKEaiSGNDIHY-DKINESIEYMKLIKERIQQdelliAEML 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  326 IQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRK--------------- 390
Cdd:PHA02876   165 LEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAiidnrsninkndlsl 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  391 --------------LLSSGFEIDTPDTFGRTCLHAAAAGGNVECI--KLLQsSGADFHKKDKCGRTPLHYAAANCH-FHC 453
Cdd:PHA02876   245 lkairnedletsllLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvpKLLE-RGADVNAKNIKGETPLYLMAKNGYdTEN 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  454 IKALVTTGANINETDNWGRTALHyaAASDMDRNKMILGNahdnseelerarevkgkdaalclefLLQNDANPSIRDKEGY 533
Cdd:PHA02876   324 IRTLIMLGADVNAADRLYITPLH--QASTLDRNKDIVIT-------------------------LLELGANVNARDYCDK 376

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  534 NSIHYAAAYGHRQCLELLLertntgfeesDGGAlksplhlaaynghhqalevllqslvDLDIRDEKGRTALYLAAFKGHT 613
Cdd:PHA02876   377 TPIHYAAVRNNVVIINTLL----------DYGA-------------------------DIEALSQKIGTALHFALCGTNP 421

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  614 -ECVEALVNQGASIFVKdNVTKRTPLHASVINGHTL-CLRLLLeiaDNPEVVDVKDAKGQTPLMLAVAYGHIdaVSLLLE 691
Cdd:PHA02876   422 yMSVKTLIDRGANVNSK-NKDLSTPLHYACKKNCKLdVIEMLL---DNGADVNAINIQNQYPLLIALEYHGI--VNILLH 495


                   ....*
gi 1958801668  692 KEANV 696
Cdd:PHA02876   496 YGAEL 500
PHA03095 PHA03095
ankyrin-like protein; Provisional
 389-725 1.36e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 87.00  E-value: 1.36e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  389 RKLLSSGFEIDTPDTFGRTCLHAAAAGGNVEC---IKLLQSSGADFHKKDKCGRTPLH-YAAANCHFHCIKALVTTGANI 464
Cdd:PHA03095    31 RRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADV 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  465 NETDNWGRTALHYAAASDMDRNKMIlgnahdnseelerarevkgkdaalclEFLLQNDANPSIRDKEGYNSIHyaaaygh 544
Cdd:PHA03095   111 NAKDKVGRTPLHVYLSGFNINPKVI--------------------------RLLLRKGADVNALDLYGMTPLA------- 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  545 rqcleLLLERTNTGFEesdggalksplhlaaynghhqALEVLLQSLVDLDIRDEKGRTAL--YLAAFKGHTECVEALVNQ 622
Cdd:PHA03095   158 -----VLLKSRNANVE---------------------LLRLLIDAGADVYAVDDRFRSLLhhHLQSFKPRARIVRELIRA 211

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  623 GASIFVKdNVTKRTPLHASVIngHTLCLRLLLE--IADNPEVvDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVD 700
Cdd:PHA03095   212 GCDPAAT-DMLGNTPLHSMAT--GSSCKRSLVLplLIAGISI-NARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVS 287

                          330       340
                   ....*....|....*....|....*
gi 1958801668  701 TVGCTALHRGIMTGHEECVQMLLEQ 725
Cdd:PHA03095   288 SDGNTPLSLMVRNNNGRAVRAALAK 312
Ank_2 pfam12796
Ankyrin repeats (3 copies);
45-170 4.43e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.08  E-value: 4.43e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   45 LHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHsADVNARDKnwqspvhvaaankavkcae 124
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN------------------- 60

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958801668  125 viipllssvnvsdrgGRTALHHAALNGHMEMVNLLLAKGANINAFD 170
Cdd:pfam12796   61 ---------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
843-939 1.01e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 1.01e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  843 LHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKdlnTPLHLAISKGHEKCA 922
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77

                           90
                   ....*....|....*..
gi 1958801668  923 LLILDKIQDeslINAKN 939
Cdd:pfam12796   78 KLLLEKGAD---INVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 515-727 1.15e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 83.50  E-value: 1.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  515 LEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLerTNTGFEESDGGALKSPLHLAAYNGHHQALEVLLQS--LVD 592
Cdd:PHA02875    18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLM--KHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLgkFAD 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  593 lDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKdNVTKRTPLHASVINGHTLCLRLLLeiaDNPEVVDVKDAKGQT 672
Cdd:PHA02875    96 -DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP-NTDKFSPLHLAVMMGDIKGIELLI---DHKACLDIEDCCGCT 170

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801668  673 PLMLAVAYGHIDAVSLLLEKEANVDAVDTVGC-TALHRGIMTGHEECVQMLLEQEA 727
Cdd:PHA02875   171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGA 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
12-104 1.15e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 1.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   12 LVQAIFSGDPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLiLSGARVNAKDNMWlTPLHRAVASRSEEAVQ 91
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDNGR-TALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1958801668   92 VLIKHSADVNARD 104
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
707-796 1.89e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.89e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  707 LHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHAtwlnELVQIALSEEDCCLKDNqGYTPLHWACYNGNEN 786
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHL----EIVKLLLEHADVNLKDN-GRTALHYAARSGHLE 75

                           90
                   ....*....|
gi 1958801668  787 CIEVLLEQKC 796
Cdd:pfam12796   76 IVKLLLEKGA 85
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 391-743 2.25e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 83.96  E-value: 2.25e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  391 LLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANINetdnw 470
Cdd:PHA02876   164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN----- 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  471 grtalhyaaasdmdRNKMILGNAHDNsEELERArevkgkdaalclefLLQNDANPSIRDKEGYNSihyaaayghrqclel 550
Cdd:PHA02876   239 --------------KNDLSLLKAIRN-EDLETS--------------LLLYDAGFSVNSIDDCKN--------------- 274

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  551 llertntgfeesdggalkSPLHLAAYNGHHQAL-EVLLQSLVDLDIRDEKGRTALYLAAFKGH-TECVEALVNQGASIFV 628
Cdd:PHA02876   275 ------------------TPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNA 336

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  629 KDNVTKrTPLH-ASVINGHTLCLRLLLEIADNpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTAL 707
Cdd:PHA02876   337 ADRLYI-TPLHqASTLDRNKDIVITLLELGAN---VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTAL 412

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1958801668  708 HRGIM-TGHEECVQMLLEQEASILCKDSRGRTPLHYA 743
Cdd:PHA02876   413 HFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 571-846 2.97e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 82.70  E-value: 2.97e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  571 LHLAAYNGHHQALEVLLQSLVD-LDIRDEKGRTALYLAAFKGHTECVEALVNQGASI-FVKDNVTKrtPLHASVINGHTL 648
Cdd:PHA02874     5 LRMCIYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADInHINTKIPH--PLLTAIKIGAHD 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  649 CLRLLLE--------------------IADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALH 708
Cdd:PHA02874    83 IIKLLIDngvdtsilpipciekdmiktILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIH 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  709 RGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHATWLNELVQialSEEDCCLKDNQGYTPLHWACYNgNENCI 788
Cdd:PHA02874   163 IAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLID---HGNHIMNKCKNGFTPLHNAIIH-NRSAI 238

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801668  789 EVLLEQKCFRKFIGNPFTPLHCAIingHESCA-----SLLLGAIDSSIvscRDDKGRTTLHAA 846
Cdd:PHA02874   239 ELLINNASINDQDIDGSTPLHHAI---NPPCDidiidILLYHKADISI---KDNKGENPIDTA 295
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 233-550 5.95e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 81.85  E-value: 5.95e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  233 DEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELL-VNNGADVNIQSKDGKSPLH 311
Cdd:PHA02878    31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIrSINKCSVFYTLVAIKDAFN 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  312 MTAVH-------GRFTRSQTLiqNGGEIDCVDKDGNTPLHVaaryghellINTLITSGADTAKCGIHSM-FPLHLAALNA 383
Cdd:PHA02878   111 NRNVEifkiiltNRYKNIQTI--DLVYIDKKSKDDIIEAEI---------TKLLLSYGADINMKDRHKGnTALHYATENK 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  384 HSDCCRKLLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANC-HFHCIKALVTTGA 462
Cdd:PHA02878   180 DQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCkDYDILKLLLEHGV 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  463 NIN-ETDNWGRTALHYAAASDmDRNKMILG-----NAHDNSEELERAREVKGKDAALCLEFL-----LQNDANPSIRDKE 531
Cdd:PHA02878   260 DVNaKSYILGLTALHSSIKSE-RKLKLLLEygadiNSLNSYKLTPLSSAVKQYLCINIGRILisnicLLKRIKPDIKNSE 338

                          330
                   ....*....|....*....
gi 1958801668  532 GYnSIHYAAAYGHRQCLEL 550
Cdd:PHA02878   339 GF-IDNMDCITSNKRLNQI 356
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 549-731 7.85e-16

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 82.61  E-value: 7.85e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  549 ELLLERTntgfEESDGGALKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFV 628
Cdd:PLN03192   511 DLLGDNG----GEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI 586

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  629 KDnVTKRTPLHASVINGHTLCLRLLLEIA--DNPEVvdvkdakGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTA 706
Cdd:PLN03192   587 RD-ANGNTALWNAISAKHHKIFRILYHFAsiSDPHA-------AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658

                          170       180
                   ....*....|....*....|....*
gi 1958801668  707 LHRGIMTGHEECVQMLLEQEASILC 731
Cdd:PLN03192   659 LQVAMAEDHVDMVRLLIMNGADVDK 683
Ank_2 pfam12796
Ankyrin repeats (3 copies);
536-630 9.52e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.61  E-value: 9.52e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  536 IHYAAAYGHRQCLELLLE-RTNTGFEESDGgalKSPLHLAAYNGHHQALEVLLQSlVDLDIRDEkGRTALYLAAFKGHTE 614
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLEnGADANLQDKNG---RTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 1958801668  615 CVEALVNQGASIFVKD 630
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
409-482 1.05e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 1.05e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801668  409 LHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTgANINETDNwGRTALHYAAASD 482
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSG 72
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 141-373 1.08e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.81  E-value: 1.08e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  141 RTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQIN 220
Cdd:PHA02875     3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  221 VVKHLLNLGVEIDEInVY--GNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGAD 298
Cdd:PHA02875    83 AVEELLDLGKFADDV-FYkdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG-IELLIDHKAC 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801668  299 VNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHEL-LINTLITSGADtakCGIHSM 373
Cdd:PHA02875   161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIdIVRLFIKRGAD---CNIMFM 233
PHA03095 PHA03095
ankyrin-like protein; Provisional
 586-966 1.13e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.84  E-value: 1.13e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  586 LLQSLVDLDIRDEKGRTAL-YLAAFKGH--TECVEALVNQGASIFVKDnVTKRTPLHASVINGHTL-CLRLLLEI-ADnp 660
Cdd:PHA03095    33 LLAAGADVNFRGEYGKTPLhLYLHYSSEkvKDIVRLLLEAGADVNAPE-RCGFTPLHLYLYNATTLdVIKLLIKAgAD-- 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  661 evVDVKDAKGQTPL--MLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALH-----RGIMTgheECVQMLLEQEASILCKD 733
Cdd:PHA03095   110 --VNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvllksRNANV---ELLRLLIDAGADVYAVD 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  734 SRGRTPLHyaaarghatwlnelvQIALSeedccLKDNqgytplhwacyngnencievlleQKCFRKFIGNPFTPlhcaii 813
Cdd:PHA03095   185 DRFRSLLH---------------HHLQS-----FKPR-----------------------ARIVRELIRAGCDP------ 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  814 nghescaslllgaidssivSCRDDKGRTTLHAAAFGDHAECLQL--LLRHDAQVNAVDNSGKTALMMAAENGQAGAVDIL 891
Cdd:PHA03095   216 -------------------AATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRL 276

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801668  892 VNsAQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDESLINAKNSALQTPLHIAARNGLKVVVEELLAKGA 966
Cdd:PHA03095   277 IA-LGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTASVAGGDIPSDATRLCVAKVVLRGA 350
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 254-465 1.53e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.04  E-value: 1.53e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  254 VVNELIDYGANVNQPNNSGFTPLHFAAaSTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI- 332
Cdd:PHA02875    17 IARRLLDIGINPNFEIYDGISPIKLAM-KFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAd 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  333 DCVDKDGNTPLHVAARYGHELLINTLITSGADTakcgihsmfplhlaalnahsdccrkllssgfeiDTPDTFGRTCLHAA 412
Cdd:PHA02875    96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADP---------------------------------DIPNTDKFSPLHLA 142

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958801668  413 AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANIN 465
Cdd:PHA02875   143 VMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
Ank_2 pfam12796
Ankyrin repeats (3 copies);
776-869 1.56e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 1.56e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  776 LHWACYNGNENCIEVLLEQKC-FRKFIGNPFTPLHCAIINGHESCASLLLGAIDSSIvscrDDKGRTTLHAAAFGDHAEC 854
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL----KDNGRTALHYAARSGHLEI 76

                           90
                   ....*....|....*
gi 1958801668  855 LQLLLRHDAQVNAVD 869
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 74-281 2.55e-15

