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Conserved domains on  [gi|1046903808|ref|XP_017451840|]
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serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit B isoform X1 [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

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-343 9.99e-51

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.92  E-value: 9.99e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   54 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQSPVHVAAANKAVKCAEVIIPLLSSV 133
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  134 NVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 213
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  214 ASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLELLV 293
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1046903808  294 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 343
Cdd:COG0666    240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
504-767 8.75e-37

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.86  E-value: 8.75e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  504 NKMILGNAHDNSEELERAREVKGKDAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNTGFEESDGG 583
Cdd:COG0666      8 LLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  584 AlkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVING 663
Cdd:COG0666     88 N--TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANG 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  664 HTLCLRLLLEI-ADnpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLE 742
Cdd:COG0666    165 NLEIVKLLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260
                   ....*....|....*....|....*
gi 1046903808  743 QEASILCKDSRGRTPLHYAAARGHA 767
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
668-997 7.17e-32

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 7.17e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  668 LRLLLEIADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLEQEASI 747
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  748 LCKDSRGRTPLHYAAARGHAtwlnELVQIALSE-EDCCLKDNQGYTPLHWACYNGNENCIEVLLEQKcfrkfignpftpl 826
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDL----EIVKLLLEAgADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG------------- 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  827 hcAIINghescaslllgaidssivsCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAV 906
Cdd:COG0666    144 --ADVN-------------------AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  907 DILVNsAQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIAARNGLKVVVEELLAKGACV 986
Cdd:COG0666    203 KLLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278

                          330
                   ....*....|.
gi 1046903808  987 LAVDENGHTPA 997
Cdd:COG0666    279 AAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
253-552 3.63e-30

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.60  E-value: 3.63e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  253 AVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI 332
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  333 DCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSsgqkysivslfsnehvlsA 412
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE------------------A 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  413 GFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANINETDNWGRTA 492
Cdd:COG0666    143 GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTA 222

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  493 LHYAAASDMDRNKMILGNAHDNSEELERAREVKGKDAALCLEFLLQNDANPSIRDKEGYN 552
Cdd:COG0666    223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 2.32e-06

Ankyrin repeats (many copies);


:

Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 2.32e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1046903808   10 PPLVQAIFSGDPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLI 61
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-343 9.99e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.92  E-value: 9.99e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   54 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQSPVHVAAANKAVKCAEVIIPLLSSV 133
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  134 NVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 213
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  214 ASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLELLV 293
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1046903808  294 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 343
Cdd:COG0666    240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 86-359 2.06e-37

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 147.48  E-value: 2.06e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   86 SEEAVQVLIKHSADVNARDKNWQSPVHVAAANKAVKCAEVIIPLLSS---VNVSDRGGRTALHHAALNGH-MEMVNLLLA 161
Cdd:PHA03095    26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAgadVNAPERCGFTPLHLYLYNATtLDVIKLLIK 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  162 KGANINAFDKKDRRALHwaAYMG----HLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINV--VKHLLNLGVEIDEI 235
Cdd:PHA03095   106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  236 NVYGNTALHIACYNGQD--AVVNELIDYGANVNQPNNSGFTPLHFAAA-STHGALCLELLVNNGADVNIQSKDGKSPLHM 312
Cdd:PHA03095   184 DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1046903808  313 TAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLI 359
Cdd:PHA03095   264 AAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
504-767 8.75e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.86  E-value: 8.75e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  504 NKMILGNAHDNSEELERAREVKGKDAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNTGFEESDGG 583
Cdd:COG0666      8 LLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  584 AlkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVING 663
Cdd:COG0666     88 N--TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANG 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  664 HTLCLRLLLEI-ADnpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLE 742
Cdd:COG0666    165 NLEIVKLLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260
                   ....*....|....*....|....*
gi 1046903808  743 QEASILCKDSRGRTPLHYAAARGHA 767
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
668-997 7.17e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 7.17e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  668 LRLLLEIADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLEQEASI 747
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  748 LCKDSRGRTPLHYAAARGHAtwlnELVQIALSE-EDCCLKDNQGYTPLHWACYNGNENCIEVLLEQKcfrkfignpftpl 826
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDL----EIVKLLLEAgADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG------------- 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  827 hcAIINghescaslllgaidssivsCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAV 906
Cdd:COG0666    144 --ADVN-------------------AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  907 DILVNsAQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIAARNGLKVVVEELLAKGACV 986
Cdd:COG0666    203 KLLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278

                          330
                   ....*....|.
gi 1046903808  987 LAVDENGHTPA 997
Cdd:COG0666    279 AAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
253-552 3.63e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.60  E-value: 3.63e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  253 AVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI 332
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  333 DCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSsgqkysivslfsnehvlsA 412
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE------------------A 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  413 GFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANINETDNWGRTA 492
Cdd:COG0666    143 GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTA 222

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  493 LHYAAASDMDRNKMILGNAHDNSEELERAREVKGKDAALCLEFLLQNDANPSIRDKEGYN 552
Cdd:COG0666    223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
PHA03095 PHA03095
ankyrin-like protein; Provisional
 212-493 8.98e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 112.43  E-value: 8.98e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  212 AAASNGQINVVKHLLNLGVEIDEINVYGNTALH--IACYNGQDA-VVNELIDYGANVNQPNNSGFTPLHFAAASTHGALC 288
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  289 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGH---ELLiNTLITSGA 363
Cdd:PHA03095   100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGA 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  364 DTAKCGIHSMFPLHLAALNAHSDccrkllssgqkYSIVslfsnEHVLSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQ 443
Cdd:PHA03095   179 DVYAVDDRFRSLLHHHLQSFKPR-----------ARIV-----RELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLP 242

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903808  444 --SSGADFHKKDKCGRTPLHYAAA--NCHF--HCIKAlvttGANINETDNWGRTAL 493
Cdd:PHA03095   243 llIAGISINARNRYGQTPLHYAAVfnNPRAcrRLIAL----GADINAVSSDGNTPL 294
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-269 3.16e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 3.16e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  177 LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNlGVEIDEINvYGNTALHIACYNGQDAVVN 256
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1046903808  257 ELIDYGANVNQPN 269
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 355-682 6.72e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 97.40  E-value: 6.72e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  355 INTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRkllssgqkysIVSLfsnehVLSAGFEIDTPDTFGRTCLHAAAAGG 434
Cdd:PHA03095    30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKD----------IVRL-----LLEAGADVNAPERCGFTPLHLYLYNA 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  435 NVE-CIKLLQSSGADFHKKDKCGRTPLH-YAA-ANCHFHCIKALVTTGANINETDNWGRTALHyaaasdmdrnkmILGNA 511
Cdd:PHA03095    95 TTLdVIKLLIKAGADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLA------------VLLKS 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  512 HDNSEELerarevkgkdaalcLEFLLQNDANPSIRDKEGYNSIHYAAAYGH--RQCLELLLERTNTGFEESDGGalKSPL 589
Cdd:PHA03095   163 RNANVEL--------------LRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLG--NTPL 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  590 HLAAYNGHHQALEV--LLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLC 667
Cdd:PHA03095   227 HSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNTPLSLMVRNNNGRA 305

                          330
                   ....*....|....*
gi 1046903808  668 LRLLLEIADNPEVVD 682
Cdd:PHA03095   306 VRAALAKNPSAETVA 320
Ank_2 pfam12796
Ankyrin repeats (3 copies);
622-718 2.34e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 2.34e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  622 LYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADnpevVDVKDaKGQTPLMLAVAYGHI 701
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHL 74

                           90
                   ....*....|....*..
gi 1046903808  702 DAVSLLLEKEANVDAVD 718
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 669-1034 2.53e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 89.31  E-value: 2.53e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  669 RLLLEIADnpevVDVKDAKGQTPLMLAVAYGH---IDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEE-CVQMLLEQE 744
Cdd:PHA03095    32 RLLAAGAD----VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  745 ASILCKDSRGRTPLHyAAARGHATwlNELVQIALSEE--DCCLKDNQGYTPLHwaCYNGNENC-IEVLleqkcfrkfign 821
Cdd:PHA03095   108 ADVNAKDKVGRTPLH-VYLSGFNI--NPKVIRLLLRKgaDVNALDLYGMTPLA--VLLKSRNAnVELL------------ 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  822 pftplhcaiinghescaSLLLGAIdsSIVSCRDDKGRTTLH--AAAFGDHAECLQLLLRHDAQVNAVDNSGktalmmaae 899
Cdd:PHA03095   171 -----------------RLLIDAG--ADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLG--------- 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  900 ngqagavdilvnsaqadltvkdkdlNTPLHLAISKGHEKcALLILDKIQDESLINAKNSALQTPLHIAARNGLKVVVEEL 979
Cdd:PHA03095   223 -------------------------NTPLHSMATGSSCK-RSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRL 276

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903808  980 LAKGACVLAVDENGHTP-ALAcapnkdVADCLALILATMMTFSPSSTMTAVNFVYF 1034
Cdd:PHA03095   277 IALGADINAVSSDGNTPlSLM------VRNNNGRAVRAALAKNPSAETVAATLNTA 326
Ank_2 pfam12796
Ankyrin repeats (3 copies);
861-957 9.64e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 9.64e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  861 LHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKdlnTPLHLAISKGHEKCA 940
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77

                           90
                   ....*....|....*..
gi 1046903808  941 LLILDKIQDeslINAKN 957
Cdd:pfam12796   78 KLLLEKGAD---INVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
427-500 9.98e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 9.98e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046903808  427 LHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTgANINETDNwGRTALHYAAASD 500
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSG 72
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 74-281 2.62e-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: 2.62e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   74 WLTPLHRAVASRSEEAVQVLIK-HSADVNARDKNWQSPVHVAAANKAVKCAEVII---PLLssVNV---SD-RGGRTALH 145
Cdd:cd22192     17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaaPEL--VNEpmtSDlYQGETALH 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  146 HAALNGHMEMVNLLLAKGANIN------AFDKKDRRAL-----H---WAAYMGHLDVVALLINHGAEVTCKDKKGYTPLH 211
Cdd:cd22192     95 IAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046903808  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 ...
 556-775 3.56e-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: 3.56e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  556 YAAAYGHRQCLELLLERTNTGFEESdgGAL-KSPLHLAAYNGHHQALEVLLQS---LVDLDIRDE--KGRTALYLAAFKG 629
Cdd:cd22192     23 LAAKENDVQAIKKLLKCPSCDLFQR--GALgETALHVAALYDNLEAAVVLMEAapeLVNEPMTSDlyQGETALHIAVVNQ 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  630 HTECVEALVNQGAsifvkDNVTKRTPLHASVINGHTLCLRllleiadnpevvdvkdakGQTPLMLAVAYGHIDAVSLLLE 709
Cdd:cd22192    101 NLNLVRELIARGA-----DVVSPRATGTFFRPGPKNLIYY------------------GEHPLSFAACVGNEEIVRLLIE 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903808  710 KEANVDAVDTVGCTALHRGIMTGHEECV-QM---LLEQEASI------LCKDSRGRTPLHYAAARGHATWLNELVQ 775
Cdd:cd22192    158 HGADIRAQDSLGNTVLHILVLQPNKTFAcQMydlILSYDKEDdlqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 49-280 3.60e-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: 3.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   49 AFLGDAEIIELLILSGARVNAK-------DNMWLTPLHRAVA-SRSEEAVQVLIKHSADVNARDknwqSPVHVAAANKAV 120
Cdd:TIGR00870   20 AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAISLEYVD 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  121 KCAEVIIPLLSS---------VNVSDRG----GRTALHHAALNGHMEMVNLLLAKGANINA------FDKKDRRA----- 176
Cdd:TIGR00870   96 AVEAILLHLLAAfrksgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDsfyhg 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  177 ---LHWAAYMGHLDVVALLINHGAEVTCKDKKGytplhaaasngqiNVVKHLLNLGVEideiNVYGNTALHIACYngqda 253
Cdd:TIGR00870  176 espLNAAACLGSPSIVALLSEDPADILTADSLG-------------NTLLHLLVMENE----FKAEYEELSCQMY----- 233

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1046903808  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 ...
 340-494 3.06e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 60.80  E-value: 3.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  340 NTPLHVAARYGHELLINTLITS-GADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSgqkysiVSLFSNEHVLSAGFEidt 418
Cdd:cd22192     18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEA------APELVNEPMTSDLYQ--- 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  419 pdtfGRTCLHAAAAGGNVECIKLLQSSGAD----------FHKKDKC----GRTPLHYAAANCHFHCIKALVTTGANINE 484
Cdd:cd22192     89 ----GETALHIAVVNQNLNLVRELIARGADvvspratgtfFRPGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRA 164

                          170
                   ....*....|
gi 1046903808  485 TDNWGRTALH 494
Cdd:cd22192    165 QDSLGNTVLH 174
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 609-831 2.91e-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: 2.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  609 VDLDIRDEKGRTALYLAAFKG-HTECVEALVNQGASIFVKDNVtkrtpLHASVINGH---TLCLRLLLEIA---DNPEVV 681
Cdd:TIGR00870   43 LNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTL-----LHAISLEYVdavEAILLHLLAAFrksGPLELA 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  682 DVKDA----KGQTPLMLAVAYGHIDAVSLLLEKEANVDAvdTVGCTALHRGIM----------------TGHEECVQMLL 741
Cdd:TIGR00870  118 NDQYTseftPGITALHLAAHRQNYEIVKLLLERGASVPA--RACGDFFVKSQGvdsfyhgesplnaaacLGSPSIVALLS 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  742 EQEASILCKDSRGRTPLHYAAARGHATWLNE-------------LVQIALSEEDCCLKDNQGYTPLHWACYNGNENCIEV 808
Cdd:TIGR00870  196 EDPADILTADSLGNTLLHLLVMENEFKAEYEelscqmynfalslLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRL 275

                          250       260
                   ....*....|....*....|....
gi 1046903808  809 LLEQKCF-RKFIGNPFTPLHCAII 831
Cdd:TIGR00870  276 KLAIKYKqKKFVAWPNGQQLLSLY 299
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 2.32e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 2.32e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1046903808   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 5.02e-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: 5.02e-06
                            10        20
                    ....*....|....*....|....*....
gi 1046903808   140 GRTALHHAALNGHMEMVNLLLAKGANINA 168
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 738-982 1.68e-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: 1.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  738 QMLLEQEasiLCKDSRGR-TPLHYAAARGHATWLNELvqiaLSEEDC--CLKDNQGYTPLHWACYNGNENCIEVLLEqkC 814
Cdd:cd22192      3 QMLDELH---LLQQKRISeSPLLLAAKENDVQAIKKL----LKCPSCdlFQRGALGETALHVAALYDNLEAAVVLME--A 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  815 FRKFIGNPFT--------PLHCAIINGHESCASLLL--GAidsSIVSCRDD-----KGRTTLhaAAFGDHAeclqlllrh 879
Cdd:cd22192     74 APELVNEPMTsdlyqgetALHIAVVNQNLNLVRELIarGA---DVVSPRATgtffrPGPKNL--IYYGEHP--------- 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  880 daqvnavdnsgktaLMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCA------LLILDKIQDE-SL 952
Cdd:cd22192    140 --------------LSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVLHILVLQPNKTFAcqmydlILSYDKEDDLqPL 204

                          250       260       270
                   ....*....|....*....|....*....|
gi 1046903808  953 INAKNSALQTPLHIAARNGLKVVVEELLAK 982
Cdd:cd22192    205 DLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 456-484 1.71e-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: 1.71e-04
                            10        20
                    ....*....|....*....|....*....
gi 1046903808   456 GRTPLHYAAANCHFHCIKALVTTGANINE 484
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 332-494 2.65e-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: 45.07  E-value: 2.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  332 IDCVDKDGNTPLHVAARYG-HELLINTLITSGA-----DTAkcgihsmfpLHLAALNAH---SDCCRKLLSSGQKYSIVS 402
Cdd:TIGR00870   45 INCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISLEYVdavEAILLHLLAAFRKSGPLE 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  403 LfsnehvlsaGFEIDTPD-TFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKC--------------GRTPLHYAAANC 467
Cdd:TIGR00870  116 L---------ANDQYTSEfTPGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLG 186

                          170       180
                   ....*....|....*....|....*..
gi 1046903808  468 HFHCIKALVTTGANINETDNWGRTALH 494
Cdd:TIGR00870  187 SPSIVALLSEDPADILTADSLGNTLLH 213
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 789-811 2.02e-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: 2.02e-03
                            10        20
                    ....*....|....*....|...
gi 1046903808   789 QGYTPLHWACYNGNENCIEVLLE 811
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLD 23
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 687-716 3.40e-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: 3.40e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1046903808   687 KGQTPLMLAVAYGHIDAVSLLLEKEANVDA 716
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-343 9.99e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.92  E-value: 9.99e-51
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   54 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQSPVHVAAANKAVKCAEVIIPLLSSV 133
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  134 NVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 213
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  214 ASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLELLV 293
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1046903808  294 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 343
Cdd:COG0666    240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-307 7.84e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 172.45  E-value: 7.84e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   22 EEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVN 101
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  102 ARDKNWQSPVHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAA 181
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  182 YMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDY 261
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1046903808  262 GANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGK 307
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
11-276 1.11e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 172.06  E-value: 1.11e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   11 PLVQAIFSGDPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAV 90
Cdd:COG0666     24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   91 QVLIKHSADVNARDKNWQSPVHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFD 170
Cdd:COG0666    104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  171 KKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNG 250
Cdd:COG0666    184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263

                          250       260
                   ....*....|....*....|....*.
gi 1046903808  251 QDAVVNELIDYGANVNQPNNSGFTPL 276
Cdd:COG0666    264 AALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-243 2.24e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.04  E-value: 2.24e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808    8 DQPPLVQAIFSGDPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSE 87
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   88 EAVQVLIKHSADVNARDKNwqspvhvaaankavkcaeviipllssvnvsdrgGRTALHHAALNGHMEMVNLLLAKGANIN 167
Cdd:COG0666    167 EIVKLLLEAGADVNARDND---------------------------------GETPLHLAAENGHLEIVKLLLEAGADVN 213

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903808  168 AFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTAL 243
Cdd:COG0666    214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 86-359 2.06e-37

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 147.48  E-value: 2.06e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   86 SEEAVQVLIKHSADVNARDKNWQSPVHVAAANKAVKCAEVIIPLLSS---VNVSDRGGRTALHHAALNGH-MEMVNLLLA 161
Cdd:PHA03095    26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAgadVNAPERCGFTPLHLYLYNATtLDVIKLLIK 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  162 KGANINAFDKKDRRALHwaAYMG----HLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINV--VKHLLNLGVEIDEI 235
Cdd:PHA03095   106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  236 NVYGNTALHIACYNGQD--AVVNELIDYGANVNQPNNSGFTPLHFAAA-STHGALCLELLVNNGADVNIQSKDGKSPLHM 312
Cdd:PHA03095   184 DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1046903808  313 TAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLI 359
Cdd:PHA03095   264 AAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA03095 PHA03095
ankyrin-like protein; Provisional
 22-310 4.90e-37

