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Conserved domains on  [gi|1333587278|ref|XP_023478041|]
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serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit B isoform X1 [Equus caballus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-343 4.89e-50

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 178.99  E-value: 4.89e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   54 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSV 133
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  134 NVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAA 213
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  214 ASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALcLELLV 293
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1333587278  294 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 343
Cdd:COG0666    240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
510-778 1.38e-36

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.09  E-value: 1.38e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  510 NAHENSEELERARELKEKEAASCLEFLLQNEANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEDSDSGATksPL 589
Cdd:COG0666     14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT--LL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  590 HLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLR 669
Cdd:COG0666     92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVK 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  670 LLLEI-ADnpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSIL 748
Cdd:COG0666    171 LLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250       260       270
                   ....*....|....*....|....*....|
gi 1333587278  749 CKDSRGRTPLHYAAARGHATWLSELLQIAL 778
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
668-997 2.83e-34

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 2.83e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  668 LRLLLEIADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSI 747
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  748 LCKDSRGRTPLHYAAARGHATWLSELLQialSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQkcfrefignpftplh 827
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA--------------- 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  828 caiindhencaslllGAIdssiVNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVD 907
Cdd:COG0666    143 ---------------GAD----VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  908 ILVNsAQADLTVKDKDLNTPLHLASSKGHEKCALLILDKIQDeslINAKNNALQTPLHVAARNGLKVVVEELLAKGACVL 987
Cdd:COG0666    204 LLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279

                          330
                   ....*....|
gi 1333587278  988 AVDENGHTPA 997
Cdd:COG0666    280 AALLDLLTLL 289
PHA03095 super family cl33707
ankyrin-like protein; Provisional
 212-493 8.69e-25

ankyrin-like protein; Provisional


The actual alignment was detected with superfamily member PHA03095:

Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 109.34  E-value: 8.69e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  212 AAASNGQINVVKHLLNLGVEIDEINVYGNTALH--LACYNGQDA-VVNELTDYGANVNQPNNSGFTPLHFAAASTHGALC 288
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  289 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGH---ELLiNTLITSGA 363
Cdd:PHA03095   100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGA 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  364 DTAKCGVHSMFPLHLAALNAHSDccrkllssgqkYSIVslfsnEHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQ 443
Cdd:PHA03095   179 DVYAVDDRFRSLLHHHLQSFKPR-----------ARIV-----RELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLP 242

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1333587278  444 --SSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTAL 493
Cdd:PHA03095   243 llIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 2.41e-06

Ankyrin repeats (many copies);


:

Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 2.41e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1333587278   10 PPLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLI 61
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-343 4.89e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 178.99  E-value: 4.89e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   54 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSV 133
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  134 NVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAA 213
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  214 ASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALcLELLV 293
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1333587278  294 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 343
Cdd:COG0666    240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 22-310 3.78e-38

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 149.40  E-value: 3.78e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   22 EEIRMLIHKTEDVNALDSEKRTPLHVaaFLG-----DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAV-QVLIK 95
Cdd:PHA03095    28 EEVRRLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDViKLLIK 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   96 HSADVNARDKNWQTPLHVAAANKAVkcaeviipllssvnvsdrggrtalhhaalngHVEMVNLLLAKGANINAFDKKDRR 175
Cdd:PHA03095   106 AGADVNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMT 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  176 ALHwaAYMGH----LDVVALLITHGAEVTCKDKKGYTPLHAAASNGQIN--VVKHLLNLGVEIDEINVYGNTALHLACYN 249
Cdd:PHA03095   155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333587278  250 G--QDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALCLELLvNNGADVNIQSKDGKSPL 310
Cdd:PHA03095   233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGNTPL 294
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
510-778 1.38e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.09  E-value: 1.38e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  510 NAHENSEELERARELKEKEAASCLEFLLQNEANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEDSDSGATksPL 589
Cdd:COG0666     14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT--LL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  590 HLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLR 669
Cdd:COG0666     92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVK 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  670 LLLEI-ADnpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSIL 748
Cdd:COG0666    171 LLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250       260       270
                   ....*....|....*....|....*....|
gi 1333587278  749 CKDSRGRTPLHYAAARGHATWLSELLQIAL 778
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
668-997 2.83e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 2.83e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  668 LRLLLEIADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSI 747
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  748 LCKDSRGRTPLHYAAARGHATWLSELLQialSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQkcfrefignpftplh 827
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA--------------- 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  828 caiindhencaslllGAIdssiVNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVD 907
Cdd:COG0666    143 ---------------GAD----VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  908 ILVNsAQADLTVKDKDLNTPLHLASSKGHEKCALLILDKIQDeslINAKNNALQTPLHVAARNGLKVVVEELLAKGACVL 987
Cdd:COG0666    204 LLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279

                          330
                   ....*....|
gi 1333587278  988 AVDENGHTPA 997
Cdd:COG0666    280 AALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 212-493 8.69e-25

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 109.34  E-value: 8.69e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  212 AAASNGQINVVKHLLNLGVEIDEINVYGNTALH--LACYNGQDA-VVNELTDYGANVNQPNNSGFTPLHFAAASTHGALC 288
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  289 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGH---ELLiNTLITSGA 363
Cdd:PHA03095   100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGA 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  364 DTAKCGVHSMFPLHLAALNAHSDccrkllssgqkYSIVslfsnEHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQ 443
Cdd:PHA03095   179 DVYAVDDRFRSLLHHHLQSFKPR-----------ARIV-----RELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLP 242

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1333587278  444 --SSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTAL 493
Cdd:PHA03095   243 llIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
Ank_2 pfam12796
Ankyrin repeats (3 copies);
144-236 1.26e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.48  E-value: 1.26e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  144 LHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHgAEVTCKDkKGYTPLHAAASNGQINVVK 223
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1333587278  224 HLLNLGVEIDEIN 236
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 669-984 5.76e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 94.32  E-value: 5.76e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  669 RLLLEIADnpevVDVKDAKGQTPLMLAVAYGH---IDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEE-CVQMLLEQE 744
Cdd:PHA03095    32 RLLAAGAD----VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  745 VSILCKDSRGRTPLH-YAA-ARGHATWLSELLQIALSEEDCsfkDNQGYTPLHwaCYNGNENC----IEVLLEQKCF--- 815
Cdd:PHA03095   108 ADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNAL---DLYGMTPLA--VLLKSRNAnvelLRLLIDAGADvya 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  816 REFIGNpfTPLH--CAIINDHENCASLLLGAIDSsiVNCRDDKGRTPLHAAAFADHVECLQL--LLRHNAQVNAADNSGK 891
Cdd:PHA03095   183 VDDRFR--SLLHhhLQSFKPRARIVRELIRAGCD--PAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQ 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  892 TALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLASSKGHEKCALLILDKIQDESLINAKNNALQTPLHVAARNG 971
Cdd:PHA03095   259 TPLHYAAVFNNPRACRRLIA-LGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTASVAGGDIPSDA 337

                          330
                   ....*....|...
gi 1333587278  972 LKVVVEELLAKGA 984
Cdd:PHA03095   338 TRLCVAKVVLRGA 350
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 397-682 5.88e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 93.96  E-value: 5.88e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  397 KYSIVSLFSNEHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHF--HCIET 474
Cdd:PHA03100     9 KSRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltDVKEI 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  475 ---LVTTGANVNETDDWGRTALHYAAAsdmdrnktilgnahenseelerarelKEKEAASCLEFLLQNEANPSIRDKEGY 551
Cdd:PHA03100    89 vklLLEYGANVNAPDNNGITPLLYAIS--------------------------KKSNSYSIVEYLLDNGANVNIKNSDGE 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  552 NSIHYAAAYGHR--QCLELLLERTNsgfedsdsgatksplHLAAYNghhqALEVLLQSLVDLDIRDEKGRTALDLAAFKG 629
Cdd:PHA03100   143 NLLHLYLESNKIdlKILKLLIDKGV---------------DINAKN----RVNYLLSYGVPINIKDVYGFTPLHYAVYNN 203

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1333587278  630 HTECVEALINQGASIFVKDNVTKrTPLHASVINGHTLCLRLLLEIADNPEVVD 682
Cdd:PHA03100   204 NPEFVKYLLDLGANPNLVNKYGD-TPLHIAILNNNKEIFKLLLNNGPSIKTII 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
622-718 4.07e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 4.07e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  622 LDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADnpevVDVKDaKGQTPLMLAVAYGHI 701
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHL 74

                           90
                   ....*....|....*..
gi 1333587278  702 DAVSLLLEKEANVDAVD 718
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
794-887 5.42e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.08  E-value: 5.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  794 LHWACYNGNENCIEVLLEQKC-FREFIGNPFTPLHCAIINDHENCASLLLGAIDSSIvncrDDKGRTPLHAAAFADHVEC 872
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL----KDNGRTALHYAARSGHLEI 76

                           90
                   ....*....|....*
gi 1333587278  873 LQLLLRHNAQVNAAD 887
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 74-281 2.53e-16

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: 83.91  E-value: 2.53e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   74 WLTPLHRAVASRSEEAVQVLIK-HSADVNARDKNWQTPLHVAAANKAVKCAEVII---PLLssVNV---SD-RGGRTALH 145
Cdd:cd22192     17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaaPEL--VNEpmtSDlYQGETALH 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  146 HAALNGHVEMVNLLLAKGANIN------AFDKKDRRAL-----H---WAAYMGHLDVVALLITHGAEVTCKDKKGYTPLH 211
Cdd:cd22192     95 IAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333587278  212 AAASNGQINVVKH----LLNLGVEIDEINVYgntalhlacyngqdavvneltdyganvNQPNNSGFTPLHFAAA 281
Cdd:cd22192    175 ILVLQPNKTFACQmydlILSYDKEDDLQPLD---------------------------LVPNNQGLTPFKLAAK 221
Ank_2 pfam12796
Ankyrin repeats (3 copies);
427-500 5.59e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.30  E-value: 5.59e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333587278  427 LHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTgANVNETDDwGRTALHYAAASD 500
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSG 72
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 49-280 1.16e-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: 65.87  E-value: 1.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   49 AFLGDAEIIELLILSGARVNAK-------DNMWLTPLHRAVA-SRSEEAVQVLIKHSADVNARDknwqTPLHVAAANKAV 120
Cdd:TIGR00870   20 AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAISLEYVD 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  121 KCAEVIIPLLSS---------VNVSDRG----GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRA----- 176
Cdd:TIGR00870   96 AVEAILLHLLAAfrksgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDsfyhg 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  177 ---LHWAAYMGHLDVVALLITHGAEVTCKDKKGytplhaaasngqiNVVKHLLNLGVEideiNVYGNTALHLACYngqda 253
Cdd:TIGR00870  176 espLNAAACLGSPSIVALLSEDPADILTADSLG-------------NTLLHLLVMENE----FKAEYEELSCQMY----- 233

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1333587278  254 vvNELTDYGANVNQ-------PNNSGFTPLHFAA 280
Cdd:TIGR00870  234 --NFALSLLDKLRDskeleviLNHQGLTPLKLAA 265
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 585-775 8.85e-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: 8.85e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  585 TKSPLHLAAYNGHHQALEVLL-QSLVDLDIRDEKGRTALDLAAFKGHTECVEALINqGASIFVKDNVTK-----RTPLHA 658
Cdd:cd22192     17 SESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLME-AAPELVNEPMTSdlyqgETALHI 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  659 SVINGHTLCLRLLLEI-AD--NPEVVD---VKDAK-----GQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHR 727
Cdd:cd22192     96 AVVNQNLNLVRELIARgADvvSPRATGtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333587278  728 GIMTGHEECV-QM---LLEQEVSI------LCKDSRGRTPLHYAAARGHATWLSELLQ 775
Cdd:cd22192    176 LVLQPNKTFAcQMydlILSYDKEDdlqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 340-494 2.07e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 58.10  E-value: 2.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  340 NTPLHVAARYGHELLINTLITS-GADTAKCGVHSMFPLHLAALNAHSDCCRKLLSSgqkysiVSLFSNEHVLSAGFEidt 418
Cdd:cd22192     18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEA------APELVNEPMTSDLYQ--- 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  419 pdkfGRTCLHAAAAGGNVECIKLLQSSGAD----------FHKKDKC----GRTPLHYAAANCHFHCIETLVTTGANVNE 484
Cdd:cd22192     89 ----GETALHIAVVNQNLNLVRELIARGADvvspratgtfFRPGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRA 164

                          170
                   ....*....|
gi 1333587278  485 TDDWGRTALH 494
Cdd:cd22192    165 QDSLGNTVLH 174
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 792-982 5.83e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.48  E-value: 5.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  792 TPLHWACYNGNENCIEVLLEQK----CFREFIGNpfTPLHCAIINDHENCASLLLGAiDSSIVN--CRDD--KGRTPLHA 863
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCPscdlFQRGALGE--TALHVAALYDNLEAAVVLMEA-APELVNepMTSDlyQGETALHI 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  864 AAFADHVECLQLLLRHNAQVNAADNS--------------GKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLH 929
Cdd:cd22192     96 AVVNQNLNLVRELIARGADVVSPRATgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVLH 174

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  930 LASSKGHEKCA------LLILDKIQDE-SLINAKNNALQTPLHVAARNGLKVVVEELLAK 982
Cdd:cd22192    175 ILVLQPNKTFAcqmydlILSYDKEDDLqPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 738-981 8.16e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 53.16  E-value: 8.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  738 QMLLE-QEVSILCKDSRGRTPLHYAAARGHATWLSELLQialseedcsFKDNQGY---TPLHWACYNGNENCIEVLLEQK 813
Cdd:TIGR00870   35 RDLEEpKKLNINCPDRLGRSALFVAAIENENLELTELLL---------NLSCRGAvgdTLLHAISLEYVDAVEAILLHLL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  814 CFREFIGNPF--------------TPLHCAIINDHENCASLLL--GAIDSSIVNCRDDK----------GRTPLHAAAFA 867
Cdd:TIGR00870  106 AAFRKSGPLElandqytseftpgiTALHLAAHRQNYEIVKLLLerGASVPARACGDFFVksqgvdsfyhGESPLNAAACL 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  868 DHVECLQLLLRHNAQVNAADNSGKTALMMAAEngqagavdilvnsaQADLTVKDKDLNTPLHLAsskghekcALLILDKI 947
Cdd:TIGR00870  186 GSPSIVALLSEDPADILTADSLGNTLLHLLVM--------------ENEFKAEYEELSCQMYNF--------ALSLLDKL 243

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1333587278  948 QD-ESLINAKNNALQTPLHVAARNGLKVVVEELLA 981
Cdd:TIGR00870  244 RDsKELEVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 587-831 1.34e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 52.39  E-value: 1.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  587 SPLHLAAYNGHHQALEVLLQSLvdlDIRDEKGRTALdLAAFKGHTECVEALIN--------QGASIFVKDNVTKR----- 653
Cdd:TIGR00870   54 SALFVAAIENENLELTELLLNL---SCRGAVGDTLL-HAISLEYVDAVEAILLhllaafrkSGPLELANDQYTSEftpgi 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  654 TPLHASVINGHTLCLRLLLEIADNPEV----VDVKDAKGQT-------PLMLAVAYGHIDAVSLLLEKEANVDAVDIMGC 722
Cdd:TIGR00870  130 TALHLAAHRQNYEIVKLLLERGASVPAracgDFFVKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  723 TALHRGIMtgheECVQMLLEQEVSILCKDsrgrtplhYAaarghatwLSELLQIALSEEDCSFKDNQGYTPLHWACYNGN 802
Cdd:TIGR00870  210 TLLHLLVM----ENEFKAEYEELSCQMYN--------FA--------LSLLDKLRDSKELEVILNHQGLTPLKLAAKEGR 269