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: 80.44  E-value: 2.55e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   74 WLTPLHRAVASRSEEAVQVLIK-HSADVNARDKNWQSPVHVAAANKAVKCAEVII---PLLssVNV---SD-RGGRTALH 145
Cdd:cd22192     17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaaPEL--VNEpmtSDlYQGETALH 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  146 HAALNGHMEMVNLLLAKGANIN------AFDKKDRRAL-----H---WAAYMGHLDVVALLINHGAEVTCKDKKGYTPLH 211
Cdd:cd22192     95 IAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801668  212 AAASNGQINVVKH----LLNLGVEIDEINVYgntalHIacyngqdavvnelidyganvnqPNNSGFTPLHFAAA 281
Cdd:cd22192    175 ILVLQPNKTFACQmydlILSYDKEDDLQPLD-----LV----------------------PNNQGLTPFKLAAK 221
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 20-170 4.80e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 79.15  E-value: 4.80e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   20 DPEEIRLLIHKTEDVNALDSEK-RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSA 98
Cdd:PHA02878   146 EAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801668   99 DVNARDKNWQSPVHVAAAnkAVKCAEVIIPLL---SSVNV-SDRGGRTALHHAAlngHMEMV-NLLLAKGANINAFD 170
Cdd:PHA02878   226 STDARDKCGNTPLHISVG--YCKDYDILKLLLehgVDVNAkSYILGLTALHSSI---KSERKlKLLLEYGADINSLN 297
PHA03095 PHA03095
ankyrin-like protein; Provisional
 17-168 1.21e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.76  E-value: 1.21e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   17 FSGDPEEIRLLIHKTEDVNALDSEKRTPLHVaaFLG----DAEIIELLILSGARVNAKDNMWLTPLHR-AVASRSEEAV- 90
Cdd:PHA03095   128 FNINPKVIRLLLRKGADVNALDLYGMTPLAV--LLKsrnaNVELLRLLIDAGADVYAVDDRFRSLLHHhLQSFKPRARIv 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   91 QVLIKHSADVNARDKNWQSPVHVAAANKAVKcAEVIIPLL---SSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANIN 167
Cdd:PHA03095   206 RELIRAGCDPAATDMLGNTPLHSMATGSSCK-RSLVLPLLiagISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284


                   .
gi 1958801668  168 A 168
Cdd:PHA03095   285 A 285
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 617-980 1.31e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 78.57  E-value: 1.31e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  617 EALVNQGASIFVKDnVTKRTPLHASVINGHTLCLRLLLEIADNPEVVDVKDAkgqTPLMLAVAYGHIDAVSLLLEKEANV 696
Cdd:PHA02876   162 EMLLEGGADVNAKD-IYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDL---SVLECAVDSKNIDTIKAIIDNRSNI 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  697 DAVDTvgctALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAargHATWLNELVQIALSE-EDCCLKDNQGYTP 775
Cdd:PHA02876   238 NKNDL----SLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHAS---QAPSLSRLVPKLLERgADVNAKNIKGETP 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  776 LHWACYNGNENcievlleqkcfrkfignpftplhcaiinghESCASLLLGAIDssiVSCRDDKGRTTLHAAAFGD-HAEC 854
Cdd:PHA02876   311 LYLMAKNGYDT------------------------------ENIRTLIMLGAD---VNAADRLYITPLHQASTLDrNKDI 357

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  855 LQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCALLILdkIQDESL 934
Cdd:PHA02876   358 VITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG-ADIEALSQKIGTALHFALCGTNPYMSVKTL--IDRGAN 434

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1958801668  935 INAKNSALQTPLHIAARNGLKV-VVEELLAKGACVLAVDENGHTPAL 980
Cdd:PHA02876   435 VNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAINIQNQYPLL 481
Ank_2 pfam12796
Ankyrin repeats (3 copies);
674-748 1.32e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 1.32e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801668  674 LMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLEQEAsiLCKDSRGRTPLHYAAARGH 748
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGH 73
PHA02798 PHA02798
ankyrin-like protein; Provisional
 78-364 1.35e-14

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 77.57  E-value: 1.35e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   78 LHRAvaSRSEEAVQVLIKHSADVNARDKNWQSPVhvaaankavkCAeviipLLSsvNVSDrggrtalhhaaLNGHMEMVN 157
Cdd:PHA02798    44 LQRD--SPSTDIVKLFINLGANVNGLDNEYSTPL----------CT-----ILS--NIKD-----------YKHMLDIVK 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  158 LLLAKGANINAFDKKDRRALHWA---AYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNG---QINVVKHLLNLGVE 231
Cdd:PHA02798    94 ILIENGADINKKNSDGETPLYCLlsnGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVD 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  232 IDEI-NVYGNTALHiaCY-----NGQDA-VVNELIDYGANVNQPNNSgftplhfaAASTHGALCLELLVNNG-------- 296
Cdd:PHA02798   174 INTHnNKEKYDTLH--CYfkyniDRIDAdILKLFVDNGFIINKENKS--------HKKKFMEYLNSLLYDNKrfkknild 243

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801668  297 ---ADVNIQSKD--GKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGAD 364
Cdd:PHA02798   244 fifSYIDINQVDelGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 498-908 4.08e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.64  E-value: 4.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  498 EELERAREVKGKDAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLER-TNTGFEESDGgalkspLHLAAY 576
Cdd:PHA02876   144 EYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYgADVNIIALDD------LSVLEC 217

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  577 NGHHQALEVLlQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDnVTKRTPLHASVingHTLCL-RLLLE 655
Cdd:PHA02876   218 AVDSKNIDTI-KAIIDNRSNINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSID-DCKNTPLHHAS---QAPSLsRLVPK 292

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  656 IADNPEVVDVKDAKGQTPLMLAVAYGH-IDAVSLLLEKEANVDAVDTVGCTALHRG-IMTGHEECVQMLLEQEASILCKD 733
Cdd:PHA02876   293 LLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARD 372

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  734 SRGRTPLHYAAARGHATWLNELVQIALSEEdcCLKDNQGyTPLHWACYNGNencievlleqkcfrkfignPFTPLHCAII 813
Cdd:PHA02876   373 YCDKTPIHYAAVRNNVVIINTLLDYGADIE--ALSQKIG-TALHFALCGTN-------------------PYMSVKTLID 430

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  814 NGHEscaslllgaidssiVSCRDDKGRTTLHAAAFGD-HAECLQLLLRHDAQVNAVDNSGKTALMMAAenGQAGAVDILV 892
Cdd:PHA02876   431 RGAN--------------VNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILL 494

                          410
                   ....*....|....*...
gi 1958801668  893 NSAQA--DLTVKDKDLNT 908
Cdd:PHA02876   495 HYGAElrDSRVLHKSLND 512
Ank_2 pfam12796
Ankyrin repeats (3 copies);
740-824 5.11e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 5.11e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  740 LHYAAARGHAtwlnELVQIALSEE-DCCLKDNQGYTPLHWACYNGNENCIEVLLEQKCFRKFiGNPFTPLHCAIINGHES 818
Cdd:pfam12796    1 LHLAAKNGNL----ELVKLLLENGaDANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-DNGRTALHYAARSGHLE 75


                   ....*.
gi 1958801668  819 CASLLL 824
Cdd:pfam12796   76 IVKLLL 81
Ank_2 pfam12796
Ankyrin repeats (3 copies);
343-435 1.05e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 1.05e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  343 LHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSgFEIDtPDTFGRTCLHAAAAGGNVECIK 422
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1958801668  423 LLQSSGADFHKKD 435
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 567-743 1.20e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 74.23  E-value: 1.20e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  567 LKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNVTKrTPLHASVINGH 646
Cdd:PHA02874   124 LKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGE-SPLHNAAEYGD 202

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  647 TLCLRLLLeiaDNPEVVDVKDAKGQTPLMLAVAYGHiDAVSLLLeKEANVDAVDTVGCTALHRGIMTG-HEECVQMLLEQ 725
Cdd:PHA02874   203 YACIKLLI---DHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI-NNASINDQDIDGSTPLHHAINPPcDIDIIDILLYH 277

                          170
                   ....*....|....*...
gi 1958801668  726 EASILCKDSRGRTPLHYA 743
Cdd:PHA02874   278 KADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
876-972 3.26e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.29  E-value: 3.26e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  876 LMMAAENGQAGAVDILVNSaQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQdeslINAKNSAlQTPLHIAARNGLK 955
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD----VNLKDNG-RTALHYAARSGHL 74

                           90
                   ....*....|....*..
gi 1958801668  956 VVVEELLAKGACVLAVD 972
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 584-966 3.43e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 73.94  E-value: 3.43e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  584 EVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGA--SIFVKDNVTkrtplhasvinghtlclrlLLEIADNPE 661
Cdd:PHA02876   162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGAdvNIIALDDLS-------------------VLECAVDSK 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  662 VVDVKDA---------KGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGH-EECVQMLLEQEASILC 731
Cdd:PHA02876   223 NIDTIKAiidnrsninKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNA 302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  732 KDSRGRTPLHYAAARGHATwlNELVQIALSEEDCCLKDNQGYTPLHWA-CYNGNENCIEVLLEqkcfrkfignpftplhc 810
Cdd:PHA02876   303 KNIKGETPLYLMAKNGYDT--ENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLE----------------- 363

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  811 aiinghescasllLGAidssIVSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMA-AENGQAGAVD 889
Cdd:PHA02876   364 -------------LGA----NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVK 426

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801668  890 ILVNSAqADLTVKDKDLNTPLHLAISKgheKCALLILDKIQDESL-INAKNSALQTPLHIAArnGLKVVVEELLAKGA 966
Cdd:PHA02876   427 TLIDRG-ANVNSKNKDLSTPLHYACKK---NCKLDVIEMLLDNGAdVNAINIQNQYPLLIAL--EYHGIVNILLHYGA 498
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 166-445 1.18e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.45  E-value: 1.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  166 INAFDKKDRRA----------LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEI 235
Cdd:PHA02878    20 IEYIDHTENYStsaslipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVF 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  236 NVYgnTALHIACYNGQDAVVNE-LIDYGANVNQPNNSGFTPLHFAAASThgALCLELLVNNGADVNIQSKD-GKSPLHMT 313
Cdd:PHA02878   100 YTL--VAIKDAFNNRNVEIFKIiLTNRYKNIQTIDLVYIDKKSKDDIIE--AEITKLLLSYGADINMKDRHkGNTALHYA 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  314 AVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHS-DCCRKLL 392
Cdd:PHA02878   176 TENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLL 255

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958801668  393 SSGFEIDTPDTF-GRTCLHAAAAGGNVecIKLLQSSGADFHKKDKCGRTPLHYA 445
Cdd:PHA02878   256 EHGVDVNAKSYIlGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 9-167 1.34e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 71.18  E-value: 1.34e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668    9 QPPLVQAIFSGDPEEIRLLIHKTEDVNALDSEK-RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSE 87
Cdd:PHA02875    69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   88 EAVQVLIKHSADVNARDKNWQSPVHVAAANKAVKCAEVIIPLLSSVN-VSDRGGRTALHHAALNGHMEMVNLLLAKGANI 166
Cdd:PHA02875   149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGADC 228


                   .
gi 1958801668  167 N 167
Cdd:PHA02875   229 N 229
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 134-276 1.57e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.82  E-value: 1.57e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  134 NVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLiNHGAEVTCKDKKGyTPLHAA 213
Cdd:PLN03192   552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL-YHFASISDPHAAG-DLLCTA 629

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801668  214 ASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPN-NSGFTPL 276
Cdd:PLN03192   630 AKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDDDFSPT 693
PHA02798 PHA02798
ankyrin-like protein; Provisional
 55-273 2.39e-12

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 70.63  E-value: 2.39e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   55 EIIELLILSGARVNAKDNMWLTPLHRAVASRSE-----EAVQVLIKHSADVNARDKNWQSPVHVAAANKAVKCAEVIIPL 129
Cdd:PHA02798    52 DIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFM 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  130 L---SSVNVSDRGGRTALHHAALNGH---MEMVNLLLAKGANINAFDKKDR-RALHwaAYMGH------LDVVALLINHG 196
Cdd:PHA02798   132 IengADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNNKEKyDTLH--CYFKYnidridADILKLFVDNG 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  197 ---------------------------------------AEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINV 237
Cdd:PHA02798   210 fiinkenkshkkkfmeylnsllydnkrfkknildfifsyIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITE 289

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1958801668  238 YGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGF 273
Cdd:PHA02798   290 LGNTCLFTAFENESKFIFNSILNKKPNKNTISYTYY 325
Ank_2 pfam12796
Ankyrin repeats (3 copies);
514-597 3.15e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.60  E-value: 3.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  514 CLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNTGFEESDggalKSPLHLAAYNGHHQALEVLLQSLVDL 593
Cdd:pfam12796   12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNG----RTALHYAARSGHLEIVKLLLEKGADI 87


                   ....
gi 1958801668  594 DIRD 597
Cdd:pfam12796   88 NVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
140-193 6.89e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.14  E-value: 6.89e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958801668  140 GRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLI 193
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 48-201 8.00e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 69.51  E-value: 8.00e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   48 AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQSPVHVAAANKAVKCAEVII 127
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801668  128 PLLSSVNVSDRGgrTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTC 201
Cdd:PLN03192   612 HFASISDPHAAG--DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 107-328 8.64e-12