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 146.32  E-value: 4.90e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   22 EEIRLLIHKTEDVNALDSEKRTPLHVaaFLG-----DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAV-QVLIK 95
Cdd:PHA03095    28 EEVRRLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDViKLLIK 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   96 HSADVNARDKNWQSPVHVAAANKAVkcaeviipllssvnvsdrggrtalhhaalngHMEMVNLLLAKGANINAFDKKDRR 175
Cdd:PHA03095   106 AGADVNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMT 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  176 ALHwaAYMGH----LDVVALLINHGAEVTCKDKKGYTPLHAAASNGQIN--VVKHLLNLGVEIDEINVYGNTALHIACYN 249
Cdd:PHA03095   155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046903808  250 G--QDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLvNNGADVNIQSKDGKSPL 310
Cdd:PHA03095   233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGNTPL 294
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
504-767 8.75e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.86  E-value: 8.75e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  504 NKMILGNAHDNSEELERAREVKGKDAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNTGFEESDGG 583
Cdd:COG0666      8 LLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  584 AlkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVING 663
Cdd:COG0666     88 N--TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANG 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  664 HTLCLRLLLEI-ADnpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLE 742
Cdd:COG0666    165 NLEIVKLLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260
                   ....*....|....*....|....*
gi 1046903808  743 QEASILCKDSRGRTPLHYAAARGHA 767
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
154-523 4.36e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.55  E-value: 4.36e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  154 EMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEID 233
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  234 EINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQskdgksplhmt 313
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI-VKLLLEAGADVNAQ----------- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  314 avhgrftrsqtliqnggeidcvDKDGNTPLHVAARYGHELLINTLITSGADtakcgihsmfplhlaalnahsdccrklls 393
Cdd:COG0666    150 ----------------------DNDGNTPLHLAAANGNLEIVKLLLEAGAD----------------------------- 178

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  394 sgqkysivslfsnehvlsagfeIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIK 473
Cdd:COG0666    179 ----------------------VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|
gi 1046903808  474 ALVTTGANINETDNWGRTALHYAAASDMDRNKMILGNAHDNSEELERARE 523
Cdd:COG0666    237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
533-813 8.12e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.78  E-value: 8.12e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  533 LEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNTGFEESDGGALKSPLHLAAYNGHHQALEVLLQSLVDLD 612
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  613 IRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEI-ADnpevVDVKDAKGQTP 691
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAgAD----VNAQDNDGNTP 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  692 LMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHATWLN 771
Cdd:COG0666    157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1046903808  772 ELVQIALSEEDcclKDNQGYTPLHWACYNGNENCIEVLLEQK 813
Cdd:COG0666    237 LLLEAGADLNA---KDKDGLTALLLAAAAGAALIVKLLLLAL 275
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 55-301 2.49e-35

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 140.19  E-value: 2.49e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   55 EIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQSPVHVAAANKAV-----KCAEVIIPL 129
Cdd:PHA03100    16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEY 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  130 LSSVNVSDRGGRTALHHAALN--GHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGH--LDVVALLINHGAEVTCKDKk 205
Cdd:PHA03100    96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNR- 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  206 gytplhaaasngqinvVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHG 285
Cdd:PHA03100   175 ----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238

                          250
                   ....*....|....*.
gi 1046903808  286 ALcLELLVNNGADVNI 301
Cdd:PHA03100   239 EI-FKLLLNNGPSIKT 253
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 23-266 1.61e-33

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 134.79  E-value: 1.61e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   23 EIRLLIHKTEDVN-ALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLH-----RAVASRSEEAVQVLIKH 96
Cdd:PHA03100    16 KNIKYIIMEDDLNdYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEY 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   97 SADVNARDKNWQSPVHVAAANKavKCAEVIIPLLSS----VNVSDRGGRTALHHAALNGH--MEMVNLLLAKGANINAfd 170
Cdd:PHA03100    96 GANVNAPDNNGITPLLYAISKK--SNSYSIVEYLLDnganVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINA-- 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  171 kKDRralhwaaymghldvVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNG 250
Cdd:PHA03100   172 -KNR--------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNN 236

                          250
                   ....*....|....*.
gi 1046903808  251 QDAVVNELIDYGANVN 266
Cdd:PHA03100   237 NKEIFKLLLNNGPSIK 252
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 26-364 3.65e-33

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 137.50  E-value: 3.65e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   26 LLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDK 105
Cdd:PHA02876   163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDL 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  106 NWQSpvhvAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHM-EMVNLLLAKGANINAFDKKDRRALHWAAYMG 184
Cdd:PHA02876   243 SLLK----AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNG 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  185 H-LDVVALLINHGAEVTCKDKKGYTPLHAAAS-NGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYG 262
Cdd:PHA02876   319 YdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  263 ANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHG-RFTRSQTLIQNGGEIDCVDKDGNT 341
Cdd:PHA02876   399 ADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQY 478

                          330       340
                   ....*....|....*....|...
gi 1046903808  342 PLHVAarYGHELLINTLITSGAD 364
Cdd:PHA02876   479 PLLIA--LEYHGIVNILLHYGAE 499
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 16-367 6.56e-33

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 133.17  E-value: 6.56e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   16 IFSGDPEEIRLLI-HKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLI 94
Cdd:PHA02874     9 IYSGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   95 KHSADVNArdknwqspvhvaaankavkcaeVIIPLLSSvnvsdrggrtalhhaalnghmEMVNLLLAKGANINAFDKKDR 174
Cdd:PHA02874    89 DNGVDTSI----------------------LPIPCIEK---------------------DMIKTILDCGIDVNIKDAELK 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  175 RALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAV 254
Cdd:PHA02874   126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  255 VNELIDYGANVNQPNNSGFTPLHfaAASTHGALCLELLVNNgADVNIQSKDGKSPLHMtAVHGRFTRS--QTLIQNGGEI 332
Cdd:PHA02874   206 IKLLIDHGNHIMNKCKNGFTPLH--NAIIHNRSAIELLINN-ASINDQDIDGSTPLHH-AINPPCDIDiiDILLYHKADI 281

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1046903808  333 DCVDKDGNTPLHVAARYGH------ELLINTLITSGADTAK 367
Cdd:PHA02874   282 SIKDNKGENPIDTAFKYINkdpvikDIIANAVLIKEADKLK 322
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
668-997 7.17e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 7.17e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  668 LRLLLEIADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLEQEASI 747
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  748 LCKDSRGRTPLHYAAARGHAtwlnELVQIALSE-EDCCLKDNQGYTPLHWACYNGNENCIEVLLEQKcfrkfignpftpl 826
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDL----EIVKLLLEAgADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG------------- 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  827 hcAIINghescaslllgaidssivsCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAV 906
Cdd:COG0666    144 --ADVN-------------------AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  907 DILVNsAQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIAARNGLKVVVEELLAKGACV 986
Cdd:COG0666    203 KLLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278

                          330
                   ....*....|.
gi 1046903808  987 LAVDENGHTPA 997
Cdd:COG0666    279 AAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 56-385 2.32e-31

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 131.72  E-value: 2.32e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   56 IIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQSPVHVAAANKAVKCAEVIIPLLSSVNV 135
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  136 SDrggrTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLD-VVALLINHGAEVTCKDKKGYTPLHAAA 214
Cdd:PHA02876   240 ND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMA 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  215 SNG-QINVVKHLLNLGVEIDEINVYGNTALHIACY--NGQDAVVNeLIDYGANVNQPNNSGFTPLHFAAAStHGALCLEL 291
Cdd:PHA02876   316 KNGyDTENIRTLIMLGADVNAADRLYITPLHQASTldRNKDIVIT-LLELGANVNARDYCDKTPIHYAAVR-NNVVIINT 393

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  292 LVNNGADVNIQSKDGKSPLHMtAVHGR--FTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHEL-LINTLITSGADTAKC 368
Cdd:PHA02876   394 LLDYGADIEALSQKIGTALHF-ALCGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAI 472

                          330
                   ....*....|....*..
gi 1046903808  369 GIHSMFPLhLAALNAHS 385
Cdd:PHA02876   473 NIQNQYPL-LIALEYHG 488
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
289-622 2.97e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.68  E-value: 2.97e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  289 LELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKC 368
Cdd:COG0666      4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  369 GIHSMFPLHLAALNAHSDCCRKLLSsgqkysivslfsnehvlsAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGAD 448
Cdd:COG0666     84 DDGGNTLLHAAARNGDLEIVKLLLE------------------AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  449 FHKKDKCGRTPLHYAAANCHFHCIKALVTTGANINETDNWGRTALHYAAASdmdrnkmilgnahdNSEELerarevkgkd 528
Cdd:COG0666    146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN--------------GHLEI---------- 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  529 aalcLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNTGFEESDGGalKSPLHLAAYNGHHQALEVLLQSL 608
Cdd:COG0666    202 ----VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG--LTALLLAAAAGAALIVKLLLLAL 275

                          330
                   ....*....|....
gi 1046903808  609 VDLDIRDEKGRTAL 622
Cdd:COG0666    276 LLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 186-496 4.34e-31

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 128.22  E-value: 4.34e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  186 LDVVALLINHGAEVTCKDKKGYTPLHAAASNGQIN---VVKHLLNLGVEIDEINVYGNTALHI-ACYNGQDAVVNELIDY 261
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKA 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  262 GANVNQPNNSGFTPLH--FAAASTHgALCLELLVNNGADVNIQSKDGKSPLHMtavhgrFTRS--------QTLIQNGGE 331
Cdd:PHA03095   107 GADVNAKDKVGRTPLHvyLSGFNIN-PKVIRLLLRKGADVNALDLYGMTPLAV------LLKSrnanvellRLLIDAGAD 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  332 IDCVDKDGNTPLHVAARYGH--ELLINTLITSGADTAKCGIHSMFPLHLAAlnAHSDCCRkllssgqkySIVSLFsnehv 409
Cdd:PHA03095   180 VYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNTPLHSMA--TGSSCKR---------SLVLPL----- 243

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  410 LSAGFEIDTPDTFGRTCLHAAAAGGN-VECIKLLQSsGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANINETDNw 488
Cdd:PHA03095   244 LIAGISINARNRYGQTPLHYAAVFNNpRACRRLIAL-GADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA- 321


                   ....*...
gi 1046903808  489 grtALHYA 496
Cdd:PHA03095   322 ---TLNTA 326
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
480-758 1.14e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.76  E-value: 1.14e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  480 ANINETDNWGRTALHYAAASDMDRNKMILGNAHDNSEELERAREVKGKDAALcLEFLLQNDANPSIRDKEGYNSIHYAAA 559
Cdd:COG0666     18 LLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLV-ALLLLAAGADINAKDDGGNTLLHAAAR 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  560 YGHRQCLELLLER-TNTGFEESDGGalkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALV 638
Cdd:COG0666     97 NGDLEIVKLLLEAgADVNARDKDGE---TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  639 NQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLE-IADnpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAV 717
Cdd:COG0666    174 EAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEaGAD----VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1046903808  718 DTVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPL 758
Cdd:COG0666    249 DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
253-552 3.63e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.60  E-value: 3.63e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  253 AVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI 332
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  333 DCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSsgqkysivslfsnehvlsA 412
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE------------------A 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  413 GFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANINETDNWGRTA 492
Cdd:COG0666    143 GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTA 222

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  493 LHYAAASDMDRNKMILGNAHDNSEELERAREVKGKDAALCLEFLLQNDANPSIRDKEGYN 552
Cdd:COG0666    223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
770-1015 6.67e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.83  E-value: 6.67e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  770 LNELVQIALSEEDCCLKDNQGYTPLHWACYNGNENCIEVLLEQKCFR-KFIGNPFTPLHCAIINGHESCASLLLGAIDSs 848
Cdd:COG0666     34 LLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADInAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD- 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  849 iVSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPL 928
Cdd:COG0666    113 -VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPL 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  929 HLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIAARNGLKVVVEELLAKGACVLAVDENGHTPALACAPNKDVAD 1008
Cdd:COG0666    191 HLAAENGHLEIVKLLLEAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALI 267


                   ....*..
gi 1046903808 1009 CLALILA 1015
Cdd:COG0666    268 VKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
770-1015 2.39e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.90  E-value: 2.39e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  770 LNELVQIALSEEDCCLKDNQGYTPLHWACYNGNENCIEVLLEQKCFRKFIGNPFTPLHCAIINGHESCASLLLGAIDSSI 849
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  850 VScRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLH 929
Cdd:COG0666     81 NA-KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE-AGADVNAQDNDGNTPLH 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  930 LAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIAARNGLKVVVEELLAKGACVLAVDENGHTPALACAPNKDVADC 1009
Cdd:COG0666    159 LAAANGNLEIVKLLLEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235


                   ....*.
gi 1046903808 1010 LALILA 1015
Cdd:COG0666    236 KLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
410-687 6.73e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.75  E-value: 6.73e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  410 LSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANINETDNWG 489
Cdd:COG0666     41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  490 RTALHYAAASdmdrnkmilgnahdNSEELerarevkgkdaalcLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELL 569
Cdd:COG0666    121 ETPLHLAAYN--------------GNLEI--------------VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  570 LER-TNTGFEESDGGalkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKD 648
Cdd:COG0666    173 LEAgADVNARDNDGE---TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1046903808  649 NVTKRTPLHASVINGHTLCLRLLLEIADNPEVVDVKDAK 687
Cdd:COG0666    250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 123-483 1.00e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 120.55  E-value: 1.00e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  123 AEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCK 202
Cdd:PHA02876   161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKN 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  203 DkkgyTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQ-DAVVNELIDYGANVNQPNNSGFTPLHFAAA 281
Cdd:PHA02876   241 D----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAK 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  282 STHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQ-TLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLIT 360
Cdd:PHA02876   317 NGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIViTLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  361 SGADtakcgihsmfplhLAALNahsdccrkllssgQKYSivslfsnehvlsagfeidtpdtfgrTCLHAAAAGGN-VECI 439
Cdd:PHA02876   397 YGAD-------------IEALS-------------QKIG-------------------------TALHFALCGTNpYMSV 425

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1046903808  440 KLLQSSGADFHKKDKCGRTPLHYAAA-NCHFHCIKALVTTGANIN 483
Cdd:PHA02876   426 KTLIDRGANVNSKNKDLSTPLHYACKkNCKLDVIEMLLDNGADVN 470
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 12-265 3.79e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 118.63  E-value: 3.79e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   12 LVQAIFSGDPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGD-AEIIELLILSGARVNAKDNMWLTPLH-RAVASRSEEA 89
Cdd:PHA02876   244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYlMAKNGYDTEN 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   90 VQVLIKHSADVNARDKNWQSPVHVAAANKAVKcaEVIIPLL---SSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANI 166
Cdd:PHA02876   324 IRTLIMLGADVNAADRLYITPLHQASTLDRNK--DIVITLLelgANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  167 NAFDKKDRRALHWAAY-MGHLDVVALLINHGAEVTCKDKKGYTPLH-AAASNGQINVVKHLLNLGVEIDEINVYGNTALH 244
Cdd:PHA02876   402 EALSQKIGTALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHyACKKNCKLDVIEMLLDNGADVNAINIQNQYPLL 481

                          250       260
                   ....*....|....*....|.
gi 1046903808  245 IACynGQDAVVNELIDYGANV 265
Cdd:PHA02876   482 IAL--EYHGIVNILLHYGAEL 500
PHA03095 PHA03095
ankyrin-like protein; Provisional
 212-493 8.98e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 112.43  E-value: 8.98e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  212 AAASNGQINVVKHLLNLGVEIDEINVYGNTALH--IACYNGQDA-VVNELIDYGANVNQPNNSGFTPLHFAAASTHGALC 288
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  289 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGH---ELLiNTLITSGA 363
Cdd:PHA03095   100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGA 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  364 DTAKCGIHSMFPLHLAALNAHSDccrkllssgqkYSIVslfsnEHVLSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQ 443
Cdd:PHA03095   179 DVYAVDDRFRSLLHHHLQSFKPR-----------ARIV-----RELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLP 242

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903808  444 --SSGADFHKKDKCGRTPLHYAAA--NCHF--HCIKAlvttGANINETDNWGRTAL 493
Cdd:PHA03095   243 llIAGISINARNRYGQTPLHYAAVfnNPRAcrRLIAL----GADINAVSSDGNTPL 294
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 11-310 1.57e-25

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 113.62  E-value: 1.57e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   11 PLVQAIFSGDPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDnmwlTPLHRAVASRSEEAV 90
Cdd:PHA02876   181 PIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND----LSLLKAIRNEDLETS 256

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   91 QVLIKHSADVNARDKNWQSPVHVAAanKAVKCAEVIIPLL---SSVNVSDRGGRTALHHAALNGH-MEMVNLLLAKGANI 166
Cdd:PHA02876   257 LLLYDAGFSVNSIDDCKNTPLHHAS--QAPSLSRLVPKLLergADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADV 334

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  167 NAFDKKDRRALHWAAYMG-HLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHI 245
Cdd:PHA02876   335 NAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHF 414

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903808  246 ACYNGQDAV-VNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPL 310
Cdd:PHA02876   415 ALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIEMLLDNGADVNAINIQNQYPL 480
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 75-346 4.84e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 109.97  E-value: 4.84e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   75 LTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQSPVHVA--AANKavkcaEVIIPLLSSVNVSDRG-GRTALHHAALNG 151
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckEPNK-----LGMKEMIRSINKCSVFyTLVAIKDAFNNR 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  152 HMEMVNLLLakganINAFDKK---DRRALHWAAYMGHLD--VVALLINHGAEVTCKDK-KGYTPLHAAASNGQINVVKHL 225
Cdd:PHA02878   113 NVEIFKIIL-----TNRYKNIqtiDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELL 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  226 LNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSK- 304
Cdd:PHA02878   188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYi 267

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1046903808  305 DGKSPLHMTAVHGRFTRsqTLIQNGGEIDCVDKDGNTPLHVA 346
Cdd:PHA02878   268 LGLTALHSSIKSERKLK--LLLEYGADINSLNSYKLTPLSSA 307
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 22-295 1.49e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 102.65  E-value: 1.49e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   22 EEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIK------ 95
Cdd:PHA02878    18 KYIEYIDHTENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcs 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   96 ------------HSADV--------NARDKNWQSP-VHVAAANKAVKCAEVIIPLL----SSVNVSDR-GGRTALHHAAL 149
Cdd:PHA02878    98 vfytlvaikdafNNRNVeifkiiltNRYKNIQTIDlVYIDKKSKDDIIEAEITKLLlsygADINMKDRhKGNTALHYATE 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  150 NGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASN-GQINVVKHLLNL 228
Cdd:PHA02878   178 NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEH 257