                          250       260       270
                   ....*....|....*....|....*....|
gi 1333587278  803 ENCIEVLLEQKCF-REFIGNPFTPLHCAII 831
Cdd:TIGR00870  270 IVLFRLKLAIKYKqKKFVAWPNGQQLLSLY 299
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 2.41e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 2.41e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1333587278   10 PPLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLI 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 4.24e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.12  E-value: 4.24e-06
                            10        20
                    ....*....|....*....|....*....
gi 1333587278   140 GRTALHHAALNGHVEMVNLLLAKGANINA 168
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 456-484 7.25e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 7.25e-04
                            10        20
                    ....*....|....*....|....*....
gi 1333587278   456 GRTPLHYAAANCHFHCIETLVTTGANVNE 484
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 856-885 1.11e-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: 37.18  E-value: 1.11e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1333587278   856 KGRTPLHAAAFADHVECLQLLLRHNAQVNA 885
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 687-716 3.05e-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: 3.05e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1333587278   687 KGQTPLMLAVAYGHIDAVSLLLEKEANVDA 716
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 332-494 3.83e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.22  E-value: 3.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  332 IDCVDKDGNTPLHVAARYG-HELLINTLITSGA-----DTAkcgvhsmfpLHLAALNAHSDC--CRKLLSSGQKYSIVSL 403
Cdd:TIGR00870   45 INCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISLEYVDAVeaILLHLLAAFRKSGPLE 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  404 FSNEHVLSAGFeidtpdkFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKC--------------GRTPLHYAAANCHF 469
Cdd:TIGR00870  116 LANDQYTSEFT-------PGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSP 188

                          170       180
                   ....*....|....*....|....*
gi 1333587278  470 HCIETLVTTGANVNETDDWGRTALH 494
Cdd:TIGR00870  189 SIVALLSEDPADILTADSLGNTLLH 213
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-343 4.89e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 178.99  E-value: 4.89e-50
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   54 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSV 133
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  134 NVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAA 213
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  214 ASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALcLELLV 293
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1333587278  294 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 343
Cdd:COG0666    240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
11-276 2.49e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.99  E-value: 2.49e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   11 PLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAV 90
Cdd:COG0666     24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   91 QVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFD 170
Cdd:COG0666    104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  171 KKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNG 250
Cdd:COG0666    184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263

                          250       260
                   ....*....|....*....|....*.
gi 1333587278  251 QDAVVNELTDYGANVNQPNNSGFTPL 276
Cdd:COG0666    264 AALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-307 3.42e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.60  E-value: 3.42e-48
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   22 EEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVN 101
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  102 ARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAA 181
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  182 YMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDY 261
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1333587278  262 GANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGK 307
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-243 5.08e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.44  E-value: 5.08e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278    1 MAVLKLTDQPPLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHR 80
Cdd:COG0666     47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   81 AVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLL 160
Cdd:COG0666    127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  161 AKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGN 240
Cdd:COG0666    207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286


                   ...
gi 1333587278  241 TAL 243
Cdd:COG0666    287 TLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 22-310 3.78e-38

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 149.40  E-value: 3.78e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   22 EEIRMLIHKTEDVNALDSEKRTPLHVaaFLG-----DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAV-QVLIK 95
Cdd:PHA03095    28 EEVRRLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDViKLLIK 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   96 HSADVNARDKNWQTPLHVAAANKAVkcaeviipllssvnvsdrggrtalhhaalngHVEMVNLLLAKGANINAFDKKDRR 175
Cdd:PHA03095   106 AGADVNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMT 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  176 ALHwaAYMGH----LDVVALLITHGAEVTCKDKKGYTPLHAAASNGQIN--VVKHLLNLGVEIDEINVYGNTALHLACYN 249
Cdd:PHA03095   155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333587278  250 G--QDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALCLELLvNNGADVNIQSKDGKSPL 310
Cdd:PHA03095   233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGNTPL 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
 86-359 6.99e-38

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 148.63  E-value: 6.99e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   86 SEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSS---VNVSDRGGRTALHHAALNGHVE-MVNLLLA 161
Cdd:PHA03095    26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAgadVNAPERCGFTPLHLYLYNATTLdVIKLLIK 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  162 KGANINAFDKKDRRALHwaAYMG----HLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINV--VKHLLNLGVEIDEI 235
Cdd:PHA03095   106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  236 NVYGNTALHLACYNGQD--AVVNELTDYGANVNQPNNSGFTPLHFAAA-STHGALCLELLVNNGADVNIQSKDGKSPLHM 312
Cdd:PHA03095   184 DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1333587278  313 TAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLI 359
Cdd:PHA03095   264 AAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
510-778 1.38e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.09  E-value: 1.38e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  510 NAHENSEELERARELKEKEAASCLEFLLQNEANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEDSDSGATksPL 589
Cdd:COG0666     14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT--LL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  590 HLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLR 669
Cdd:COG0666     92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVK 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  670 LLLEI-ADnpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSIL 748
Cdd:COG0666    171 LLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250       260       270
                   ....*....|....*....|....*....|
gi 1333587278  749 CKDSRGRTPLHYAAARGHATWLSELLQIAL 778
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
533-813 9.45e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.78  E-value: 9.45e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  533 LEFLLQNEANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEDSDSGATKSPLHLAAYNGHHQALEVLLQSLVDLD 612
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  613 IRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEI-ADnpevVDVKDAKGQTP 691
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAgAD----VNAQDNDGNTP 156

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  692 LMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLS 771
Cdd:COG0666    157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1333587278  772 ELLQIALSEEDcsfKDNQGYTPLHWACYNGNENCIEVLLEQK 813
Cdd:COG0666    237 LLLEAGADLNA---KDKDGLTALLLAAAAGAALIVKLLLLAL 275
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 55-301 2.08e-35

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 140.19  E-value: 2.08e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   55 EIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAV-----KCAEVIIPL 129
Cdd:PHA03100    16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEY 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  130 LSSVNVSDRGGRTALHHAALN--GHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGH--LDVVALLITHGAEVTCKDKk 205
Cdd:PHA03100    96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNR- 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  206 gytplhaaasngqinvVKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHG 285
Cdd:PHA03100   175 ----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238

                          250
                   ....*....|....*.
gi 1333587278  286 ALcLELLVNNGADVNI 301
Cdd:PHA03100   239 EI-FKLLLNNGPSIKT 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
153-525 4.79e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.47  E-value: 4.79e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  153 VEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEI 232
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  233 DEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQskdgksplhm 312
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI-VKLLLEAGADVNAQ---------- 149

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  313 tavhgrftrsqtliqnggeidcvDKDGNTPLHVAARYGHELLINTLITSGADtakcgvhsmfplhlaalnahsdccrkll 392
Cdd:COG0666    150 -----------------------DNDGNTPLHLAAANGNLEIVKLLLEAGAD---------------------------- 178

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  393 ssgqkysivslfsnehvlsagfeIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCI 472
Cdd:COG0666    179 -----------------------VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1333587278  473 ETLVTTGANVNETDDWGRTALHYAAASDMDRNKTILGNAHENSEELERARELK 525
Cdd:COG0666    236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
668-997 2.83e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 2.83e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  668 LRLLLEIADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSI 747
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  748 LCKDSRGRTPLHYAAARGHATWLSELLQialSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQkcfrefignpftplh 827
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA--------------- 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  828 caiindhencaslllGAIdssiVNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVD 907
Cdd:COG0666    143 ---------------GAD----VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  908 ILVNsAQADLTVKDKDLNTPLHLASSKGHEKCALLILDKIQDeslINAKNNALQTPLHVAARNGLKVVVEELLAKGACVL 987
Cdd:COG0666    204 LLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279

                          330
                   ....*....|
gi 1333587278  988 AVDENGHTPA 997
Cdd:COG0666    280 AALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 26-364 1.18e-33

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 139.04  E-value: 1.18e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   26 MLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDK 105
Cdd:PHA02876   163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDL 242

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  106 NwqtpLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHV-EMVNLLLAKGANINAFDKKDRRALHWAAYMG 184
Cdd:PHA02876   243 S----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNG 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  185 H-LDVVALLITHGAEVTCKDKKGYTPLHAAAS-NGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYG 262
Cdd:PHA02876   319 YdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  263 ANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHG-RFTRSQTLIQNGGEIDCVDKDGNT 341
Cdd:PHA02876   399 ADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQY 478

                          330       340
                   ....*....|....*....|...
gi 1333587278  342 PLHVAarYGHELLINTLITSGAD 364
Cdd:PHA02876   479 PLLIA--LEYHGIVNILLHYGAE 499
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 16-367 2.45e-32

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 131.24  E-value: 2.45e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   16 IFSGDPEEIRMLI-HKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLI 94
Cdd:PHA02874     9 IYSGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   95 KHSADVNArdknwqtplhvaaankavkcaeVIIPLLSSvnvsdrggrtalhhaalnghvEMVNLLLAKGANINAFDKKDR 174
Cdd:PHA02874    89 DNGVDTSI----------------------LPIPCIEK---------------------DMIKTILDCGIDVNIKDAELK 125

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  175 RALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQDAV 254
Cdd:PHA02874   126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  255 VNELTDYGANVNQPNNSGFTPLHfaAASTHGALCLELLVNNgADVNIQSKDGKSPLHMtAVHGRFTRS--QTLIQNGGEI 332
Cdd:PHA02874   206 IKLLIDHGNHIMNKCKNGFTPLH--NAIIHNRSAIELLINN-ASINDQDIDGSTPLHH-AINPPCDIDiiDILLYHKADI 281

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1333587278  333 DCVDKDGNTPLHVAARYGH------ELLINTLITSGADTAK 367
Cdd:PHA02874   282 SIKDNKGENPIDTAFKYINkdpvikDIIANAVLIKEADKLK 322
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
770-1015 1.51e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.45  E-value: 1.51e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  770 LSELLQIALSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQKCFRE-FIGNPFTPLHCAIINDHENCASLLLGAIDSs 848
Cdd:COG0666     34 LLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINaKDDGGNTLLHAAARNGDLEIVKLLLEAGAD- 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  849 iVNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPL 928
Cdd:COG0666    113 -VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPL 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  929 HLASSKGHEKCALLILDKIQDeslINAKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVDENGHTPALACAPNKDVAD 1008
Cdd:COG0666    191 HLAAENGHLEIVKLLLEAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALI 267


                   ....*..
gi 1333587278 1009 CLALILA 1015
Cdd:COG0666    268 VKLLLLA 274
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 56-385 4.49e-31

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 130.95  E-value: 4.49e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   56 IIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNV 135
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  136 SDrggrTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLD-VVALLITHGAEVTCKDKKGYTPLHAAA 214
Cdd:PHA02876   240 ND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMA 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  215 SNG-QINVVKHLLNLGVEIDEINVYGNTALHLACY--NGQDAVVNeLTDYGANVNQPNNSGFTPLHFAAAStHGALCLEL 291
Cdd:PHA02876   316 KNGyDTENIRTLIMLGADVNAADRLYITPLHQASTldRNKDIVIT-LLELGANVNARDYCDKTPIHYAAVR-NNVVIINT 393

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  292 LVNNGADVNIQSKDGKSPLHMtAVHGR--FTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHEL-LINTLITSGADTAKC 368
Cdd:PHA02876   394 LLDYGADIEALSQKIGTALHF-ALCGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAI 472

                          330
                   ....*....|....*..
gi 1333587278  369 GVHSMFPLhLAALNAHS 385
Cdd:PHA02876   473 NIQNQYPL-LIALEYHG 488
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
289-622 5.88e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.91  E-value: 5.88e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  289 LELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKC 368
Cdd:COG0666      4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  369 GVHSMFPLHLAALNAHSDCCRKLLSsgqkysivslfsnehvlsAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGAD 448
Cdd:COG0666     84 DDGGNTLLHAAARNGDLEIVKLLLE------------------AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD 145

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  449 FHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAaasdmdrnktilgnAHENSEELerarelkeke 528
Cdd:COG0666    146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA--------------AENGHLEI---------- 201

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  529 aascLEFLLQNEANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEDSDSGATksPLHLAAYNGHHQALEVLLQSL 608
Cdd:COG0666    202 ----VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLT--ALLLAAAAGAALIVKLLLLAL 275

                          330
                   ....*....|....
gi 1333587278  609 VDLDIRDEKGRTAL 622
Cdd:COG0666    276 LLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
770-1015 2.43e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.98  E-value: 2.43e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  770 LSELLQIALSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQKCFREFIGNPFTPLHCAIINDHENCASLLLGAIDSSI 849
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  850 vNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLH 929
Cdd:COG0666     81 -NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE-AGADVNAQDNDGNTPLH 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  930 LASSKGHEKCALLILDKIQDeslINAKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVDENGHTPALACAPNKDVADC 1009
Cdd:COG0666    159 LAAANGNLEIVKLLLEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235


                   ....*.
gi 1333587278 1010 LALILA 1015
Cdd:COG0666    236 KLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
533-758 4.06e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.21  E-value: 4.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  533 LEFLLQNEANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEDSDSGATksPLHLAAYNGHHQALEVLLQSLVDLD 612
Cdd:COG0666     70 ALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGET--PLHLAAYNGNLEIVKLLLEAGADVN 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  613 IRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLE-IADnpevVDVKDAKGQTP 691
Cdd:COG0666    148 AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEaGAD----VNAKDNDGKTA 222

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333587278  692 LMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPL 758
Cdd:COG0666    223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
410-687 2.41e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.90  E-value: 2.41e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  410 LSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWG 489
Cdd:COG0666     41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  490 RTALHYAAasdmdrnktilgnaHENSEELerarelkekeaascLEFLLQNEANPSIRDKEGYNSIHYAAAYGHRQCLELL 569
Cdd:COG0666    121 ETPLHLAA--------------YNGNLEI--------------VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  570 LERTNSGFEDSDSGATksPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDN 649
Cdd:COG0666    173 LEAGADVNARDNDGET--PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1333587278  650 VTKRTPLHASVINGHTLCLRLLLEIADNPEVVDVKDAK 687
Cdd:COG0666    251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
403-725 1.42e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.98  E-value: 1.42e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  403 LFSNEHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANV 482
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  483 NETDDWGRTALHYAAASDMdrnktilgnahenseelerarelkekeaASCLEFLLQNEANPSIRDKEGYNSIHYAAAYGH 562
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGD----------------------------LEIVKLLLEAGADVNARDKDGETPLHLAAYNGN 132

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  563 RQCLELLLERtnsGFE-DSDSGATKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQG 641
Cdd:COG0666    133 LEIVKLLLEA---GADvNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  642 ASIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADNpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMG 721
Cdd:COG0666    210 ADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285


                   ....
gi 1333587278  722 CTAL 725
Cdd:COG0666    286 LTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 123-483 1.24e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 120.17  E-value: 1.24e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  123 AEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCK 202
Cdd:PHA02876   161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKN 240

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  203 DkkgyTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQ-DAVVNELTDYGANVNQPNNSGFTPLHFAAA 281
Cdd:PHA02876   241 D----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAK 316

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  282 STHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQ-TLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLIT 360
Cdd:PHA02876   317 NGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIViTLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  361 SGADtakcgvhsmfplhLAALNahsdccrkllssgqkysivslfsnehvlsagfeidtpDKFGrTCLHAAAAGGN-VECI 439
Cdd:PHA02876   397 YGAD-------------IEALS-------------------------------------QKIG-TALHFALCGTNpYMSV 425

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1333587278  440 KLLQSSGADFHKKDKCGRTPLHYAAA-NCHFHCIETLVTTGANVN 483
Cdd:PHA02876   426 KTLIDRGANVNSKNKDLSTPLHYACKkNCKLDVIEMLLDNGADVN 470
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 12-265 3.78e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 118.63  E-value: 3.78e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   12 LVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGD-AEIIELLILSGARVNAKDNMWLTPLH-RAVASRSEEA 89
Cdd:PHA02876   244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYlMAKNGYDTEN 323