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: 69.27  E-value: 8.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  107 WQSPVHVAAANKAVKCaevIIPLL--SSVNVSDRG--GRTALHHAALNGHMEMVNLLLakganinafdkkdrralhwaay 182
Cdd:cd22192     17 SESPLLLAAKENDVQA---IKKLLkcPSCDLFQRGalGETALHVAALYDNLEAAVVLM---------------------- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  183 mghlDVVALLINHgaEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEI--------------DEINVYGNTALHIACY 248
Cdd:cd22192     72 ----EAAPELVNE--PMTSDLYQGETALHIAVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAAC 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  249 NGQDAVVNELIDYGANVNQPNNSGFTPLH---FAAASTHGALCLELLVNNGADVN------IQSKDGKSPLHMTAVHGRF 319
Cdd:cd22192    146 VGNEEIVRLLIEHGADIRAQDSLGNTVLHilvLQPNKTFACQMYDLILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNI 225


                   ....*....
gi 1958801668  320 TRSQTLIQN 328
Cdd:cd22192    226 VMFQHLVQK 234
Ank_2 pfam12796
Ankyrin repeats (3 copies);
243-336 1.15e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.67  E-value: 1.15e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  243 LHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGAlCLELLVNNgADVNIQSkDGKSPLHMTAVHGRFTRS 322
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLE-IVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 1958801668  323 QTLIQNGGEIDCVD 336
Cdd:pfam12796   78 KLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
174-226 1.19e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 1.19e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958801668  174 RRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLL 226
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 774-992 1.35e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.07  E-value: 1.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  774 TPLHWACYNGNENCIEVLLEQKCFRKFIG-NPFTPLHCAI-INGHESCASLLLGAIDSSI-------------------- 831
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINtKIPHPLLTAIkIGAHDIIKLLIDNGVDTSIlpipciekdmiktildcgid 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  832 VSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLH 911
Cdd:PHA02874   117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLH 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  912 LAISKGHEKCALLILDkiqDESLINAKNSALQTPLHIAARNGLKVVveELLAKGACVLAVDENGHTP---ALACAPNKDV 988
Cdd:PHA02874   196 NAAEYGDYACIKLLID---HGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPlhhAINPPCDIDI 270


                   ....
gi 1958801668  989 ADCL 992
Cdd:PHA02874   271 IDIL 274
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 441-678 1.44e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.98  E-value: 1.44e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  441 PLHYAAANCHFHCIKALVTTGANINETDNWGRTALH--------------------------YAAASDMDRN------KM 488
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHiickepnklgmkemirsinkcsvfytLVAIKDAFNNrnveifKI 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  489 ILGNAHDNSE--ELERAREVKGKDA--ALCLEFLLQNDANPSIRDKEGYNS-IHYAAAYGHRQCLELLL---------ER 554
Cdd:PHA02878   120 ILTNRYKNIQtiDLVYIDKKSKDDIieAEITKLLLSYGADINMKDRHKGNTaLHYATENKDQRLTELLLsyganvnipDK 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  555 TNtgfeesdggalKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLA-AFKGHTECVEALVNQGASIFVKDNVT 633
Cdd:PHA02878   200 TN-----------NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYIL 268

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1958801668  634 KRTPLHASVINGHTlcLRLLLEIADNPEVVdvkDAKGQTPLMLAV 678
Cdd:PHA02878   269 GLTALHSSIKSERK--LKLLLEYGADINSL---NSYKLTPLSSAV 308
Ank_2 pfam12796
Ankyrin repeats (3 copies);
310-402 1.58e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 1.58e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  310 LHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGAdtAKCGIHSMFPLHLAALNAHSDCCR 389
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1958801668  390 KLLSSGFEIDTPD 402
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
405-458 2.06e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 2.06e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958801668  405 GRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALV 458
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 538-757 3.48e-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: 67.35  E-value: 3.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  538 YAAAYGHRQCLELLLERTNTGFEESdgGAL-KSPLHLAAYNGHHQALEVLLQS---LVDLDIRDE--KGRTALYLAAFKG 611
Cdd:cd22192     23 LAAKENDVQAIKKLLKCPSCDLFQR--GALgETALHVAALYDNLEAAVVLMEAapeLVNEPMTSDlyQGETALHIAVVNQ 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  612 HTECVEALVNQGAsifvkDNVTKRTPLHASVINGHTLCLRllleiadnpevvdvkdakGQTPLMLAVAYGHIDAVSLLLE 691
Cdd:cd22192    101 NLNLVRELIARGA-----DVVSPRATGTFFRPGPKNLIYY------------------GEHPLSFAACVGNEEIVRLLIE 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801668  692 KEANVDAVDTVGCTALHRGIMTGHEECV-QM---LLEQEASI------LCKDSRGRTPLHYAAARGHATWLNELVQ 757
Cdd:cd22192    158 HGADIRAQDSLGNTVLHILVLQPNKTFAcQMydlILSYDKEDdlqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 769-968 3.95e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.83  E-value: 3.95e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  769 DNQGYTPLHWACYNGNENCIEVLLEQKCFRKfIGNPFTPLHCAIINGHESCASLLL-----GAIDSSIVSCRDDKGRTTL 843
Cdd:PHA02878    67 DHRDLTPLHIICKEPNKLGMKEMIRSINKCS-VFYTLVAIKDAFNNRNVEIFKIILtnrykNIQTIDLVYIDKKSKDDII 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  844 haaafgdHAECLQLLLRHDAQVNAVD-NSGKTALMMAAENGQAGAVDILVnSAQADLTVKDKDLNTPLHLAISKGHEKcA 922
Cdd:PHA02878   146 -------EAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLL-SYGANVNIPDKTNNSPLHHAVKHYNKP-I 216

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1958801668  923 LLILdkIQDESLINAKNSALQTPLHIAARNGLKV-VVEELLAKGACV 968
Cdd:PHA02878   217 VHIL--LENGASTDARDKCGNTPLHISVGYCKDYdILKLLLEHGVDV 261
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 309-610 3.98e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.83  E-value: 3.98e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  309 PLHMtAVHGR-FTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSgadTAKCGI-HSMFPLHLAALNAHSD 386
Cdd:PHA02878    40 PLHQ-AVEARnLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS---INKCSVfYTLVAIKDAFNNRNVE 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  387 CCRKLLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDK-CGRTPLHYAAANCHFHCIKALVTTGANIN 465
Cdd:PHA02878   116 IFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVN 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  466 ETDNWGRTALHYAAASdmdRNKMIlgnahdnseelerarevkgkdaalcLEFLLQNDANPSIRDKEGYNSIHYAAAY-GH 544
Cdd:PHA02878   196 IPDKTNNSPLHHAVKH---YNKPI-------------------------VHILLENGASTDARDKCGNTPLHISVGYcKD 247

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801668  545 RQCLELLLERTNTGFEESDGGALkSPLHLAAYNghHQALEVLLQSLVDLDIRDEKGRTALYLAAFK 610
Cdd:PHA02878   248 YDILKLLLEHGVDVNAKSYILGL-TALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 743-912 4.83e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.20  E-value: 4.83e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  743 AAARGHATWLNELVQIALSEEdccLKDNQGYTPLHWACYNGNENCIEVLLEQKC---FRKFIGNpfTPLHCAIINGHESC 819
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPD---IGDSKGRTPLHIAASKGYEDCVLVLLKHACnvhIRDANGN--TALWNAISAKHHKI 606

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  820 ASLLLgaiDSSIVSCRDDKGRTTLHAAAFGDhAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILV-NSAQAD 898
Cdd:PLN03192   607 FRILY---HFASISDPHAAGDLLCTAAKRND-LTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLImNGADVD 682

                          170
                   ....*....|....
gi 1958801668  899 LTVKDKDLnTPLHL 912
Cdd:PLN03192   683 KANTDDDF-SPTEL 695
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 150-275 5.10e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 63.30  E-value: 5.10e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  150 NGHMEMVNLLLAKGANINAFDKKDRRAL--HWAAYMGHL--DVVALLINHGAEVTCKDKKGYTPLHAAASNG--QINVVK 223
Cdd:PHA02859    63 KVNVEILKFLIENGADVNFKTRDNNLSAlhHYLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHMYMCNFnvRINVIK 142

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958801668  224 HLLNLGVEIDEINVYGNTALH-IACYNGQDAVVNELIDYGANVNQPNNSGFTP 275
Cdd:PHA02859   143 LLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 638-908 5.73e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.84  E-value: 5.73e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  638 LHASVINGHTLCLRLLLE--IADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGH 715
Cdd:PHA03100     1 LYSYIVLTKSRIIKVKNIkyIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  716 E-----ECVQMLLEQEASILCKDSRGRTPLHYAAAR--GHATWLNELVQIALseeDCCLKDNQGYTPLHWA--CYNGNEN 786
Cdd:PHA03100    81 NltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGA---NVNIKNSDGENLLHLYleSNKIDLK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  787 CIEVLLEqkcfrkfignpftplHCAIINGHESCASLL-LGA-IDSsivscRDDKGRTTLHAAAFGDHAECLQLLLRHDAQ 864
Cdd:PHA03100   158 ILKLLID---------------KGVDINAKNRVNYLLsYGVpINI-----KDVYGFTPLHYAVYNNNPEFVKYLLDLGAN 217

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958801668  865 VNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTV-------KDKDLNT 908
Cdd:PHA03100   218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIietllyfKDKDLNT 268
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 183-430 8.49e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.04  E-value: 8.49e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  183 MGHLDVVALLINHGAEVTckDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYG 262
Cdd:PLN03192   504 LHDLNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  263 ANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSkdGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTP 342
Cdd:PLN03192   582 CNVHIRDANGNTALWNAISAKHHKI-FRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  343 LHVAARYGHELLINTLITSGADTAKCGIHSMF-PLHLaalnahsdccRKLLSS---GFEIDTPDTFGRTCLHAAAAGGNV 418
Cdd:PLN03192   659 LQVAMAEDHVDMVRLLIMNGADVDKANTDDDFsPTEL----------RELLQKrelGHSITIVDSVPADEPDLGRDGGSR 728

                          250
                   ....*....|..
gi 1958801668  419 ECikLLQSSGAD 430
Cdd:PLN03192   729 PG--RLQGTSSD 738
PHA02798 PHA02798
ankyrin-like protein; Provisional
 129-412 9.35e-11

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 65.63  E-value: 9.35e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  129 LLSSVNVSDRGGRTALHHAAL---NGHMEMVNLLLAKGANINAFDKKDRRAL-----HWAAYMGHLDVVALLINHGAEVT 200
Cdd:PHA02798    24 LIKSCNPNEIVNEYSIFQKYLqrdSPSTDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADIN 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  201 CKDKKGYTPLHAAASNGQIN---VVKHLLNLGVEIDEINVYGNTALHIACYNG---QDAVVNELIDYGANVNQPNNS-GF 273
Cdd:PHA02798   104 KKNSDGETPLYCLLSNGYINnleILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDINTHNNKeKY 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  274 TPLHFAAASTHGAL---CLELLVNNGADVNIQSKDGKSPLHMTAVhgrftrsqTLIQNGGEidcVDKDgntplhvaaryg 350
Cdd:PHA02798   184 DTLHCYFKYNIDRIdadILKLFVDNGFIINKENKSHKKKFMEYLN--------SLLYDNKR---FKKN------------ 240

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958801668  351 hellINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDTFGRTCLHAA 412
Cdd:PHA02798   241 ----ILDFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 635-747 1.88e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 64.24  E-value: 1.88e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  635 RTPLHASVINGHTLCLRLLLEIadNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTG 714
Cdd:PHA02875    69 ESELHDAVEEGDVKAVEELLDL--GKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958801668  715 HEECVQMLLEQEASILCKDSRGRTPLHYAAARG 747
Cdd:PHA02875   147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 602-784 2.34e-10

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 64.65  E-value: 2.34e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  602 TALYLAAFKGHTECVEAL-VNQGASIFVKDNVTKrTPLHASVINGHTLCLRLLLEIAdnPEVVDVKDA----KGQTPLML 676
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLlKCPSCDLFQRGALGE-TALHVAALYDNLEAAVVLMEAA--PELVNEPMTsdlyQGETALHI 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  677 AVAYGHIDAVSLLLEKEANVDAVDTVGcTALHRGI---------------MTGHEECVQMLLEQEASILCKDSRGRTPLH 741
Cdd:cd22192     96 AVVNQNLNLVRELIARGADVVSPRATG-TFFRPGPknliyygehplsfaaCVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958801668  742 YAAARGHATWLNELVQIALSEE----DCCL---KDNQGYTPLHWACYNGN 784
Cdd:cd22192    175 ILVLQPNKTFACQMYDLILSYDkeddLQPLdlvPNNQGLTPFKLAAKEGN 224
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 556-739 3.47e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.47  E-value: 3.47e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  556 NTGFEESDGgalKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGAsiFVKDNVTKR 635
Cdd:PHA02875    27 NPNFEIYDG---ISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK--FADDVFYKD 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  636 --TPLHASVINGHTLCLRLLLEIADNPevvDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMT 713
Cdd:PHA02875   102 gmTPLHLATILKKLDIMKLLIARGADP---DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAK 178