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046903808  229 GVEID-EINVYGNTALHIACYNGQdaVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNN 295
Cdd:PHA02878   258 GVDVNaKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISN 323
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 192-548 7.38e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 99.74  E-value: 7.38e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  192 LINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIAC---YNGQDAV--VNELIDYGANVN 266
Cdd:PHA03100    21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikYNLTDVKeiVKLLLEYGANVN 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  267 QPNNSGFTPLHFAAASTHGALCL-ELLVNNGADVNIQSKDGKSPLHMtavhgrFTRSqtliqnggeiDCVDKDgntplhv 345
Cdd:PHA03100   101 APDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHL------YLES----------NKIDLK------- 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  346 aaryghelLINTLITSGADtakcgihsmfplhlaaLNAhsdCCRkllssgqkysivslfsnehvlsagfeidtpdtfgrt 425
Cdd:PHA03100   158 --------ILKLLIDKGVD----------------INA---KNR------------------------------------ 174

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  426 clhaaaaggnvecIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANINETDNWGRTALHYAAASdmdRNK 505
Cdd:PHA03100   175 -------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILN---NNK 238

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|...
gi 1046903808  506 MILgnahdnSEELERAREVKGKDAALclefLLQNDANPSIRDK 548
Cdd:PHA03100   239 EIF------KLLLNNGPSIKTIIETL----LYFKDKDLNTITK 271
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 323-625 2.03e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 98.50  E-value: 2.03e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  323 QTLIQNGGE-IDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGQKYSIV 401
Cdd:PHA02874    18 EKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  402 SL--FSNEHV---LSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALV 476
Cdd:PHA02874    98 PIpcIEKDMIktiLDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  477 TTGANINETDNWGRTALHYAaasdmdrnkmilgnahdnseelerareVKGKDAAlCLEFLLQNDANPSIRDKEGYNSIHY 556
Cdd:PHA02874   178 EKGAYANVKDNNGESPLHNA---------------------------AEYGDYA-CIKLLIDHGNHIMNKCKNGFTPLHN 229

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  557 AAAYgHRQCLELLLERTNTGFEESDGgalKSPLHLA-AYNGHHQALEVLLQSLVDLDIRDEKGRTALYLA 625
Cdd:PHA02874   230 AIIH-NRSAIELLINNASINDQDIDG---STPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-269 3.16e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 3.16e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  177 LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNlGVEIDEINvYGNTALHIACYNGQDAVVN 256
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1046903808  257 ELIDYGANVNQPN 269
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 355-682 6.72e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 97.40  E-value: 6.72e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  355 INTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRkllssgqkysIVSLfsnehVLSAGFEIDTPDTFGRTCLHAAAAGG 434
Cdd:PHA03095    30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKD----------IVRL-----LLEAGADVNAPERCGFTPLHLYLYNA 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  435 NVE-CIKLLQSSGADFHKKDKCGRTPLH-YAA-ANCHFHCIKALVTTGANINETDNWGRTALHyaaasdmdrnkmILGNA 511
Cdd:PHA03095    95 TTLdVIKLLIKAGADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLA------------VLLKS 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  512 HDNSEELerarevkgkdaalcLEFLLQNDANPSIRDKEGYNSIHYAAAYGH--RQCLELLLERTNTGFEESDGGalKSPL 589
Cdd:PHA03095   163 RNANVEL--------------LRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLG--NTPL 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  590 HLAAYNGHHQALEV--LLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLC 667
Cdd:PHA03095   227 HSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNTPLSLMVRNNNGRA 305

                          330
                   ....*....|....*
gi 1046903808  668 LRLLLEIADNPEVVD 682
Cdd:PHA03095   306 VRAALAKNPSAETVA 320
Ank_2 pfam12796
Ankyrin repeats (3 copies);
144-236 8.95e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 8.95e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  144 LHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHgAEVTCKDkKGYTPLHAAASNGQINVVK 223
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1046903808  224 HLLNLGVEIDEIN 236
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 24-235 2.36e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 95.48  E-value: 2.36e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   24 IRLLIHKTEDVNALDSEKRTPLHV--AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASR--SEEAVQVLIKHSAD 99
Cdd:PHA03095   100 IKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGAD 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  100 VNARDKNWQSPVHVAAAN--KAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNL--LLAKGANINAFDKKDRR 175
Cdd:PHA03095   180 VYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQT 259

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  176 ALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEI 235
Cdd:PHA03095   260 PLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 182-714 6.10e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 95.52  E-value: 6.10e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  182 YMGHLDVVALLIN-----HGAEvTCKDKK-GYTPLHAAASNGQINVVKHLLNLGVEIDEINVYG-NTALHIACY--NGQD 252
Cdd:PHA02876    12 RGNCIDILSAIDNydlhkHGAN-QCENESiPFTAIHQALQLRQIDIVEEIIQQNPELIYITDHKcHSTLHTICIipNVMD 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  253 AVVNELIDYGANVNQPNNSGFTPLHfaaasTHGALCLELLVN--NGADVNIqSKDGKSPLHMTAVHGRFTR-----SQTL 325
Cdd:PHA02876    91 IVISLTLDCDIILDIKYASIILNKH-----KLDEACIHILKEaiSGNDIHY-DKINESIEYMKLIKERIQQdelliAEML 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  326 IQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLS-----SGQKYSI 400
Cdd:PHA02876   165 LEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDnrsniNKNDLSL 244

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  401 VSLFSNEH------VLSAGFEIDTPDTFGRTCLHAAAAGGNVECI--KLLQsSGADFHKKDKCGRTPLHYAAANCH-FHC 471
Cdd:PHA02876   245 LKAIRNEDletsllLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvpKLLE-RGADVNAKNIKGETPLYLMAKNGYdTEN 323

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  472 IKALVTTGANINETDNWGRTALHyaAASDMDRNKMILGNahdnseelerarevkgkdaalclefLLQNDANPSIRDKEGY 551
Cdd:PHA02876   324 IRTLIMLGADVNAADRLYITPLH--QASTLDRNKDIVIT-------------------------LLELGANVNARDYCDK 376

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  552 NSIHYAAAYGHRQCLELLLertntgfeesDGGAlksplhlaaynghhqalevllqslvDLDIRDEKGRTALYLAAFKGHT 631
Cdd:PHA02876   377 TPIHYAAVRNNVVIINTLL----------DYGA-------------------------DIEALSQKIGTALHFALCGTNP 421

                          490       500       510       520       530       540       550       560
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  632 -ECVEALVNQGASIFVKdNVTKRTPLHASVINGHTL-CLRLLLeiaDNPEVVDVKDAKGQTPLMLAVAYGHIdaVSLLLE 709
Cdd:PHA02876   422 yMSVKTLIDRGANVNSK-NKDLSTPLHYACKKNCKLdVIEMLL---DNGADVNAINIQNQYPLLIALEYHGI--VNILLH 495


                   ....*
gi 1046903808  710 KEANV 714
Cdd:PHA02876   496 YGAEL 500
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 48-266 7.01e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 93.52  E-value: 7.01e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   48 AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQSPVHVAAANKAVKCAEVII 127
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  128 PLLSSVN-VSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKG 206
Cdd:PHA02875    89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046903808  207 YTPLHAAASNGQINVVKHLLNLGVEIDEINVYGN-TALHIACYNGQDAVVNELIDYGANVN 266
Cdd:PHA02875   169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCN 229
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 397-682 1.34e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 92.81  E-value: 1.34e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  397 KYSIVSLFSNEHVLSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCH-----FHC 471
Cdd:PHA03100     9 KSRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEI 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  472 IKALVTTGANINETDNWGRTALHYAAASDMDRNKMIlgnahdnseelerarevkgkdaalclEFLLQNDANPSIRDKEGY 551
Cdd:PHA03100    89 VKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIV--------------------------EYLLDNGANVNIKNSDGE 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  552 NSIHYAAAYGHR--QCLELLLERTNtgfeesdggalksplHLAAYNghhqALEVLLQSLVDLDIRDEKGRTALYLAAFKG 629
Cdd:PHA03100   143 NLLHLYLESNKIdlKILKLLIDKGV---------------DINAKN----RVNYLLSYGVPINIKDVYGFTPLHYAVYNN 203

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1046903808  630 HTECVEALVNQGASIFVKDNVTKrTPLHASVINGHTLCLRLLLEIADNPEVVD 682
Cdd:PHA03100   204 NPEFVKYLLDLGANPNLVNKYGD-TPLHIAILNNNKEIFKLLLNNGPSIKTII 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
622-718 2.34e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 2.34e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  622 LYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADnpevVDVKDaKGQTPLMLAVAYGHI 701
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHL 74

                           90
                   ....*....|....*..
gi 1046903808  702 DAVSLLLEKEANVDAVD 718
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 669-1034 2.53e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 89.31  E-value: 2.53e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  669 RLLLEIADnpevVDVKDAKGQTPLMLAVAYGH---IDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEE-CVQMLLEQE 744
Cdd:PHA03095    32 RLLAAGAD----VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  745 ASILCKDSRGRTPLHyAAARGHATwlNELVQIALSEE--DCCLKDNQGYTPLHwaCYNGNENC-IEVLleqkcfrkfign 821
Cdd:PHA03095   108 ADVNAKDKVGRTPLH-VYLSGFNI--NPKVIRLLLRKgaDVNALDLYGMTPLA--VLLKSRNAnVELL------------ 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  822 pftplhcaiinghescaSLLLGAIdsSIVSCRDDKGRTTLH--AAAFGDHAECLQLLLRHDAQVNAVDNSGktalmmaae 899
Cdd:PHA03095   171 -----------------RLLIDAG--ADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLG--------- 222

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  900 ngqagavdilvnsaqadltvkdkdlNTPLHLAISKGHEKcALLILDKIQDESLINAKNSALQTPLHIAARNGLKVVVEEL 979
Cdd:PHA03095   223 -------------------------NTPLHSMATGSSCK-RSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRL 276

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903808  980 LAKGACVLAVDENGHTP-ALAcapnkdVADCLALILATMMTFSPSSTMTAVNFVYF 1034
Cdd:PHA03095   277 IALGADINAVSSDGNTPlSLM------VRNNNGRAVRAALAKNPSAETVAATLNTA 326
Ank_2 pfam12796
Ankyrin repeats (3 copies);
112-203 2.90e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 2.90e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  112 HVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKgANINAFDkKDRRALHWAAYMGHLDVVAL 191
Cdd:pfam12796    2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|..
gi 1046903808  192 LINHGAEVTCKD 203
Cdd:pfam12796   80 LLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
589-682 5.30e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 5.30e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  589 LHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQgasIFVKDNVTKRTPLHASVINGHTLCL 668
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 1046903808  669 RLLLEIADNPEVVD 682
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 150-563 2.58e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 85.79  E-value: 2.58e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  150 NGHMEMV-NLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNL 228
Cdd:PHA02874    11 SGDIEAIeKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  229 GVEideinvygNTALHIACYNGQdaVVNELIDYGANVNQPNNSGFTPLHFAAASthGAL-CLELLVNNGADVNIQSKDGK 307
Cdd:PHA02874    91 GVD--------TSILPIPCIEKD--MIKTILDCGIDVNIKDAELKTFLHYAIKK--GDLeSIKMLFEYGADVNIEDDNGC 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  308 SPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGhellintlitsgadtakcgihsmfplhlaalnahsdc 387
Cdd:PHA02874   159 YPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYG------------------------------------- 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  388 crkllssgqkysivslfsnehvlsagfeidtpdtfgrtclhaaaaggNVECIKLLQSSGADFHKKDKCGRTPLHYAAanC 467
Cdd:PHA02874   202 -----------------------------------------------DYACIKLLIDHGNHIMNKCKNGFTPLHNAI--I 232

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  468 HFHCIKALVTTGANINETDNWGRTALHYAAASDMDRNkmilgnahdnseelerarevkgkdaalCLEFLLQNDANPSIRD 547
Cdd:PHA02874   233 HNRSAIELLINNASINDQDIDGSTPLHHAINPPCDID---------------------------IIDILLYHKADISIKD 285

                          410
                   ....*....|....*.
gi 1046903808  548 KEGYNSIHYAAAYGHR 563
Cdd:PHA02874   286 NKGENPIDTAFKYINK 301
Ank_2 pfam12796
Ankyrin repeats (3 copies);
45-170 4.13e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 4.13e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   45 LHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHsADVNARDKnwqspvhvaaankavkcae 124
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN------------------- 60

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1046903808  125 viipllssvnvsdrgGRTALHHAALNGHMEMVNLLLAKGANINAFD 170
Cdd:pfam12796   61 ---------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
861-957 9.64e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 9.64e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  861 LHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKdlnTPLHLAISKGHEKCA 940
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77

                           90
                   ....*....|....*..
gi 1046903808  941 LLILDKIQDeslINAKN 957
Cdd:pfam12796   78 KLLLEKGAD---INVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
12-104 1.08e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 1.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   12 LVQAIFSGDPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLiLSGARVNAKDNMWlTPLHRAVASRSEEAVQ 91
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDNGR-TALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1046903808   92 VLIKHSADVNARD 104
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 533-745 1.14e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 83.50  E-value: 1.14e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  533 LEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLerTNTGFEESDGGALKSPLHLAAYNGHHQALEVLLQS--LVD 610
Cdd:PHA02875    18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLM--KHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLgkFAD 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  611 lDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKdNVTKRTPLHASVINGHTLCLRLLLeiaDNPEVVDVKDAKGQT 690
Cdd:PHA02875    96 -DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP-NTDKFSPLHLAVMMGDIKGIELLI---DHKACLDIEDCCGCT 170

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903808  691 PLMLAVAYGHIDAVSLLLEKEANVDAVDTVGC-TALHRGIMTGHEECVQMLLEQEA 745
Cdd:PHA02875   171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGA 226
PHA03095 PHA03095
ankyrin-like protein; Provisional
 410-743 1.26e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.92  E-value: 1.26e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  410 LSAGFEIDTPDTFGRTCLHAAAAGGNVEC---IKLLQSSGADFHKKDKCGRTPLH-YAAANCHFHCIKALVTTGANINET 485
Cdd:PHA03095    34 LAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADVNAK 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  486 DNWGRTALHYAAASDMDRNKMIlgnahdnseelerarevkgkdaalclEFLLQNDANPSIRDKEGYNSIHyaaayghrqc 565
Cdd:PHA03095   114 DKVGRTPLHVYLSGFNINPKVI--------------------------RLLLRKGADVNALDLYGMTPLA---------- 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  566 leLLLERTNTGFEesdggalksplhlaaynghhqALEVLLQSLVDLDIRDEKGRTAL--YLAAFKGHTECVEALVNQGAS 643
Cdd:PHA03095   158 --VLLKSRNANVE---------------------LLRLLIDAGADVYAVDDRFRSLLhhHLQSFKPRARIVRELIRAGCD 214

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  644 IFVKdNVTKRTPLHASVIngHTLCLRLLLE--IADNPEVvDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVG 721
Cdd:PHA03095   215 PAAT-DMLGNTPLHSMAT--GSSCKRSLVLplLIAGISI-NARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDG 290

                          330       340
                   ....*....|....*....|..
gi 1046903808  722 CTALHRGIMTGHEECVQMLLEQ 743
Cdd:PHA03095   291 NTPLSLMVRNNNGRAVRAALAK 312
Ank_2 pfam12796
Ankyrin repeats (3 copies);
725-814 1.75e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.75e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  725 LHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHAtwlnELVQIALSEEDCCLKDNqGYTPLHWACYNGNEN 804
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHL----EIVKLLLEHADVNLKDN-GRTALHYAARSGHLE 75

                           90
                   ....*....|
gi 1046903808  805 CIEVLLEQKC 814
Cdd:pfam12796   76 IVKLLLEKGA 85
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 407-761 2.29e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 83.96  E-value: 2.29e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  407 EHVLSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANINetd 486
Cdd:PHA02876   162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN--- 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  487 nwgrtalhyaaasdmdRNKMILGNAHDNsEELERArevkgkdaalclefLLQNDANPSIRDKEGYNSihyaaayghrqcl 566
Cdd:PHA02876   239 ----------------KNDLSLLKAIRN-EDLETS--------------LLLYDAGFSVNSIDDCKN------------- 274

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  567 elllertntgfeesdggalkSPLHLAAYNGHHQAL-EVLLQSLVDLDIRDEKGRTALYLAAFKGH-TECVEALVNQGASI 644
Cdd:PHA02876   275 --------------------TPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADV 334

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  645 FVKDNVTKrTPLH-ASVINGHTLCLRLLLEIADNpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCT 723
Cdd:PHA02876   335 NAADRLYI-TPLHqASTLDRNKDIVITLLELGAN---VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGT 410

                          330       340       350
                   ....*....|....*....|....*....|....*....
gi 1046903808  724 ALHRGIM-TGHEECVQMLLEQEASILCKDSRGRTPLHYA 761
Cdd:PHA02876   411 ALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 589-864 3.07e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 82.70  E-value: 3.07e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  589 LHLAAYNGHHQALEVLLQSLVD-LDIRDEKGRTALYLAAFKGHTECVEALVNQGASI-FVKDNVTKrtPLHASVINGHTL 666
Cdd:PHA02874     5 LRMCIYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADInHINTKIPH--PLLTAIKIGAHD 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  667 CLRLLLE--------------------IADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALH 726
Cdd:PHA02874    83 IIKLLIDngvdtsilpipciekdmiktILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIH 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  727 RGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHATWLNELVQialSEEDCCLKDNQGYTPLHWACYNgNENCI 806
Cdd:PHA02874   163 IAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLID---HGNHIMNKCKNGFTPLHNAIIH-NRSAI 238

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046903808  807 EVLLEQKCFRKFIGNPFTPLHCAIingHESCA-----SLLLGAIDSSIvscRDDKGRTTLHAA 864
Cdd:PHA02874   239 ELLINNASINDQDIDGSTPLHHAI---NPPCDidiidILLYHKADISI---KDNKGENPIDTA 295
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 567-749 8.04e-16

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 82.61  E-value: 8.04e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  567 ELLLERTntgfEESDGGALKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFV 646
Cdd:PLN03192   511 DLLGDNG----GEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI 586

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  647 KDnVTKRTPLHASVINGHTLCLRLLLEIA--DNPEVvdvkdakGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTA 724
Cdd:PLN03192   587 RD-ANGNTALWNAISAKHHKIFRILYHFAsiSDPHA-------AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658

                          170       180
                   ....*....|....*....|....*
gi 1046903808  725 LHRGIMTGHEECVQMLLEQEASILC 749
Cdd:PLN03192   659 LQVAMAEDHVDMVRLLIMNGADVDK 683
Ank_2 pfam12796
Ankyrin repeats (3 copies);
554-648 8.54e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.61  E-value: 8.54e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  554 IHYAAAYGHRQCLELLLE-RTNTGFEESDGgalKSPLHLAAYNGHHQALEVLLQSlVDLDIRDEkGRTALYLAAFKGHTE 632
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLEnGADANLQDKNG---RTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 1046903808  633 CVEALVNQGASIFVKD 648
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 604-984 9.43e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 81.22  E-value: 9.43e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  604 LLQSLVDLDIRDEKGRTAL-YLAAFKGH--TECVEALVNQGASIFVKDnVTKRTPLHASVINGHTL-CLRLLLEI-ADnp 678
Cdd:PHA03095    33 LLAAGADVNFRGEYGKTPLhLYLHYSSEkvKDIVRLLLEAGADVNAPE-RCGFTPLHLYLYNATTLdVIKLLIKAgAD-- 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  679 evVDVKDAKGQTPL--MLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALH-----RGIMTgheECVQMLLEQEASILCKD 751
Cdd:PHA03095   110 --VNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvllksRNANV---ELLRLLIDAGADVYAVD 184