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   90 VQVLIKHSADVNARDKNWQTPLHVAAANKAVKcaEVIIPLL---SSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANI 166
Cdd:PHA02876   324 IRTLIMLGADVNAADRLYITPLHQASTLDRNK--DIVITLLelgANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  167 NAFDKKDRRALHWAAY-MGHLDVVALLITHGAEVTCKDKKGYTPLH-AAASNGQINVVKHLLNLGVEIDEINVYGNTALH 244
Cdd:PHA02876   402 EALSQKIGTALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHyACKKNCKLDVIEMLLDNGADVNAINIQNQYPLL 481

                          250       260
                   ....*....|....*....|.
gi 1333587278  245 LACynGQDAVVNELTDYGANV 265
Cdd:PHA02876   482 IAL--EYHGIVNILLHYGAEL 500
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 75-346 6.00e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 113.05  E-value: 6.00e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   75 LTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVA--AANKavkcaEVIIPLLSSVNVSDRG-GRTALHHAALNG 151
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckEPNK-----LGMKEMIRSINKCSVFyTLVAIKDAFNNR 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  152 HVEMVNLLLakganINAFDKK---DRRALHWAAYMGHLD--VVALLITHGAEVTCKDK-KGYTPLHAAASNGQINVVKHL 225
Cdd:PHA02878   113 NVEIFKIIL-----TNRYKNIqtiDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELL 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  226 LNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSK- 304
Cdd:PHA02878   188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYi 267

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1333587278  305 DGKSPLHMTAVHGRFTRsqTLIQNGGEIDCVDKDGNTPLHVA 346
Cdd:PHA02878   268 LGLTALHSSIKSERKLK--LLLEYGADINSLNSYKLTPLSSA 307
PHA03095 PHA03095
ankyrin-like protein; Provisional
 212-493 8.69e-25

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 109.34  E-value: 8.69e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  212 AAASNGQINVVKHLLNLGVEIDEINVYGNTALH--LACYNGQDA-VVNELTDYGANVNQPNNSGFTPLHFAAASTHGALC 288
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  289 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGH---ELLiNTLITSGA 363
Cdd:PHA03095   100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGA 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  364 DTAKCGVHSMFPLHLAALNAHSDccrkllssgqkYSIVslfsnEHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQ 443
Cdd:PHA03095   179 DVYAVDDRFRSLLHHHLQSFKPR-----------ARIV-----RELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLP 242

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1333587278  444 --SSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTAL 493
Cdd:PHA03095   243 llIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 28-238 1.49e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 107.83  E-value: 1.49e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   28 IHKTEDVN-ALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLH-----RAVASRSEEAVQVLIKHSADVN 101
Cdd:PHA03100    21 IIMEDDLNdYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVN 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  102 ARDKNWQTPLHVAAANKavKCAEVIIPLLSS----VNVSDRGGRTALHHAALNGHV--EMVNLLLAKGANINAFDK---- 171
Cdd:PHA03100   101 APDNNGITPLLYAISKK--SNSYSIVEYLLDnganVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRvnyl 178

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333587278  172 ---------KDRR---ALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVY 238
Cdd:PHA03100   179 lsygvpiniKDVYgftPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 192-483 5.65e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 105.90  E-value: 5.65e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  192 LITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLAC---YNGQDAV--VNELTDYGANVN 266
Cdd:PHA03100    21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikYNLTDVKeiVKLLLEYGANVN 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  267 QPNNSGFTPLHFAAASTHGALCL-ELLVNNGADVNIQSKDGKSPLHMtavhgrFTRSqtliqnggeiDCVDKDgntplhv 345
Cdd:PHA03100   101 APDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHL------YLES----------NKIDLK------- 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  346 aaryghelLINTLITSGADtakcgvhsmfplhlaaLNAhsdCCRkllssgqkysiVSLFsnehvLSAGFEIDTPDKFGRT 425
Cdd:PHA03100   158 --------ILKLLIDKGVD----------------INA---KNR-----------VNYL-----LSYGVPINIKDVYGFT 194

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333587278  426 CLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVN 483
Cdd:PHA03100   195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 22-295 6.98e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 100.34  E-value: 6.98e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   22 EEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIK------ 95
Cdd:PHA02878    18 KYIEYIDHTENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcs 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   96 ------------HSADVNA-------RDKNWQTP--LHVAAANKAVKCAEVIIPLL----SSVNVSDR-GGRTALHHAAL 149
Cdd:PHA02878    98 vfytlvaikdafNNRNVEIfkiiltnRYKNIQTIdlVYIDKKSKDDIIEAEITKLLlsygADINMKDRhKGNTALHYATE 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  150 NGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASN-GQINVVKHLLNL 228
Cdd:PHA02878   178 NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEH 257

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333587278  229 GVEID-EINVYGNTALHLACYNGQdaVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNN 295
Cdd:PHA02878   258 GVDVNaKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISN 323
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 323-625 1.38e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 98.88  E-value: 1.38e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  323 QTLIQNGGE-IDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGVHSMFPLHLAALNAHSDCCRKLLSSGQKYSIV 401
Cdd:PHA02874    18 EKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  402 SL--FSNEHV---LSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLV 476
Cdd:PHA02874    98 PIpcIEKDMIktiLDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  477 TTGANVNETDDWGRTALHYAAasdmdrnktilgnahenseelerarelkEKEAASCLEFLLQNEANPSIRDKEGYNSIHY 556
Cdd:PHA02874   178 EKGAYANVKDNNGESPLHNAA----------------------------EYGDYACIKLLIDHGNHIMNKCKNGFTPLHN 229

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333587278  557 AAAYgHRQCLELLLerTNSGFEDSD-SGATksPLHLA-AYNGHHQALEVLLQSLVDLDIRDEKGRTALDLA 625
Cdd:PHA02874   230 AIIH-NRSAIELLI--NNASINDQDiDGST--PLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
144-236 1.26e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.48  E-value: 1.26e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  144 LHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHgAEVTCKDkKGYTPLHAAASNGQINVVK 223
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1333587278  224 HLLNLGVEIDEIN 236
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 24-227 1.97e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 95.86  E-value: 1.97e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   24 IRMLIHKTEDVNALDSEKRTPLHV--AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASR--SEEAVQVLIKHSAD 99
Cdd:PHA03095   100 IKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGAD 179

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  100 VNARDKNWQTPLHVAAAN--KAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNL--LLAKGANINAFDKKDRR 175
Cdd:PHA03095   180 VYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQT 259

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1333587278  176 ALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLN 227
Cdd:PHA03095   260 PLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-269 3.05e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 3.05e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  177 LHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNlGVEIDEINvYGNTALHLACYNGQDAVVN 256
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1333587278  257 ELTDYGANVNQPN 269
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 669-984 5.76e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 94.32  E-value: 5.76e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  669 RLLLEIADnpevVDVKDAKGQTPLMLAVAYGH---IDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEE-CVQMLLEQE 744
Cdd:PHA03095    32 RLLAAGAD----VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  745 VSILCKDSRGRTPLH-YAA-ARGHATWLSELLQIALSEEDCsfkDNQGYTPLHwaCYNGNENC----IEVLLEQKCF--- 815
Cdd:PHA03095   108 ADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNAL---DLYGMTPLA--VLLKSRNAnvelLRLLIDAGADvya 182

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  816 REFIGNpfTPLH--CAIINDHENCASLLLGAIDSsiVNCRDDKGRTPLHAAAFADHVECLQL--LLRHNAQVNAADNSGK 891
Cdd:PHA03095   183 VDDRFR--SLLHhhLQSFKPRARIVRELIRAGCD--PAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQ 258

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  892 TALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLASSKGHEKCALLILDKIQDESLINAKNNALQTPLHVAARNG 971
Cdd:PHA03095   259 TPLHYAAVFNNPRACRRLIA-LGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTASVAGGDIPSDA 337

                          330
                   ....*....|...
gi 1333587278  972 LKVVVEELLAKGA 984
Cdd:PHA03095   338 TRLCVAKVVLRGA 350
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 397-682 5.88e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 93.96  E-value: 5.88e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  397 KYSIVSLFSNEHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHF--HCIET 474
Cdd:PHA03100     9 KSRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltDVKEI 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  475 ---LVTTGANVNETDDWGRTALHYAAAsdmdrnktilgnahenseelerarelKEKEAASCLEFLLQNEANPSIRDKEGY 551
Cdd:PHA03100    89 vklLLEYGANVNAPDNNGITPLLYAIS--------------------------KKSNSYSIVEYLLDNGANVNIKNSDGE 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  552 NSIHYAAAYGHR--QCLELLLERTNsgfedsdsgatksplHLAAYNghhqALEVLLQSLVDLDIRDEKGRTALDLAAFKG 629
Cdd:PHA03100   143 NLLHLYLESNKIdlKILKLLIDKGV---------------DINAKN----RVNYLLSYGVPINIKDVYGFTPLHYAVYNN 203

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1333587278  630 HTECVEALINQGASIFVKDNVTKrTPLHASVINGHTLCLRLLLEIADNPEVVD 682
Cdd:PHA03100   204 NPEFVKYLLDLGANPNLVNKYGD-TPLHIAILNNNKEIFKLLLNNGPSIKTII 255
PHA03095 PHA03095
ankyrin-like protein; Provisional
 355-682 8.93e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 93.94  E-value: 8.93e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  355 INTLITSGADTAKCGVHSMFPLHLAALNAHSDCCRkllssgqkysIVSLfsnehVLSAGFEIDTPDKFGRTCLHAAAAGG 434
Cdd:PHA03095    30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKD----------IVRL-----LLEAGADVNAPERCGFTPLHLYLYNA 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  435 NVE-CIKLLQSSGADFHKKDKCGRTPLH-YAA-ANCHFHCIETLVTTGANVNETDDWGRTALHYAAASdmdRNKTIlgna 511
Cdd:PHA03095    95 TTLdVIKLLIKAGADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKS---RNANV---- 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  512 henseelerarELkekeaascLEFLLQNEANPSIRDKEGYNSIHYAAAYGH--RQCLELLLERTNSGFEDSDSGATksPL 589
Cdd:PHA03095   168 -----------EL--------LRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNT--PL 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  590 HLAAYNGHHQALEV--LLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLC 667
Cdd:PHA03095   227 HSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNTPLSLMVRNNNGRA 305

                          330
                   ....*....|....*
gi 1333587278  668 LRLLLEIADNPEVVD 682
Cdd:PHA03095   306 VRAALAKNPSAETVA 320
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 192-714 1.62e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 94.36  E-value: 1.62e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  192 LITHGAEvTCKDKK-GYTPLHAAASNGQINVVKHLLNLGVEIDEINVYG-NTALHLACY--NGQDAVVNELTDYGANVNQ 267
Cdd:PHA02876    27 LHKHGAN-QCENESiPFTAIHQALQLRQIDIVEEIIQQNPELIYITDHKcHSTLHTICIipNVMDIVISLTLDCDIILDI 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  268 PNNSGFTPLHfaaasTHGALCLELLVN--NGADVNIqSKDGKSPLHMTAVHGRFTR-----SQTLIQNGGEIDCVDKDGN 340
Cdd:PHA02876   106 KYASIILNKH-----KLDEACIHILKEaiSGNDIHY-DKINESIEYMKLIKERIQQdelliAEMLLEGGADVNAKDIYCI 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  341 TPLHVAARYGHELLINTLITSGADTAKCGVHSMFPLHLAALNAHSDCCRKLLS-----SGQKYSIVSLFSNEH------V 409
Cdd:PHA02876   180 TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDnrsniNKNDLSLLKAIRNEDletsllL 259

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  410 LSAGFEIDTPDKFGRTCLHAAAAGGNVECI--KLLQsSGADFHKKDKCGRTPLHYAAANCH-FHCIETLVTTGANVNETD 486
Cdd:PHA02876   260 YDAGFSVNSIDDCKNTPLHHASQAPSLSRLvpKLLE-RGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAAD 338

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  487 DWGRTALHyaAASDMDRNKTILGNahenseelerarelkekeaasclefLLQNEANPSIRDKEGYNSIHYAAAYGHRQCL 566
Cdd:PHA02876   339 RLYITPLH--QASTLDRNKDIVIT-------------------------LLELGANVNARDYCDKTPIHYAAVRNNVVII 391

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  567 ELLLertnsgfedsDSGAtksplhlaaynghhqalevllqslvDLDIRDEKGRTALDLAAFKGHT-ECVEALINQGASIF 645
Cdd:PHA02876   392 NTLL----------DYGA-------------------------DIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANVN 436

                          490       500       510       520       530       540       550
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  646 VKdNVTKRTPLHASVINGHTL-CLRLLLeiaDNPEVVDVKDAKGQTPLMLAVAYGHIdaVSLLLEKEANV 714
Cdd:PHA02876   437 SK-NKDLSTPLHYACKKNCKLdVIEMLL---DNGADVNAINIQNQYPLLIALEYHGI--VNILLHYGAEL 500
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 48-266 2.36e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 91.98  E-value: 2.36e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   48 AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 127
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  128 PLLSSVN-VSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKG 206
Cdd:PHA02875    89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333587278  207 YTPLHAAASNGQINVVKHLLNLGVEIDEINVYGN-TALHLACYNGQDAVVNELTDYGANVN 266
Cdd:PHA02875   169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCN 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
111-203 5.17e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 5.17e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  111 LHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKgANINAFDkKDRRALHWAAYMGHLDVVA 190
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1333587278  191 LLITHGAEVTCKD 203
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 150-463 6.57e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 90.79  E-value: 6.57e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  150 NGHVEMV-NLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNL 228
Cdd:PHA02874    11 SGDIEAIeKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  229 GVEideinvygNTALHLACYNGQdaVVNELTDYGANVNQPNNSGFTPLHFAAASthGAL-CLELLVNNGADVNIQSKDGK 307
Cdd:PHA02874    91 GVD--------TSILPIPCIEKD--MIKTILDCGIDVNIKDAELKTFLHYAIKK--GDLeSIKMLFEYGADVNIEDDNGC 158

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  308 SPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGAD-TAKCGvHSMFPLHLAALnahsd 386
Cdd:PHA02874   159 YPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHiMNKCK-NGFTPLHNAII----- 232

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333587278  387 ccrkllssgQKYSIVSLFSNEHvlsagfEIDTPDKFGRTCLH-AAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYA 463
Cdd:PHA02874   233 ---------HNRSAIELLINNA------SINDQDIDGSTPLHhAINPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 589-864 3.28e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 88.48  E-value: 3.28e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  589 LHLAAYNGHHQALEVLLQSLVD-LDIRDEKGRTALDLAAFKGHTECVEALINQGASI-FVKDNVTKrtPLHASVINGHTL 666
Cdd:PHA02874     5 LRMCIYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADInHINTKIPH--PLLTAIKIGAHD 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  667 CLRLLLE--------------------IADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALH 726
Cdd:PHA02874    83 IIKLLIDngvdtsilpipciekdmiktILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIH 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  727 RGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQialSEEDCSFKDNQGYTPLHWACYNgNENCI 806
Cdd:PHA02874   163 IAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLID---HGNHIMNKCKNGFTPLHNAIIH-NRSAI 238

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  807 EVLLEQKCFREFIGNPFTPLHCAIIN--DHENCASLLLGAIDSSIvncRDDKGRTPLHAA 864
Cdd:PHA02874   239 ELLINNASINDQDIDGSTPLHHAINPpcDIDIIDILLYHKADISI---KDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
622-718 4.07e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 4.07e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  622 LDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADnpevVDVKDaKGQTPLMLAVAYGHI 701
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHL 74

                           90
                   ....*....|....*..
gi 1333587278  702 DAVSLLLEKEANVDAVD 718
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
45-170 1.47e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 1.47e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   45 LHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHsADVNARDKnwqtplhvaaankavkcae 124
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN------------------- 60