                          170       180
                   ....*....|....*....|....*.
gi 1958801668  714 GHEECVQMLLEQEASIlckDSRGRTP 739
Cdd:PHA02875   179 GDIAICKMLLDSGANI---DYFGKNG 201
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 49-280 3.52e-10

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: 64.33  E-value: 3.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   49 AFLGDAEIIELLILSGARVNAK-------DNMWLTPLHRAVA-SRSEEAVQVLIKHSADVNARDknwqSPVHVAAANKAV 120
Cdd:TIGR00870   20 AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAISLEYVD 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  121 KCAEVIIPLLSS---------VNVSDRG----GRTALHHAALNGHMEMVNLLLAKGANINA------FDKKDRRA----- 176
Cdd:TIGR00870   96 AVEAILLHLLAAfrksgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDsfyhg 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  177 ---LHWAAYMGHLDVVALLINHGAEVTCKDKKGytplhaaasngqiNVVKHLLNLGVEideiNVYGNTALHIACYngqda 253
Cdd:TIGR00870  176 espLNAAACLGSPSIVALLSEDPADILTADSLG-------------NTLLHLLVMENE----FKAEYEELSCQMY----- 233

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1958801668  254 vvNELIDYGANVNQ-------PNNSGFTPLHFAA 280
Cdd:TIGR00870  234 --NFALSLLDKLRDskeleviLNHQGLTPLKLAA 265
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 289-475 3.65e-10

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 64.16  E-value: 3.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  289 LELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRS--QTLIQNGGEIDCVDKDGNTPLH---VAARYGHELLINTLITSGA 363
Cdd:PHA02716   195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASviKKIIELGGDMDMKCVNGMSPIMtyiINIDNINPEITNIYIESLD 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  364 DTAKCGIHSMFPLHLA-ALNAHSDCCRKLLSSGFEIDTPDTFGRTCLHAAAAGGNV--ECIKLLQSSGADFHKKDKCGRT 440
Cdd:PHA02716   275 GNKVKNIPMILHSYITlARNIDISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIGNT 354

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958801668  441 PLH-YAAANCHFH-------------CIKALVTTGANINETDNWGRTAL 475
Cdd:PHA02716   355 VLHtYLSMLSVVNildpetdndirldVIQCLISLGADITAVNCLGYTPL 403
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 20-317 5.87e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 62.84  E-value: 5.87e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   20 DPEEIRLLIHKTEDVNaldSEKRTPLHVAAFLG----DAEIIELLILSGARVNAKDNMwLTPL-----HRAVAS-RSEEA 89
Cdd:PHA02989    15 DKNALEFLLRTGFDVN---EEYRGNSILLLYLKrkdvKIKIVKLLIDNGADVNYKGYI-ETPLcavlrNREITSnKIKKI 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   90 VQVLIKHSADVNARDKNWQSPvhvaaankavkcaevIIPLLSSVNVSDrggrtalhhaalnghMEMVNLLLAKGANINaf 169
Cdd:PHA02989    91 VKLLLKFGADINLKTFNGVSP---------------IVCFIYNSNINN---------------CDMLRFLLSKGINVN-- 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  170 DKKDRRA---LH--WAAYMGHLDVVALLINHGAEV-TCKDKKGYTP----LHAAASNGQINVVKHLLNLGVEIDEINVYG 239
Cdd:PHA02989   139 DVKNSRGynlLHmyLESFSVKKDVIKILLSFGVNLfEKTSLYGLTPmniyLRNDIDVISIKVIKYLIKKGVNIETNNNGS 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  240 NTAL------HIACYNGQDAVVNELIDYgANVNQPNNSGFTPLhFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMT 313
Cdd:PHA02989   219 ESVLesfldnNKILSKKEFKVLNFILKY-IKINKKDKKGFNPL-LISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296


                   ....
gi 1958801668  314 AVHG 317
Cdd:PHA02989   297 IKHG 300
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 340-476 7.27e-10

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 63.11  E-value: 7.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  340 NTPLHVAARYGHELLINTLITS-GADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSG----FEIDTPDTF-GRTCLHAAA 413
Cdd:cd22192     18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelvNEPMTSDLYqGETALHIAV 97

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801668  414 AGGNVECIKLLQSSGAD----------FHKKDKC----GRTPLHYAAANCHFHCIKALVTTGANINETDNWGRTALH 476
Cdd:cd22192     98 VNQNLNLVRELIARGADvvspratgtfFRPGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
Ank_4 pfam13637
Ankyrin repeats (many copies);
672-723 1.63e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 1.63e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958801668  672 TPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLL 723
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 144-226 1.75e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.84  E-value: 1.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  144 LHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVK 223
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165


                   ...
gi 1958801668  224 HLL 226
Cdd:PTZ00322   166 LLS 168
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 3-114 2.00e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.05  E-value: 2.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668    3 VLKLCDQPPLVQAIFSGDPEEIRLLIHKTEDVNALDSEKRTPLHVA-AFLGDAEIIELLILSGARVNAKDNMW-LTPLHR 80
Cdd:PHA02878   196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILgLTALHS 275

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1958801668   81 AVasRSEEAVQVLIKHSADVNARDKNWQSPVHVA 114
Cdd:PHA02878   276 SI--KSERKLKLLLEYGADINSLNSYKLTPLSSA 307
Ank_4 pfam13637
Ankyrin repeats (many copies);
569-620 2.41e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 2.41e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958801668  569 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALV 620
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 692-978 2.83e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.66  E-value: 2.83e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  692 KEANVDAVDTVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHATWLNELVQIALseedcclKDNQ 771
Cdd:PHA02878    26 TENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSIN-------KCSV 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  772 GYT--PLHWACYNGNENCIEVLLeqkcFRKFIGNpftplhcAIINGHESCASLLLGAIDSSIVSC-----------RDDK 838
Cdd:PHA02878    99 FYTlvAIKDAFNNRNVEIFKIIL----TNRYKNI-------QTIDLVYIDKKSKDDIIEAEITKLllsygadinmkDRHK 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  839 GRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGH 918
Cdd:PHA02878   168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHISVGYCK 246

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958801668  919 EKCALLILdkIQDESLINAKNSALQ-TPLHIAARNGLKVVVeeLLAKGACVLAVDENGHTP 978
Cdd:PHA02878   247 DYDILKLL--LEHGVDVNAKSYILGlTALHSSIKSERKLKL--LLEYGADINSLNSYKLTP 303
Ank_4 pfam13637
Ankyrin repeats (many copies);
375-424 3.33e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 3.33e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958801668  375 PLHLAALNAHSDCCRKLLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLL 424
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 208-345 8.38e-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: 59.64  E-value: 8.38e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  208 TPLHAAASNGQINVVKHLL-NLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGAN-VNQPNNS----GFTPLHFAAA 281
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSdlyqGETALHIAVV 98

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801668  282 STHGALcLELLVNNGADVN---------IQSKD-----GKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHV 345
Cdd:cd22192     99 NQNLNL-VRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
Ank_4 pfam13637
Ankyrin repeats (many copies);
438-480 1.25e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 1.25e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1958801668  438 GRTPLHYAAANCHFHCIKALVTTGANINETDNWGRTALHYAAA 480
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAAS 43
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 111-282 1.42e-08

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: 58.74  E-value: 1.42e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  111 VHVAAANKAVKCAEVIIPLLSSVNVSDRG--------------GRTALHHAALNGHMEMVNLLLAKGANINA-----FDK 171
Cdd:cd21882     30 LHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAratgrFFR 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  172 KDRR--------ALHWAAYMGHLDVVALLINHGAE---VTCKDKKGYTPLHAAasngqinvvkhllnlgVEIDEiNVYGN 240
Cdd:cd21882    110 KSPGnlfyfgelPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHAL----------------VLQAD-NTPEN 172

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1958801668  241 TALHIACYNGqdavvneLIDYGANVNQ-------PNNSGFTPLHFAAAS 282
Cdd:cd21882    173 SAFVCQMYNL-------LLSYGAHLDPtqqleeiPNHQGLTPLKLAAVE 214
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 672-978 1.82e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.05  E-value: 1.82e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  672 TPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLEQ--EASILckdsrgrtPLhyaaarghA 749
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNgvDTSIL--------PI--------P 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  750 TWLNELVQIAL-SEEDCCLKDNQGYTPLHWACYNGNENCIEVLLEQKcfrkfignpftplhcaiinghescaslllgaid 828
Cdd:PHA02874   101 CIEKDMIKTILdCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYG--------------------------------- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  829 sSIVSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNT 908
Cdd:PHA02874   148 -ADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG-NHIMNKCKNGFT 225

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958801668  909 PLHLAISKGHEKCALLIldkiqDESLINAKNSALQTPLHIAARNGLKV-VVEELLAKGACVLAVDENGHTP 978
Cdd:PHA02874   226 PLHNAIIHNRSAIELLI-----NNASINDQDIDGSTPLHHAINPPCDIdIIDILLYHKADISIKDNKGENP 291
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 274-443 2.04e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 58.10  E-value: 2.04e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  274 TPLhFAAASTHGALCLE-LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGE-----IDCVDKDGNTPLHVAA 347
Cdd:cd22192     19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  348 RYGHELLINTLITSGADTAK---CGihSMFplhlaALNAHSDCcrkllssgfeidtpdTFGRTCLHAAAAGGNVECIKLL 424
Cdd:cd22192     98 VNQNLNLVRELIARGADVVSpraTG--TFF-----RPGPKNLI---------------YYGEHPLSFAACVGNEEIVRLL 155

                          170
                   ....*....|....*....
gi 1958801668  425 QSSGADFHKKDKCGRTPLH 443
Cdd:cd22192    156 IEHGADIRAQDSLGNTVLH 174
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 49-326 2.30e-08

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 58.38  E-value: 2.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   49 AFLG----DAEIIELLILSGARVNAKDNMWLTPLHRAV--ASRSEEAVQVLIKHSADVNARDKNWQSPVHVAAANKAVKC 122
Cdd:PHA02716   183 AYLGnmyvDIDILEWLCNNGVNVNLQNNHLITPLHTYLitGNVCASVIKKIIELGGDMDMKCVNGMSPIMTYIINIDNIN 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  123 AEVI----------------------IPLLSSVNVS---------------DRGGRTALHHAAL--NGHMEMVNLLLAKG 163
Cdd:PHA02716   263 PEITniyiesldgnkvknipmilhsyITLARNIDISvvysflqpgvklhykDSAGRTCLHQYILrhNISTDIIKLLHEYG 342

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  164 ANINAFDKKDRRALHwaAYMG----------------HLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQ--------- 218
Cdd:PHA02716   343 NDLNEPDNIGNTVLH--TYLSmlsvvnildpetdndiRLDVIQCLISLGADITAVNCLGYTPLTSYICTAQnymyydiid 420

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  219 -------INVVKH--LLNLGVEIDE---------------INVYGNTALHIACYNGQDAVVNELIDYGANVNQPnNSGFT 274
Cdd:PHA02716   421 clisdkvLNMVKHriLQDLLIRVDDtpciihhiiakynipTDLYTDEYEPYDSTKIHDVYHCAIIERYNNAVCE-TSGMT 499

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801668  275 PLHFAAASTHGAL----CLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI 326
Cdd:PHA02716   500 PLHVSIISHTNANivmdSFVYLLSIQYNINIPTKNGVTPLMLTMRNNRLSGHQWYI 555
PHA02946 PHA02946
ankyin-like protein; Provisional
 289-553 2.38e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 57.76  E-value: 2.38e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  289 LELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELL--INTLITSGA--- 363
Cdd:PHA02946    55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAkin 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  364 ---DTAKCGihsmfPLhLAALNAHSDCCRKLLSSGFEIDTPDTFGRTCLHAAAAGGN--VECIKLLQSSGADFHKKDKCG 438
Cdd:PHA02946   135 nsvDEEGCG-----PL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHDG 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  439 RTPLHYAAANCHFHC-IKALVTTGANINETDNWGRTALHYAAASdmdrnkmiLGNAHDNSEELERAREVKGKDAALCLeF 517
Cdd:PHA02946   209 NTPLHIVCSKTVKNVdIINLLLPSTDVNKQNKFGDSPLTLLIKT--------LSPAHLINKLLSTSNVITDQTVNICI-F 279

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1958801668  518 LLQNDANPSIRDK-EGYNSIHY--AAAYGHRQCLELLLE 553
Cdd:PHA02946   280 YDRDDVLEIINDKgKQYDSTDFkmAVEVGSIRCVKYLLD 318
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 591-813 2.85e-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: 57.78  E-value: 2.85e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  591 VDLDIRDEKGRTALYLAAFKG-HTECVEALVNQGASIFVKDNVtkrtpLHASVINGH---TLCLRLLLEIA---DNPEVV 663
Cdd:TIGR00870   43 LNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTL-----LHAISLEYVdavEAILLHLLAAFrksGPLELA 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  664 DVKDA----KGQTPLMLAVAYGHIDAVSLLLEKEANVDAvdTVGCTALHRGIM----------------TGHEECVQMLL 723
Cdd:TIGR00870  118 NDQYTseftPGITALHLAAHRQNYEIVKLLLERGASVPA--RACGDFFVKSQGvdsfyhgesplnaaacLGSPSIVALLS 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  724 EQEASILCKDSRGRTPLHYAAARGHATWLNE-------------LVQIALSEEDCCLKDNQGYTPLHWACYNGNENCIEV 790
Cdd:TIGR00870  196 EDPADILTADSLGNTLLHLLVMENEFKAEYEelscqmynfalslLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRL 275