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  752 SRGRTPLHyaaarghatwlnelvQIALSeedccLKDNqgytplhwacyngnencievlleQKCFRKFIGNPFTPlhcaii 831
Cdd:PHA03095   185 DRFRSLLH---------------HHLQS-----FKPR-----------------------ARIVRELIRAGCDP------ 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  832 nghescaslllgaidssivSCRDDKGRTTLHAAAFGDHAECLQL--LLRHDAQVNAVDNSGKTALMMAAENGQAGAVDIL 909
Cdd:PHA03095   216 -------------------AATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRL 276

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046903808  910 VNsAQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDESLINAKNSALQTPLHIAARNGLKVVVEELLAKGA 984
Cdd:PHA03095   277 IA-LGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTASVAGGDIPSDATRLCVAKVVLRGA 350
Ank_2 pfam12796
Ankyrin repeats (3 copies);
427-500 9.98e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 9.98e-16
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046903808  427 LHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTgANINETDNwGRTALHYAAASD 500
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSG 72
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 141-373 1.09e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.81  E-value: 1.09e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  141 RTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQIN 220
Cdd:PHA02875     3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  221 VVKHLLNLGVEIDEInVY--GNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGAD 298
Cdd:PHA02875    83 AVEELLDLGKFADDV-FYkdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG-IELLIDHKAC 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903808  299 VNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHEL-LINTLITSGADtakCGIHSM 373
Cdd:PHA02875   161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIdIVRLFIKRGAD---CNIMFM 233
Ank_2 pfam12796
Ankyrin repeats (3 copies);
794-887 1.47e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 1.47e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  794 LHWACYNGNENCIEVLLEQKC-FRKFIGNPFTPLHCAIINGHESCASLLLGAIDSSIvscrDDKGRTTLHAAAFGDHAEC 872
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL----KDNGRTALHYAARSGHLEI 76

                           90
                   ....*....|....*
gi 1046903808  873 LQLLLRHDAQVNAVD 887
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 74-281 2.62e-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: 2.62e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   74 WLTPLHRAVASRSEEAVQVLIK-HSADVNARDKNWQSPVHVAAANKAVKCAEVII---PLLssVNV---SD-RGGRTALH 145
Cdd:cd22192     17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaaPEL--VNEpmtSDlYQGETALH 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  146 HAALNGHMEMVNLLLAKGANIN------AFDKKDRRAL-----H---WAAYMGHLDVVALLINHGAEVTCKDKKGYTPLH 211
Cdd:cd22192     95 IAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046903808  212 AAASNGQINVVKH----LLNLGVEIDEINVYgntalHIacyngqdavvnelidyganvnqPNNSGFTPLHFAAA 281
Cdd:cd22192    175 ILVLQPNKTFACQmydlILSYDKEDDLQPLD-----LV----------------------PNNQGLTPFKLAAK 221
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 20-170 4.91e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 79.15  E-value: 4.91e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   20 DPEEIRLLIHKTEDVNALDSEK-RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSA 98
Cdd:PHA02878   146 EAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046903808   99 DVNARDKNWQSPVHVAAAnkAVKCAEVIIPLL---SSVNV-SDRGGRTALHHAAlngHMEMV-NLLLAKGANINAFD 170
Cdd:PHA02878   226 STDARDKCGNTPLHISVG--YCKDYDILKLLLehgVDVNAkSYILGLTALHSSI---KSERKlKLLLEYGADINSLN 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
376-486 9.01e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.53  E-value: 9.01e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  376 LHLAALNAHSDCCRKLLSSGqkysivslfsnehvlsagFEIDTPDTFGRTCLHAAAAGGNVECIKLLqSSGADFHKKDKc 455
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG------------------ADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDN- 60

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1046903808  456 GRTPLHYAAANCHFHCIKALVTTGANINETD 486
Cdd:pfam12796   61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 17-168 1.14e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.76  E-value: 1.14e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   17 FSGDPEEIRLLIHKTEDVNALDSEKRTPLHVaaFLG----DAEIIELLILSGARVNAKDNMWLTPLHR-AVASRSEEAV- 90
Cdd:PHA03095   128 FNINPKVIRLLLRKGADVNALDLYGMTPLAV--LLKsrnaNVELLRLLIDAGADVYAVDDRFRSLLHHhLQSFKPRARIv 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   91 QVLIKHSADVNARDKNWQSPVHVAAANKAVKcAEVIIPLL---SSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANIN 167
Cdd:PHA03095   206 RELIRAGCDPAATDMLGNTPLHSMATGSSCK-RSLVLPLLiagISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284


                   .
gi 1046903808  168 A 168
Cdd:PHA03095   285 A 285
Ank_2 pfam12796
Ankyrin repeats (3 copies);
692-766 1.22e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 1.22e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046903808  692 LMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLEQEAsiLCKDSRGRTPLHYAAARGH 766
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGH 73
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 635-998 1.35e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 78.57  E-value: 1.35e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  635 EALVNQGASIFVKDnVTKRTPLHASVINGHTLCLRLLLEIADNPEVVDVKDAkgqTPLMLAVAYGHIDAVSLLLEKEANV 714
Cdd:PHA02876   162 EMLLEGGADVNAKD-IYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDL---SVLECAVDSKNIDTIKAIIDNRSNI 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  715 DAVDTvgctALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAargHATWLNELVQIALSE-EDCCLKDNQGYTP 793
Cdd:PHA02876   238 NKNDL----SLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHAS---QAPSLSRLVPKLLERgADVNAKNIKGETP 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  794 LHWACYNGNENcievlleqkcfrkfignpftplhcaiinghESCASLLLGAIDssiVSCRDDKGRTTLHAAAFGD-HAEC 872
Cdd:PHA02876   311 LYLMAKNGYDT------------------------------ENIRTLIMLGAD---VNAADRLYITPLHQASTLDrNKDI 357

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  873 LQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCALLILdkIQDESL 952
Cdd:PHA02876   358 VITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG-ADIEALSQKIGTALHFALCGTNPYMSVKTL--IDRGAN 434

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*..
gi 1046903808  953 INAKNSALQTPLHIAARNGLKV-VVEELLAKGACVLAVDENGHTPAL 998
Cdd:PHA02876   435 VNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAINIQNQYPLL 481
PHA02798 PHA02798
ankyrin-like protein; Provisional
 78-364 1.62e-14

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 77.57  E-value: 1.62e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   78 LHRAvaSRSEEAVQVLIKHSADVNARDKNWQSPVhvaaankavkCAeviipLLSsvNVSDrggrtalhhaaLNGHMEMVN 157
Cdd:PHA02798    44 LQRD--SPSTDIVKLFINLGANVNGLDNEYSTPL----------CT-----ILS--NIKD-----------YKHMLDIVK 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  158 LLLAKGANINAFDKKDRRALHWA---AYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNG---QINVVKHLLNLGVE 231
Cdd:PHA02798    94 ILIENGADINKKNSDGETPLYCLlsnGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVD 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  232 IDEI-NVYGNTALHiaCY-----NGQDA-VVNELIDYGANVNQPNNSgftplhfaAASTHGALCLELLVNNG-------- 296
Cdd:PHA02798   174 INTHnNKEKYDTLH--CYfkyniDRIDAdILKLFVDNGFIINKENKS--------HKKKFMEYLNSLLYDNKrfkknild 243

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046903808  297 ---ADVNIQSKD--GKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGAD 364
Cdd:PHA02798   244 fifSYIDINQVDelGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 516-926 4.25e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.64  E-value: 4.25e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  516 EELERAREVKGKDAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLER-TNTGFEESDGgalkspLHLAAY 594
Cdd:PHA02876   144 EYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYgADVNIIALDD------LSVLEC 217

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  595 NGHHQALEVLlQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDnVTKRTPLHASVingHTLCL-RLLLE 673
Cdd:PHA02876   218 AVDSKNIDTI-KAIIDNRSNINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSID-DCKNTPLHHAS---QAPSLsRLVPK 292

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  674 IADNPEVVDVKDAKGQTPLMLAVAYGH-IDAVSLLLEKEANVDAVDTVGCTALHRG-IMTGHEECVQMLLEQEASILCKD 751
Cdd:PHA02876   293 LLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARD 372

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  752 SRGRTPLHYAAARGHATWLNELVQIALSEEdcCLKDNQGyTPLHWACYNGNencievlleqkcfrkfignPFTPLHCAII 831
Cdd:PHA02876   373 YCDKTPIHYAAVRNNVVIINTLLDYGADIE--ALSQKIG-TALHFALCGTN-------------------PYMSVKTLID 430

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  832 NGHEscaslllgaidssiVSCRDDKGRTTLHAAAFGD-HAECLQLLLRHDAQVNAVDNSGKTALMMAAenGQAGAVDILV 910
Cdd:PHA02876   431 RGAN--------------VNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILL 494

                          410
                   ....*....|....*...
gi 1046903808  911 NSAQA--DLTVKDKDLNT 926
Cdd:PHA02876   495 HYGAElrDSRVLHKSLND 512
Ank_2 pfam12796
Ankyrin repeats (3 copies);
758-842 4.77e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 4.77e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  758 LHYAAARGHAtwlnELVQIALSEE-DCCLKDNQGYTPLHWACYNGNENCIEVLLEQKCFRKFiGNPFTPLHCAIINGHES 836
Cdd:pfam12796    1 LHLAAKNGNL----ELVKLLLENGaDANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-DNGRTALHYAARSGHLE 75


                   ....*.
gi 1046903808  837 CASLLL 842
Cdd:pfam12796   76 IVKLLL 81
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 585-761 1.22e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 74.61  E-value: 1.22e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  585 LKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNVTKrTPLHASVINGH 664
Cdd:PHA02874   124 LKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGE-SPLHNAAEYGD 202

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  665 TLCLRLLLeiaDNPEVVDVKDAKGQTPLMLAVAYGHiDAVSLLLeKEANVDAVDTVGCTALHRGIMTG-HEECVQMLLEQ 743
Cdd:PHA02874   203 YACIKLLI---DHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI-NNASINDQDIDGSTPLHHAINPPcDIDIIDILLYH 277

                          170
                   ....*....|....*...
gi 1046903808  744 EASILCKDSRGRTPLHYA 761
Cdd:PHA02874   278 KADISIKDNKGENPIDTA 295
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 254-483 2.67e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 73.10  E-value: 2.67e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  254 VVNELIDYGANVNQPNNSGFTPLHFAAaSTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI- 332
Cdd:PHA02875    17 IARRLLDIGINPNFEIYDGISPIKLAM-KFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAd 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  333 DCVDKDGNTPLHVAARYGHELLINTLITSGADTakcgihsmfplhlaalnahsdccrkllssgqkysivslfsnehvlsa 412
Cdd:PHA02875    96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADP----------------------------------------------- 128

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046903808  413 gfeiDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANIN 483
Cdd:PHA02875   129 ----DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
Ank_2 pfam12796
Ankyrin repeats (3 copies);
894-990 3.10e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.29  E-value: 3.10e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  894 LMMAAENGQAGAVDILVNSaQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQdeslINAKNSAlQTPLHIAARNGLK 973
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD----VNLKDNG-RTALHYAARSGHL 74

                           90
                   ....*....|....*..
gi 1046903808  974 VVVEELLAKGACVLAVD 990
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 602-984 3.51e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 73.94  E-value: 3.51e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  602 EVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGA--SIFVKDNVTkrtplhasvinghtlclrlLLEIADNPE 679
Cdd:PHA02876   162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGAdvNIIALDDLS-------------------VLECAVDSK 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  680 VVDVKDA---------KGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGH-EECVQMLLEQEASILC 749
Cdd:PHA02876   223 NIDTIKAiidnrsninKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNA 302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  750 KDSRGRTPLHYAAARGHATwlNELVQIALSEEDCCLKDNQGYTPLHWA-CYNGNENCIEVLLEqkcfrkfignpftplhc 828
Cdd:PHA02876   303 KNIKGETPLYLMAKNGYDT--ENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLE----------------- 363

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  829 aiinghescasllLGAidssIVSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMA-AENGQAGAVD 907
Cdd:PHA02876   364 -------------LGA----NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVK 426

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046903808  908 ILVNSAqADLTVKDKDLNTPLHLAISKgheKCALLILDKIQDESL-INAKNSALQTPLHIAArnGLKVVVEELLAKGA 984
Cdd:PHA02876   427 TLIDRG-ANVNSKNKDLSTPLHYACKK---NCKLDVIEMLLDNGAdVNAINIQNQYPLLIAL--EYHGIVNILLHYGA 498
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 9-167 1.37e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 71.18  E-value: 1.37e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808    9 QPPLVQAIFSGDPEEIRLLIHKTEDVNALDSEK-RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSE 87
Cdd:PHA02875    69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   88 EAVQVLIKHSADVNARDKNWQSPVHVAAANKAVKCAEVIIPLLSSVN-VSDRGGRTALHHAALNGHMEMVNLLLAKGANI 166
Cdd:PHA02875   149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGADC 228


                   .
gi 1046903808  167 N 167
Cdd:PHA02875   229 N 229
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 233-568 1.43e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.45  E-value: 1.43e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  233 DEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELL-VNNGADVNIQSKDGKSPLH 311
Cdd:PHA02878    31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIrSINKCSVFYTLVAIKDAFN 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  312 MTAVH-------GRFTRSQTLiqNGGEIDCVDKDGNTPLHVaaryghellINTLITSGADTAKCGIHSM-FPLHLAALNA 383
Cdd:PHA02878   111 NRNVEifkiiltNRYKNIQTI--DLVYIDKKSKDDIIEAEI---------TKLLLSYGADINMKDRHKGnTALHYATENK 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  384 HSDCCRKLLSSGQkysivslfsnehvlsagfEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYA 463
Cdd:PHA02878   180 DQRLTELLLSYGA------------------NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  464 AANC-HFHCIKALVTTGANIN-ETDNWGRTALHYAAASDmDRNKMILG-----NAHDNSEELERAREVKGKDAALCLEFL 536
Cdd:PHA02878   242 VGYCkDYDILKLLLEHGVDVNaKSYILGLTALHSSIKSE-RKLKLLLEygadiNSLNSYKLTPLSSAVKQYLCINIGRIL 320

                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1046903808  537 -----LQNDANPSIRDKEGYnSIHYAAAYGHRQCLEL 568
Cdd:PHA02878   321 isnicLLKRIKPDIKNSEGF-IDNMDCITSNKRLNQI 356
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 134-276 1.59e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.82  E-value: 1.59e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  134 NVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLiNHGAEVTCKDKKGyTPLHAA 213
Cdd:PLN03192   552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL-YHFASISDPHAAG-DLLCTA 629

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046903808  214 ASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPN-NSGFTPL 276
Cdd:PLN03192   630 AKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDDDFSPT 693
PHA02798 PHA02798
ankyrin-like protein; Provisional
 55-273 2.78e-12

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 70.25  E-value: 2.78e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   55 EIIELLILSGARVNAKDNMWLTPLHRAVASRSE-----EAVQVLIKHSADVNARDKNWQSPVHVAAANKAVKCAEVIIPL 129
Cdd:PHA02798    52 DIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFM 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  130 L---SSVNVSDRGGRTALHHAALNGH---MEMVNLLLAKGANINAFDKKDR-RALHwaAYMGH------LDVVALLINHG 196
Cdd:PHA02798   132 IengADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNNKEKyDTLH--CYFKYnidridADILKLFVDNG 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  197 ---------------------------------------AEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINV 237
Cdd:PHA02798   210 fiinkenkshkkkfmeylnsllydnkrfkknildfifsyIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITE 289

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1046903808  238 YGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGF 273
Cdd:PHA02798   290 LGNTCLFTAFENESKFIFNSILNKKPNKNTISYTYY 325
Ank_2 pfam12796
Ankyrin repeats (3 copies);
532-615 2.91e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.60  E-value: 2.91e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  532 CLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNTGFEESDggalKSPLHLAAYNGHHQALEVLLQSLVDL 611
Cdd:pfam12796   12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNG----RTALHYAARSGHLEIVKLLLEKGADI 87


                   ....
gi 1046903808  612 DIRD 615
Cdd:pfam12796   88 NVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
140-193 6.68e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.14  E-value: 6.68e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1046903808  140 GRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLI 193
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
343-453 6.87e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 6.87e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  343 LHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGQKYSivslfsnehvlsagfeidtpDTF 422
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--------------------KDN 60

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1046903808  423 GRTCLHAAAAGGNVECIKLLQSSGADFHKKD 453
Cdd:pfam12796   61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 48-201 8.18e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 69.51  E-value: 8.18e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   48 AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQSPVHVAAANKAVKCAEVII 127
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046903808  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 8.84e-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: 8.84e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  107 WQSPVHVAAANKAVKCaevIIPLL--SSVNVSDRG--GRTALHHAALNGHMEMVNLLLakganinafdkkdrralhwaay 182
Cdd:cd22192     17 SESPLLLAAKENDVQA---IKKLLkcPSCDLFQRGalGETALHVAALYDNLEAAVVLM---------------------- 71

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  183 mghlDVVALLINHgaEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEI--------------DEINVYGNTALHIACY 248
Cdd:cd22192     72 ----EAAPELVNE--PMTSDLYQGETALHIAVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAAC 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  249 NGQDAVVNELIDYGANVNQPNNSGFTPLH---FAAASTHGALCLELLVNNGADVN------IQSKDGKSPLHMTAVHGRF 319
Cdd:cd22192    146 VGNEEIVRLLIEHGADIRAQDSLGNTVLHilvLQPNKTFACQMYDLILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNI 225


                   ....*....
gi 1046903808  320 TRSQTLIQN 328
Cdd:cd22192    226 VMFQHLVQK 234
Ank_2 pfam12796
Ankyrin repeats (3 copies);
243-336 1.09e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 1.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  243 LHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGAlCLELLVNNgADVNIQSkDGKSPLHMTAVHGRFTRS 322
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLE-IVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 1046903808  323 QTLIQNGGEIDCVD 336
Cdd:pfam12796   78 KLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
174-226 1.18e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.75  E-value: 1.18e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1046903808  174 RRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLL 226
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 792-1010 1.36e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.07  E-value: 1.36e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  792 TPLHWACYNGNENCIEVLLEQKCFRKFIG-NPFTPLHCAI-INGHESCASLLLGAIDSSI-------------------- 849
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINtKIPHPLLTAIkIGAHDIIKLLIDNGVDTSIlpipciekdmiktildcgid 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  850 VSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLH 929
Cdd:PHA02874   117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLH 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  930 LAISKGHEKCALLILDkiqDESLINAKNSALQTPLHIAARNGLKVVveELLAKGACVLAVDENGHTP---ALACAPNKDV 1006
Cdd:PHA02874   196 NAAEYGDYACIKLLID---HGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPlhhAINPPCDIDI 270