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1333587278  125 viipllssvnvsdrgGRTALHHAALNGHVEMVNLLLAKGANINAFD 170
Cdd:pfam12796   61 ---------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 155-616 2.26e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 87.43  E-value: 2.26e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  155 MVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDE 234
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  235 -----INVYGNTALHLACYngqdavvneLTDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSP 309
Cdd:PHA02876   240 ndlslLKAIRNEDLETSLL---------LYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETP 310

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  310 LHMTAVHGRFTRS-QTLIQNGGEIDCVDKDGNTPLHVAAryghellintlitsgadtakcgvhsmfplhlaalnahsdcc 388
Cdd:PHA02876   311 LYLMAKNGYDTENiRTLIMLGADVNAADRLYITPLHQAS----------------------------------------- 349

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  389 rkllssgqkysivslfsnehvlsagfeidTPDKFGRTClhaaaaggnvecIKLLQSsGADFHKKDKCGRTPLHYAAANCH 468
Cdd:PHA02876   350 -----------------------------TLDRNKDIV------------ITLLEL-GANVNARDYCDKTPIHYAAVRNN 387

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  469 FHCIETLVTTGANVNETDDWGRTALHYAAASD---MDRNKTILGNAHENSEELERARELKEKEAASC----LEFLLQNEA 541
Cdd:PHA02876   388 VVIINTLLDYGADIEALSQKIGTALHFALCGTnpyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCkldvIEMLLDNGA 467

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333587278  542 NPSIRDKEgyNSIHYAAAYGHRQCLELLLertNSGFEDSDSGATKSPLHLAAYNGHHQALEVLLQSLVDLDIRDE 616
Cdd:PHA02876   468 DVNAINIQ--NQYPLLIALEYHGIVNILL---HYGAELRDSRVLHKSLNDNMFSFRYIIAHICIQDFIRHDIRNE 537
Ank_2 pfam12796
Ankyrin repeats (3 copies);
794-887 5.42e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.08  E-value: 5.42e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  794 LHWACYNGNENCIEVLLEQKC-FREFIGNPFTPLHCAIINDHENCASLLLGAIDSSIvncrDDKGRTPLHAAAFADHVEC 872
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL----KDNGRTALHYAARSGHLEI 76

                           90
                   ....*....|....*
gi 1333587278  873 LQLLLRHNAQVNAAD 887
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
589-682 6.10e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.69  E-value: 6.10e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  589 LHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQgasIFVKDNVTKRTPLHASVINGHTLCL 668
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 1333587278  669 RLLLEIADNPEVVD 682
Cdd:pfam12796   78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
656-751 2.00e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 2.00e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  656 LHASVINGHTLCLRLLLEIADNPevvDVKDAKGQTPLMLAVAYGHIDAVSLLLEKeANVDAVDiMGCTALHRGIMTGHEE 735
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADA---NLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLE 75

                           90
                   ....*....|....*.
gi 1333587278  736 CVQMLLEQEVSILCKD 751
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
861-957 2.12e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 2.12e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  861 LHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKdlnTPLHLASSKGHEKCA 940
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77

                           90
                   ....*....|....*..
gi 1333587278  941 LLILDKIQDeslINAKN 957
Cdd:pfam12796   78 KLLLEKGAD---INVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 738-991 2.31e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 83.96  E-value: 2.31e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  738 QMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQIAlseEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQkcfRE 817
Cdd:PHA02876   162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYG---ADVNIIALDDLSVLECAVDSKNIDTIKAIIDN---RS 235

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  818 FIGNPFTPLHCAIINDHENCASLLLGAIDSsiVNCRDDKGRTPLHAAAFADHVECL-QLLLRHNAQVNAADNSGKTALMM 896
Cdd:PHA02876   236 NINKNDLSLLKAIRNEDLETSLLLYDAGFS--VNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYL 313

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  897 AAENGQAGAVDILVNSAQADLTVKDKDLNTPLHLASSKGHEKCALLILdkIQDESLINAKNNALQTPLHVAARNGLKVVV 976
Cdd:PHA02876   314 MAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITL--LELGANVNARDYCDKTPIHYAAVRNNVVII 391

                          250
                   ....*....|....*
gi 1333587278  977 EELLAKGACVLAVDE 991
Cdd:PHA02876   392 NTLLDYGADIEALSQ 406
PHA03095 PHA03095
ankyrin-like protein; Provisional
 701-1016 2.48e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.15  E-value: 2.48e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  701 IDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEEC---VQMLLEQEVSILCKDSRGRTPLHYaaarghatwlsellqia 777
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHL----------------- 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  778 lseedcsfkdnqgytplhWACYNGNENCIEVLLEQKC-FREFIGNPFTPLH--CAIINDHENCASLLLGA-IDssiVNCR 853
Cdd:PHA03095    90 ------------------YLYNATTLDVIKLLIKAGAdVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKgAD---VNAL 148

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  854 DDKGRTPLHA---AAFADhVECLQLLLRHNAQVNAADNSGKTALMMAAEN--GQAGAVDILVnSAQADLTVKDKDLNTPL 928
Cdd:PHA03095   149 DLYGMTPLAVllkSRNAN-VELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELI-RAGCDPAATDMLGNTPL 226

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  929 HLASSKGHEKcALLILDKIQDESLINAKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVDENGHTPALACAPNKDVaD 1008
Cdd:PHA03095   227 HSMATGSSCK-RSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNG-R 304


                   ....*...
gi 1333587278 1009 CLALILAT 1016
Cdd:PHA03095   305 AVRAALAK 312
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 74-281 2.53e-16

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: 83.91  E-value: 2.53e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   74 WLTPLHRAVASRSEEAVQVLIK-HSADVNARDKNWQTPLHVAAANKAVKCAEVII---PLLssVNV---SD-RGGRTALH 145
Cdd:cd22192     17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaaPEL--VNEpmtSDlYQGETALH 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  146 HAALNGHVEMVNLLLAKGANIN------AFDKKDRRAL-----H---WAAYMGHLDVVALLITHGAEVTCKDKKGYTPLH 211
Cdd:cd22192     95 IAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333587278  212 AAASNGQINVVKH----LLNLGVEIDEINVYgntalhlacyngqdavvneltdyganvNQPNNSGFTPLHFAAA 281
Cdd:cd22192    175 ILVLQPNKTFACQmydlILSYDKEDDLQPLD---------------------------LVPNNQGLTPFKLAAK 221
Ank_2 pfam12796
Ankyrin repeats (3 copies);
12-104 2.63e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 2.63e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   12 LVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLiLSGARVNAKDNMWlTPLHRAVASRSEEAVQ 91
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDNGR-TALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1333587278   92 VLIKHSADVNARD 104
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 533-743 5.58e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 81.58  E-value: 5.58e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  533 LEFLLQNEANPSIRDKEGYNSIHYAAAYGHRQCLELLLerTNSGFEDSDSGATKSPLHLAAYNGHHQALEVLLQS--LVD 610
Cdd:PHA02875    18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLM--KHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLgkFAD 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  611 lDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKdNVTKRTPLHASVINGHTLCLRLLLeiaDNPEVVDVKDAKGQT 690
Cdd:PHA02875    96 -DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP-NTDKFSPLHLAVMMGDIKGIELLI---DHKACLDIEDCCGCT 170

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1333587278  691 PLMLAVAYGHIDAVSLLLEKEANVDAVDIMGC-TALHRGIMTGHEECVQMLLEQ 743
Cdd:PHA02875   171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKR 224
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 20-170 6.59e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 81.85  E-value: 6.59e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   20 DPEEIRMLIHKTEDVNALDSEK-RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSA 98
Cdd:PHA02878   146 EAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587278   99 DVNARDKNWQTPLHVAAAnkAVKCAEVIIPLL---SSVNV-SDRGGRTALHHAALNGHVemVNLLLAKGANINAFD 170
Cdd:PHA02878   226 STDARDKCGNTPLHISVG--YCKDYDILKLLLehgVDVNAkSYILGLTALHSSIKSERK--LKLLLEYGADINSLN 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
725-814 7.52e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.61  E-value: 7.52e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  725 LHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHAtwlsELLQIALSEEDCSFKDNqGYTPLHWACYNGNEN 804
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHL----EIVKLLLEHADVNLKDN-GRTALHYAARSGHLE 75

                           90
                   ....*....|
gi 1333587278  805 CIEVLLEQKC 814
Cdd:pfam12796   76 IVKLLLEKGA 85
PHA03095 PHA03095
ankyrin-like protein; Provisional
 17-168 1.28e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.84  E-value: 1.28e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   17 FSGDPEEIRMLIHKTEDVNALDSEKRTPLHVaaFLG----DAEIIELLILSGARVNAKDNMWLTPLHR-AVASRSEEAV- 90
Cdd:PHA03095   128 FNINPKVIRLLLRKGADVNALDLYGMTPLAV--LLKsrnaNVELLRLLIDAGADVYAVDDRFRSLLHHhLQSFKPRARIv 205

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   91 QVLIKHSADVNARDKNWQTPLHVAAANKAVKcAEVIIPLL---SSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANIN 167
Cdd:PHA03095   206 RELIRAGCDPAATDMLGNTPLHSMATGSSCK-RSLVLPLLiagISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284


                   .
gi 1333587278  168 A 168
Cdd:PHA03095   285 A 285
Ank_2 pfam12796
Ankyrin repeats (3 copies);
554-648 2.26e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 2.26e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  554 IHYAAAYGHRQCLELLLERTNSGFEDSDSGATksPLHLAAYNGHHQALEVLLQSlVDLDIRDEkGRTALDLAAFKGHTEC 633
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRT--ALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEI 76

                           90
                   ....*....|....*
gi 1333587278  634 VEALINQGASIFVKD 648
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 602-984 2.94e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 80.49  E-value: 2.94e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  602 EVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGA--SIFVKDNVTkrtplhasvinghtlclrlLLEIADNPE 679
Cdd:PHA02876   162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGAdvNIIALDDLS-------------------VLECAVDSK 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  680 VVDVKDA---------KGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGH-EECVQMLLEQEVSILC 749
Cdd:PHA02876   223 NIDTIKAiidnrsninKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNA 302

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  750 KDSRGRTPLHYAAARGHATwlSELLQIALSEEDCSFKDNQGYTPLHWA-CYNGNENCIEVLLEqkcfrefignpftplhc 828
Cdd:PHA02876   303 KNIKGETPLYLMAKNGYDT--ENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLE----------------- 363

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  829 aiindhencasllLGAidssIVNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMA-AENGQAGAVD 907
Cdd:PHA02876   364 -------------LGA----NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVK 426

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333587278  908 ILVNSAqADLTVKDKDLNTPLHLASSKgheKCALLILDKIQDESL-INAKNNALQTPLHVAArnGLKVVVEELLAKGA 984
Cdd:PHA02876   427 TLIDRG-ANVNSKNKDLSTPLHYACKK---NCKLDVIEMLLDNGAdVNAINIQNQYPLLIAL--EYHGIVNILLHYGA 498
Ank_2 pfam12796
Ankyrin repeats (3 copies);
427-500 5.59e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.30  E-value: 5.59e-15
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333587278  427 LHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTgANVNETDDwGRTALHYAAASD 500
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSG 72
PHA02798 PHA02798
ankyrin-like protein; Provisional
 78-364 5.82e-15

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 79.11  E-value: 5.82e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   78 LHRAvaSRSEEAVQVLIKHSADVNARDKNWQTPLhvaaankavkCAeviipLLSsvNVSDrggrtalhhaaLNGHVEMVN 157
Cdd:PHA02798    44 LQRD--SPSTDIVKLFINLGANVNGLDNEYSTPL----------CT-----ILS--NIKD-----------YKHMLDIVK 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  158 LLLAKGANINAFDKKDRRALHWA---AYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNG---QINVVKHLLNLGVE 231
Cdd:PHA02798    94 ILIENGADINKKNSDGETPLYCLlsnGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVD 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  232 IDEI-NVYGNTALHlaCY-----NGQDA-VVNELTDYGANVNQPNNSgftplhfaAASTHGALCLELLVNNG-------- 296
Cdd:PHA02798   174 INTHnNKEKYDTLH--CYfkyniDRIDAdILKLFVDNGFIINKENKS--------HKKKFMEYLNSLLYDNKrfkknild 243

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333587278  297 ---ADVNIQSKD--GKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGAD 364
Cdd:PHA02798   244 fifSYIDINQVDelGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
Ank_2 pfam12796
Ankyrin repeats (3 copies);
692-766 1.52e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 1.52e-14
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333587278  692 LMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEvsILCKDSRGRTPLHYAAARGH 766
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--DVNLKDNGRTALHYAARSGH 73
Ank_2 pfam12796
Ankyrin repeats (3 copies);
376-486 1.54e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 1.54e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  376 LHLAALNAHSDCCRKLLSSGqkysivslfsnehvlsagFEIDTPDKFGRTCLHAAAAGGNVECIKLLqSSGADFHKKDKc 455
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENG------------------ADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDN- 60

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1333587278  456 GRTPLHYAAANCHFHCIETLVTTGANVNETD 486
Cdd:pfam12796   61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 9-167 2.16e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.57  E-value: 2.16e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278    9 QPPLVQAIFSGDPEEIRMLIHKTEDVNALDSEK-RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSE 87
Cdd:PHA02875    69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   88 EAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVN-VSDRGGRTALHHAALNGHVEMVNLLLAKGANI 166
Cdd:PHA02875   149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGADC 228


                   .
gi 1333587278  167 N 167
Cdd:PHA02875   229 N 229
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 585-926 2.27e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.80  E-value: 2.27e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  585 TKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKD---------------- 648
Cdd:PHA02876   178 CITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDlsllkairnedletsl 257

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  649 ------------NVTKRTPLHASVingHTLCL-RLLLEIADNPEVVDVKDAKGQTPLMLAVAYGH-IDAVSLLLEKEANV 714
Cdd:PHA02876   258 llydagfsvnsiDDCKNTPLHHAS---QAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADV 334

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  715 DAVDIMGCTALHRG-IMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQIALSEEDCSFKDNqgyTP 793
Cdd:PHA02876   335 NAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG---TA 411

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  794 LHWACYNgnencievlleqkcfrefiGNPFTPLHcAIINDHENcaslllgaidssiVNCRDDKGRTPLHAAAFAD-HVEC 872
Cdd:PHA02876   412 LHFALCG-------------------TNPYMSVK-TLIDRGAN-------------VNSKNKDLSTPLHYACKKNcKLDV 458

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587278  873 LQLLLRHNAQVNAADNSGKTALMMAAenGQAGAVDILVNSAQA--DLTVKDKDLNT 926
Cdd:PHA02876   459 IEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAElrDSRVLHKSLND 512
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 681-998 2.39e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.41  E-value: 2.39e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  681 VDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQ----------------- 743
Cdd:PHA02876   171 VNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNrsninkndlsllkairn 250

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  744 ---EVSILCKDSR---------GRTPLHYAAargHATWLSELLQIALSE-EDCSFKDNQGYTPLHWACYNGnencievll 810
Cdd:PHA02876   251 edlETSLLLYDAGfsvnsiddcKNTPLHHAS---QAPSLSRLVPKLLERgADVNAKNIKGETPLYLMAKNG--------- 318

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  811 eqkcfrefignpftplhcaiiNDHENCASLLLGAIDssiVNCRDDKGRTPLHAAAFAD-HVECLQLLLRHNAQVNAADNS 889
Cdd:PHA02876   319 ---------------------YDTENIRTLIMLGAD---VNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYC 374

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  890 GKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLASSKGHEKCALLILdkIQDESLINAKNNALQTPLHVAAR 969
Cdd:PHA02876   375 DKTPIHYAAVRNNVVIINTLLDYG-ADIEALSQKIGTALHFALCGTNPYMSVKTL--IDRGANVNSKNKDLSTPLHYACK 451