                          250       260
                   ....*....|....*....|....
gi 1958801668  791 LLEQKCF-RKFIGNPFTPLHCAII 813
Cdd:TIGR00870  276 KLAIKYKqKKFVAWPNGQQLLSLY 299
Ank_4 pfam13637
Ankyrin repeats (many copies);
206-259 3.02e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 3.02e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958801668  206 GYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELI 259
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 12-97 4.45e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 4.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   12 LVQAIFSGDPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQ 91
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165


                   ....*.
gi 1958801668   92 VLIKHS 97
Cdd:PTZ00322   166 LLSRHS 171
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 476-701 5.83e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.19  E-value: 5.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  476 HYAAASDMDRNKMILGNA--HDNSEELERAREVKGKDAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQClellle 553
Cdd:PLN03192   500 HHKELHDLNVGDLLGDNGgeHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDC------ 573

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  554 rtntgfeesdggalksplhlaaynghhqaLEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALvNQGASIfvKDNVT 633
Cdd:PLN03192   574 -----------------------------VLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL-YHFASI--SDPHA 621

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801668  634 KRTPLHASVINGHTLCLRLLLEIADNpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDT 701
Cdd:PLN03192   622 AGDLLCTAAKRNDLTAMKELLKQGLN---VDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANT 686
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 11-171 6.81e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.13  E-value: 6.81e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   11 PLVQAIFSGDPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVA-SRSeeA 89
Cdd:PHA02874   160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIhNRS--A 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   90 VQVLIkHSADVNARDKNWQSPVHVAAankAVKCAEVIIPLL----SSVNVSDRGGRTALHHA-ALNGHMEMVNLLLAKGA 164
Cdd:PHA02874   238 IELLI-NNASINDQDIDGSTPLHHAI---NPPCDIDIIDILlyhkADISIKDNKGENPIDTAfKYINKDPVIKDIIANAV 313


                   ....*..
gi 1958801668  165 NINAFDK 171
Cdd:PHA02874   314 LIKEADK 320
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 853-1042 7.32e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.21  E-value: 7.32e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  853 ECLQLLLRHDAQVNAVDNSGKTALMMAAEN--GQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEK---CALLILD 927
Cdd:PHA03100    87 EIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDlkiLKLLIDK 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  928 K------------IQDESLINAKNSALQTPLHIAARNGLKVVVEELLAKGACVLAVDENGHTPALACAPNKDVAdclalI 995
Cdd:PHA03100   166 GvdinaknrvnylLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKE-----I 240

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1958801668  996 LATMMTFSPSSTMTAVNFVYFRKDNLSRRTLSNMGSRVSLCSNNLDS 1042
Cdd:PHA03100   241 FKLLLNNGPSIKTIIETLLYFKDKDLNTITKIKMLKKSIMYMFLLDP 287
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 411-626 1.17e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 1.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  411 AAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANINETDNWGRTALHYAAASDMDRNKMIL 490
Cdd:PLN03192   531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  491 gnahdnseelerarevkgkdaalclefllqndanpsirdkegynsIHYAAAyghrqclelllertntgfeeSDGGALKSP 570
Cdd:PLN03192   611 ---------------------------------------------YHFASI--------------------SDPHAAGDL 625

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801668  571 LHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASI 626
Cdd:PLN03192   626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 281-350 1.82e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 1.82e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  281 ASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYG 350
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
Ank_4 pfam13637
Ankyrin repeats (many copies);
705-748 1.85e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 1.85e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958801668  705 TALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGH 748
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
PHA03095 PHA03095
ankyrin-like protein; Provisional
 20-168 2.25e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.65  E-value: 2.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   20 DPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGD--AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHS 97
Cdd:PHA03095   201 RARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1958801668   98 ADVNARDKNwqspvhvaaankavkcaeviipllssvnvsdrgGRTALHHAALNGHMEMVNLLLAKGANINA 168
Cdd:PHA03095   281 ADINAVSSD---------------------------------GNTPLSLMVRNNNGRAVRAALAKNPSAET 318
Ank_5 pfam13857
Ankyrin repeats (many copies);
192-246 2.25e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 2.25e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801668  192 LINHG-AEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIA 246
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 325-464 2.34e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.87  E-value: 2.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  325 LIQNGGEIDCVDKDGNtpLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDTF 404
Cdd:PLN03192   513 LGDNGGEHDDPNMASN--LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDAN 590

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  405 GRTCL------------------------HA-------AAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHC 453
Cdd:PLN03192   591 GNTALwnaisakhhkifrilyhfasisdpHAagdllctAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDM 670

                          170
                   ....*....|.
gi 1958801668  454 IKALVTTGANI 464
Cdd:PLN03192   671 VRLLIMNGADV 681
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 209-368 2.66e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 52.51  E-value: 2.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  209 PLHAAASNGQINVVKHLLNLgveIDEINVYGNTALHiACYNGQDAVVNE---LIDYGANVN-QPNNSGFTPLHFAAASTH 284
Cdd:PHA02859    24 PLFYYVEKDDIEGVKKWIKF---VNDCNDLYETPIF-SCLEKDKVNVEIlkfLIENGADVNfKTRDNNLSALHHYLSFNK 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  285 GAL--CLELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLI-NTLI 359
Cdd:PHA02859   100 NVEpeILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKKIfDFLT 179


                   ....*....
gi 1958801668  360 TSGADTAKC 368
Cdd:PHA02859   180 SLGIDINET 188
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 77-250 3.39e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 52.13  E-value: 3.39e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   77 PLHRAVASRSEEAVQVLIKHSADVNardKNWQSPVHVAAANKAV--KCAEVIIPLLSSVNVSDRGGRTALHHAAL----N 150
Cdd:PHA02859    24 PLFYYVEKDDIEGVKKWIKFVNDCN---DLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRDNNLSALHHYLsfnkN 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  151 GHMEMVNLLLAKGANINAFDKKDRRALHwaAYMGH----LDVVALLINHGAEVTCKDKKGYTPLHA-AASNGQINVVKHL 225
Cdd:PHA02859   101 VEPEILKILIDSGSSITEEDEDGKNLLH--MYMCNfnvrINVIKLLIDSGVSFLNKDFDNNNILYSyILFHSDKKIFDFL 178

                          170       180
                   ....*....|....*....|....*
gi 1958801668  226 LNLGVEIDEINVYGNTALHIACYNG 250
Cdd:PHA02859   179 TSLGIDINETNKSGYNCYDLIKFRN 203
Ank_4 pfam13637
Ankyrin repeats (many copies);
42-94 4.21e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 4.21e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958801668   42 RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLI 94
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
239-293 4.29e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 4.29e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958801668  239 GNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGAlCLELLV 293
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
74-160 5.65e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 5.65e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   74 WLTPLHRAVASRSEEAVQVLIKHSADVNARDKNwqspvhvaaankavkcaeviipllssvnvsdrgGRTALHHAALNGHM 153
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN---------------------------------GETALHFAASNGNV 47


                   ....*..
gi 1958801668  154 EMVNLLL 160
Cdd:pfam13637   48 EVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 69-198 7.03e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 7.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   69 AKDNMWLTPLHRAVasrSEEAVQVLIKHSADVNArdknwqspVHVAAANKAVKcAEVIIPLLSSVNVSDRGGRTALHHAA 148
Cdd:PTZ00322    56 ATENKDATPDHNLT---TEEVIDPVVAHMLTVEL--------CQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIAC 123

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958801668  149 LNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAE 198
Cdd:PTZ00322   124 ANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 377-482 8.85e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 8.85e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  377 HLAALNAHSDccrKLLSSGFEIDTPDTFGRTCLHAA-------AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANC 449
Cdd:PTZ00322    50 HLEALEATEN---KDATPDHNLTTEEVIDPVVAHMLtvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANG 126

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1958801668  450 HFHCIKALVTTGANINETDNWGRTALHYAAASD 482
Cdd:PTZ00322   127 HVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 11-171 1.25e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 50.59  E-value: 1.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   11 PLVQAIFSGDPEEIRLLIHKTEDVNALDsekRTPLH--VAAFLGDAEIIELLILSGARVNAK---DNmwLTPLHRAVA-- 83
Cdd:PHA02859    24 PLFYYVEKDDIEGVKKWIKFVNDCNDLY---ETPIFscLEKDKVNVEILKFLIENGADVNFKtrdNN--LSALHHYLSfn 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   84 -SRSEEAVQVLIKHSADVNARDKNWQSPVHVAAANKAVKCAevIIPLLSSVNVS----DRGGRTALH-HAALNGHMEMVN 157
Cdd:PHA02859    99 kNVEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRIN--VIKLLIDSGVSflnkDFDNNNILYsYILFHSDKKIFD 176

                          170
                   ....*....|....
gi 1958801668  158 LLLAKGANINAFDK 171
Cdd:PHA02859   177 FLTSLGIDINETNK 190
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 189-261 1.56e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 1.56e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801668  189 VALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDY 261
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 852-995 1.68e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.53  E-value: 1.68e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  852 AECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKDLNTPLHLA-ISKGHEKCALLILDKIQ 930
Cdd:PHA02875    48 SEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLAtILKKLDIMKLLIARGAD 127

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801668  931 DEslinAKNSALQTPLHIAARNGLKVVVEELLAKGACVLAVDENGHTPALACAPNKDVADCLALI 995
Cdd:PHA02875   128 PD----IPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188
Ank_4 pfam13637
Ankyrin repeats (many copies);
736-792 1.76e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 1.76e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801668  736 GRTPLHYAAARGHatwlNELVQIAL-SEEDCCLKDNQGYTPLHWACYNGNENCIEVLL 792
Cdd:pfam13637    1 ELTALHAAAASGH----LELLRLLLeKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
839-892 2.08e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 2.08e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958801668  839 GRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILV 892
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 391-495 2.13e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.79  E-value: 2.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  391 LLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPL-------HYAAANCHFHC---------- 453
Cdd:PLN03192   544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHHKIFRILYHFasisdphaag 623

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801668  454 --------------IKALVTTGANINETDNWGRTALHYAAASD-MDRNKMILGNAHD 495
Cdd:PLN03192   624 dllctaakrndltaMKELLKQGLNVDSEDHQGATALQVAMAEDhVDMVRLLIMNGAD 680
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 2.34e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 2.34e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958801668   10 PPLVQAIFSGDPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLI 61
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 569-795 3.47e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.03  E-value: 3.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  569 SPLHLAAYNGHHQALEVLLQSLVDLDIRDE--KGRTALY---LAAFKghtecvEALVNQGASIFVKDNVTKRTPLHASVI 643
Cdd:PHA02878    72 TPLHIICKEPNKLGMKEMIRSINKCSVFYTlvAIKDAFNnrnVEIFK------IILTNRYKNIQTIDLVYIDKKSKDDII 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  644 NghTLCLRLLLEIADNPEVVDvkDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLL 723
Cdd:PHA02878   146 E--AEITKLLLSYGADINMKD--RHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL 221

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801668  724 EQEASILCKDSRGRTPLHYAAARghatWLNELVQIALSEEDCCLKDNQ---GYTPLHWACYngNENCIEVLLEQK 795
Cdd:PHA02878   222 ENGASTDARDKCGNTPLHISVGY----CKDYDILKLLLEHGVDVNAKSyilGLTALHSSIK--SERKLKLLLEYG 290
Ank_4 pfam13637
Ankyrin repeats (many copies);
772-824 3.51e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 3.51e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958801668  772 GYTPLHWACYNGNENCIEVLLEQKC-FRKFIGNPFTPLHCAIINGHESCASLLL 824
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGAdINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
308-359 4.75e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 4.75e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958801668  308 SPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLI 359
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 140-168 5.03e-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: 5.03e-06
                            10        20
                    ....*....|....*....|....*....
gi 1958801668   140 GRTALHHAALNGHMEMVNLLLAKGANINA 168
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 635-892 6.13e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.99  E-value: 6.13e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  635 RTPLHASVINGHTLCLRLLLEIADNP--EVVDvkdakGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIM 712
Cdd:PHA02875     3 QVALCDAILFGELDIARRLLDIGINPnfEIYD-----GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  713 TGHEECVQMLLEQEA---SILCKDsrGRTPLHYAAARGHATWLNELVQialSEEDCCLKDNQGYTPLHWACYNGNENCIE 789
Cdd:PHA02875    78 EGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIA---RGADPDIPNTDKFSPLHLAVMMGDIKGIE 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  790 VLLEQK-CFRKFIGNPFTPLHCAIINGH-ESCASLLLGAIDSSIVSCRDDKgrTTLHAAAFGDHAECLQLLLRHDAQVN- 866
Cdd:PHA02875   153 LLIDHKaCLDIEDCCGCTPLIIAMAKGDiAICKMLLDSGANIDYFGKNGCV--AALCYAIENNKIDIVRLFIKRGADCNi 230