                   ....
gi 1046903808 1007 ADCL 1010
Cdd:PHA02874   271 IDIL 274
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 459-696 1.48e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.98  E-value: 1.48e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  459 PLHYAAANCHFHCIKALVTTGANINETDNWGRTALH--------------------------YAAASDMDRN------KM 506
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHiickepnklgmkemirsinkcsvfytLVAIKDAFNNrnveifKI 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  507 ILGNAHDNSE--ELERAREVKGKDA--ALCLEFLLQNDANPSIRDKEGYNS-IHYAAAYGHRQCLELLL---------ER 572
Cdd:PHA02878   120 ILTNRYKNIQtiDLVYIDKKSKDDIieAEITKLLLSYGADINMKDRHKGNTaLHYATENKDQRLTELLLsyganvnipDK 199

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  573 TNtgfeesdggalKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLA-AFKGHTECVEALVNQGASIFVKDNVT 651
Cdd:PHA02878   200 TN-----------NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYIL 268

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1046903808  652 KRTPLHASVINGHTlcLRLLLEIADNPEVVdvkDAKGQTPLMLAV 696
Cdd:PHA02878   269 GLTALHSSIKSERK--LKLLLEYGADINSL---NSYKLTPLSSAV 308
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 166-463 1.68e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.98  E-value: 1.68e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  166 INAFDKKDRRA----------LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEI 235
Cdd:PHA02878    20 IEYIDHTENYStsaslipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVF 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  236 NVYgnTALHIACYNGQDAVVNE-LIDYGANVNQPNNSGFTPLHFAAASThgALCLELLVNNGADVNIQSKD-GKSPLHMT 313
Cdd:PHA02878   100 YTL--VAIKDAFNNRNVEIFKIiLTNRYKNIQTIDLVYIDKKSKDDIIE--AEITKLLLSYGADINMKDRHkGNTALHYA 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  314 AVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAAlnahsdccrkllS 393
Cdd:PHA02878   176 TENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV------------G 243

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046903808  394 SGQKYSIVSLfsnehVLSAGFEIDTPDTF-GRTCLHAAAAGGNVecIKLLQSSGADFHKKDKCGRTPLHYA 463
Cdd:PHA02878   244 YCKDYDILKL-----LLEHGVDVNAKSYIlGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
Ank_4 pfam13637
Ankyrin repeats (many copies);
423-476 2.01e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 2.01e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1046903808  423 GRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALV 476
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 556-775 3.56e-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: 3.56e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  556 YAAAYGHRQCLELLLERTNTGFEESdgGAL-KSPLHLAAYNGHHQALEVLLQS---LVDLDIRDE--KGRTALYLAAFKG 629
Cdd:cd22192     23 LAAKENDVQAIKKLLKCPSCDLFQR--GALgETALHVAALYDNLEAAVVLMEAapeLVNEPMTSDlyQGETALHIAVVNQ 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  630 HTECVEALVNQGAsifvkDNVTKRTPLHASVINGHTLCLRllleiadnpevvdvkdakGQTPLMLAVAYGHIDAVSLLLE 709
Cdd:cd22192    101 NLNLVRELIARGA-----DVVSPRATGTFFRPGPKNLIYY------------------GEHPLSFAACVGNEEIVRLLIE 157

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903808  710 KEANVDAVDTVGCTALHRGIMTGHEECV-QM---LLEQEASI------LCKDSRGRTPLHYAAARGHATWLNELVQ 775
Cdd:cd22192    158 HGADIRAQDSLGNTVLHILVLQPNKTFAcQMydlILSYDKEDdlqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 787-986 4.07e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.83  E-value: 4.07e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  787 DNQGYTPLHWACYNGNENCIEVLLEQKCFRKfIGNPFTPLHCAIINGHESCASLLL-----GAIDSSIVSCRDDKGRTTL 861
Cdd:PHA02878    67 DHRDLTPLHIICKEPNKLGMKEMIRSINKCS-VFYTLVAIKDAFNNRNVEIFKIILtnrykNIQTIDLVYIDKKSKDDII 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  862 haaafgdHAECLQLLLRHDAQVNAVD-NSGKTALMMAAENGQAGAVDILVnSAQADLTVKDKDLNTPLHLAISKGHEKcA 940
Cdd:PHA02878   146 -------EAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLL-SYGANVNIPDKTNNSPLHHAVKHYNKP-I 216

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1046903808  941 LLILdkIQDESLINAKNSALQTPLHIAARNGLKV-VVEELLAKGACV 986
Cdd:PHA02878   217 VHIL--LENGASTDARDKCGNTPLHISVGYCKDYdILKLLLEHGVDV 261
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 761-930 4.86e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.20  E-value: 4.86e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  761 AAARGHATWLNELVQIALSEEdccLKDNQGYTPLHWACYNGNENCIEVLLEQKC---FRKFIGNpfTPLHCAIINGHESC 837
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPD---IGDSKGRTPLHIAASKGYEDCVLVLLKHACnvhIRDANGN--TALWNAISAKHHKI 606

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  838 ASLLLgaiDSSIVSCRDDKGRTTLHAAAFGDhAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILV-NSAQAD 916
Cdd:PLN03192   607 FRILY---HFASISDPHAAGDLLCTAAKRND-LTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLImNGADVD 682

                          170
                   ....*....|....
gi 1046903808  917 LTVKDKDLnTPLHL 930
Cdd:PLN03192   683 KANTDDDF-SPTEL 695
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 150-275 5.50e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 63.30  E-value: 5.50e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  150 NGHMEMVNLLLAKGANINAFDKKDRRAL--HWAAYMGHL--DVVALLINHGAEVTCKDKKGYTPLHAAASNG--QINVVK 223
Cdd:PHA02859    63 KVNVEILKFLIENGADVNFKTRDNNLSAlhHYLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHMYMCNFnvRINVIK 142

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1046903808  224 HLLNLGVEIDEINVYGNTALH-IACYNGQDAVVNELIDYGANVNQPNNSGFTP 275
Cdd:PHA02859   143 LLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 656-926 6.68e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.84  E-value: 6.68e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  656 LHASVINGHTLCLRLLLE--IADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGH 733
Cdd:PHA03100     1 LYSYIVLTKSRIIKVKNIkyIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  734 E-----ECVQMLLEQEASILCKDSRGRTPLHYAAAR--GHATWLNELVQIALseeDCCLKDNQGYTPLHWA--CYNGNEN 804
Cdd:PHA03100    81 NltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGA---NVNIKNSDGENLLHLYleSNKIDLK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  805 CIEVLLEqkcfrkfignpftplHCAIINGHESCASLL-LGA-IDSsivscRDDKGRTTLHAAAFGDHAECLQLLLRHDAQ 882
Cdd:PHA03100   158 ILKLLID---------------KGVDINAKNRVNYLLsYGVpINI-----KDVYGFTPLHYAVYNNNPEFVKYLLDLGAN 217

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1046903808  883 VNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTV-------KDKDLNT 926
Cdd:PHA03100   218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIietllyfKDKDLNT 268
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 183-374 1.27e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 65.66  E-value: 1.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  183 MGHLDVVALLINHGAEVTckDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYG 262
Cdd:PLN03192   504 LHDLNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  263 ANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSkdGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTP 342
Cdd:PLN03192   582 CNVHIRDANGNTALWNAISAKHHKI-FRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1046903808  343 LHVAARYGHELLINTLITSGADTAKCGIHSMF 374
Cdd:PLN03192   659 LQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 309-628 1.42e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.90  E-value: 1.42e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  309 PLHMtAVHGR-FTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSgadTAKCGIHSmfplhlaALNAHSDC 387
Cdd:PHA02878    40 PLHQ-AVEARnLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS---INKCSVFY-------TLVAIKDA 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  388 CRKLLSSGQKYSIVSLFSNEHVLSAgFEIDTPDTFGRTclhaaaaggNVECIKLLQSSGADFHKKDK-CGRTPLHYAAAN 466
Cdd:PHA02878   109 FNNRNVEIFKIILTNRYKNIQTIDL-VYIDKKSKDDII---------EAEITKLLLSYGADINMKDRhKGNTALHYATEN 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  467 CHFHCIKALVTTGANINETDNWGRTALHYAAASdmdRNKMIlgnahdnseelerarevkgkdaalcLEFLLQNDANPSIR 546
Cdd:PHA02878   179 KDQRLTELLLSYGANVNIPDKTNNSPLHHAVKH---YNKPI-------------------------VHILLENGASTDAR 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  547 DKEGYNSIHYAAAY-GHRQCLELLLERTNTGFEESDGGALkSPLHLAAYNghHQALEVLLQSLVDLDIRDEKGRTALYLA 625
Cdd:PHA02878   231 DKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGL-TALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307


                   ...
gi 1046903808  626 AFK 628
Cdd:PHA02878   308 VKQ 310
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 653-765 1.87e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 64.24  E-value: 1.87e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  653 RTPLHASVINGHTLCLRLLLEIadNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTG 732
Cdd:PHA02875    69 ESELHDAVEEGDVKAVEELLDL--GKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1046903808  733 HEECVQMLLEQEASILCKDSRGRTPLHYAAARG 765
Cdd:PHA02875   147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 620-802 2.39e-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: 2.39e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  620 TALYLAAFKGHTECVEAL-VNQGASIFVKDNVTKrTPLHASVINGHTLCLRLLLEIAdnPEVVDVKDA----KGQTPLML 694
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLlKCPSCDLFQRGALGE-TALHVAALYDNLEAAVVLMEAA--PELVNEPMTsdlyQGETALHI 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  695 AVAYGHIDAVSLLLEKEANVDAVDTVGcTALHRGI---------------MTGHEECVQMLLEQEASILCKDSRGRTPLH 759
Cdd:cd22192     96 AVVNQNLNLVRELIARGADVVSPRATG-TFFRPGPknliyygehplsfaaCVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1046903808  760 YAAARGHATWLNELVQIALSEE----DCCL---KDNQGYTPLHWACYNGN 802
Cdd:cd22192    175 ILVLQPNKTFACQMYDLILSYDkeddLQPLdlvPNNQGLTPFKLAAKEGN 224
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 574-757 3.43e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.47  E-value: 3.43e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  574 NTGFEESDGgalKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGAsiFVKDNVTKR 653
Cdd:PHA02875    27 NPNFEIYDG---ISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK--FADDVFYKD 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  654 --TPLHASVINGHTLCLRLLLEIADNPevvDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMT 731
Cdd:PHA02875   102 gmTPLHLATILKKLDIMKLLIARGADP---DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAK 178

                          170       180
                   ....*....|....*....|....*.
gi 1046903808  732 GHEECVQMLLEQEASIlckDSRGRTP 757
Cdd:PHA02875   179 GDIAICKMLLDSGANI---DYFGKNG 201
Ank_2 pfam12796
Ankyrin repeats (3 copies);
310-400 3.56e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 3.56e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  310 LHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGAdtAKCGIHSMFPLHLAALNAHSDCCR 389
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 1046903808  390 KLLSSGQKYSI 400
Cdd:pfam12796   79 LLLEKGADINV 89
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 49-280 3.60e-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: 3.60e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   49 AFLGDAEIIELLILSGARVNAK-------DNMWLTPLHRAVA-SRSEEAVQVLIKHSADVNARDknwqSPVHVAAANKAV 120
Cdd:TIGR00870   20 AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAISLEYVD 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  121 KCAEVIIPLLSS---------VNVSDRG----GRTALHHAALNGHMEMVNLLLAKGANINA------FDKKDRRA----- 176
Cdd:TIGR00870   96 AVEAILLHLLAAfrksgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDsfyhg 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  177 ---LHWAAYMGHLDVVALLINHGAEVTCKDKKGytplhaaasngqiNVVKHLLNLGVEideiNVYGNTALHIACYngqda 253
Cdd:TIGR00870  176 espLNAAACLGSPSIVALLSEDPADILTADSLG-------------NTLLHLLVMENE----FKAEYEELSCQMY----- 233

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1046903808  254 vvNELIDYGANVNQ-------PNNSGFTPLHFAA 280
Cdd:TIGR00870  234 --NFALSLLDKLRDskeleviLNHQGLTPLKLAA 265
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 20-317 6.54e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 62.84  E-value: 6.54e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   20 DPEEIRLLIHKTEDVNaldSEKRTPLHVAAFLG----DAEIIELLILSGARVNAKDNMwLTPL-----HRAVAS-RSEEA 89
Cdd:PHA02989    15 DKNALEFLLRTGFDVN---EEYRGNSILLLYLKrkdvKIKIVKLLIDNGADVNYKGYI-ETPLcavlrNREITSnKIKKI 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   90 VQVLIKHSADVNARDKNWQSPvhvaaankavkcaevIIPLLSSVNVSDrggrtalhhaalnghMEMVNLLLAKGANINaf 169
Cdd:PHA02989    91 VKLLLKFGADINLKTFNGVSP---------------IVCFIYNSNINN---------------CDMLRFLLSKGINVN-- 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  170 DKKDRRA---LH--WAAYMGHLDVVALLINHGAEV-TCKDKKGYTP----LHAAASNGQINVVKHLLNLGVEIDEINVYG 239
Cdd:PHA02989   139 DVKNSRGynlLHmyLESFSVKKDVIKILLSFGVNLfEKTSLYGLTPmniyLRNDIDVISIKVIKYLIKKGVNIETNNNGS 218

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  240 NTAL------HIACYNGQDAVVNELIDYgANVNQPNNSGFTPLhFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMT 313
Cdd:PHA02989   219 ESVLesfldnNKILSKKEFKVLNFILKY-IKINKKDKKGFNPL-LISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296


                   ....
gi 1046903808  314 AVHG 317
Cdd:PHA02989   297 IKHG 300
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 173-448 8.09e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.32  E-value: 8.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  173 DRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVeIDEINVYG-NTALHIACYNGQ 251
Cdd:PHA02875     2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDiESELHDAVEEGD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  252 DAVVNELIDYGANVNQP-NNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGG 330
Cdd:PHA02875    81 VKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDI-MKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  331 EIDCVDKDGNTPLHVAARYGhellintlitsgaDTAkcgihsmfplhlaalnahsdCCRKLLSSGQkysivslfsnehvl 410
Cdd:PHA02875   160 CLDIEDCCGCTPLIIAMAKG-------------DIA--------------------ICKMLLDSGA-------------- 192

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1046903808  411 sagfeidTPDTFGR----TCLHAAAAGGNVECIKLLQSSGAD 448
Cdd:PHA02875   193 -------NIDYFGKngcvAALCYAIENNKIDIVRLFIKRGAD 227
Ank_4 pfam13637
Ankyrin repeats (many copies);
690-741 1.58e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 1.58e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1046903808  690 TPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLL 741
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 144-226 1.78e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.84  E-value: 1.78e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  144 LHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVK 223
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165


                   ...
gi 1046903808  224 HLL 226
Cdd:PTZ00322   166 LLS 168
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 3-114 2.11e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.05  E-value: 2.11e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808    3 VLKLCDQPPLVQAIFSGDPEEIRLLIHKTEDVNALDSEKRTPLHVA-AFLGDAEIIELLILSGARVNAKDNMW-LTPLHR 80
Cdd:PHA02878   196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILgLTALHS 275

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1046903808   81 AVasRSEEAVQVLIKHSADVNARDKNWQSPVHVA 114
Cdd:PHA02878   276 SI--KSERKLKLLLEYGADINSLNSYKLTPLSSA 307
Ank_4 pfam13637
Ankyrin repeats (many copies);
587-638 2.38e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 2.38e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1046903808  587 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALV 638
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 710-996 2.91e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.66  E-value: 2.91e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  710 KEANVDAVDTVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHATWLNELVQIALseedcclKDNQ 789
Cdd:PHA02878    26 TENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSIN-------KCSV 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  790 GYT--PLHWACYNGNENCIEVLLeqkcFRKFIGNpftplhcAIINGHESCASLLLGAIDSSIVSC-----------RDDK 856
Cdd:PHA02878    99 FYTlvAIKDAFNNRNVEIFKIIL----TNRYKNI-------QTIDLVYIDKKSKDDIIEAEITKLllsygadinmkDRHK 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  857 GRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGH 936
Cdd:PHA02878   168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHISVGYCK 246

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046903808  937 EKCALLILdkIQDESLINAKNSALQ-TPLHIAARNGLKVVVeeLLAKGACVLAVDENGHTP 996
Cdd:PHA02878   247 DYDILKLL--LEHGVDVNAKSYILGlTALHSSIKSERKLKL--LLEYGADINSLNSYKLTP 303
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 340-494 3.06e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 60.80  E-value: 3.06e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  340 NTPLHVAARYGHELLINTLITS-GADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSgqkysiVSLFSNEHVLSAGFEidt 418
Cdd:cd22192     18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEA------APELVNEPMTSDLYQ--- 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  419 pdtfGRTCLHAAAAGGNVECIKLLQSSGAD----------FHKKDKC----GRTPLHYAAANCHFHCIKALVTTGANINE 484
Cdd:cd22192     89 ----GETALHIAVVNQNLNLVRELIARGADvvspratgtfFRPGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRA 164

                          170
                   ....*....|
gi 1046903808  485 TDNWGRTALH 494
Cdd:cd22192    165 QDSLGNTVLH 174
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 208-345 8.56e-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: 8.56e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  208 TPLHAAASNGQINVVKHLL-NLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGAN-VNQPNNS----GFTPLHFAAA 281
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSdlyqGETALHIAVV 98

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046903808  282 STHGALcLELLVNNGADVN---------IQSKD-----GKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHV 345
Cdd:cd22192     99 NQNLNL-VRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
Ank_4 pfam13637
Ankyrin repeats (many copies);
456-498 1.22e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 1.22e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1046903808  456 GRTPLHYAAANCHFHCIKALVTTGANINETDNWGRTALHYAAA 498
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAAS 43
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 111-282 1.45e-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: 1.45e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  111 VHVAAANKAVKCAEVIIPLLSSVNVSDRG--------------GRTALHHAALNGHMEMVNLLLAKGANINA-----FDK 171
Cdd:cd21882     30 LHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAratgrFFR 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  172 KDRR--------ALHWAAYMGHLDVVALLINHGAE---VTCKDKKGYTPLHAAasngqinvvkhllnlgVEIDEiNVYGN 240
Cdd:cd21882    110 KSPGnlfyfgelPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHAL----------------VLQAD-NTPEN 172