                          330       340       350
                   ....*....|....*....|....*....|
gi 1333587278  970 NGLKV-VVEELLAKGACVLAVDENGHTPAL 998
Cdd:PHA02876   452 KNCKLdVIEMLLDNGADVNAINIQNQYPLL 481
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 567-749 3.75e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 77.22  E-value: 3.75e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  567 ELLLERTnsgfEDSDSGATKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFV 646
Cdd:PLN03192   511 DLLGDNG----GEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI 586

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  647 KDnVTKRTPLHASVINGHTLCLRLLLEIA--DNPEVvdvkdakGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTA 724
Cdd:PLN03192   587 RD-ANGNTALWNAISAKHHKIFRILYHFAsiSDPHA-------AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658

                          170       180
                   ....*....|....*....|....*
gi 1333587278  725 LHRGIMTGHEECVQMLLEQEVSILC 749
Cdd:PLN03192   659 LQVAMAEDHVDMVRLLIMNGADVDK 683
Ank_2 pfam12796
Ankyrin repeats (3 copies);
758-842 6.08e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.22  E-value: 6.08e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  758 LHYAAARGHATWLSELLQialSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQKCFREFiGNPFTPLHCAIINDHENC 837
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLE---NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-DNGRTALHYAARSGHLEI 76


                   ....*
gi 1333587278  838 ASLLL 842
Cdd:pfam12796   77 VKLLL 81
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 173-408 2.16e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 73.49  E-value: 2.16e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  173 DRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVeIDEINVYG-NTALHLACYNGQ 251
Cdd:PHA02875     2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDiESELHDAVEEGD 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  252 DAVVNELTDYGANVNQP-NNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGG 330
Cdd:PHA02875    81 VKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDI-MKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1333587278  331 EIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGVHSMFPLHLAAL-NAHSDCCRKLLSSGQKYSIVSLFSNEH 408
Cdd:PHA02875   160 CLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIeNNKIDIVRLFIKRGADCNIMFMIEGEE 238
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 48-201 3.57e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 74.13  E-value: 3.57e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   48 AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 127
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333587278  128 PLLSSVNVSDRGgrTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTC 201
Cdd:PLN03192   612 HFASISDPHAAG--DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 792-1010 5.07e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 72.30  E-value: 5.07e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  792 TPLHWACYNGNENCIEVLLEQKCFREFIG-NPFTPLHCAI-INDHENCASLLLGAIDSSI-------------------- 849
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINtKIPHPLLTAIkIGAHDIIKLLIDNGVDTSIlpipciekdmiktildcgid 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  850 VNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLH 929
Cdd:PHA02874   117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLH 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  930 LASSKGHEKCALLILDkiqDESLINAKNNALQTPLHVAARNGLKVVveELLAKGACVLAVDENGHTP---ALACAPNKDV 1006
Cdd:PHA02874   196 NAAEYGDYACIKLLID---HGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPlhhAINPPCDIDI 270


                   ....
gi 1333587278 1007 ADCL 1010
Cdd:PHA02874   271 IDIL 274
Ank_2 pfam12796
Ankyrin repeats (3 copies);
894-990 5.34e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 5.34e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  894 LMMAAENGQAGAVDILVNSaQADLTVKDKDLNTPLHLASSKGHEKCALLILDKIQdeslINAKNNAlQTPLHVAARNGLK 973
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD----VNLKDNG-RTALHYAARSGHL 74

                           90
                   ....*....|....*..
gi 1333587278  974 VVVEELLAKGACVLAVD 990
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
526-615 5.50e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 5.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  526 EKEAASCLEFLLQNEANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSgfEDSDSGATksPLHLAAYNGHHQALEVLL 605
Cdd:pfam12796    6 KNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRT--ALHYAARSGHLEIVKLLL 81

                           90
                   ....*....|
gi 1333587278  606 QSLVDLDIRD 615
Cdd:pfam12796   82 EKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 656-926 9.56e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.62  E-value: 9.56e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  656 LHASVINGHTLCLRLLLE--IADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGH 733
Cdd:PHA03100     1 LYSYIVLTKSRIIKVKNIkyIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKY 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  734 E-----ECVQMLLEQEVSILCKDSRGRTPLHYAAAR--GHATWLSELLQIALseeDCSFKDNQGYTPLHWA--CYNGNEN 804
Cdd:PHA03100    81 NltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGA---NVNIKNSDGENLLHLYleSNKIDLK 157

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  805 CIEVLLEqkcfrefignpftplHCAIINDHENCASLLLGAIDssiVNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVN 884
Cdd:PHA03100   158 ILKLLID---------------KGVDINAKNRVNYLLSYGVP---INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPN 219

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1333587278  885 AADNSGKTALMMAAENGQAGAVDILVNSAQADLTV-------KDKDLNT 926
Cdd:PHA03100   220 LVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIietllyfKDKDLNT 268
PHA02798 PHA02798
ankyrin-like protein; Provisional
 55-273 1.16e-12

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 71.79  E-value: 1.16e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   55 EIIELLILSGARVNAKDNMWLTPLHRAVASRSE-----EAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPL 129
Cdd:PHA02798    52 DIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFM 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  130 L---SSVNVSDRGGRTALHHAALNGH---VEMVNLLLAKGANINA----------------------------------- 168
Cdd:PHA02798   132 IengADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINThnnkekydtlhcyfkynidridadilklfvdngfi 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  169 ---FDKKDRRALhwAAYMGHL---------DVVALLITHgAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEIN 236
Cdd:PHA02798   212 inkENKSHKKKF--MEYLNSLlydnkrfkkNILDFIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIIT 288

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1333587278  237 VYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGF 273
Cdd:PHA02798   289 ELGNTCLFTAFENESKFIFNSILNKKPNKNTISYTYY 325
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 407-761 2.51e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 71.25  E-value: 2.51e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  407 EHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNetd 486
Cdd:PHA02876   162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN--- 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  487 dwgrtalhyaaasdmdRNKTILGNAHENSEelerarelkekeaasclefllqneanpsirdkegynsihyaaayghrqcL 566
Cdd:PHA02876   239 ----------------KNDLSLLKAIRNED-------------------------------------------------L 253

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  567 ELLLERTNSGFE-DSDSGATKSPLHLAAYNGHHQAL-EVLLQSLVDLDIRDEKGRTALDLAAFKGH-TECVEALINQGAS 643
Cdd:PHA02876   254 ETSLLLYDAGFSvNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGAD 333

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  644 IFVKDNVTKrTPLH-ASVINGHTLCLRLLLEIADNpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGC 722
Cdd:PHA02876   334 VNAADRLYI-TPLHqASTLDRNKDIVITLLELGAN---VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG 409

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|
gi 1333587278  723 TALHRGIM-TGHEECVQMLLEQEVSILCKDSRGRTPLHYA 761
Cdd:PHA02876   410 TALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 233-568 3.06e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 70.29  E-value: 3.06e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  233 DEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALCLELL-VNNGADVNIQSKDGKSPLH 311
Cdd:PHA02878    31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIrSINKCSVFYTLVAIKDAFN 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  312 MTAVH-------GRFTRSQTLiqNGGEIDCVDKDGNTPLHVaaryghellINTLITSGADTAKCGVHSM-FPLHLAALNA 383
Cdd:PHA02878   111 NRNVEifkiiltNRYKNIQTI--DLVYIDKKSKDDIIEAEI---------TKLLLSYGADINMKDRHKGnTALHYATENK 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  384 HSDCCRKLLSSGQkysivslfsnehvlsagfEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYA 463
Cdd:PHA02878   180 DQRLTELLLSYGA------------------NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  464 AANC-HFHCIETLVTTGANVN-ETDDWGRTALHYAAASDMDRNKTILGNAHENSEELERAREL----KEKEAASCLEFL- 536
Cdd:PHA02878   242 VGYCkDYDILKLLLEHGVDVNaKSYILGLTALHSSIKSERKLKLLLEYGADINSLNSYKLTPLssavKQYLCINIGRILi 321

                          330       340       350
                   ....*....|....*....|....*....|....*.
gi 1333587278  537 ----LQNEANPSIRDKEGYnSIHYAAAYGHRQCLEL 568
Cdd:PHA02878   322 snicLLKRIKPDIKNSEGF-IDNMDCITSNKRLNQI 356
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 309-628 4.12e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.91  E-value: 4.12e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  309 PLHMtAVHGR-FTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSgadTAKCGVHSmfplhlaALNAHSDC 387
Cdd:PHA02878    40 PLHQ-AVEARnLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS---INKCSVFY-------TLVAIKDA 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  388 CRKLLSSGQKYSIVSLFSNEHVLSAgFEIDTPDKFGRTclhaaaaggNVECIKLLQSSGADFHKKDK-CGRTPLHYAAAN 466
Cdd:PHA02878   109 FNNRNVEIFKIILTNRYKNIQTIDL-VYIDKKSKDDII---------EAEITKLLLSYGADINMKDRhKGNTALHYATEN 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  467 CHFHCIETLVTTGANVNETDDWGRTALHYAAASdmdRNKTIlgnahenseelerarelkekeaascLEFLLQNEANPSIR 546
Cdd:PHA02878   179 KDQRLTELLLSYGANVNIPDKTNNSPLHHAVKH---YNKPI-------------------------VHILLENGASTDAR 230

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  547 DKEGYNSIHYAAAY-GHRQCLELLLER-TNSGFEDSDSGATksPLHLAAYNghHQALEVLLQSLVDLDIRDEKGRTALDL 624
Cdd:PHA02878   231 DKCGNTPLHISVGYcKDYDILKLLLEHgVDVNAKSYILGLT--ALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSS 306


                   ....
gi 1333587278  625 AAFK 628
Cdd:PHA02878   307 AVKQ 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
140-193 5.12e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.52  E-value: 5.12e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1333587278  140 GRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLI 193
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 254-483 5.23e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 69.25  E-value: 5.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  254 VVNELTDYGANVNQPNNSGFTPLHFAAaSTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI- 332
Cdd:PHA02875    17 IARRLLDIGINPNFEIYDGISPIKLAM-KFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAd 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  333 DCVDKDGNTPLHVAARYGHELLINTLITSGADTakcgvhsmfplhlaalnahsdccrkllssgqkysivslfsnehvlsa 412
Cdd:PHA02875    96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADP----------------------------------------------- 128

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333587278  413 gfEIDTPDKFgrTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVN 483
Cdd:PHA02875   129 --DIPNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 781-992 1.37e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.77  E-value: 1.37e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  781 EDCSFKDNqgYTPLHWACYNGNENCIEVLLEQKCF-REFIGNPFTPLH-----CAIINDHENCASLLL--GAIdssiVNC 852
Cdd:PHA03100    28 NDYSYKKP--VLPLYLAKEARNIDVVKILLDNGADiNSSTKNNSTPLHylsniKYNLTDVKEIVKLLLeyGAN----VNA 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  853 RDDKGRTPLHAAAFA--DHVECLQLLLRHNAQVNAADNSGKTALMMAAENG------------------QAGAVDILVNS 912
Cdd:PHA03100   102 PDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNkidlkilkllidkgvdinAKNRVNYLLSY 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  913 AqADLTVKDKDLNTPLHLASSKGHEKCALLILDKIQDeslINAKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVDEN 992
Cdd:PHA03100   182 G-VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGAN---PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 761-930 1.40e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 68.74  E-value: 1.40e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  761 AAARGHATWLSELLQIALseeDCSFKDNQGYTPLHWACYNGNENCIEVLLEQKC---FREFIGNpfTPLHCAIINDHENC 837
Cdd:PLN03192   532 VASTGNAALLEELLKAKL---DPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACnvhIRDANGN--TALWNAISAKHHKI 606

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  838 ASLLLGAIDSSIVNCRDDKgrtpLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVDILV-NSAQAD 916
Cdd:PLN03192   607 FRILYHFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLImNGADVD 682

                          170
                   ....*....|....
gi 1333587278  917 LTVKDKDLnTPLHL 930
Cdd:PLN03192   683 KANTDDDF-SPTEL 695
Ank_2 pfam12796
Ankyrin repeats (3 copies);
343-453 1.54e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.67  E-value: 1.54e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  343 LHVAARYGHELLINTLITSGADTAKCGVHSMFPLHLAALNAHSDCCRKLLSSGQKYSIVSlfsnehvlsagfeidtpdkf 422
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN-------------------- 60

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1333587278  423 GRTCLHAAAAGGNVECIKLLQSSGADFHKKD 453
Cdd:pfam12796   61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 710-996 1.94e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.60  E-value: 1.94e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  710 KEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQIALseedcsfKDNQ 789
Cdd:PHA02878    26 TENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSIN-------KCSV 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  790 GYT--PLHWACYNGNENCIEVLLEQKCFREFignpftplhcaIINDHENCASLLLGAIDSSI----------VNCRD-DK 856
Cdd:PHA02878    99 FYTlvAIKDAFNNRNVEIFKIILTNRYKNIQ-----------TIDLVYIDKKSKDDIIEAEItklllsygadINMKDrHK 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  857 GRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLASSKGH 936
Cdd:PHA02878   168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHISVGYCK 246

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333587278  937 EKCALLILdkIQDESLINAKNNALQ-TPLHVAARNGLKVVVeeLLAKGACVLAVDENGHTP 996
Cdd:PHA02878   247 DYDILKLL--LEHGVDVNAKSYILGlTALHSSIKSERKLKL--LLEYGADINSLNSYKLTP 303
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 1333587278  423 GRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLV 476
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 166-463 2.04e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.60  E-value: 2.04e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  166 INAFDKKDRRA----------LHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEI 235
Cdd:PHA02878    20 IEYIDHTENYStsaslipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVF 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  236 NVYgnTALHLACYNGQDAVVNE-LTDYGANVNQPNNSGFTPLHFAAASThgALCLELLVNNGADVNIQSKD-GKSPLHMT 313
Cdd:PHA02878   100 YTL--VAIKDAFNNRNVEIFKIiLTNRYKNIQTIDLVYIDKKSKDDIIE--AEITKLLLSYGADINMKDRHkGNTALHYA 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  314 AVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADT---AKCGVHsmfPLHLAAlnahsdccrk 390
Cdd:PHA02878   176 TENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTdarDKCGNT---PLHISV---------- 242

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333587278  391 llSSGQKYSIVSLfsnehVLSAGFEIDTPDKF-GRTCLHAAAAGGNVecIKLLQSSGADFHKKDKCGRTPLHYA 463
Cdd:PHA02878   243 --GYCKDYDILKL-----LLEHGVDVNAKSYIlGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 150-275 5.98e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 63.30  E-value: 5.98e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  150 NGHVEMVNLLLAKGANINAFDKKDRRAL--HWAAYMGHL--DVVALLITHGAEVTCKDKKGYTPLHAAASNG--QINVVK 223
Cdd:PHA02859    63 KVNVEILKFLIENGADVNFKTRDNNLSAlhHYLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHMYMCNFnvRINVIK 142

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1333587278  224 HLLNLGVEIDEINVYGNTALH-LACYNGQDAVVNELTDYGANVNQPNNSGFTP 275
Cdd:PHA02859   143 LLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
Ank_4 pfam13637
Ankyrin repeats (many copies);
174-226 6.57e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 6.57e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1333587278  174 RRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLL 226
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 544-721 7.86e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 65.76  E-value: 7.86e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  544 SIRDKEGYNSIHYAAAYGHRQCLELLLE-RTNSGFEDsDSGATksPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTAL 622
Cdd:PHA02874   118 NIKDAELKTFLHYAIKKGDLESIKMLFEyGADVNIED-DNGCY--PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  623 DLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGhtlclRLLLEIADNPEVVDVKDAKGQTPLMLAVAYG-HI 701
Cdd:PHA02874   195 HNAAEYGDYACIKLLIDHGNHIMNKCK-NGFTPLHNAIIHN-----RSAIELLINNASINDQDIDGSTPLHHAINPPcDI 268