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1958801668  867 --AVDNSGKTALMMAAE---NGQAGAVDILV 892
Cdd:PHA02875   231 mfMIEGEECTILDMICNmctNLESEAIDALI 261
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 543-782 6.65e-06

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 50.26  E-value: 6.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  543 GHRQCLELLLertnTGFEESDGGALKSPLHLAAYNGHHQALE---VLLQS---------LVDLDIRDE--KGRTALYLAA 608
Cdd:cd21882      6 GLLECLRWYL----TDSAYQRGATGKTCLHKAALNLNDGVNEaimLLLEAapdsgnpkeLVNAPCTDEfyQGQTALHIAI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  609 FKGHTECVEALVNQGASIFVKDNVT--KRTPlhasvingHTLCLRllleiadnpevvdvkdakGQTPLMLAVAYGHIDAV 686
Cdd:cd21882     82 ENRNLNLVRLLVENGADVSARATGRffRKSP--------GNLFYF------------------GELPLSLAACTNQEEIV 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  687 SLLLE---KEANVDAVDTVGCTALHRGIMTGHEE------CVQM---LLEQEASI-------LCKDSRGRTPLHYAAARG 747
Cdd:cd21882    136 RLLLEngaQPAALEAQDSLGNTVLHALVLQADNTpensafVCQMynlLLSYGAHLdptqqleEIPNHQGLTPLKLAAVEG 215

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1958801668  748 HATWLNELVQIALSEEDCCL--KDNQ-GYTPLHWACYN 782
Cdd:cd21882    216 KIVMFQHILQREFSGPYQPLsrKFTEwTYGPVTSSLYD 253
Ank_5 pfam13857
Ankyrin repeats (many copies);
158-213 7.12e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 7.12e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801668  158 LLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 213
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 836-972 7.78e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.25  E-value: 7.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  836 DDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKDLntpLHLAIS 915
Cdd:PLN03192   555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL---LCTAAK 631

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1958801668  916 KGHekcaLLILDKIQDESL-INAKNSALQTPLHIAARNGLKVVVEELLAKGACVLAVD 972
Cdd:PLN03192   632 RND----LTAMKELLKQGLnVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 43-180 8.25e-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: 8.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   43 TPLHVAAFLGDAEIIELLILSGARVNA-----------KDNMWL---TPLHRAVASRSEEAVQVLIKHSADVNARDKNWQ 108
Cdd:cd22192     91 TALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgPKNLIYygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  109 SPVH--VAAANKAVKCaEVIIPLLSSV---------NVSDRGGRTALHHAALNGHMEMVNLLLAKganinafdkkdRRAL 177
Cdd:cd22192    171 TVLHilVLQPNKTFAC-QMYDLILSYDkeddlqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQK-----------RRHI 238


                   ...
gi 1958801668  178 HWA 180
Cdd:cd22192    239 QWT 241
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 140-282 1.01e-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: 1.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  140 GRTALHHAALN---GHMEMVNLLL---AKGANINAF------DK--KDRRALHWAAYMGHLDVVALLINHGAEVTC---- 201
Cdd:cd22196     47 GKTCLLKAMLNlhnGQNDTISLLLdiaEKTGNLKEFvnaaytDSyyKGQTALHIAIERRNMHLVELLVQNGADVHArasg 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  202 ------KDKKGY----TPLHAAASNGQINVVKHLLN---LGVEIDEINVYGNTALH----IAcYNGQD------AVVNEL 258
Cdd:cd22196    127 effkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLHalveVA-DNTPEntkfvtKMYNEI 205

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1958801668  259 IDYGANVNQ-------PNNSGFTPLHFAAAS 282
Cdd:cd22196    206 LILGAKIRPllkleeiTNKKGLTPLKLAAKT 236
Ank_4 pfam13637
Ankyrin repeats (many copies);
806-859 1.13e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 1.13e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958801668  806 TPLHCAIINGHESCASLLLGAidSSIVSCRDDKGRTTLHAAAFGDHAECLQLLL 859
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEK--GADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 20-210 1.46e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 48.90  E-value: 1.46e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   20 DPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSE--EAVQVLIKHS 97
Cdd:PHA02946    51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEviERINLLVQYG 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668   98 ADV-NARDKNWQSPVhVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAAL--NGHMEMVNLLLAKGANINAFDKKDR 174
Cdd:PHA02946   131 AKInNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMsdNPKASTISWMMKLGISPSKPDHDGN 209

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1958801668  175 RALH--WAAYMGHLDVVALLINhGAEVTCKDKKGYTPL 210
Cdd:PHA02946   210 TPLHivCSKTVKNVDIINLLLP-STDVNKQNKFGDSPL 246
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 140-171 1.47e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 1.47e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1958801668  140 GRTALHHAAL-NGHMEMVNLLLAKGANINAFDK 171
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 720-964 1.65e-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: 48.86  E-value: 1.65e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  720 QMLLEQEasiLCKDSRGR-TPLHYAAARGHATWLNELvqiaLSEEDC--CLKDNQGYTPLHWACYNGNENCIEVLLEqkC 796
Cdd:cd22192      3 QMLDELH---LLQQKRISeSPLLLAAKENDVQAIKKL----LKCPSCdlFQRGALGETALHVAALYDNLEAAVVLME--A 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  797 FRKFIGNPFT--------PLHCAIINGHESCASLLL--GAidsSIVSCRDD-----KGRTTLhaAAFGDHAeclqlllrh 861
Cdd:cd22192     74 APELVNEPMTsdlyqgetALHIAVVNQNLNLVRELIarGA---DVVSPRATgtffrPGPKNL--IYYGEHP--------- 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  862 daqvnavdnsgktaLMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCA------LLILDKIQDE-SL 934
Cdd:cd22192    140 --------------LSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVLHILVLQPNKTFAcqmydlILSYDKEDDLqPL 204

                          250       260       270
                   ....*....|....*....|....*....|
gi 1958801668  935 INAKNSALQTPLHIAARNGLKVVVEELLAK 964
Cdd:cd22192    205 DLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 644-723 1.67e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 1.67e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  644 NGHTLCLRLLLEIADNPevvDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLL 723
Cdd:PTZ00322    92 SGDAVGARILLTGGADP---NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 880-975 1.77e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 1.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  880 AENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDESLINAKNsalQTPLHIAARNGLKVVVE 959
Cdd:PTZ00322    90 AASGDAVGARILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDG---KTPLELAEENGFREVVQ 165

                           90
                   ....*....|....*.
gi 1958801668  960 ELLAKGACVLAVDENG 975
Cdd:PTZ00322   166 LLSRHSQCHFELGANA 181
Ank_5 pfam13857
Ankyrin repeats (many copies);
26-81 1.84e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 1.84e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801668   26 LLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRA 81
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
423-478 1.90e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 1.90e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801668  423 LLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANINETDNWGRTALHYA 478
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 213-350 1.97e-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: 48.60  E-value: 1.97e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  213 AASNGqinVVKHLLNlgVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVN--------QP--NNSGF----TPLHF 278
Cdd:cd22194    120 AEENG---ILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffNPkyKHEGFyfgeTPLAL 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  279 AAASTHGALcLELLVNNGADvNIQSKD--GKSPLHMTAVHGRFTRSQT-----------LIQNGGEIDCV-DKDGNTPLH 344
Cdd:cd22194    195 AACTNQPEI-VQLLMEKEST-DITSQDsrGNTVLHALVTVAEDSKTQNdfvkrmydmilLKSENKNLETIrNNEGLTPLQ 272


                   ....*.
gi 1958801668  345 VAARYG 350
Cdd:cd22194    273 LAAKMG 278
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 822-898 2.01e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 2.01e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801668  822 LLLGAIDSSivsCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQAD 898
Cdd:PTZ00322   101 LLTGGADPN---CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCH 174
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 674-759 2.43e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.33  E-value: 2.43e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  674 LMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHATWLN 753
Cdd:PLN03192   529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608


                   ....*.
gi 1958801668  754 ELVQIA 759
Cdd:PLN03192   609 ILYHFA 614
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 211-314 2.54e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 2.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  211 HAAASNGQINVvKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLE 290
Cdd:PTZ00322    88 QLAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV-VQ 165

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1958801668  291 LLV-------NNGADVNIQSKDGK------SPLHMTA 314
Cdd:PTZ00322   166 LLSrhsqchfELGANAKPDSFTGKppsledSPISSHH 202
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 140-168 3.03e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.86  E-value: 3.03e-05
                           10        20
                   ....*....|....*....|....*....
gi 1958801668  140 GRTALHHAALNGHMEMVNLLLAKGANINA 168
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 651-783 3.18e-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: 47.83  E-value: 3.18e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  651 RLLLEIADNPEVVDV--------KDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDT--------------VGCTALH 708
Cdd:cd22194    114 RILLAFAEENGILDRfinaeyteEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLA 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  709 RGIMTGHEECVQMLLEQEAS-ILCKDSRGRTPLHYAA-----ARGHATWLNELV-QIALSEEDCCL---KDNQGYTPLHW 778
Cdd:cd22194    194 LAACTNQPEIVQLLMEKESTdITSQDSRGNTVLHALVtvaedSKTQNDFVKRMYdMILLKSENKNLetiRNNEGLTPLQL 273


                   ....*
gi 1958801668  779 ACYNG 783
Cdd:cd22194    274 AAKMG 278
Ank_5 pfam13857
Ankyrin repeats (many copies);
236-279 3.49e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.49e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1958801668  236 NVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFA 279
Cdd:pfam13857   13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 874-968 3.50e-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: 47.70  E-value: 3.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  874 TALMMAAENGQAGAVDILVNSAQADLTVKDKDLNTPLHLAISKGHEKCALLILDkiQDESLIN-AKNSAL---QTPLHIA 949
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNePMTSDLyqgETALHIA 96

                           90
                   ....*....|....*....
gi 1958801668  950 ARNGLKVVVEELLAKGACV 968
Cdd:cd22192     97 VVNQNLNLVRELIARGADV 115
Ank_4 pfam13637
Ankyrin repeats (many copies);
600-654 3.81e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 3.81e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1958801668  600 GRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLCLRLLL 654
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
635-690 3.93e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 3.93e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801668  635 RTPLHASVINGHTLCLRLLLEiadNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLL 690
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLE---KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
258-312 3.93e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.93e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801668  258 LIDYG-ANVNQPNNSGFTPLHFAAasTHGAL-CLELLVNNGADVNIQSKDGKSPLHM 312
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAA--KYGALeIVRVLLAYGVDLNLKDEEGLTALDL 55
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 332-476 4.16e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.77  E-value: 4.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  332 IDCVDKDGNTPLHVAARYG-HELLINTLITSGA-----DTAkcgihsmfpLHLAALNAH---SDCCRKLLSSGFEIDTPD 402
Cdd:TIGR00870   45 INCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISLEYVdavEAILLHLLAAFRKSGPLE 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  403 ----------TFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKC--------------GRTPLHYAAANCHFHCIKALV 458
Cdd:TIGR00870  116 landqytsefTPGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLS 195

                          170
                   ....*....|....*...
gi 1958801668  459 TTGANINETDNWGRTALH 476
Cdd:TIGR00870  196 EDPADILTADSLGNTLLH 213
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 844-937 4.23e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 4.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  844 HAAAFGDhAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCAL 923
Cdd:PTZ00322    88 QLAASGD-AVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFREVVQ 165

                           90
                   ....*....|....
gi 1958801668  924 LILDKIQDESLINA 937
Cdd:PTZ00322   166 LLSRHSQCHFELGA 179
PHA02791 PHA02791
ankyrin-like protein; Provisional
 750-945 4.68e-05

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 46.57  E-value: 4.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  750 TWLNELVQIALSEEDCCLKDNQGYTPLHWACYNGNENCIEVLLEQKCFRKFIGNPFtPLH-CAIINGHESCASLLLGAID 828
Cdd:PHA02791     8 TWKSKQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF-PLHqAATLEDTKIVKILLFSGMD 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  829 SSIVscrDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSG-KTALMMAAENGQAGAVDILVNSAQA--DLTVkdkd 905
Cdd:PHA02791    87 DSQF---DDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPStfDLAI---- 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1958801668  906 LNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTP 945
Cdd:PHA02791   160 LLSCIHITIKNGHVDMMILLLDYMTS---TNTNNSLLFIP 196
Ank_5 pfam13857
Ankyrin repeats (many copies);
857-913 4.74e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 4.74e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1958801668  857 LLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLA 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 5.04e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.03  E-value: 5.04e-05
                            10        20
                    ....*....|....*....|....*....
gi 1958801668   238 YGNTALHIACYNGQDAVVNELIDYGANVN 266
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 214-478 5.73e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 47.04  E-value: 5.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  214 ASNGQINVVKHLLNLGVEIDEinVY-GNTAL--HIACYNGQDAVVNELIDYGANVNQpnnSGF--TPL-----HFAAAST 283
Cdd:PHA02989    11 SDTVDKNALEFLLRTGFDVNE--EYrGNSILllYLKRKDVKIKIVKLLIDNGADVNY---KGYieTPLcavlrNREITSN 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  284 HGALCLELLVNNGADVNIQSKDGKSPLhMTAVHG---------RFtrsqtLIQNGGEIDCV-DKDGNTPLHVaarYGHEL 353
Cdd:PHA02989    86 KIKKIVKLLLKFGADINLKTFNGVSPI-VCFIYNsninncdmlRF-----LLSKGINVNDVkNSRGYNLLHM---YLESF 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  354 LINT-----LITSGADT-AKCGIHSMFPLHLAALNAHS----DCCRKLLSSGFEIDTPDTFGRTCLHAAAAGGNV---EC 420
Cdd:PHA02989   157 SVKKdvikiLLSFGVNLfEKTSLYGLTPMNIYLRNDIDvisiKVIKYLIKKGVNIETNNNGSESVLESFLDNNKIlskKE 236