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1046903808  241 TALHIACYNGqdavvneLIDYGANVNQ-------PNNSGFTPLHFAAAS 282
Cdd:cd21882    173 SAFVCQMYNL-------LLSYGAHLDPtqqleeiPNHQGLTPLKLAAVE 214
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 690-996 1.87e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.05  E-value: 1.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  690 TPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLEQ--EASILckdsrgrtPLhyaaarghA 767
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNgvDTSIL--------PI--------P 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  768 TWLNELVQIAL-SEEDCCLKDNQGYTPLHWACYNGNENCIEVLLEQKcfrkfignpftplhcaiinghescaslllgaid 846
Cdd:PHA02874   101 CIEKDMIKTILdCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYG--------------------------------- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  847 sSIVSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNT 926
Cdd:PHA02874   148 -ADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG-NHIMNKCKNGFT 225

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046903808  927 PLHLAISKGHEKCALLIldkiqDESLINAKNSALQTPLHIAARNGLKV-VVEELLAKGACVLAVDENGHTP 996
Cdd:PHA02874   226 PLHNAIIHNRSAIELLI-----NNASINDQDIDGSTPLHHAINPPCDIdIIDILLYHKADISIKDNKGENP 291
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 49-326 2.50e-08

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 58.00  E-value: 2.50e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   49 AFLG----DAEIIELLILSGARVNAKDNMWLTPLHRAV--ASRSEEAVQVLIKHSADVNARDKNWQSPVHVAAANKAVKC 122
Cdd:PHA02716   183 AYLGnmyvDIDILEWLCNNGVNVNLQNNHLITPLHTYLitGNVCASVIKKIIELGGDMDMKCVNGMSPIMTYIINIDNIN 262

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  123 AEVI----------------------IPLLSSVNVS---------------DRGGRTALHHAAL--NGHMEMVNLLLAKG 163
Cdd:PHA02716   263 PEITniyiesldgnkvknipmilhsyITLARNIDISvvysflqpgvklhykDSAGRTCLHQYILrhNISTDIIKLLHEYG 342

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  164 ANINAFDKKDRRALHwaAYMG----------------HLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQ--------- 218
Cdd:PHA02716   343 NDLNEPDNIGNTVLH--TYLSmlsvvnildpetdndiRLDVIQCLISLGADITAVNCLGYTPLTSYICTAQnymyydiid 420

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  219 -------INVVKH--LLNLGVEIDE---------------INVYGNTALHIACYNGQDAVVNELIDYGANVNQPnNSGFT 274
Cdd:PHA02716   421 clisdkvLNMVKHriLQDLLIRVDDtpciihhiiakynipTDLYTDEYEPYDSTKIHDVYHCAIIERYNNAVCE-TSGMT 499

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903808  275 PLHFAAASTHGAL----CLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI 326
Cdd:PHA02716   500 PLHVSIISHTNANivmdSFVYLLSIQYNINIPTKNGVTPLMLTMRNNRLSGHQWYI 555
Ank_4 pfam13637
Ankyrin repeats (many copies);
206-259 2.86e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 2.86e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1046903808  206 GYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELI 259
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 609-831 2.91e-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: 2.91e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  609 VDLDIRDEKGRTALYLAAFKG-HTECVEALVNQGASIFVKDNVtkrtpLHASVINGH---TLCLRLLLEIA---DNPEVV 681
Cdd:TIGR00870   43 LNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTL-----LHAISLEYVdavEAILLHLLAAFrksGPLELA 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  682 DVKDA----KGQTPLMLAVAYGHIDAVSLLLEKEANVDAvdTVGCTALHRGIM----------------TGHEECVQMLL 741
Cdd:TIGR00870  118 NDQYTseftPGITALHLAAHRQNYEIVKLLLERGASVPA--RACGDFFVKSQGvdsfyhgesplnaaacLGSPSIVALLS 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  742 EQEASILCKDSRGRTPLHYAAARGHATWLNE-------------LVQIALSEEDCCLKDNQGYTPLHWACYNGNENCIEV 808
Cdd:TIGR00870  196 EDPADILTADSLGNTLLHLLVMENEFKAEYEelscqmynfalslLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRL 275

                          250       260
                   ....*....|....*....|....
gi 1046903808  809 LLEQKCF-RKFIGNPFTPLHCAII 831
Cdd:TIGR00870  276 KLAIKYKqKKFVAWPNGQQLLSLY 299
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 274-461 3.84e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 57.33  E-value: 3.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  274 TPLhFAAASTHGALCLE-LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGE-----IDCVDKDGNTPLHVAA 347
Cdd:cd22192     19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  348 RYGHELLINTLITSGADTAK---CGihSMFPLHLAALnahsdccrkllssgqkysivsLFSNEHVLSagfeidtpdtFgr 424
Cdd:cd22192     98 VNQNLNLVRELIARGADVVSpraTG--TFFRPGPKNL---------------------IYYGEHPLS----------F-- 142

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1046903808  425 tclhaAAAGGNVECIKLLQSSGADFHKKDKCGRTPLH 461
Cdd:cd22192    143 -----AACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 12-97 4.51e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 4.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   12 LVQAIFSGDPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQ 91
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165


                   ....*.
gi 1046903808   92 VLIKHS 97
Cdd:PTZ00322   166 LLSRHS 171
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 494-719 5.96e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.19  E-value: 5.96e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  494 HYAAASDMDRNKMILGNA--HDNSEELERAREVKGKDAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQClellle 571
Cdd:PLN03192   500 HHKELHDLNVGDLLGDNGgeHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDC------ 573

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  572 rtntgfeesdggalksplhlaaynghhqaLEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALvNQGASIfvKDNVT 651
Cdd:PLN03192   574 -----------------------------VLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL-YHFASI--SDPHA 621

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046903808  652 KRTPLHASVINGHTLCLRLLLEIADNpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDT 719
Cdd:PLN03192   622 AGDLLCTAAKRNDLTAMKELLKQGLN---VDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANT 686
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 11-171 7.02e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.13  E-value: 7.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   11 PLVQAIFSGDPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVA-SRSeeA 89
Cdd:PHA02874   160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIhNRS--A 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   90 VQVLIkHSADVNARDKNWQSPVHVAAankAVKCAEVIIPLL----SSVNVSDRGGRTALHHA-ALNGHMEMVNLLLAKGA 164
Cdd:PHA02874   238 IELLI-NNASINDQDIDGSTPLHHAI---NPPCDIDIIDILlyhkADISIKDNKGENPIDTAfKYINKDPVIKDIIANAV 313


                   ....*..
gi 1046903808  165 NINAFDK 171
Cdd:PHA02874   314 LIKEADK 320
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 871-1060 7.87e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.83  E-value: 7.87e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  871 ECLQLLLRHDAQVNAVDNSGKTALMMAAEN--GQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEK---CALLILD 945
Cdd:PHA03100    87 EIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDlkiLKLLIDK 165

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  946 K------------IQDESLINAKNSALQTPLHIAARNGLKVVVEELLAKGACVLAVDENGHTPALACAPNKDVAdclalI 1013
Cdd:PHA03100   166 GvdinaknrvnylLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKE-----I 240

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*..
gi 1046903808 1014 LATMMTFSPSSTMTAVNFVYFRKDNLSRRTLSNMGSRVSLCSNNLDS 1060
Cdd:PHA03100   241 FKLLLNNGPSIKTIIETLLYFKDKDLNTITKIKMLKKSIMYMFLLDP 287
PHA02946 PHA02946
ankyin-like protein; Provisional
 323-571 9.35e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 55.83  E-value: 9.35e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  323 QTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHL-------------------AALNA 383
Cdd:PHA02946    56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsgtddevierinllvqygAKINN 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  384 HSD--CCRKLLSSGQKYSIVSlfsnEHVLSAGFEIDTPDTFGRTCLHAAAAGGN--VECIKLLQSSGADFHKKDKCGRTP 459
Cdd:PHA02946   136 SVDeeGCGPLLACTDPSERVF----KKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHDGNTP 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  460 LHYAAANCHFHC-IKALVTTGANINETDNWGRTALHYAAASdmdrnkmiLGNAHDNSEELERAREVKGKDAALCLeFLLQ 538
Cdd:PHA02946   212 LHIVCSKTVKNVdIINLLLPSTDVNKQNKFGDSPLTLLIKT--------LSPAHLINKLLSTSNVITDQTVNICI-FYDR 282

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1046903808  539 NDANPSIRDK-EGYNSIHY--AAAYGHRQCLELLLE 571
Cdd:PHA02946   283 DDVLEIINDKgKQYDSTDFkmAVEVGSIRCVKYLLD 318
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 289-493 1.15e-07

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 56.07  E-value: 1.15e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  289 LELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRS--QTLIQNGGEIDCVDKDGNTPLH---VAARYGHELLINTLITSGA 363
Cdd:PHA02716   195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASviKKIIELGGDMDMKCVNGMSPIMtyiINIDNINPEITNIYIESLD 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  364 DTAKCGIHSMFPLHLAalnahsdccrklLSSGQKYSIVslfsnEHVLSAGFEIDTPDTFGRTCLHAAAAGGNV--ECIKL 441
Cdd:PHA02716   275 GNKVKNIPMILHSYIT------------LARNIDISVV-----YSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKL 337

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903808  442 LQSSGADFHKKDKCGRTPLH-YAAANCHFH-------------CIKALVTTGANINETDNWGRTAL 493
Cdd:PHA02716   338 LHEYGNDLNEPDNIGNTVLHtYLSMLSVVNildpetdndirldVIQCLISLGADITAVNCLGYTPL 403
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 429-644 1.20e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 1.20e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  429 AAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANINETDNWGRTALHYAAASDMDRNKMIL 508
Cdd:PLN03192   531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  509 gnahdnseelerarevkgkdaalclefllqndanpsirdkegynsIHYAAAyghrqclelllertntgfeeSDGGALKSP 588
Cdd:PLN03192   611 ---------------------------------------------YHFASI--------------------SDPHAAGDL 625

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903808  589 LHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASI 644
Cdd:PLN03192   626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_4 pfam13637
Ankyrin repeats (many copies);
723-766 1.83e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 1.83e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1046903808  723 TALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGH 766
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 281-350 1.85e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 1.85e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  281 ASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYG 350
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
Ank_5 pfam13857
Ankyrin repeats (many copies);
192-246 2.10e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 2.10e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903808  192 LINHG-AEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIA 246
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 20-168 2.18e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.65  E-value: 2.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   20 DPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGD--AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHS 97
Cdd:PHA03095   201 RARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1046903808   98 ADVNARDKNwqspvhvaaankavkcaeviipllssvnvsdrgGRTALHHAALNGHMEMVNLLLAKGANINA 168
Cdd:PHA03095   281 ADINAVSSD---------------------------------GNTPLSLMVRNNNGRAVRAALAKNPSAET 318
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 209-368 2.81e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 52.51  E-value: 2.81e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  209 PLHAAASNGQINVVKHLLNLgveIDEINVYGNTALHiACYNGQDAVVNE---LIDYGANVN-QPNNSGFTPLHFAAASTH 284
Cdd:PHA02859    24 PLFYYVEKDDIEGVKKWIKF---VNDCNDLYETPIF-SCLEKDKVNVEIlkfLIENGADVNfKTRDNNLSALHHYLSFNK 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  285 GAL--CLELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLI-NTLI 359
Cdd:PHA02859   100 NVEpeILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKKIfDFLT 179


                   ....*....
gi 1046903808  360 TSGADTAKC 368
Cdd:PHA02859   180 SLGIDINET 188
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 77-250 3.66e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 52.13  E-value: 3.66e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   77 PLHRAVASRSEEAVQVLIKHSADVNardKNWQSPVHVAAANKAV--KCAEVIIPLLSSVNVSDRGGRTALHHAAL----N 150
Cdd:PHA02859    24 PLFYYVEKDDIEGVKKWIKFVNDCN---DLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRDNNLSALHHYLsfnkN 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  151 GHMEMVNLLLAKGANINAFDKKDRRALHwaAYMGH----LDVVALLINHGAEVTCKDKKGYTPLHA-AASNGQINVVKHL 225
Cdd:PHA02859   101 VEPEILKILIDSGSSITEEDEDGKNLLH--MYMCNfnvrINVIKLLIDSGVSFLNKDFDNNNILYSyILFHSDKKIFDFL 178

                          170       180
                   ....*....|....*....|....*
gi 1046903808  226 LNLGVEIDEINVYGNTALHIACYNG 250
Cdd:PHA02859   179 TSLGIDINETNKSGYNCYDLIKFRN 203
Ank_4 pfam13637
Ankyrin repeats (many copies);
239-293 4.24e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 4.24e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1046903808  239 GNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGAlCLELLV 293
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
42-94 4.33e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 4.33e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1046903808   42 RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLI 94
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 325-482 5.18e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.10  E-value: 5.18e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  325 LIQNGGEIDCVDKDGNtpLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGQKYSIVSLF 404
Cdd:PLN03192   513 LGDNGGEHDDPNMASN--LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDAN 590

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  405 SNE---HVLSAG----FEI-------DTPDTFGrTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFH 470
Cdd:PLN03192   591 GNTalwNAISAKhhkiFRIlyhfasiSDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVD 669

                          170
                   ....*....|..
gi 1046903808  471 CIKALVTTGANI 482
Cdd:PLN03192   670 MVRLLIMNGADV 681
Ank_4 pfam13637
Ankyrin repeats (many copies);
74-160 5.53e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 5.53e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   74 WLTPLHRAVASRSEEAVQVLIKHSADVNARDKNwqspvhvaaankavkcaeviipllssvnvsdrgGRTALHHAALNGHM 153
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN---------------------------------GETALHFAASNGNV 47


                   ....*..
gi 1046903808  154 EMVNLLL 160
Cdd:pfam13637   48 EVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 69-198 7.12e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 7.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   69 AKDNMWLTPLHRAVasrSEEAVQVLIKHSADVNArdknwqspVHVAAANKAVKcAEVIIPLLSSVNVSDRGGRTALHHAA 148
Cdd:PTZ00322    56 ATENKDATPDHNLT---TEEVIDPVVAHMLTVEL--------CQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIAC 123

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1046903808  149 LNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAE 198
Cdd:PTZ00322   124 ANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 407-513 7.72e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.33  E-value: 7.72e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  407 EHVLSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPL-------HYAAANCHFHC-------- 471
Cdd:PLN03192   542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHHKIFRILYHFasisdpha 621

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1046903808  472 ----------------IKALVTTGANINETDNWGRTALHYAAASD-MDRNKMILGNAHD 513
Cdd:PLN03192   622 agdllctaakrndltaMKELLKQGLNVDSEDHQGATALQVAMAEDhVDMVRLLIMNGAD 680
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 11-171 1.32e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 50.20  E-value: 1.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   11 PLVQAIFSGDPEEIRLLIHKTEDVNALDsekRTPLH--VAAFLGDAEIIELLILSGARVNAK---DNmwLTPLHRAVA-- 83
Cdd:PHA02859    24 PLFYYVEKDDIEGVKKWIKFVNDCNDLY---ETPIFscLEKDKVNVEILKFLIENGADVNFKtrdNN--LSALHHYLSfn 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   84 -SRSEEAVQVLIKHSADVNARDKNWQSPVHVAAANKAVKCAevIIPLLSSVNVS----DRGGRTALH-HAALNGHMEMVN 157
Cdd:PHA02859    99 kNVEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRIN--VIKLLIDSGVSflnkDFDNNNILYsYILFHSDKKIFD 176

                          170
                   ....*....|....
gi 1046903808  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 1046903808  189 VALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDY 261
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 870-1013 1.70e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.53  E-value: 1.70e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  870 AECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKDLNTPLHLA-ISKGHEKCALLILDKIQ 948
Cdd:PHA02875    48 SEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLAtILKKLDIMKLLIARGAD 127

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046903808  949 DEslinAKNSALQTPLHIAARNGLKVVVEELLAKGACVLAVDENGHTPALACAPNKDVADCLALI 1013
Cdd:PHA02875   128 PD----IPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188
Ank_4 pfam13637
Ankyrin repeats (many copies);
754-810 1.72e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 1.72e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046903808  754 GRTPLHYAAARGHatwlNELVQIAL-SEEDCCLKDNQGYTPLHWACYNGNENCIEVLL 810
Cdd:pfam13637    1 ELTALHAAAASGH----LELLRLLLeKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
857-910 2.04e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 2.04e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1046903808  857 GRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILV 910
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 2.32e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 2.32e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1046903808   10 PPLVQAIFSGDPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLI 61
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
790-842 3.57e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 3.57e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1046903808  790 GYTPLHWACYNGNENCIEVLLEQKC-FRKFIGNPFTPLHCAIINGHESCASLLL 842
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGAdINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 587-813 3.63e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.65  E-value: 3.63e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  587 SPLHLAAYNGHHQALEVLLQSLVDLDIRDE--KGRTALY---LAAFKghtecvEALVNQGASIFVKDNVTKRTPLHASVI 661
Cdd:PHA02878    72 TPLHIICKEPNKLGMKEMIRSINKCSVFYTlvAIKDAFNnrnVEIFK------IILTNRYKNIQTIDLVYIDKKSKDDII 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  662 NghTLCLRLLLEIADNPEVVDvkDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLL 741
Cdd:PHA02878   146 E--AEITKLLLSYGADINMKD--RHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL 221

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046903808  742 EQEASILCKDSRGRTPLHYAAARghatWLNELVQIALSEEDCCLKDNQ---GYTPLHWACYngNENCIEVLLEQK 813
Cdd:PHA02878   222 ENGASTDARDKCGNTPLHISVGY----CKDYDILKLLLEHGVDVNAKSyilGLTALHSSIK--SERKLKLLLEYG 290
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 431-500 4.35e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 4.35e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  431 AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANINETDNWGRTALHYAAASD 500
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
Ank_4 pfam13637
Ankyrin repeats (many copies);
308-359 4.74e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 4.74e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1046903808  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 5.02e-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: 5.02e-06
                            10        20
                    ....*....|....*....|....*....
gi 1046903808   140 GRTALHHAALNGHMEMVNLLLAKGANINA 168
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 653-910 6.20e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.99  E-value: 6.20e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  653 RTPLHASVINGHTLCLRLLLEIADNP--EVVDvkdakGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIM 730
Cdd:PHA02875     3 QVALCDAILFGELDIARRLLDIGINPnfEIYD-----GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVE 77

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  731 TGHEECVQMLLEQEA---SILCKDsrGRTPLHYAAARGHATWLNELVQialSEEDCCLKDNQGYTPLHWACYNGNENCIE 807
Cdd:PHA02875    78 EGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIA---RGADPDIPNTDKFSPLHLAVMMGDIKGIE 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  808 VLLEQK-CFRKFIGNPFTPLHCAIINGH-ESCASLLLGAIDSSIVSCRDDKgrTTLHAAAFGDHAECLQLLLRHDAQVN- 884
Cdd:PHA02875   153 LLIDHKaCLDIEDCCGCTPLIIAMAKGDiAICKMLLDSGANIDYFGKNGCV--AALCYAIENNKIDIVRLFIKRGADCNi 230