                          170       180
                   ....*....|....*....|
gi 1333587278  702 DAVSLLLEKEANVDAVDIMG 721
Cdd:PHA02874   269 DIIDILLYHKADISIKDNKG 288
Ank_2 pfam12796
Ankyrin repeats (3 copies);
243-336 9.82e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 9.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  243 LHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGAlCLELLVNNgADVNIQSkDGKSPLHMTAVHGRFTRS 322
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLE-IVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                           90
                   ....*....|....
gi 1333587278  323 QTLIQNGGEIDCVD 336
Cdd:pfam12796   78 KLLLEKGADINVKD 91
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 49-280 1.16e-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: 65.87  E-value: 1.16e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   49 AFLGDAEIIELLILSGARVNAK-------DNMWLTPLHRAVA-SRSEEAVQVLIKHSADVNARDknwqTPLHVAAANKAV 120
Cdd:TIGR00870   20 AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAISLEYVD 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  121 KCAEVIIPLLSS---------VNVSDRG----GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRA----- 176
Cdd:TIGR00870   96 AVEAILLHLLAAfrksgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDsfyhg 175

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  177 ---LHWAAYMGHLDVVALLITHGAEVTCKDKKGytplhaaasngqiNVVKHLLNLGVEideiNVYGNTALHLACYngqda 253
Cdd:TIGR00870  176 espLNAAACLGSPSIVALLSEDPADILTADSLG-------------NTLLHLLVMENE----FKAEYEELSCQMY----- 233

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1333587278  254 vvNELTDYGANVNQ-------PNNSGFTPLHFAA 280
Cdd:TIGR00870  234 --NFALSLLDKLRDskeleviLNHQGLTPLKLAA 265
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 459-761 1.59e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.90  E-value: 1.59e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  459 PLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAasdMDRNKtiLGNAHENSEELERARELKEKeaasclefllq 538
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIC---KEPNK--LGMKEMIRSINKCSVFYTLV----------- 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  539 neanpSIRDKEGYNSIHYAAA-----YGHRQCLELLLERTNSGFEDSDSGATKsplhlaaynghhqaleVLLQSLVDLDI 613
Cdd:PHA02878   104 -----AIKDAFNNRNVEIFKIiltnrYKNIQTIDLVYIDKKSKDDIIEAEITK----------------LLLSYGADINM 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  614 RDE-KGRTALDLAAFKGHTECVEALINQGASIFVKDnVTKRTPLHASVINGHTLCLRLLLEiadNPEVVDVKDAKGQTPL 692
Cdd:PHA02878   163 KDRhKGNTALHYATENKDQRLTELLLSYGANVNIPD-KTNNSPLHHAVKHYNKPIVHILLE---NGASTDARDKCGNTPL 238

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1333587278  693 MLAVAY-GHIDAVSLLLEKEANVDAVD-IMGCTALHRGIMTghEECVQMLLEQEVSILCKDSRGRTPLHYA 761
Cdd:PHA02878   239 HISVGYcKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 153-315 1.82e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 64.24  E-value: 1.82e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  153 VEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVT-CKDKKGYTPLHAAASNGQINVVKHLLNLGVE 231
Cdd:PHA02875    48 SEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGAD 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  232 IDEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALClELLVNNGADVNIQSKDGKSPLH 311
Cdd:PHA02875   128 PDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAIC-KMLLDSGANIDYFGKNGCVAAL 206


                   ....
gi 1333587278  312 MTAV 315
Cdd:PHA02875   207 CYAI 210
Ank_2 pfam12796
Ankyrin repeats (3 copies);
310-400 2.08e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 2.08e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  310 LHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGAdtAKCGVHSMFPLHLAALNAHSDCCR 389
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 1333587278  390 KLLSSGQKYSI 400
Cdd:pfam12796   79 LLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 799-1003 5.11e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 62.76  E-value: 5.11e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  799 YNGNENCIEVLLEQKCFREFIGN------PFTPLHCAIindHENCASLLLGAIDSSI-VNCRDDKGRTPLHAAAFADHV- 870
Cdd:PHA03100     6 VLTKSRIIKVKNIKYIIMEDDLNdysykkPVLPLYLAK---EARNIDVVKILLDNGAdINSSTKNNSTPLHYLSNIKYNl 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  871 ----ECLQLLLRHNAQVNAADNSGKTALMMAAEN--GQAGAVDILVNSAqADLTVKDKDLNTPLHLASSKGHEK---CAL 941
Cdd:PHA03100    83 tdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDlkiLKL 161

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1333587278  942 LILDK------------IQDESLINAKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVDENGHTPA-LACAPN 1003
Cdd:PHA03100   162 LIDKGvdinaknrvnylLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLhIAILNN 236
Ank_4 pfam13637
Ankyrin repeats (many copies);
690-741 5.70e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 5.70e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1333587278  690 TPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLL 741
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 3-114 6.44e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 6.44e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278    3 VLKLTDQPPLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVA-AFLGDAEIIELLILSGARVNAKDNMW-LTPLHR 80
Cdd:PHA02878   196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILgLTALHS 275

                           90       100       110
                   ....*....|....*....|....*....|....
gi 1333587278   81 AVasRSEEAVQVLIKHSADVNARDKNWQTPLHVA 114
Cdd:PHA02878   276 SI--KSERKLKLLLEYGADINSLNSYKLTPLSSA 307
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 183-374 1.54e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.19  E-value: 1.54e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  183 MGHLDVVALLITHGAEVTckDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYG 262
Cdd:PLN03192   504 LHDLNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  263 ANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSkdGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTP 342
Cdd:PLN03192   582 CNVHIRDANGNTALWNAISAKHHKI-FRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1333587278  343 LHVAARYGHELLINTLITSGADTAKCGVHSMF 374
Cdd:PLN03192   659 LQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
Ank_4 pfam13637
Ankyrin repeats (many copies);
587-638 1.74e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 1.74e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1333587278  587 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALI 638
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 144-226 1.97e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.84  E-value: 1.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  144 LHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQINVVK 223
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165


                   ...
gi 1333587278  224 HLL 226
Cdd:PTZ00322   166 LLS 168
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 147-305 2.71e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.42  E-value: 2.71e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  147 AALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQ---INVVK 223
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHhkiFRILY 611

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  224 HLLNLGveideiNVY-GNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQ 302
Cdd:PLN03192   612 HFASIS------DPHaAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDM-VRLLIMNGADVDKA 684


                   ...
gi 1333587278  303 SKD 305
Cdd:PLN03192   685 NTD 687
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 653-765 5.64e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.62  E-value: 5.64e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  653 RTPLHASVINGHTLCLRLLLEIadNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTG 732
Cdd:PHA02875    69 ESELHDAVEEGDVKAVEELLDL--GKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                           90       100       110
                   ....*....|....*....|....*....|...
gi 1333587278  733 HEECVQMLLEQEVSILCKDSRGRTPLHYAAARG 765
Cdd:PHA02875   147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179
PHA03095 PHA03095
ankyrin-like protein; Provisional
 20-164 6.17e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.65  E-value: 6.17e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   20 DPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGD--AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHS 97
Cdd:PHA03095   201 RARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333587278   98 ADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRggrtALHHAALNGHV-------EMVNLLLAKGA 164
Cdd:PHA03095   281 ADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA----TLNTASVAGGDipsdatrLCVAKVVLRGA 350
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 829-1050 8.82e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.85  E-value: 8.82e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  829 AIINDHENCASLLLgaiDSSI-VNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVD 907
Cdd:PHA02875     9 AILFGELDIARRLL---DIGInPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  908 ILVNSAQADLTVKDKDLNTPLHLASSKGHEKCALLILDKIQDESLINAKNNalqTPLHVAARNGLKVVVEELLAKGACVL 987
Cdd:PHA02875    86 ELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKF---SPLHLAVMMGDIKGIELLIDHKACLD 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333587278  988 AVDENGHTPALACAPNKDVADCLALILATMTLSPSSAMTAVNFVCFKKDN---------LSRTTLSNLGSMV 1050
Cdd:PHA02875   163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENnkidivrlfIKRGADCNIMFMI 234
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 585-775 8.85e-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: 8.85e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  585 TKSPLHLAAYNGHHQALEVLL-QSLVDLDIRDEKGRTALDLAAFKGHTECVEALINqGASIFVKDNVTK-----RTPLHA 658
Cdd:cd22192     17 SESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLME-AAPELVNEPMTSdlyqgETALHI 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  659 SVINGHTLCLRLLLEI-AD--NPEVVD---VKDAK-----GQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHR 727
Cdd:cd22192     96 AVVNQNLNLVRELIARgADvvSPRATGtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333587278  728 GIMTGHEECV-QM---LLEQEVSI------LCKDSRGRTPLHYAAARGHATWLSELLQ 775
Cdd:cd22192    176 LVLQPNKTFAcQMydlILSYDKEDdlqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 690-996 1.02e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.82  E-value: 1.02e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  690 TPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEV--SILckdsrgrtPLHYAAARGHA 767
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVdtSIL--------PIPCIEKDMIK 108

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  768 TWLSellqialSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQKcfrefignpftplhcaiindhencaslllgaids 847
Cdd:PHA02874   109 TILD-------CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYG---------------------------------- 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  848 SIVNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTP 927
Cdd:PHA02874   148 ADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG-NHIMNKCKNGFTP 226

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  928 LHLASSKGHEKCALLIldkiqDESLINAKNNALQTPLHVAARNGLKV-VVEELLAKGACVLAVDENGHTP 996
Cdd:PHA02874   227 LHNAIIHNRSAIELLI-----NNASINDQDIDGSTPLHHAINPPCDIdIIDILLYHKADISIKDNKGENP 291
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 620-802 1.18e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 58.87  E-value: 1.18e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  620 TALDLAAFKGHTECVEALI-NQGASIFVKDNVTKrTPLHASVINGHTLCLRLLLEIAdnPEVVDVKDA----KGQTPLML 694
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGE-TALHVAALYDNLEAAVVLMEAA--PELVNEPMTsdlyQGETALHI 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  695 AVAYGHIDAVSLLLEKEANVDAVDIMGcTALHRGI---------------MTGHEECVQMLLEQEVSILCKDSRGRTPLH 759
Cdd:cd22192     96 AVVNQNLNLVRELIARGADVVSPRATG-TFFRPGPknliyygehplsfaaCVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1333587278  760 YAAARGHATWLSELLQIALS--EEDCS-----FKDNQGYTPLHWACYNGN 802
Cdd:cd22192    175 ILVLQPNKTFACQMYDLILSydKEDDLqpldlVPNNQGLTPFKLAAKEGN 224
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 55-317 1.30e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 58.60  E-value: 1.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   55 EIIELLILSGARVNAKDNMwLTPL-----HRAVAS-RSEEAVQVLIKHSADVNARDKNWQTPlhvaaankavkcaevIIP 128
Cdd:PHA02989    51 KIVKLLIDNGADVNYKGYI-ETPLcavlrNREITSnKIKKIVKLLLKFGADINLKTFNGVSP---------------IVC 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  129 LLSSVNVSDrggrtalhhaalnghVEMVNLLLAKGANINafDKKDRRA---LH--WAAYMGHLDVVALLITHGAEV-TCK 202
Cdd:PHA02989   115 FIYNSNINN---------------CDMLRFLLSKGINVN--DVKNSRGynlLHmyLESFSVKKDVIKILLSFGVNLfEKT 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  203 DKKGYTP----LHAAASNGQINVVKHLLNLGVEIDEINVYGNTAL------HLACYNGQDAVVNELTDYgANVNQPNNSG 272
Cdd:PHA02989   178 SLYGLTPmniyLRNDIDVISIKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLNFILKY-IKINKKDKKG 256

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1333587278  273 FTPLhFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHG 317
Cdd:PHA02989   257 FNPL-LISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHG 300
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 689-910 1.54e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 1.54e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  689 QTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHAT 768
Cdd:PHA02875     3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  769 WLSELLQIALSEEDCSFKDnqGYTPLHWACYNGNENCIEVLLEQKCFREFIG-NPFTPLHCAIINDHENCASLLLGaiDS 847
Cdd:PHA02875    83 AVEELLDLGKFADDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNtDKFSPLHLAVMMGDIKGIELLID--HK 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1333587278  848 SIVNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALM-MAAENGQAGAVDILV 910
Cdd:PHA02875   159 ACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFI 222
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 206-359 1.68e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 58.49  E-value: 1.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  206 GYTPLHAAASNGQINVVKHLLNLGVEIdeINV------Y-GNTALHLACYNGQDAVVNELTDYGANVNQPNNSG--FT-- 274
Cdd:cd22192     51 GETALHVAALYDNLEAAVVLMEAAPEL--VNEpmtsdlYqGETALHIAVVNQNLNLVRELIARGADVVSPRATGtfFRpg 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  275 ----------PLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI---------QNGGEIDCV 335
Cdd:cd22192    129 pknliyygehPLSFAACVGNEEI-VRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYdlilsydkeDDLQPLDLV 207

                          170       180
                   ....*....|....*....|....*
gi 1333587278  336 -DKDGNTPLHVAARYGHELLINTLI 359
Cdd:cd22192    208 pNNQGLTPFKLAAKEGNIVMFQHLV 232
PHA02946 PHA02946
ankyin-like protein; Provisional
 53-312 1.98e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 58.14  E-value: 1.98e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   53 DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKavkcAEVIipllss 132
Cdd:PHA02946    51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTD----DEVI------ 120

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  133 vnvsdrggrtalhhaalnghvEMVNLLLAKGANINafdkkdrralhwaaymghldvvallithgaevTCKDKKGYTPLHA 212
Cdd:PHA02946   121 ---------------------ERINLLVQYGAKIN--------------------------------NSVDEEGCGPLLA 147

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  213 AASNGQiNVVKHLLNLGVEIDEINVYGNTAL--HLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALCLE 290
Cdd:PHA02946   148 CTDPSE-RVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKNVDII 226

                          250       260
                   ....*....|....*....|..
gi 1333587278  291 LLVNNGADVNIQSKDGKSPLHM 312
Cdd:PHA02946   227 NLLLPSTDVNKQNKFGDSPLTL 248
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 340-494 2.07e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 58.10  E-value: 2.07e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  340 NTPLHVAARYGHELLINTLITS-GADTAKCGVHSMFPLHLAALNAHSDCCRKLLSSgqkysiVSLFSNEHVLSAGFEidt 418
Cdd:cd22192     18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEA------APELVNEPMTSDLYQ--- 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  419 pdkfGRTCLHAAAAGGNVECIKLLQSSGAD----------FHKKDKC----GRTPLHYAAANCHFHCIETLVTTGANVNE 484
Cdd:cd22192     89 ----GETALHIAVVNQNLNLVRELIARGADvvspratgtfFRPGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRA 164

                          170
                   ....*....|
gi 1333587278  485 TDDWGRTALH 494
Cdd:cd22192    165 QDSLGNTVLH 174
Ank_4 pfam13637
Ankyrin repeats (many copies);
456-498 2.09e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 2.09e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1333587278  456 GRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAA 498
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAAS 43
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 429-644 2.20e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.34  E-value: 2.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  429 AAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAASDMDRNKTIL 508
Cdd:PLN03192   531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  509 gnahenseelerarelkekeaasclefllqneanpsirdkegynsIHYAAAyghrqclelllertnsgfedSDSGATKSP 588
Cdd:PLN03192   611 ---------------------------------------------YHFASI--------------------SDPHAAGDL 625

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587278  589 LHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASI 644
Cdd:PLN03192   626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 587-757 2.39e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.69  E-value: 2.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  587 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGAsiFVKDNVTKR--TPLHASVINGH 664
Cdd:PHA02875    37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK--FADDVFYKDgmTPLHLATILKK 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  665 TLCLRLLLEIADNPevvDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQE 744
Cdd:PHA02875   115 LDIMKLLIARGADP---DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191