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  421 IKLLQS--SGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANINETDNWGRTALHYA 478
Cdd:PHA02989   237 FKVLNFilKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 236-313 7.59e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 46.13  E-value: 7.59e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  236 NVYGNTALHIACYNGQDAVVNeLIDYGANVNQ-PNNSGFTPLHFAAasTHGAL-CLELLVNNGADVNIQSKDGKSPLHMT 313
Cdd:PHA02884    68 NSKTNPLIYAIDCDNDDAAKL-LIRYGADVNRyAEEAKITPLYISV--LHGCLkCLEILLSYGADINIQTNDMVTPIELA 144
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 310-404 8.66e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 8.66e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  310 LHMTAVH-------GRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALN 382
Cdd:PTZ00322    79 AHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158

                           90       100
                   ....*....|....*....|....*...
gi 1958801668  383 AHSDCCRKLLS---SGFEIDT---PDTF 404
Cdd:PTZ00322   159 GFREVVQLLSRhsqCHFELGAnakPDSF 186
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 140-282 9.29e-05

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 46.33  E-value: 9.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  140 GRTALHHAALNGHMEMVNLLLAKGANINA------FDKKDRRA--------LHWAAYMGHLDVVALLINHG---AEVTCK 202
Cdd:cd22193     76 GQTALHIAIERRQGDIVALLVENGADVHAhakgrfFQPKYQGEgfyfgelpLSLAACTNQPDIVQYLLENEhqpADIEAQ 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  203 DKKGYTPLHAAasngqinvvkhllnlgVEIDEiNVYGNTALHIACYNGqdavvneLIDYGANVNQP-------NNSGFTP 275
Cdd:cd22193    156 DSRGNTVLHAL----------------VTVAD-NTKENTKFVTRMYDM-------ILIRGAKLCPTveleeirNNDGLTP 211


                   ....*..
gi 1958801668  276 LHFAAAS 282
Cdd:cd22193    212 LQLAAKM 218
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 140-280 9.54e-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: 46.29  E-value: 9.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  140 GRTALHHAALNGHMEMVNLLLAKGANINA------FDKKDRR--------ALHWAAYMGHLDVVALLINHGAE-VTCKDK 204
Cdd:cd22194    141 GQTALNIAIERRQGDIVKLLIAKGADVNAhakgvfFNPKYKHegfyfgetPLALAACTNQPEIVQLLMEKESTdITSQDS 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  205 KGYTPLHAAA-----SNGQINVVKHLLnlgveiDEI-NVYGNTALhiacyngqdavvnELIdyganvnqPNNSGFTPLHF 278
Cdd:cd22194    221 RGNTVLHALVtvaedSKTQNDFVKRMY------DMIlLKSENKNL-------------ETI--------RNNEGLTPLQL 273


                   ..
gi 1958801668  279 AA 280
Cdd:cd22194    274 AA 275
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 238-270 1.06e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 1.06e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958801668  238 YGNTALHIACY-NGQDAVVNELIDYGANVNQPNN 270
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
132-180 1.17e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 1.17e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958801668  132 SVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWA 180
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 7-114 1.60e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 1.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668    7 CDQPPLVQAIFSGDPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEI-IELLILSGARVNAKDNMWLTPLHRAVASR 85
Cdd:PHA02876   374 CDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKN 453

                           90       100       110
                   ....*....|....*....|....*....|
gi 1958801668   86 SE-EAVQVLIKHSADVNARDKNWQSPVHVA 114
Cdd:PHA02876   454 CKlDVIEMLLDNGADVNAINIQNQYPLLIA 483
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 672-883 1.62e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.77  E-value: 1.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  672 TPLMLAVAYGHIDAVS-LLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLEqeasilckdsrgrtplhyaAARghat 750
Cdd:cd22192     19 SPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME-------------------AAP---- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  751 wlnELVQIALSEEDcclkdNQGYTPLHWACYNGNENCIEVLLEQ-----------KCFRKFIGNPFT----PLHCAIING 815
Cdd:cd22192     76 ---ELVNEPMTSDL-----YQGETALHIAVVNQNLNLVRELIARgadvvspratgTFFRPGPKNLIYygehPLSFAACVG 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  816 HESCASLLL--GAidsSIVScRDDKGRTTLHAAAFGDHA----ECLQLLLRHDAQVNAV------DNSGKTALMMAAENG 883
Cdd:cd22192    148 NEEIVRLLIehGA---DIRA-QDSLGNTVLHILVLQPNKtfacQMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEG 223
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 438-466 1.74e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 1.74e-04
                            10        20
                    ....*....|....*....|....*....
gi 1958801668   438 GRTPLHYAAANCHFHCIKALVTTGANINE 466
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 606-690 1.80e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 1.80e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  606 LAAfKGHTECVEALVNQGASIFVKDnVTKRTPLHASVINGHTLCLRLLLEIADNPEVVDvKDakGQTPLMLAVAYGHIDA 685
Cdd:PTZ00322    89 LAA-SGDAVGARILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLD-KD--GKTPLELAEENGFREV 163


                   ....*
gi 1958801668  686 VSLLL 690
Cdd:PTZ00322   164 VQLLS 168
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 140-280 1.90e-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: 45.62  E-value: 1.90e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  140 GRTALHHAALNGHMEMVNLLLAKGANINA------FDKKDRRALhwaaYMGHLdvvallinhgaevtckdkkgytPLHAA 213
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGADVHAracgrfFQKKQGTCF----YFGEL----------------------PLSLA 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  214 ASNGQINVVKHLLNLGVE---IDEINVYGNTALHIACYNGQDAVVN---------ELIDYGANVNQ-------PNNSGFT 274
Cdd:cd22197    148 ACTKQWDVVNYLLENPHQpasLQAQDSLGNTVLHALVMIADNSPENsalvikmydGLLQAGARLCPtvqleeiSNHEGLT 227


                   ....*.
gi 1958801668  275 PLHFAA 280
Cdd:cd22197    228 PLKLAA 233
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 405-558 1.95e-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: 45.23  E-value: 1.95e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  405 GRTCLHAAAAGGNVECIKLLQSSGADFH----------KKDKC---GRTPLHYAAANCHFHCIKALVTTG---ANINETD 468
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGADVHaracgrffqkKQGTCfyfGELPLSLAACTKQWDVVNYLLENPhqpASLQAQD 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  469 NWGRTALHYAAasdmdrnkMILGNAHDNSEELERA-REVKGKDAALCLEFLLQndanpSIRDKEGYNSIHYAAAYGHRQC 547
Cdd:cd22197    174 SLGNTVLHALV--------MIADNSPENSALVIKMyDGLLQAGARLCPTVQLE-----EISNHEGLTPLKLAAKEGKIEI 240

                          170
                   ....*....|.
gi 1958801668  548 LELLLERTNTG 558
Cdd:cd22197    241 FRHILQREFSG 251
Ank_4 pfam13637
Ankyrin repeats (many copies);
514-552 2.19e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 2.19e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1958801668  514 CLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLL 552
Cdd:pfam13637   16 LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 438-469 2.29e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 2.29e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1958801668  438 GRTPLHYAAANC-HFHCIKALVTTGANINETDN 469
Cdd:pfam00023    2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 822-985 2.40e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 2.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  822 LLLGAIDssiVSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQadlTV 901
Cdd:PHA02876   164 LLEGGAD---VNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS---NI 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  902 KDKDLNtpLHLAISKGHEKCALLILDKiqdESLINAKNSALQTPLHIAARN-GLKVVVEELLAKGACVLAVDENGHTPAL 980
Cdd:PHA02876   238 NKNDLS--LLKAIRNEDLETSLLLYDA---GFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLY 312


                   ....*
gi 1958801668  981 ACAPN 985
Cdd:PHA02876   313 LMAKN 317
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 205-234 2.42e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 2.42e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1958801668   205 KGYTPLHAAASNGQINVVKHLLNLGVEIDE 234
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 272-304 2.71e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 2.71e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1958801668  272 GFTPLHFAAASTHGALCLELLVNNGADVNIQSK 304
Cdd:pfam00023    2 GNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 843-996 2.98e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.86  E-value: 2.98e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  843 LHAAAFGDhAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCa 922
Cdd:PLN03192   530 LTVASTGN-AALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDANGNTALWNAISAKHHKI- 606

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1958801668  923 LLILDKIQDESLINAKNSALQTplhiAARNGLKVVVEELLAKGACVLAVDENGHTpALACAPNKDVADCLALIL 996
Cdd:PLN03192   607 FRILYHFASISDPHAAGDLLCT----AAKRNDLTAMKELLKQGLNVDSEDHQGAT-ALQVAMAEDHVDMVRLLI 675
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 643-765 3.01e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 3.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  643 INGHTLCLRLLLEIADNP-------EVVDVKDAKgqtplMLAVAYGHIDA------VSLLLEKEANVDAVDTVGCTALHR 709
Cdd:PTZ00322    47 IDTHLEALEATENKDATPdhnltteEVIDPVVAH-----MLTVELCQLAAsgdavgARILLTGGADPNCRDYDGRTPLHI 121

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801668  710 GIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGhatwLNELVQIALSEEDC 765
Cdd:PTZ00322   122 ACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG----FREVVQLLSRHSQC 173
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 376-476 3.09e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 44.87  E-value: 3.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  376 LHLAALNAHS---DCCRKLLSSGFEIDTPDTF-----------GRTCLHAAAAGGNVECIKLLQSSGADFH--------K 433
Cdd:cd21882     30 LHKAALNLNDgvnEAIMLLLEAAPDSGNPKELvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSaratgrffR 109

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1958801668  434 KDKC-----GRTPLHYAAANCHFHCIKALVTTGANI---NETDNWGRTALH 476
Cdd:cd21882    110 KSPGnlfyfGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNTVLH 160
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 201-347 3.30e-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: 44.69  E-value: 3.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  201 CKDKKGYTPL-HAAASNGQINVVKHLLNLGVEIDEinvyGNTALHIACYNGQDAVvNELI----------DYGANVNQPN 269
Cdd:TIGR00870   47 CPDRLGRSALfVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLEYVDAV-EAILlhllaafrksGPLELANDQY 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  270 NSGF----TPLHFAAaSTHGALCLELLVNNGADVNIQSKDG---KSPLHMTAVHGRFTRS-----------QTLIQNGGE 331
Cdd:TIGR00870  122 TSEFtpgiTALHLAA-HRQNYEIVKLLLERGASVPARACGDffvKSQGVDSFYHGESPLNaaaclgspsivALLSEDPAD 200

                          170
                   ....*....|....*.
gi 1958801668  332 IDCVDKDGNTPLHVAA 347
Cdd:TIGR00870  201 ILTADSLGNTLLHLLV 216
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 669-700 3.37e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 3.37e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1958801668  669 KGQTPLMLAVA-YGHIDAVSLLLEKEANVDAVD 700
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 671-894 3.68e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.21  E-value: 3.68e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  671 QTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHAT 750
Cdd:PHA02875     3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  751 WLNELVQIALSEEDCCLKDnqGYTPLHWACYNGNENCIEVLLEQKCFRKFIG-NPFTPLHCAIINGhescaslllgaids 829
Cdd:PHA02875    83 AVEELLDLGKFADDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNtDKFSPLHLAVMMG-------------- 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1958801668  830 sivscrDDKGrttlhaaafgdhaecLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNS 894
Cdd:PHA02875   147 ------DIKG---------------IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDS 190
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 46-117 4.05e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 4.05e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958801668   46 HVAAFlGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQSPVHVAAAN 117
Cdd:PTZ00322    88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
PHA02791 PHA02791
ankyrin-like protein; Provisional
 517-691 4.40e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 43.49  E-value: 4.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  517 FLLQNDANPSirDKEGYNSIHYAAAYGHRQCLELLLertntgfeesDGGALKS------PLHLAAYNGHHQALEVLLQSL 590
Cdd:PHA02791    17 FLSSKDAFKA--DVHGHSALYYAIADNNVRLVCTLL----------NAGALKNllenefPLHQAATLEDTKIVKILLFSG 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  591 VDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNVTKRTPL-HASVINGHTLCLRLLLEIadnPEVVDVkdAK 669
Cdd:PHA02791    85 MDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWKTSFyHAVMLNDVSIVSYFLSEI---PSTFDL--AI 159