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1046903808  885 --AVDNSGKTALMMAAE---NGQAGAVDILV 910
Cdd:PHA02875   231 mfMIEGEECTILDMICNmctNLESEAIDALI 261
Ank_5 pfam13857
Ankyrin repeats (many copies);
158-213 6.76e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 6.76e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903808  158 LLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 213
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 561-800 6.78e-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: 6.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  561 GHRQCLELLLertnTGFEESDGGALKSPLHLAAYNGHHQALE---VLLQS---------LVDLDIRDE--KGRTALYLAA 626
Cdd:cd21882      6 GLLECLRWYL----TDSAYQRGATGKTCLHKAALNLNDGVNEaimLLLEAapdsgnpkeLVNAPCTDEfyQGQTALHIAI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  627 FKGHTECVEALVNQGASIFVKDNVT--KRTPlhasvingHTLCLRllleiadnpevvdvkdakGQTPLMLAVAYGHIDAV 704
Cdd:cd21882     82 ENRNLNLVRLLVENGADVSARATGRffRKSP--------GNLFYF------------------GELPLSLAACTNQEEIV 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  705 SLLLE---KEANVDAVDTVGCTALHRGIMTGHEE------CVQM---LLEQEASI-------LCKDSRGRTPLHYAAARG 765
Cdd:cd21882    136 RLLLEngaQPAALEAQDSLGNTVLHALVLQADNTpensafVCQMynlLLSYGAHLdptqqleEIPNHQGLTPLKLAAVEG 215

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1046903808  766 HATWLNELVQIALSEEDCCL--KDNQ-GYTPLHWACYN 800
Cdd:cd21882    216 KIVMFQHILQREFSGPYQPLsrKFTEwTYGPVTSSLYD 253
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 854-990 8.01e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.25  E-value: 8.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  854 DDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKDLntpLHLAIS 933
Cdd:PLN03192   555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL---LCTAAK 631

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046903808  934 KGHekcaLLILDKIQDESL-INAKNSALQTPLHIAARNGLKVVVEELLAKGACVLAVD 990
Cdd:PLN03192   632 RND----LTAMKELLKQGLnVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 43-180 8.42e-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: 8.42e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   43 TPLHVAAFLGDAEIIELLILSGARVNA-----------KDNMWL---TPLHRAVASRSEEAVQVLIKHSADVNARDKNWQ 108
Cdd:cd22192     91 TALHIAVVNQNLNLVRELIARGADVVSpratgtffrpgPKNLIYygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  109 SPVH--VAAANKAVKCaEVIIPLLSSV---------NVSDRGGRTALHHAALNGHMEMVNLLLAKganinafdkkdRRAL 177
Cdd:cd22192    171 TVLHilVLQPNKTFAC-QMYDLILSYDkeddlqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQK-----------RRHI 238


                   ...
gi 1046903808  178 HWA 180
Cdd:cd22192    239 QWT 241
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 140-282 1.03e-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: 1.03e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  140 GRTALHHAALN---GHMEMVNLLL---AKGANINAF------DK--KDRRALHWAAYMGHLDVVALLINHGAEVTC---- 201
Cdd:cd22196     47 GKTCLLKAMLNlhnGQNDTISLLLdiaEKTGNLKEFvnaaytDSyyKGQTALHIAIERRNMHLVELLVQNGADVHArasg 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  202 ------KDKKGY----TPLHAAASNGQINVVKHLLN---LGVEIDEINVYGNTALH----IAcYNGQD------AVVNEL 258
Cdd:cd22196    127 effkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLHalveVA-DNTPEntkfvtKMYNEI 205

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1046903808  259 IDYGANVNQ-------PNNSGFTPLHFAAAS 282
Cdd:cd22196    206 LILGAKIRPllkleeiTNKKGLTPLKLAAKT 236
Ank_4 pfam13637
Ankyrin repeats (many copies);
824-877 1.14e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 1.14e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1046903808  824 TPLHCAIINGHESCASLLLGAidSSIVSCRDDKGRTTLHAAAFGDHAECLQLLL 877
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEK--GADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 140-171 1.39e-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: 1.39e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1046903808  140 GRTALHHAAL-NGHMEMVNLLLAKGANINAFDK 171
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
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 1046903808   20 DPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSE--EAVQVLIKHS 97
Cdd:PHA02946    51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEviERINLLVQYG 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808   98 ADV-NARDKNWQSPVhVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAAL--NGHMEMVNLLLAKGANINAFDKKDR 174
Cdd:PHA02946   131 AKInNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMsdNPKASTISWMMKLGISPSKPDHDGN 209

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1046903808  175 RALH--WAAYMGHLDVVALLINhGAEVTCKDKKGYTPL 210
Cdd:PHA02946   210 TPLHivCSKTVKNVDIINLLLP-STDVNKQNKFGDSPL 246
Ank_5 pfam13857
Ankyrin repeats (many copies);
26-81 1.67e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 1.67e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903808   26 LLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRA 81
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 738-982 1.68e-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: 1.68e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  738 QMLLEQEasiLCKDSRGR-TPLHYAAARGHATWLNELvqiaLSEEDC--CLKDNQGYTPLHWACYNGNENCIEVLLEqkC 814
Cdd:cd22192      3 QMLDELH---LLQQKRISeSPLLLAAKENDVQAIKKL----LKCPSCdlFQRGALGETALHVAALYDNLEAAVVLME--A 73

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  815 FRKFIGNPFT--------PLHCAIINGHESCASLLL--GAidsSIVSCRDD-----KGRTTLhaAAFGDHAeclqlllrh 879
Cdd:cd22192     74 APELVNEPMTsdlyqgetALHIAVVNQNLNLVRELIarGA---DVVSPRATgtffrPGPKNL--IYYGEHP--------- 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  880 daqvnavdnsgktaLMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCA------LLILDKIQDE-SL 952
Cdd:cd22192    140 --------------LSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVLHILVLQPNKTFAcqmydlILSYDKEDDLqPL 204

                          250       260       270
                   ....*....|....*....|....*....|
gi 1046903808  953 INAKNSALQTPLHIAARNGLKVVVEELLAK 982
Cdd:cd22192    205 DLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 662-741 1.69e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 1.69e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  662 NGHTLCLRLLLEIADNPevvDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLL 741
Cdd:PTZ00322    92 SGDAVGARILLTGGADP---NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 898-993 1.81e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 1.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  898 AENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDESLINAKNsalQTPLHIAARNGLKVVVE 977
Cdd:PTZ00322    90 AASGDAVGARILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDG---KTPLELAEENGFREVVQ 165

                           90
                   ....*....|....*.
gi 1046903808  978 ELLAKGACVLAVDENG 993
Cdd:PTZ00322   166 LLSRHSQCHFELGANA 181
Ank_5 pfam13857
Ankyrin repeats (many copies);
441-496 1.82e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 1.82e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903808  441 LLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANINETDNWGRTALHYA 496
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 213-350 2.01e-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: 2.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  213 AASNGqinVVKHLLNlgVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVN--------QP--NNSGF----TPLHF 278
Cdd:cd22194    120 AEENG---ILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffNPkyKHEGFyfgeTPLAL 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  279 AAASTHGALcLELLVNNGADvNIQSKD--GKSPLHMTAVHGRFTRSQT-----------LIQNGGEIDCV-DKDGNTPLH 344
Cdd:cd22194    195 AACTNQPEI-VQLLMEKEST-DITSQDsrGNTVLHALVTVAEDSKTQNdfvkrmydmilLKSENKNLETIrNNEGLTPLQ 272


                   ....*.
gi 1046903808  345 VAARYG 350
Cdd:cd22194    273 LAAKMG 278
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 840-916 2.04e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 2.04e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1046903808  840 LLLGAIDSSivsCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQAD 916
Cdd:PTZ00322   101 LLTGGADPN---CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCH 174
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 692-777 2.48e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.33  E-value: 2.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  692 LMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHATWLN 771
Cdd:PLN03192   529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608


                   ....*.
gi 1046903808  772 ELVQIA 777
Cdd:PLN03192   609 ILYHFA 614
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 211-314 2.57e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 2.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  211 HAAASNGQINVvKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLE 290
Cdd:PTZ00322    88 QLAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV-VQ 165

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1046903808  291 LLV-------NNGADVNIQSKDGK------SPLHMTA 314
Cdd:PTZ00322   166 LLSrhsqchfELGANAKPDSFTGKppsledSPISSHH 202
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 376-494 2.60e-05

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 48.34  E-value: 2.60e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  376 LHLAALNAHS---DCCRKLLSSGQKYSIVSLFSNEHVLSAGFEidtpdtfGRTCLHAAAAGGNVECIKLLQSSGADFH-- 450
Cdd:cd21882     30 LHKAALNLNDgvnEAIMLLLEAAPDSGNPKELVNAPCTDEFYQ-------GQTALHIAIENRNLNLVRLLVENGADVSar 102

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046903808  451 ------KKDKC-----GRTPLHYAAANCHFHCIKALVTTGANI---NETDNWGRTALH 494
Cdd:cd21882    103 atgrffRKSPGnlfyfGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNTVLH 160
Ank_4 pfam13637
Ankyrin repeats (many copies);
375-442 2.94e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 2.94e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1046903808  375 PLHLAALNAHSDCCRKLLSSGqkysivslfsnehvlsagFEIDTPDTFGRTCLHAAAAGGNVECIKLL 442
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKG------------------ADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 140-168 3.02e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.86  E-value: 3.02e-05
                           10        20
                   ....*....|....*....|....*....
gi 1046903808  140 GRTALHHAALNGHMEMVNLLLAKGANINA 168
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
236-279 3.32e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.32e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1046903808  236 NVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFA 279
Cdd:pfam13857   13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 669-801 3.33e-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: 3.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  669 RLLLEIADNPEVVDV--------KDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDT--------------VGCTALH 726
Cdd:cd22194    114 RILLAFAEENGILDRfinaeyteEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLA 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  727 RGIMTGHEECVQMLLEQEAS-ILCKDSRGRTPLHYAA-----ARGHATWLNELV-QIALSEEDCCL---KDNQGYTPLHW 796
Cdd:cd22194    194 LAACTNQPEIVQLLMEKESTdITSQDSRGNTVLHALVtvaedSKTQNDFVKRMYdMILLKSENKNLetiRNNEGLTPLQL 273


                   ....*
gi 1046903808  797 ACYNG 801
Cdd:cd22194    274 AAKMG 278
Ank_5 pfam13857
Ankyrin repeats (many copies);
258-312 3.55e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.55e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1046903808  258 LIDYG-ANVNQPNNSGFTPLHFAAasTHGAL-CLELLVNNGADVNIQSKDGKSPLHM 312
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAA--KYGALeIVRVLLAYGVDLNLKDEEGLTALDL 55
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 892-986 3.57e-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: 3.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  892 TALMMAAENGQAGAVDILVNSAQADLTVKDKDLNTPLHLAISKGHEKCALLILDkiQDESLIN-AKNSAL---QTPLHIA 967
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNePMTSDLyqgETALHIA 96

                           90
                   ....*....|....*....
gi 1046903808  968 ARNGLKVVVEELLAKGACV 986
Cdd:cd22192     97 VVNQNLNLVRELIARGADV 115
Ank_4 pfam13637
Ankyrin repeats (many copies);
618-672 3.69e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 3.69e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1046903808  618 GRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLCLRLLL 672
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
653-708 3.92e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 3.92e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903808  653 RTPLHASVINGHTLCLRLLLEiadNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLL 708
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLE---KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 862-955 4.32e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 4.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  862 HAAAFGDhAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCAL 941
Cdd:PTZ00322    88 QLAASGD-AVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFREVVQ 165

                           90
                   ....*....|....
gi 1046903808  942 LILDKIQDESLINA 955
Cdd:PTZ00322   166 LLSRHSQCHFELGA 179
Ank_5 pfam13857
Ankyrin repeats (many copies);
875-931 4.37e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 4.37e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1046903808  875 LLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLA 931
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
PHA02791 PHA02791
ankyrin-like protein; Provisional
 768-963 4.73e-05

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 46.57  E-value: 4.73e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  768 TWLNELVQIALSEEDCCLKDNQGYTPLHWACYNGNENCIEVLLEQKCFRKFIGNPFtPLH-CAIINGHESCASLLLGAID 846
Cdd:PHA02791     8 TWKSKQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF-PLHqAATLEDTKIVKILLFSGMD 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  847 SSIVscrDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSG-KTALMMAAENGQAGAVDILVNSAQA--DLTVkdkd 923
Cdd:PHA02791    87 DSQF---DDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPStfDLAI---- 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1046903808  924 LNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTP 963
Cdd:PHA02791   160 LLSCIHITIKNGHVDMMILLLDYMTS---TNTNNSLLFIP 196
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 238-266 4.98e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.03  E-value: 4.98e-05
                            10        20
                    ....*....|....*....|....*....
gi 1046903808   238 YGNTALHIACYNGQDAVVNELIDYGANVN 266
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 236-313 8.53e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 45.74  E-value: 8.53e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  236 NVYGNTALHIACYNGQDAVVNeLIDYGANVNQ-PNNSGFTPLHFAAasTHGAL-CLELLVNNGADVNIQSKDGKSPLHMT 313
Cdd:PHA02884    68 NSKTNPLIYAIDCDNDDAAKL-LIRYGADVNRyAEEAKITPLYISV--LHGCLkCLEILLSYGADINIQTNDMVTPIELA 144
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 310-399 8.91e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 8.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  310 LHMTAVH-------GRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALN 382
Cdd:PTZ00322    79 AHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158

                           90
                   ....*....|....*..
gi 1046903808  383 AHSDCCRKLLSSGQKYS 399
Cdd:PTZ00322   159 GFREVVQLLSRHSQCHF 175
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 140-282 9.48e-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: 9.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  140 GRTALHHAALNGHMEMVNLLLAKGANINA------FDKKDRRA--------LHWAAYMGHLDVVALLINHG---AEVTCK 202
Cdd:cd22193     76 GQTALHIAIERRQGDIVALLVENGADVHAhakgrfFQPKYQGEgfyfgelpLSLAACTNQPDIVQYLLENEhqpADIEAQ 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  203 DKKGYTPLHAAasngqinvvkhllnlgVEIDEiNVYGNTALHIACYNGqdavvneLIDYGANVNQP-------NNSGFTP 275
Cdd:cd22193    156 DSRGNTVLHAL----------------VTVAD-NTKENTKFVTRMYDM-------ILIRGAKLCPTveleeirNNDGLTP 211


                   ....*..
gi 1046903808  276 LHFAAAS 282
Cdd:cd22193    212 LQLAAKM 218
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 140-280 9.91e-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: 9.91e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  140 GRTALHHAALNGHMEMVNLLLAKGANINA------FDKKDRR--------ALHWAAYMGHLDVVALLINHGAE-VTCKDK 204
Cdd:cd22194    141 GQTALNIAIERRQGDIVKLLIAKGADVNAhakgvfFNPKYKHegfyfgetPLALAACTNQPEIVQLLMEKESTdITSQDS 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  205 KGYTPLHAAA-----SNGQINVVKHLLnlgveiDEI-NVYGNTALhiacyngqdavvnELIdyganvnqPNNSGFTPLHF 278
Cdd:cd22194    221 RGNTVLHALVtvaedSKTQNDFVKRMY------DMIlLKSENKNL-------------ETI--------RNNEGLTPLQL 273


                   ..
gi 1046903808  279 AA 280
Cdd:cd22194    274 AA 275
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 238-270 1.00e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 1.00e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1046903808  238 YGNTALHIACY-NGQDAVVNELIDYGANVNQPNN 270
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
132-180 1.10e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 1.10e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1046903808  132 SVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWA 180
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
339-392 1.48e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 1.48e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1046903808  339 GNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLL 392
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 7-114 1.63e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 1.63e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808    7 CDQPPLVQAIFSGDPEEIRLLIHKTEDVNALDSEKRTPLHVAAFLGDAEI-IELLILSGARVNAKDNMWLTPLHRAVASR 85
Cdd:PHA02876   374 CDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKN 453

                           90       100       110
                   ....*....|....*....|....*....|
gi 1046903808   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 ...
 690-901 1.65e-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: 1.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  690 TPLMLAVAYGHIDAVS-LLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLEqeasilckdsrgrtplhyaAARghat 768
Cdd:cd22192     19 SPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME-------------------AAP---- 75

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  769 wlnELVQIALSEEDcclkdNQGYTPLHWACYNGNENCIEVLLEQ-----------KCFRKFIGNPFT----PLHCAIING 833
Cdd:cd22192     76 ---ELVNEPMTSDL-----YQGETALHIAVVNQNLNLVRELIARgadvvspratgTFFRPGPKNLIYygehPLSFAACVG 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  834 HESCASLLL--GAidsSIVScRDDKGRTTLHAAAFGDHA----ECLQLLLRHDAQVNAV------DNSGKTALMMAAENG 901
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 ...
 456-484 1.71e-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: 1.71e-04
                            10        20
                    ....*....|....*....|....*....
gi 1046903808   456 GRTPLHYAAANCHFHCIKALVTTGANINE 484
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 624-708 1.82e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 1.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  624 LAAfKGHTECVEALVNQGASIFVKDnVTKRTPLHASVINGHTLCLRLLLEIADNPEVVDvKDakGQTPLMLAVAYGHIDA 703
Cdd:PTZ00322    89 LAA-SGDAVGARILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLD-KD--GKTPLELAEENGFREV 163


                   ....*
gi 1046903808  704 VSLLL 708
Cdd:PTZ00322   164 VQLLS 168
PHA02946 PHA02946
ankyin-like protein; Provisional
 156-442 1.91e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.04  E-value: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  156 VNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLH-AAASNGQInvvkhllnlgveIDE 234
Cdd:PHA02946    55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYyLSGTDDEV------------IER 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  235 INVygntalhiacyngqdavvneLIDYGANVNQP-NNSGFTPLhfAAASTHGALCLELLVNNGADVNIQSKDGKSPLH-- 311
Cdd:PHA02946   123 INL--------------------LVQYGAKINNSvDEEGCGPL--LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHrh 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  312 MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLH-VAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALN-AHSDCCR 389
Cdd:PHA02946   181 LMSDNPKASTISWMMKLGISPSKPDHDGNTPLHiVCSKTVKNVDIINLLLPSTDVNKQNKFGDSPLTLLIKTlSPAHLIN 260

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  390 KLLSSG-----QKYSIVSLFSNEHVLsagfEI--DTPDTFGRTCLHAAAAGGNVECIKLL 442
Cdd:PHA02946   261 KLLSTSnvitdQTVNICIFYDRDDVL----EIinDKGKQYDSTDFKMAVEVGSIRCVKYL 316
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 423-576 2.09e-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: 2.09e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  423 GRTCLHAAAAGGNVECIKLLQSSGADFH----------KKDKC---GRTPLHYAAANCHFHCIKALVTTG---ANINETD 486
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGADVHaracgrffqkKQGTCfyfGELPLSLAACTKQWDVVNYLLENPhqpASLQAQD 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  487 NWGRTALHYAAasdmdrnkMILGNAHDNSEELERA-REVKGKDAALCLEFLLQndanpSIRDKEGYNSIHYAAAYGHRQC 565
Cdd:cd22197    174 SLGNTVLHALV--------MIADNSPENSALVIKMyDGLLQAGARLCPTVQLE-----EISNHEGLTPLKLAAKEGKIEI 240