                          170
                   ....*....|...
gi 1333587278  745 VSIlckDSRGRTP 757
Cdd:PHA02875   192 ANI---DYFGKNG 201
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 11-147 2.74e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.67  E-value: 2.74e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   11 PLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVA-SRSeeA 89
Cdd:PHA02874   160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIhNRS--A 237

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333587278   90 VQVLIkHSADVNARDKNWQTPLHVAAankAVKCAEVIIPLL----SSVNVSDRGGRTALHHA 147
Cdd:PHA02874   238 IELLI-NNASINDQDIDGSTPLHHAI---NPPCDIDIIDILlyhkADISIKDNKGENPIDTA 295
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 108-282 3.62e-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: 57.58  E-value: 3.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  108 QTPLHVAAANKAVKCAEVIIPLLSSVNVSDRG--------------GRTALHHAALNGHVEMVNLLLAKGANINA----- 168
Cdd:cd21882     27 KTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAratgr 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  169 FDKKDRR--------ALHWAAYMGHLDVVALLITHGAE---VTCKDKKGYTPLHAAasngqinvvkhllnlgVEIDEiNV 237
Cdd:cd21882    107 FFRKSPGnlfyfgelPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHAL----------------VLQAD-NT 169

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1333587278  238 YGNTALHLACYNGqdavvneLTDYGANVNQ-------PNNSGFTPLHFAAAS 282
Cdd:cd21882    170 PENSAFVCQMYNL-------LLSYGAHLDPtqqleeiPNHQGLTPLKLAAVE 214
Ank_4 pfam13637
Ankyrin repeats (many copies);
109-160 3.66e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 3.66e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1333587278  109 TPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLL 160
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 274-461 3.83e-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: 3.83e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  274 TPLhFAAASTHGALCLE-LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGE-----IDCVDKDGNTPLHVAA 347
Cdd:cd22192     19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  348 RYGHELLINTLITSGADTAK---CGvhSMFPLHLAALnahsdccrkllssgqkysivsLFSNEHVLSagfeidtpdkFgr 424
Cdd:cd22192     98 VNQNLNLVRELIARGADVVSpraTG--TFFRPGPKNL---------------------IYYGEHPLS----------F-- 142

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1333587278  425 tclhaAAAGGNVECIKLLQSSGADFHKKDKCGRTPLH 461
Cdd:cd22192    143 -----AACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
Ank_4 pfam13637
Ankyrin repeats (many copies);
74-127 4.45e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 4.45e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1333587278   74 WLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 127
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 45-326 5.75e-08

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 56.84  E-value: 5.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   45 LHvaAFLG----DAEIIELLILSGARVNAKDNMWLTPLHRAV--ASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANK 118
Cdd:PHA02716   181 LH--AYLGnmyvDIDILEWLCNNGVNVNLQNNHLITPLHTYLitGNVCASVIKKIIELGGDMDMKCVNGMSPIMTYIINI 258

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  119 AVKCAEVI----------------------IPLLSSVNVS---------------DRGGRTALHHAAL--NGHVEMVNLL 159
Cdd:PHA02716   259 DNINPEITniyiesldgnkvknipmilhsyITLARNIDISvvysflqpgvklhykDSAGRTCLHQYILrhNISTDIIKLL 338

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  160 LAKGANINAFDKKDRRALHwaAYMG----------------HLDVVALLITHGAEVTCKDKKGYTPLHAAASNGQ----- 218
Cdd:PHA02716   339 HEYGNDLNEPDNIGNTVLH--TYLSmlsvvnildpetdndiRLDVIQCLISLGADITAVNCLGYTPLTSYICTAQnymyy 416

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  219 -----------INVVKH--LLNLGVEIDE--------INVYG-NTALHLACYNGQDAVVNELTDYGANVNQPNN-----S 271
Cdd:PHA02716   417 diidclisdkvLNMVKHriLQDLLIRVDDtpciihhiIAKYNiPTDLYTDEYEPYDSTKIHDVYHCAIIERYNNavcetS 496

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1333587278  272 GFTPLHFAAASTHGAL----CLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI 326
Cdd:PHA02716   497 GMTPLHVSIISHTNANivmdSFVYLLSIQYNINIPTKNGVTPLMLTMRNNRLSGHQWYI 555
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 77-250 6.30e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 54.44  E-value: 6.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   77 PLHRAVASRSEEAVQVLIKHSADVNardKNWQTPLHVAAANKAV--KCAEVIIPLLSSVNVSDRG-GRTALHH-AALNGH 152
Cdd:PHA02859    24 PLFYYVEKDDIEGVKKWIKFVNDCN---DLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRDnNLSALHHyLSFNKN 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  153 V--EMVNLLLAKGANINAFDKKDRRALHwaAYMGH----LDVVALLITHGAEVTCKDKKGYTPLHA-AASNGQINVVKHL 225
Cdd:PHA02859   101 VepEILKILIDSGSSITEEDEDGKNLLH--MYMCNfnvrINVIKLLIDSGVSFLNKDFDNNNILYSyILFHSDKKIFDFL 178

                          170       180
                   ....*....|....*....|....*
gi 1333587278  226 LNLGVEIDEINVYGNTALHLACYNG 250
Cdd:PHA02859   179 TSLGIDINETNKSGYNCYDLIKFRN 203
PHA02946 PHA02946
ankyin-like protein; Provisional
 323-571 7.20e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 56.22  E-value: 7.20e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  323 QTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGVHSMFPLHL-------------------AALNA 383
Cdd:PHA02946    56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsgtddevierinllvqygAKINN 135

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  384 HSD--CCRKLLSSGQKYSIVSlfsnEHVLSAGFEIDTPDKFGRTCLHAAAAGGN--VECIKLLQSSGADFHKKDKCGRTP 459
Cdd:PHA02946   136 SVDeeGCGPLLACTDPSERVF----KKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHDGNTP 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  460 LHYAAANCHFHC-IETLVTTGANVNETDDWGRTALHYAAASdmdrnktiLGNAHENSEELERARELKEKEAASCLeFLLQ 538
Cdd:PHA02946   212 LHIVCSKTVKNVdIINLLLPSTDVNKQNKFGDSPLTLLIKT--------LSPAHLINKLLSTSNVITDQTVNICI-FYDR 282

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1333587278  539 NEANPSIRDK-EGYNSIHY--AAAYGHRQCLELLLE 571
Cdd:PHA02946   283 DDVLEIINDKgKQYDSTDFkmAVEVGSIRCVKYLLD 318
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 12-97 7.78e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 7.78e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   12 LVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQ 91
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165


                   ....*.
gi 1333587278   92 VLIKHS 97
Cdd:PTZ00322   166 LLSRHS 171
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 208-345 1.05e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.17  E-value: 1.05e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  208 TPLHAAASNGQINVVKHLL-NLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYGAN-VNQPNNS----GFTPLHFAAA 281
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSdlyqGETALHIAVV 98

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333587278  282 STHGALcLELLVNNGADVN---------IQSKD-----GKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHV 345
Cdd:cd22192     99 NQNLNL-VRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 840-916 1.09e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 1.09e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1333587278  840 LLLGAIDSsivNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVDILVNSAQAD 916
Cdd:PTZ00322   101 LLTGGADP---NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCH 174
Ank_4 pfam13637
Ankyrin repeats (many copies);
857-910 1.50e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 1.50e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1333587278  857 GRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVDILV 910
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 7-114 1.56e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.27  E-value: 1.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278    7 TDQPPLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVAS-R 85
Cdd:PHA02878   167 KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcK 246

                           90       100       110
                   ....*....|....*....|....*....|
gi 1333587278   86 SEEAVQVLIKHSADVNARDKNWQ-TPLHVA 114
Cdd:PHA02878   247 DYDILKLLLEHGVDVNAKSYILGlTALHSS 276
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 281-350 1.92e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 1.92e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  281 ASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYG 350
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 11-171 1.95e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 52.90  E-value: 1.95e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   11 PLVQAIFSGDPEEIRMLIHKTEDVNALDsekRTPLH--VAAFLGDAEIIELLILSGARVNAK---DNmwLTPLHRAVA-- 83
Cdd:PHA02859    24 PLFYYVEKDDIEGVKKWIKFVNDCNDLY---ETPIFscLEKDKVNVEILKFLIENGADVNFKtrdNN--LSALHHYLSfn 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   84 -SRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAevIIPLLSSVNVS----DRGGRTALH-HAALNGHVEMVN 157
Cdd:PHA02859    99 kNVEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRIN--VIKLLIDSGVSflnkDFDNNNILYsYILFHSDKKIFD 176

                          170
                   ....*....|....
gi 1333587278  158 LLLAKGANINAFDK 171
Cdd:PHA02859   177 FLTSLGIDINETNK 190
Ank_4 pfam13637
Ankyrin repeats (many copies);
723-766 1.97e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.97e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1333587278  723 TALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGH 766
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
Ank_4 pfam13637
Ankyrin repeats (many copies);
206-251 2.42e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 2.42e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1333587278  206 GYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQ 251
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 854-990 2.57e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.87  E-value: 2.57e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  854 DDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKDLntpLHLASS 933
Cdd:PLN03192   555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL---LCTAAK 631

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333587278  934 KGHekcaLLILDKIQDESL-INAKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVD 990
Cdd:PLN03192   632 RND----LTAMKELLKQGLnVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 189-261 2.73e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 2.73e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333587278  189 VALLITHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDY 261
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
42-94 3.80e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 3.80e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1333587278   42 RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLI 94
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 69-198 4.08e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 4.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   69 AKDNMWLTPLHRAVasrSEEAVQVLIKHSADVNArdknwqtpLHVAAANKAVKcAEVIIPLLSSVNVSDRGGRTALHHAA 148
Cdd:PTZ00322    56 ATENKDATPDHNLT---TEEVIDPVVAHMLTVEL--------CQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIAC 123

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1333587278  149 LNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAE 198
Cdd:PTZ00322   124 ANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173
Ank_5 pfam13857
Ankyrin repeats (many copies);
192-246 5.21e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 5.21e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587278  192 LITHG-AEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHLA 246
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 792-982 5.83e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.48  E-value: 5.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  792 TPLHWACYNGNENCIEVLLEQK----CFREFIGNpfTPLHCAIINDHENCASLLLGAiDSSIVN--CRDD--KGRTPLHA 863
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCPscdlFQRGALGE--TALHVAALYDNLEAAVVLMEA-APELVNepMTSDlyQGETALHI 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  864 AAFADHVECLQLLLRHNAQVNAADNS--------------GKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLH 929
Cdd:cd22192     96 AVVNQNLNLVRELIARGADVVSPRATgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVLH 174

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  930 LASSKGHEKCA------LLILDKIQDE-SLINAKNNALQTPLHVAARNGLKVVVEELLAK 982
Cdd:cd22192    175 ILVLQPNKTFAcqmydlILSYDKEDDLqPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 325-493 6.90e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 6.90e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  325 LIQNGGEIDCVDKDGNtpLHVAARYGHELLINTLITSGADTAKCGVHSMFPLHLAALNAHSDCCRKLLSSGQKYSIVSLF 404
Cdd:PLN03192   513 LGDNGGEHDDPNMASN--LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDAN 590

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  405 SNE---HVLSAG----FEI-------DTPDKFGrTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFH 470
Cdd:PLN03192   591 GNTalwNAISAKhhkiFRIlyhfasiSDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVD 669

                          170       180
                   ....*....|....*....|....*.
gi 1333587278  471 CIETLVTTGANV---NETDDWGRTAL 493
Cdd:PLN03192   670 MVRLLIMNGADVdkaNTDDDFSPTEL 695
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 738-981 8.16e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 53.16  E-value: 8.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  738 QMLLE-QEVSILCKDSRGRTPLHYAAARGHATWLSELLQialseedcsFKDNQGY---TPLHWACYNGNENCIEVLLEQK 813
Cdd:TIGR00870   35 RDLEEpKKLNINCPDRLGRSALFVAAIENENLELTELLL---------NLSCRGAvgdTLLHAISLEYVDAVEAILLHLL 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  814 CFREFIGNPF--------------TPLHCAIINDHENCASLLL--GAIDSSIVNCRDDK----------GRTPLHAAAFA 867
Cdd:TIGR00870  106 AAFRKSGPLElandqytseftpgiTALHLAAHRQNYEIVKLLLerGASVPARACGDFFVksqgvdsfyhGESPLNAAACL 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  868 DHVECLQLLLRHNAQVNAADNSGKTALMMAAEngqagavdilvnsaQADLTVKDKDLNTPLHLAsskghekcALLILDKI 947
Cdd:TIGR00870  186 GSPSIVALLSEDPADILTADSLGNTLLHLLVM--------------ENEFKAEYEELSCQMYNF--------ALSLLDKL 243

                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1333587278  948 QD-ESLINAKNNALQTPLHVAARNGLKVVVEELLA 981
Cdd:TIGR00870  244 RDsKELEVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 22-160 9.50e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 9.50e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   22 EEIRMLIHKTEDVNALDSEKRTPLHVAAflgDAEIIELLILsgarvnakdNMWLTPLHRAVASRSEEAVQVLIKHSADVN 101
Cdd:PTZ00322    42 EEIARIDTHLEALEATENKDATPDHNLT---TEEVIDPVVA---------HMLTVELCQLAASGDAVGARILLTGGADPN 109

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1333587278  102 ARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLL 160
Cdd:PTZ00322   110 CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
824-877 1.00e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 1.00e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1333587278  824 TPLHCAIINDHENCASLLLGAidSSIVNCRDDKGRTPLHAAAFADHVECLQLLL 877
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEK--GADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 898-993 1.05e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  898 AENGQAGAVDILVNSAqADLTVKDKDLNTPLHLASSKGHEKCALLILDKIQDESLINAKNNalqTPLHVAARNGLKVVVE 977
Cdd:PTZ00322    90 AASGDAVGARILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK---TPLELAEENGFREVVQ 165

                           90
                   ....*....|....*.
gi 1333587278  978 ELLAKGACVLAVDENG 993
Cdd:PTZ00322   166 LLSRHSQCHFELGANA 181
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 587-831 1.34e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 52.39  E-value: 1.34e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  587 SPLHLAAYNGHHQALEVLLQSLvdlDIRDEKGRTALdLAAFKGHTECVEALIN--------QGASIFVKDNVTKR----- 653
Cdd:TIGR00870   54 SALFVAAIENENLELTELLLNL---SCRGAVGDTLL-HAISLEYVDAVEAILLhllaafrkSGPLELANDQYTSEftpgi 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  654 TPLHASVINGHTLCLRLLLEIADNPEV----VDVKDAKGQT-------PLMLAVAYGHIDAVSLLLEKEANVDAVDIMGC 722
Cdd:TIGR00870  130 TALHLAAHRQNYEIVKLLLERGASVPAracgDFFVKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  723 TALHRGIMtgheECVQMLLEQEVSILCKDsrgrtplhYAaarghatwLSELLQIALSEEDCSFKDNQGYTPLHWACYNGN 802
Cdd:TIGR00870  210 TLLHLLVM----ENEFKAEYEELSCQMYN--------FA--------LSLLDKLRDSKELEVILNHQGLTPLKLAAKEGR 269

                          250       260       270
                   ....*....|....*....|....*....|
gi 1333587278  803 ENCIEVLLEQKCF-REFIGNPFTPLHCAII 831
Cdd:TIGR00870  270 IVLFRLKLAIKYKqKKFVAWPNGQQLLSLY 299
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 209-368 2.40e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 49.43  E-value: 2.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  209 PLHAAASNGQINVVKHLLNLgveIDEINVYGNTALHlACYNGQDAVVNE---LTDYGANVN-QPNNSGFTPLHFAAASTH 284
Cdd:PHA02859    24 PLFYYVEKDDIEGVKKWIKF---VNDCNDLYETPIF-SCLEKDKVNVEIlkfLIENGADVNfKTRDNNLSALHHYLSFNK 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  285 GAL--CLELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLI-NTLI 359
Cdd:PHA02859   100 NVEpeILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKKIfDFLT 179