                          170       180
                   ....*....|....*....|..
gi 1958801668  670 GQTPLMLAVAYGHIDAVSLLLE 691
Cdd:PHA02791   160 LLSCIHITIKNGHVDMMILLLD 181
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 344-438 4.53e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 4.53e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  344 HVAARyGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGFEIDTPDTFGRTCLHAAAAGGNVECIKL 423
Cdd:PTZ00322    88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                           90
                   ....*....|....*
gi 1958801668  424 LQSSGADFHKKDKCG 438
Cdd:PTZ00322   167 LSRHSQCHFELGANA 181
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 838-953 4.66e-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: 4.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  838 KGRTTLHAAAFGDHAECLQLLLRHDAQVNA---------VDNS-----GKTALMMAAENGQAGAVDILVNSAQADLTVKD 903
Cdd:cd22194    140 EGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQD 219

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958801668  904 KDLNTPLHLAI-----SKGHEKCALLILDKI----QDESLINAKNSALQTPLHIAARNG 953
Cdd:cd22194    220 SRGNTVLHALVtvaedSKTQNDFVKRMYDMIllksENKNLETIRNNEGLTPLQLAAKMG 278
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 629-741 5.64e-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: 44.02  E-value: 5.64e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  629 KDNVTKRTPLHASVIN---GHTLCLRLLLEIAD---------NPEVVDVKdAKGQTPLMLAVAYGHIDAVSLLLEKEANV 696
Cdd:cd22193     24 TESSTGKTCLMKALLNlnpGTNDTIRILLDIAEktdnlkrfiNAEYTDEY-YEGQTALHIAIERRQGDIVALLVENGADV 102

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958801668  697 DAVDT--------------VGCTALHRGIMTGHEECVQMLLE---QEASILCKDSRGRTPLH 741
Cdd:cd22193    103 HAHAKgrffqpkyqgegfyFGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLH 164
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 153-272 6.37e-04

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 41.73  E-value: 6.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  153 MEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVV---ALLINHGAEVTCKDKK-GYTPLHAAASNGQINVVKHLL-N 227
Cdd:PHA02743    37 MEVAPFISGDGHLLHRYDHHGRQCTHMVAWYDRANAVmkiELLVNMGADINARELGtGNTLLHIAASTKNYELAEWLCrQ 116

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1958801668  228 LGVEIDEINVYGNTALHIAcYNGQDAVVNE-LIDYGANVNQPNNSG 272
Cdd:PHA02743   117 LGVNLGAINYQHETAYHIA-YKMRDRRMMEiLRANGAVCDDPLSIG 161
PHA02946 PHA02946
ankyin-like protein; Provisional
 156-345 6.54e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 43.50  E-value: 6.54e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  156 VNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLH-AAASNGQInvvkhllnlgveIDE 234
Cdd:PHA02946    55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYyLSGTDDEV------------IER 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  235 INVygntalhiacyngqdavvneLIDYGANVNQP-NNSGFTPLhfAAASTHGALCLELLVNNGADVNIQSKDGKSPLH-- 311
Cdd:PHA02946   123 INL--------------------LVQYGAKINNSvDEEGCGPL--LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHrh 180

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1958801668  312 MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHV 345
Cdd:PHA02946   181 LMSDNPKASTISWMMKLGISPSKPDHDGNTPLHI 214
Ank_5 pfam13857
Ankyrin repeats (many copies);
688-743 6.74e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 6.74e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801668  688 LLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYA 743
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
274-326 6.94e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 6.94e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958801668  274 TPLHFAAASTHGAlCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI 326
Cdd:pfam13637    3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
907-953 6.94e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 6.94e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1958801668  907 NTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIAARNG 953
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNG 45
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 238-266 7.51e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.01  E-value: 7.51e-04
                           10        20
                   ....*....|....*....|....*....
gi 1958801668  238 YGNTALHIACYNGQDAVVNELIDYGANVN 266
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_4 pfam13637
Ankyrin repeats (many copies);
532-587 1.03e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 1.03e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801668  532 GYNSIHYAAAYGHRQCLELLLERTNTGFEESDGGAlkSPLHLAAYNGHHQALEVLL 587
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE--TALHFAASNGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 205-234 1.18e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.18e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958801668  205 KGYTPLHAAASNGQINVVKHLLNLGVEIDE 234
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
826-879 1.21e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.21e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1958801668  826 AIDSSIVSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMA 879
Cdd:pfam13857    3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 189-318 1.23e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 1.23e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  189 VALLINHGAEVTCKDKKGYTPLHAAASNGQIN-VVKHLLNlgVEIDEINVYGntalhiacyngqDAV-VNELIDYGANVN 266
Cdd:PTZ00322    44 IARIDTHLEALEATENKDATPDHNLTTEEVIDpVVAHMLT--VELCQLAASG------------DAVgARILLTGGADPN 109

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958801668  267 QPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGR 318
Cdd:PTZ00322   110 CRDYDGRTPLHIACANGHVQV-VRVLLEFGADPTLLDKDGKTPLELAEENGF 160
Ank_5 pfam13857
Ankyrin repeats (many copies);
656-708 1.27e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.27e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958801668  656 IADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALH 708
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
397-445 1.30e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 1.30e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1958801668  397 EIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYA 445
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 437-466 1.34e-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: 1.34e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958801668  437 CGRTPLHYAAANCHFHCIKALVTTGANINE 466
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 42-72 1.66e-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: 1.66e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1958801668   42 RTPLHVAA-FLGDAEIIELLILSGARVNAKDN 72
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 669-698 1.99e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 1.99e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958801668  669 KGQTPLMLAVAYGHIDAVSLLLEKEANVDA 698
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 599-631 2.00e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 2.00e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958801668  599 KGRTALYLAAFK-GHTECVEALVNQGASIFVKDN 631
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 771-793 2.00e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 2.00e-03
                            10        20
                    ....*....|....*....|...
gi 1958801668   771 QGYTPLHWACYNGNENCIEVLLE 793
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLD 23
PHA02791 PHA02791
ankyrin-like protein; Provisional
 144-275 2.11e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.18  E-value: 2.11e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  144 LHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGY-TPLHAAASNGQINVV 222
Cdd:PHA02791    65 LHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIV 144

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958801668  223 KHLLNLGVEIDEINVYgNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTP 275
Cdd:PHA02791   145 SYFLSEIPSTFDLAIL-LSCIHITIKNGHVDMMILLLDYMTSTNTNNSLLFIP 196
Ank_5 pfam13857
Ankyrin repeats (many copies);
93-147 2.16e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 2.16e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801668   93 LIKH-SADVNARDKNWQSPVHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHA 147
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 363-554 2.17e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 42.09  E-value: 2.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  363 ADTAK-CGIHSMFPLHlaalNAHSDCCRKLLSSGFEIDTPDTF-----------GRTCLHAAAAGGNVECIKLLQSSGAD 430
Cdd:cd22193     26 SSTGKtCLMKALLNLN----PGTNDTIRILLDIAEKTDNLKRFinaeytdeyyeGQTALHIAIERRQGDIVALLVENGAD 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  431 ---------FHKKDK-----CGRTPLHYAAANCHFHCIKALVT---TGANINETDNWGRTALHYAAasdmdrnkMILGNA 493
Cdd:cd22193    102 vhahakgrfFQPKYQgegfyFGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLHALV--------TVADNT 173

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1958801668  494 HDNSEELERA-REVKGKDAALCLEFLLQndanpSIRDKEGYNSIHYAAAYGHRQCLELLLER 554
Cdd:cd22193    174 KENTKFVTRMyDMILIRGAKLCPTVELE-----EIRNNDGLTPLQLAAKMGKIEILKYILQR 230
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 176-204 2.22e-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: 2.22e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1958801668  176 ALHWAAYM-GHLDVVALLINHGAEVTCKDK 204
Cdd:pfam00023    5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
727-779 2.65e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 2.65e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1958801668  727 ASILCKDSRGRTPLHYAAARGHATWLNELVqiaLSEEDCCLKDNQGYTPLHWA 779
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLL---AYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 405-433 2.74e-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: 2.74e-03
                            10        20
                    ....*....|....*....|....*....
gi 1958801668   405 GRTCLHAAAAGGNVECIKLLQSSGADFHK 433
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 338-364 2.77e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 2.77e-03
                            10        20
                    ....*....|....*....|....*..
gi 1958801668   338 DGNTPLHVAARYGHELLINTLITSGAD 364
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
PHA02795 PHA02795
ankyrin-like protein; Provisional
 124-201 2.94e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 41.52  E-value: 2.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  124 EVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMG--------HLDVVALLINH 195
Cdd:PHA02795   205 KLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHLKILEILLRE 284


                   ....*.
gi 1958801668  196 GAEVTC 201
Cdd:PHA02795   285 PLSIDC 290
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 669-698 3.37e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 3.37e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1958801668   669 KGQTPLMLAVAYGHIDAVSLLLEKEANVDA 698
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 176-201 4.71e-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: 4.71e-03
                            10        20
                    ....*....|....*....|....*.
gi 1958801668   176 ALHWAAYMGHLDVVALLINHGAEVTC 201
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 711-917 4.79e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 41.02  E-value: 4.79e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  711 IMTGHEECVQMLLEQeaSILCKDSRGRTPLHYAAARGHATWLNE---LVQIA--------LSEEDCCLKDNQGYTPLHWA 779
Cdd:cd21882      3 ELLGLLECLRWYLTD--SAYQRGATGKTCLHKAALNLNDGVNEAimlLLEAApdsgnpkeLVNAPCTDEFYQGQTALHIA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  780 CYNGNENCIEVLLEQKC----------FRKFIGNPF----TPLHCAIINGHESCASLLL-GAIDSSIVSCRDDKGRTTLH 844
Cdd:cd21882     81 IENRNLNLVRLLVENGAdvsaratgrfFRKSPGNLFyfgeLPLSLAACTNQEEIVRLLLeNGAQPAALEAQDSLGNTVLH 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1958801668  845 AaafgdhaeclqLLLRHDaqvNAVDNSgKTALMMAAENGQAGAVdiLVNSAQADLTVKDKDLnTPLHLAISKG 917
Cdd:cd21882    161 A-----------LVLQAD---NTPENS-AFVCQMYNLLLSYGAH--LDPTQQLEEIPNHQGL-TPLKLAAVEG 215
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 43-104 5.02e-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: 40.83  E-value: 5.02e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801668   43 TPLHVAAFLGDAEIIELLILSGARVNAKDN--MWLT------------PLHRAVASRSEEAVQVLIKHSADVNARD 104
Cdd:TIGR00870  130 TALHLAAHRQNYEIVKLLLERGASVPARACgdFFVKsqgvdsfyhgesPLNAAACLGSPSIVALLSEDPADILTAD 205
Ank_5 pfam13857
Ankyrin repeats (many copies);
65-114 5.13e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 5.13e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1958801668   65 ARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQSPVHVA 114
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 385-554 5.33e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 40.90  E-value: 5.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  385 SDCCRKLLSSGFEidTPDTFGRTCLHAAAAGGNVECIKLLQSSGAD---------FHKKDK-----CGRTPLHYAAANCH 450
Cdd:cd22194    123 NGILDRFINAEYT--EEAYEGQTALNIAIERRQGDIVKLLIAKGADvnahakgvfFNPKYKhegfyFGETPLALAACTNQ 200

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  451 FHCIKALVTTGA-NINETDNWGRTALH--YAAASDMDRNKMILGNAHDnseelERAREVKGKDaalcLEfllqndanpSI 527
Cdd:cd22194    201 PEIVQLLMEKEStDITSQDSRGNTVLHalVTVAEDSKTQNDFVKRMYD-----MILLKSENKN----LE---------TI 262

                          170       180
                   ....*....|....*....|....*..
gi 1958801668  528 RDKEGYNSIHYAAAYGHRQCLELLLER 554
Cdd:cd22194    263 RNNEGLTPLQLAAKMGKAEILKYILSR 289
Ank_5 pfam13857
Ankyrin repeats (many copies);
291-346 5.95e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 5.95e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1958801668  291 LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVA 346
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 599-628 6.15e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 6.15e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1958801668   599 KGRTALYLAAFKGHTECVEALVNQGASIFV 628
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 838-870 6.50e-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: 35.34  E-value: 6.50e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1958801668  838 KGRTTLHAAA-FGDHAECLQLLLRHDAQVNAVDN 870
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 568-619 6.58e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 6.58e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1958801668  568 KSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEAL 619
Cdd:PTZ00322   116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_5 pfam13857
Ankyrin repeats (many copies);
891-949 6.90e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 6.90e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1958801668  891 LVNSAQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIA 949
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD---LNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 840-997 6.94e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 6.94e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1958801668  840 RTTLHAAAFGDHAECLQLLLRHDAQVNAV-DNSGKTALMMAAENGQAGAVDILVnSAQADLTVKDKDLNTPLHLAISKGH 918
Cdd:PHA02875    69 ESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLI-ARGADPDIPNTDKFSPLHLAVMMGD 147

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1958801668  919 EKCALLILDKiqdESLINAKNSALQTPLHIAARNGLKVVVEELLAKGACVLAVDENGHTPALACAPNKDVADCLALILA 997
Cdd:PHA02875   148 IKGIELLIDH---KACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIK 223
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 405-436 7.39e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 7.39e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1958801668  405 GRTCLHAAAA-GGNVECIKLLQSSGADFHKKDK 436
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 76-105 8.08e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 8.08e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1958801668   76 TPLHRAVASR-SEEAVQVLIKHSADVNARDK 105
Cdd:pfam00023    4 TPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
 
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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