                          170
                   ....*....|.
gi 1046903808  566 LELLLERTNTG 576
Cdd:cd22197    241 FRHILQREFSG 251
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 140-280 2.13e-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: 2.13e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  140 GRTALHHAALNGHMEMVNLLLAKGANINA------FDKKDRRALhwaaYMGHLdvvallinhgaevtckdkkgytPLHAA 213
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGADVHAracgrfFQKKQGTCF----YFGEL----------------------PLSLA 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  214 ASNGQINVVKHLLNLGVE---IDEINVYGNTALHIACYNGQDAVVN---------ELIDYGANVNQ-------PNNSGFT 274
Cdd:cd22197    148 ACTKQWDVVNYLLENPHQpasLQAQDSLGNTVLHALVMIADNSPENsalvikmydGLLQAGARLCPtvqleeiSNHEGLT 227


                   ....*.
gi 1046903808  275 PLHFAA 280
Cdd:cd22197    228 PLKLAA 233
Ank_4 pfam13637
Ankyrin repeats (many copies);
532-570 2.15e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 2.15e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1046903808  532 CLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLL 570
Cdd:pfam13637   16 LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 456-487 2.26e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 2.26e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1046903808  456 GRTPLHYAAANC-HFHCIKALVTTGANINETDN 487
Cdd:pfam00023    2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
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 1046903808   205 KGYTPLHAAASNGQINVVKHLLNLGVEIDE 234
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 840-1003 2.43e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 2.43e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  840 LLLGAIDssiVSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQadlTV 919
Cdd:PHA02876   164 LLEGGAD---VNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS---NI 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  920 KDKDLNtpLHLAISKGHEKCALLILDKiqdESLINAKNSALQTPLHIAARN-GLKVVVEELLAKGACVLAVDENGHTPAL 998
Cdd:PHA02876   238 NKNDLS--LLKAIRNEDLETSLLLYDA---GFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLY 312


                   ....*
gi 1046903808  999 ACAPN 1003
Cdd:PHA02876   313 LMAKN 317
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 332-494 2.65e-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: 45.07  E-value: 2.65e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  332 IDCVDKDGNTPLHVAARYG-HELLINTLITSGA-----DTAkcgihsmfpLHLAALNAH---SDCCRKLLSSGQKYSIVS 402
Cdd:TIGR00870   45 INCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISLEYVdavEAILLHLLAAFRKSGPLE 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  403 LfsnehvlsaGFEIDTPD-TFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKC--------------GRTPLHYAAANC 467
Cdd:TIGR00870  116 L---------ANDQYTSEfTPGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLG 186

                          170       180
                   ....*....|....*....|....*..
gi 1046903808  468 HFHCIKALVTTGANINETDNWGRTALH 494
Cdd:TIGR00870  187 SPSIVALLSEDPADILTADSLGNTLLH 213
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 272-304 2.65e-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: 2.65e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1046903808  272 GFTPLHFAAASTHGALCLELLVNNGADVNIQSK 304
Cdd:pfam00023    2 GNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 661-783 3.04e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 3.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  661 INGHTLCLRLLLEIADNP-------EVVDVKDAKgqtplMLAVAYGHIDA------VSLLLEKEANVDAVDTVGCTALHR 727
Cdd:PTZ00322    47 IDTHLEALEATENKDATPdhnltteEVIDPVVAH-----MLTVELCQLAAsgdavgARILLTGGADPNCRDYDGRTPLHI 121

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903808  728 GIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGhatwLNELVQIALSEEDC 783
Cdd:PTZ00322   122 ACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG----FREVVQLLSRHSQC 173
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 861-1014 3.04e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.86  E-value: 3.04e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  861 LHAAAFGDhAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCa 940
Cdd:PLN03192   530 LTVASTGN-AALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDANGNTALWNAISAKHHKI- 606

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1046903808  941 LLILDKIQDESLINAKNSALQTplhiAARNGLKVVVEELLAKGACVLAVDENGHTpALACAPNKDVADCLALIL 1014
Cdd:PLN03192   607 FRILYHFASISDPHAAGDLLCT----AAKRNDLTAMKELLKQGLNVDSEDHQGAT-ALQVAMAEDHVDMVRLLI 675
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 687-718 3.23e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 3.23e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1046903808  687 KGQTPLMLAVA-YGHIDAVSLLLEKEANVDAVD 718
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 201-347 3.36e-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: 3.36e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  201 CKDKKGYTPL-HAAASNGQINVVKHLLNLGVEIDEinvyGNTALHIACYNGQDAVvNELI----------DYGANVNQPN 269
Cdd:TIGR00870   47 CPDRLGRSALfVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLEYVDAV-EAILlhllaafrksGPLELANDQY 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  270 NSGF----TPLHFAAaSTHGALCLELLVNNGADVNIQSKDG---KSPLHMTAVHGRFTRS-----------QTLIQNGGE 331
Cdd:TIGR00870  122 TSEFtpgiTALHLAA-HRQNYEIVKLLLERGASVPARACGDffvKSQGVDSFYHGESPLNaaaclgspsivALLSEDPAD 200

                          170
                   ....*....|....*.
gi 1046903808  332 IDCVDKDGNTPLHVAA 347
Cdd:TIGR00870  201 ILTADSLGNTLLHLLV 216
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 689-912 3.66e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.21  E-value: 3.66e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  689 QTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHAT 768
Cdd:PHA02875     3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  769 WLNELVQIALSEEDCCLKDnqGYTPLHWACYNGNENCIEVLLEQKCFRKFIG-NPFTPLHCAIINGhescaslllgaids 847
Cdd:PHA02875    83 AVEELLDLGKFADDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNtDKFSPLHLAVMMG-------------- 146

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1046903808  848 sivscrDDKGrttlhaaafgdhaecLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNS 912
Cdd:PHA02875   147 ------DIKG---------------IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDS 190
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 46-117 4.10e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 4.10e-04
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046903808   46 HVAAFlGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQSPVHVAAAN 117
Cdd:PTZ00322    88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
PHA02791 PHA02791
ankyrin-like protein; Provisional
 535-709 4.49e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 43.49  E-value: 4.49e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  535 FLLQNDANPSirDKEGYNSIHYAAAYGHRQCLELLLertntgfeesDGGALKS------PLHLAAYNGHHQALEVLLQSL 608
Cdd:PHA02791    17 FLSSKDAFKA--DVHGHSALYYAIADNNVRLVCTLL----------NAGALKNllenefPLHQAATLEDTKIVKILLFSG 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  609 VDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNVTKRTPL-HASVINGHTLCLRLLLEIadnPEVVDVkdAK 687
Cdd:PHA02791    85 MDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWKTSFyHAVMLNDVSIVSYFLSEI---PSTFDL--AI 159

                          170       180
                   ....*....|....*....|..
gi 1046903808  688 GQTPLMLAVAYGHIDAVSLLLE 709
Cdd:PHA02791   160 LLSCIHITIKNGHVDMMILLLD 181
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 856-971 4.92e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.98  E-value: 4.92e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  856 KGRTTLHAAAFGDHAECLQLLLRHDAQVNA---------VDNS-----GKTALMMAAENGQAGAVDILVNSAQADLTVKD 921
Cdd:cd22194    140 EGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQD 219

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1046903808  922 KDLNTPLHLAI-----SKGHEKCALLILDKI----QDESLINAKNSALQTPLHIAARNG 971
Cdd:cd22194    220 SRGNTVLHALVtvaedSKTQNDFVKRMYDMIllksENKNLETIRNNEGLTPLQLAAKMG 278
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 647-759 5.75e-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: 5.75e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  647 KDNVTKRTPLHASVIN---GHTLCLRLLLEIAD---------NPEVVDVKdAKGQTPLMLAVAYGHIDAVSLLLEKEANV 714
Cdd:cd22193     24 TESSTGKTCLMKALLNlnpGTNDTIRILLDIAEktdnlkrfiNAEYTDEY-YEGQTALHIAIERRQGDIVALLVENGADV 102

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1046903808  715 DAVDT--------------VGCTALHRGIMTGHEECVQMLLE---QEASILCKDSRGRTPLH 759
Cdd:cd22193    103 HAHAKgrffqpkyqgegfyFGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLH 164
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 153-272 6.55e-04

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 41.73  E-value: 6.55e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  153 MEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVV---ALLINHGAEVTCKDKK-GYTPLHAAASNGQINVVKHLL-N 227
Cdd:PHA02743    37 MEVAPFISGDGHLLHRYDHHGRQCTHMVAWYDRANAVmkiELLVNMGADINARELGtGNTLLHIAASTKNYELAEWLCrQ 116

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1046903808  228 LGVEIDEINVYGNTALHIAcYNGQDAVVNE-LIDYGANVNQPNNSG 272
Cdd:PHA02743   117 LGVNLGAINYQHETAYHIA-YKMRDRRMMEiLRANGAVCDDPLSIG 161
Ank_5 pfam13857
Ankyrin repeats (many copies);
706-761 6.79e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 6.79e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903808  706 LLLEKEANVDAVDTVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYA 761
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
274-326 6.85e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 6.85e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1046903808  274 TPLHFAAASTHGAlCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI 326
Cdd:pfam13637    3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
925-971 6.92e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 6.92e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1046903808  925 NTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIAARNG 971
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNG 45
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 238-266 7.34e-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: 7.34e-04
                           10        20
                   ....*....|....*....|....*....
gi 1046903808  238 YGNTALHIACYNGQDAVVNELIDYGANVN 266
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_4 pfam13637
Ankyrin repeats (many copies);
550-605 1.02e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 1.02e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903808  550 GYNSIHYAAAYGHRQCLELLLERTNTGFEESDGGAlkSPLHLAAYNGHHQALEVLL 605
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE--TALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 409-466 1.04e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 1.04e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1046903808  409 VLSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAAN 466
Cdd:PTZ00322   101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
Ank_5 pfam13857
Ankyrin repeats (many copies);
844-897 1.17e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.17e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1046903808  844 AIDSSIVSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMA 897
Cdd:pfam13857    3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
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 1046903808  205 KGYTPLHAAASNGQINVVKHLLNLGVEIDE 234
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
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 1046903808  189 VALLINHGAEVTCKDKKGYTPLHAAASNGQIN-VVKHLLNlgVEIDEINVYGntalhiacyngqDAV-VNELIDYGANVN 266
Cdd:PTZ00322    44 IARIDTHLEALEATENKDATPDHNLTTEEVIDpVVAHMLT--VELCQLAASG------------DAVgARILLTGGADPN 109

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1046903808  267 QPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGR 318
Cdd:PTZ00322   110 CRDYDGRTPLHIACANGHVQV-VRVLLEFGADPTLLDKDGKTPLELAEENGF 160
Ank_5 pfam13857
Ankyrin repeats (many copies);
674-726 1.25e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.25e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1046903808  674 IADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDTVGCTALH 726
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
415-463 1.28e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.28e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1046903808  415 EIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYA 463
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 455-484 1.35e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.35e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1046903808  455 CGRTPLHYAAANCHFHCIKALVTTGANINE 484
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 42-72 1.60e-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: 1.60e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1046903808   42 RTPLHVAA-FLGDAEIIELLILSGARVNAKDN 72
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 617-649 1.93e-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: 1.93e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1046903808  617 KGRTALYLAAFK-GHTECVEALVNQGASIFVKDN 649
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 687-716 1.94e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.85  E-value: 1.94e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1046903808  687 KGQTPLMLAVAYGHIDAVSLLLEKEANVDA 716
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
93-147 1.97e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 1.97e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903808   93 LIKH-SADVNARDKNWQSPVHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHA 147
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 789-811 2.02e-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: 2.02e-03
                            10        20
                    ....*....|....*....|...
gi 1046903808   789 QGYTPLHWACYNGNENCIEVLLE 811
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLD 23
PHA02791 PHA02791
ankyrin-like protein; Provisional
 144-275 2.09e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.57  E-value: 2.09e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  144 LHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGY-TPLHAAASNGQINVV 222
Cdd:PHA02791    65 LHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIV 144

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1046903808  223 KHLLNLGVEIDEINVYgNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTP 275
Cdd:PHA02791   145 SYFLSEIPSTFDLAIL-LSCIHITIKNGHVDMMILLLDYMTSTNTNNSLLFIP 196
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 176-204 2.20e-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: 2.20e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1046903808  176 ALHWAAYM-GHLDVVALLINHGAEVTCKDK 204
Cdd:pfam00023    5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
745-797 2.49e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 2.49e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1046903808  745 ASILCKDSRGRTPLHYAAARGHATWLNELVqiaLSEEDCCLKDNQGYTPLHWA 797
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLL---AYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 423-451 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 1046903808   423 GRTCLHAAAAGGNVECIKLLQSSGADFHK 451
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 2.74e-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 1046903808   338 DGNTPLHVAARYGHELLINTLITSGAD 364
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
PHA02795 PHA02795
ankyrin-like protein; Provisional
 124-201 2.97e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 41.52  E-value: 2.97e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  124 EVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMG--------HLDVVALLINH 195
Cdd:PHA02795   205 KLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHLKILEILLRE 284


                   ....*.
gi 1046903808  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 ...
 687-716 3.40e-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: 3.40e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1046903808   687 KGQTPLMLAVAYGHIDAVSLLLEKEANVDA 716
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 4.66e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 4.66e-03
                            10        20
                    ....*....|....*....|....*.
gi 1046903808   176 ALHWAAYMGHLDVVALLINHGAEVTC 201
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
65-114 4.73e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 4.73e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1046903808   65 ARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQSPVHVA 114
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 729-935 4.89e-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: 4.89e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  729 IMTGHEECVQMLLEQeaSILCKDSRGRTPLHYAAARGHATWLNE---LVQIA--------LSEEDCCLKDNQGYTPLHWA 797
Cdd:cd21882      3 ELLGLLECLRWYLTD--SAYQRGATGKTCLHKAALNLNDGVNEAimlLLEAApdsgnpkeLVNAPCTDEFYQGQTALHIA 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  798 CYNGNENCIEVLLEQKC----------FRKFIGNPF----TPLHCAIINGHESCASLLL-GAIDSSIVSCRDDKGRTTLH 862
Cdd:cd21882     81 IENRNLNLVRLLVENGAdvsaratgrfFRKSPGNLFyfgeLPLSLAACTNQEEIVRLLLeNGAQPAALEAQDSLGNTVLH 160

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1046903808  863 AaafgdhaeclqLLLRHDaqvNAVDNSgKTALMMAAENGQAGAVdiLVNSAQADLTVKDKDLnTPLHLAISKG 935
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 5.12e-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: 5.12e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903808   43 TPLHVAAFLGDAEIIELLILSGARVNAKDN--MWLT------------PLHRAVASRSEEAVQVLIKHSADVNARD 104
Cdd:TIGR00870  130 TALHLAAHRQNYEIVKLLLERGASVPARACgdFFVKsqgvdsfyhgesPLNAAACLGSPSIVALLSEDPADILTAD 205
Ank_5 pfam13857
Ankyrin repeats (many copies);
291-346 5.82e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 5.82e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1046903808  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 ...
 617-646 6.07e-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: 6.07e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1046903808   617 KGRTALYLAAFKGHTECVEALVNQGASIFV 646
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 856-888 6.30e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 6.30e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1046903808  856 KGRTTLHAAA-FGDHAECLQLLLRHDAQVNAVDN 888
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
909-967 6.61e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 6.61e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1046903808  909 LVNSAQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIA 967
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD---LNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 586-637 6.66e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 6.66e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1046903808  586 KSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEAL 637
Cdd:PTZ00322   116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 858-1015 6.95e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 6.95e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  858 RTTLHAAAFGDHAECLQLLLRHDAQVNAV-DNSGKTALMMAAENGQAGAVDILVnSAQADLTVKDKDLNTPLHLAISKGH 936
Cdd:PHA02875    69 ESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLI-ARGADPDIPNTDKFSPLHLAVMMGD 147

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046903808  937 EKCALLILDKiqdESLINAKNSALQTPLHIAARNGLKVVVEELLAKGACVLAVDENGHTPALACAPNKDVADCLALILA 1015
Cdd:PHA02875   148 IKGIELLIDH---KACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIK 223
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 423-454 7.23e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 7.23e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1046903808  423 GRTCLHAAAA-GGNVECIKLLQSSGADFHKKDK 454
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 76-105 7.67e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 7.67e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1046903808   76 TPLHRAVASR-SEEAVQVLIKHSADVNARDK 105
Cdd:pfam00023    4 TPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 363-572 7.84e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.16  E-value: 7.84e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  363 ADTAK-CGIHSMFPLHlaalNAHSDCCRKLLSSGQKYSIVSLFSNEHVLSAGFEidtpdtfGRTCLHAAAAGGNVECIKL 441
Cdd:cd22193     26 SSTGKtCLMKALLNLN----PGTNDTIRILLDIAEKTDNLKRFINAEYTDEYYE-------GQTALHIAIERRQGDIVAL 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  442 LQSSGAD---------FHKKDK-----CGRTPLHYAAANCHFHCIKALVT---TGANINETDNWGRTALHYAAasdmdrn 504
Cdd:cd22193     95 LVENGADvhahakgrfFQPKYQgegfyFGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLHALV------- 167

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1046903808  505 kMILGNAHDNSEELERA-REVKGKDAALCLEFLLQndanpSIRDKEGYNSIHYAAAYGHRQCLELLLER 572
Cdd:cd22193    168 -TVADNTKENTKFVTRMyDMILIRGAKLCPTVELE-----EIRNNDGLTPLQLAAKMGKIEILKYILQR 230
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 423-572 9.87e-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: 39.74  E-value: 9.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  423 GRTCLHAAAAGGNVECIKLLQSSGAD---------FHKKDK-----CGRTPLHYAAANCHFHCIKALVTTGA-NINETDN 487
Cdd:cd22194    141 GQTALNIAIERRQGDIVKLLIAKGADvnahakgvfFNPKYKhegfyFGETPLALAACTNQPEIVQLLMEKEStDITSQDS 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1046903808  488 WGRTALH--YAAASDMDRNKMILGNAHDnseelERAREVKGKDaalcLEfllqndanpSIRDKEGYNSIHYAAAYGHRQC 565
Cdd:cd22194    221 RGNTVLHalVTVAEDSKTQNDFVKRMYD-----MILLKSENKN----LE---------TIRNNEGLTPLQLAAKMGKAEI 282


                   ....*..
gi 1046903808  566 LELLLER 572
Cdd:cd22194    283 LKYILSR 289
 
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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