                   ....*....
gi 1333587278  360 TSGADTAKC 368
Cdd:PHA02859   180 SLGIDINET 188
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 2.41e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 2.41e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1333587278   10 PPLVQAIFSGDPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLI 61
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 587-813 2.64e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.42  E-value: 2.64e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  587 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKgrTALDLAAFKGHTECVEA-LINQGASIFVKDNVTKRTPLHASVINghT 665
Cdd:PHA02878    72 TPLHIICKEPNKLGMKEMIRSINKCSVFYTL--VAIKDAFNNRNVEIFKIiLTNRYKNIQTIDLVYIDKKSKDDIIE--A 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  666 LCLRLLLEIADNPEVVDvkDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEV 745
Cdd:PHA02878   148 EITKLLLSYGADINMKD--RHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  746 SILCKDSRGRTPLHYAAARGHATwlsELLQIALSEEDCSFKDN--QGYTPLHWACYngNENCIEVLLEQK 813
Cdd:PHA02878   226 STDARDKCGNTPLHISVGYCKDY---DILKLLLEHGVDVNAKSyiLGLTALHSSIK--SERKLKLLLEYG 290
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 407-528 3.50e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.41  E-value: 3.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  407 EHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPL-------HYAAANCHFHC-------- 471
Cdd:PLN03192   542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHHKIFRILYHFasisdpha 621

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  472 ----------------IETLVTTGANVNETDDWGRTALHYAAASD---------MDRNKTILGNAHENSEELERARELKE 526
Cdd:PLN03192   622 agdllctaakrndltaMKELLKQGLNVDSEDHQGATALQVAMAEDhvdmvrlliMNGADVDKANTDDDFSPTELRELLQK 701


                   ..
gi 1333587278  527 KE 528
Cdd:PLN03192   702 RE 703
Ank_4 pfam13637
Ankyrin repeats (many copies);
239-293 3.67e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 3.67e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1333587278  239 GNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGAlCLELLV 293
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 20-295 4.07e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 50.44  E-value: 4.07e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   20 DPEEIRMLIHKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSE--EAVQVLIKHS 97
Cdd:PHA02946    51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEviERINLLVQYG 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   98 ADV-NARDKNWQTPLhVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAAL--NGHVEMVNLLLAKGANINAFDKKDR 174
Cdd:PHA02946   131 AKInNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMsdNPKASTISWMMKLGISPSKPDHDGN 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  175 RALH--WAAYMGHLDVVALLIThGAEVTCKDKKGYTPLHAAASNGQinvVKHLLNLGVEIDeiNVYGNTALHLACYNGQD 252
Cdd:PHA02946   210 TPLHivCSKTVKNVDIINLLLP-STDVNKQNKFGDSPLTLLIKTLS---PAHLINKLLSTS--NVITDQTVNICIFYDRD 283

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1333587278  253 AVVNELTDYGANVNQPNnsgftplhFAAASTHGAL-CLELLVNN 295
Cdd:PHA02946   284 DVLEIINDKGKQYDSTD--------FKMAVEVGSIrCVKYLLDN 319
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 140-168 4.24e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.12  E-value: 4.24e-06
                            10        20
                    ....*....|....*....|....*....
gi 1333587278   140 GRTALHHAALNGHVEMVNLLLAKGANINA 168
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
308-359 4.33e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 4.33e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1333587278  308 SPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLI 359
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 431-500 4.77e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 4.77e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  431 AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAASD 500
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
PHA02791 PHA02791
ankyrin-like protein; Provisional
 768-963 5.73e-06

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 49.27  E-value: 5.73e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  768 TWLSELLQIALSEEDCSFKDNQGYTPLHWACYNGNENCIEVLLEQKCFREFIGNPFtPLH-CAIINDHENCASLLLGAID 846
Cdd:PHA02791     8 TWKSKQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF-PLHqAATLEDTKIVKILLFSGMD 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  847 SSIVncrDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSG-KTALMMAAENGQAGAVDILVNSAQA--DLTVkdkd 923
Cdd:PHA02791    87 DSQF---DDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPStfDLAI---- 159

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|
gi 1333587278  924 LNTPLHLASSKGHEKCALLILDKIQDeslINAKNNALQTP 963
Cdd:PHA02791   160 LLSCIHITIKNGHVDMMILLLDYMTS---TNTNNSLLFIP 196
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 289-493 5.81e-06

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 50.30  E-value: 5.81e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  289 LELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRS--QTLIQNGGEIDCVDKDGNTPLH---VAARYGHELLINTLITSGA 363
Cdd:PHA02716   195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASviKKIIELGGDMDMKCVNGMSPIMtyiINIDNINPEITNIYIESLD 274

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  364 DTAKCGVHSMFPLHLAalnahsdccrklLSSGQKYSIVslfsnEHVLSAGFEIDTPDKFGRTCLHAAAAGGNV--ECIKL 441
Cdd:PHA02716   275 GNKVKNIPMILHSYIT------------LARNIDISVV-----YSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKL 337

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587278  442 LQSSGADFHKKDKCGRTPLH-YAAANCHFH-------------CIETLVTTGANVNETDDWGRTAL 493
Cdd:PHA02716   338 LHEYGNDLNEPDNIGNTVLHtYLSMLSVVNildpetdndirldVIQCLISLGADITAVNCLGYTPL 403
Ank_4 pfam13637
Ankyrin repeats (many copies);
754-810 6.11e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 6.11e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333587278  754 GRTPLHYAAARGHatwlSELLQIAL-SEEDCSFKDNQGYTPLHWACYNGNENCIEVLL 810
Cdd:pfam13637    1 ELTALHAAAASGH----LELLRLLLeKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
375-442 8.53e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 8.53e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1333587278  375 PLHLAALNAHSDCCRKLLSSGqkysivslfsnehvlsagFEIDTPDKFGRTCLHAAAAGGNVECIKLL 442
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKG------------------ADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
618-672 9.41e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 9.41e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1333587278  618 GRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLL 672
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 140-171 9.97e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.05  E-value: 9.97e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1333587278  140 GRTALHHAAL-NGHVEMVNLLLAKGANINAFDK 171
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
158-213 1.19e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.19e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587278  158 LLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLITHGAEVTCKDKKGYTPLHAA 213
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 669-818 2.23e-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: 2.23e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  669 RLLLEIADNPEVVDV--------KDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDA---------VDIMGC-----TALH 726
Cdd:cd22194    114 RILLAFAEENGILDRfinaeyteEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHEGfyfgeTPLA 193

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  727 RGIMTGHEECVQMLLEQE-VSILCKDSRGRTPLHYAA-----ARGHATWLSELL-QIALSEEDCSF---KDNQGYTPLHW 796
Cdd:cd22194    194 LAACTNQPEIVQLLMEKEsTDITSQDSRGNTVLHALVtvaedSKTQNDFVKRMYdMILLKSENKNLetiRNNEGLTPLQL 273

                          170       180
                   ....*....|....*....|..
gi 1333587278  797 ACYNGNENCIEVLLEqkcfREF 818
Cdd:cd22194    274 AAKMGKAEILKYILS----REI 291
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 140-168 2.25e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 42.24  E-value: 2.25e-05
                           10        20
                   ....*....|....*....|....*....
gi 1333587278  140 GRTALHHAALNGHVEMVNLLLAKGANINA 168
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
550-605 2.59e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 2.59e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587278  550 GYNSIHYAAAYGHRQCLELLLERTNSGFEDSDSGATksPLHLAAYNGHHQALEVLL 605
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGET--ALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 561-800 2.78e-05

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 47.95  E-value: 2.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  561 GHRQCLELLLerTNSGFEDSDSGatKSPLHLAAYNGHHQALE---VLLQS---------LVDLDIRDE--KGRTALDLAA 626
Cdd:cd21882      6 GLLECLRWYL--TDSAYQRGATG--KTCLHKAALNLNDGVNEaimLLLEAapdsgnpkeLVNAPCTDEfyQGQTALHIAI 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  627 FKGHTECVEALINQGASIFVKDNVT--KRTPlhasvingHTLCLRllleiadnpevvdvkdakGQTPLMLAVAYGHIDAV 704
Cdd:cd21882     82 ENRNLNLVRLLVENGADVSARATGRffRKSP--------GNLFYF------------------GELPLSLAACTNQEEIV 135

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  705 SLLLE---KEANVDAVDIMGCTALHRGIMTGHEE------CVQM--LLEQEVSILC--------KDSRGRTPLHYAAARG 765
Cdd:cd21882    136 RLLLEngaQPAALEAQDSLGNTVLHALVLQADNTpensafVCQMynLLLSYGAHLDptqqleeiPNHQGLTPLKLAAVEG 215

                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1333587278  766 HATWLSELLQIALSE--EDCSFKDNQ-GYTPLHWACYN 800
Cdd:cd21882    216 KIVMFQHILQREFSGpyQPLSRKFTEwTYGPVTSSLYD 253
Ank_4 pfam13637
Ankyrin repeats (many copies);
790-842 2.83e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 2.83e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1333587278  790 GYTPLHWACYNGNENCIEVLLEQK-CFREFIGNPFTPLHCAIINDHENCASLLL 842
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGaDINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
 631-900 3.01e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.91  E-value: 3.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  631 TECVEALINQGASIFVKDNvTKRTPLHA--SVINGHTLCLRLLLEIADNPEVVDVKDAKGQTPLMLAVAYGHIDA---VS 705
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDN-EYSTPLCTilSNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNleiLL 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  706 LLLEKEANVDAVDIMGCTALHRGIMTGHE---ECVQMLLEQEVSIlckdsrgrtplhyaaaRGHATWlsellqialseed 782
Cdd:PHA02798   130 FMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDI----------------NTHNNK------------- 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  783 csfkdnQGYTPLHwaCY-NGNENCIEV-LLEQKCFREFIGNPFTPLH--------CAIINDHENCASLLLGAIDSSI-VN 851
Cdd:PHA02798   181 ------EKYDTLH--CYfKYNIDRIDAdILKLFVDNGFIINKENKSHkkkfmeylNSLLYDNKRFKKNILDFIFSYIdIN 252

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1333587278  852 CRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAEN 900
Cdd:PHA02798   253 QVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFEN 301
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 662-741 3.01e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 3.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  662 NGHTLCLRLLLEIADNPevvDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLL 741
Cdd:PTZ00322    92 SGDAVGARILLTGGADP---NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
93-147 3.19e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.19e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587278   93 LIKH-SADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHA 147
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
132-180 3.25e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.25e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1333587278  132 SVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWA 180
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 735-897 3.29e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.57  E-value: 3.29e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  735 ECVQMLLEQEVSILCKD-SRGRTPLHYAAARGHaTWLSELLQIALSEEDCSFKDNQgyTPLHWACYNGNENCIEVLLEQK 813
Cdd:PHA02878   148 EITKLLLSYGADINMKDrHKGNTALHYATENKD-QRLTELLLSYGANVNIPDKTNN--SPLHHAVKHYNKPIVHILLENG 224

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  814 CF---REFIGNpfTPLHCAI--INDHENCASLLLGAIDssiVNCRDD-KGRTPLHAAAFADHVecLQLLLRHNAQVNAAD 887
Cdd:PHA02878   225 AStdaRDKCGN--TPLHISVgyCKDYDILKLLLEHGVD---VNAKSYiLGLTALHSSIKSERK--LKLLLEYGADINSLN 297

                          170
                   ....*....|
gi 1333587278  888 NSGKTALMMA 897
Cdd:PHA02878   298 SYKLTPLSSA 307
Ank_4 pfam13637
Ankyrin repeats (many copies);
653-708 3.48e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 3.48e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587278  653 RTPLHASVINGHTLCLRLLLEiadNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLL 708
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLE---KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
29-81 3.66e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.66e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1333587278   29 HKTEDVNALDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRA 81
Cdd:pfam13857    4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 140-282 4.56e-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: 47.49  E-value: 4.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  140 GRTALHHAALN---GHVEMVNLLL---AKGANINAF------DK--KDRRALHWAAYMGHLDVVALLITHGAEVTC---- 201
Cdd:cd22196     47 GKTCLLKAMLNlhnGQNDTISLLLdiaEKTGNLKEFvnaaytDSyyKGQTALHIAIERRNMHLVELLVQNGADVHArasg 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  202 ------KDKKGY----TPLHAAASNGQINVVKHLLN---LGVEIDEINVYGNTALHL---ACYNGQD------AVVNELT 259
Cdd:cd22196    127 effkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLHAlveVADNTPEntkfvtKMYNEIL 206

                          170       180       190
                   ....*....|....*....|....*....|
gi 1333587278  260 DYGANVNQ-------PNNSGFTPLHFAAAS 282
Cdd:cd22196    207 ILGAKIRPllkleeiTNKKGLTPLKLAAKT 236
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 525-711 5.47e-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: 47.31  E-value: 5.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  525 KEKEAASCLEFLLQNEANPSIRDKEGYNSIHYAAAYGHRQCLELLLErtnsgfED---------SDSGATKSPLHLAAYN 595
Cdd:cd22192     26 KENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME------AApelvnepmtSDLYQGETALHIAVVN 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  596 GHHQALEVLLQSLVDLD--------IRDEK------GRTALDLAAFKGHTECVEALINQGASIFVKDNVTKrTPLHASVI 661
Cdd:cd22192    100 QNLNLVRELIARGADVVspratgtfFRPGPknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN-TVLHILVL 178

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333587278  662 NGHTL--C----LRLLLEIADNPEVVD-VKDAKGQTPLMLAVAYGHIDAVSLLLEKE 711
Cdd:cd22192    179 QPNKTfaCqmydLILSYDKEDDLQPLDlVPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 856-888 5.50e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.12  E-value: 5.50e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1333587278  856 KGRTPLHAAA-FADHVECLQLLLRHNAQVNAADN 888
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
441-496 5.53e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 5.53e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587278  441 LLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYA 496
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
875-931 5.92e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 5.92e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1333587278  875 LLLRHNAQVNAADNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLA 931
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
844-897 6.16e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 6.16e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1333587278  844 AIDSSIVNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMA 897
Cdd:pfam13857    3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 310-399 7.90e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 7.90e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  310 LHMTAVH-------GRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGVHSMFPLHLAALN 382
Cdd:PTZ00322    79 AHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158

                           90
                   ....*....|....*..
gi 1333587278  383 AHSDCCRKLLSSGQKYS 399
Cdd:PTZ00322   159 GFREVVQLLSRHSQCHF 175
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 338-498 8.77e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.14  E-value: 8.77e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  338 DGNTPLHVAARYGHELLINTLITSGA--DTAKCGVHSmfPLHLAALNAHSDCCRKLLSSGQkysivslfsnehvlsagFE 415
Cdd:PHA02875    34 DGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIES--ELHDAVEEGDVKAVEELLDLGK-----------------FA 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  416 IDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHY 495
Cdd:PHA02875    95 DDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLII 174


                   ...
gi 1333587278  496 AAA 498
Cdd:PHA02875   175 AMA 177
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 140-280 9.01e-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: 46.68  E-value: 9.01e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  140 GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRR--------ALHWAAYMGHLDVVALLITHGAE-VTCKDK 204
Cdd:cd22194    141 GQTALNIAIERRQGDIVKLLIAKGADVNAhakgvfFNPKYKHegfyfgetPLALAACTNQPEIVQLLMEKESTdITSQDS 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  205 KGYTPLHAAA-----SNGQINVVKHLLnlgveiDEInvygntalHLACYNgqdavvneltdygANVNQ-PNNSGFTPLHF 278
Cdd:cd22194    221 RGNTVLHALVtvaedSKTQNDFVKRMY------DMI--------LLKSEN-------------KNLETiRNNEGLTPLQL 273


                   ..
gi 1333587278  279 AA 280
Cdd:cd22194    274 AA 275
Ank_5 pfam13857
Ankyrin repeats (many copies);
258-312 9.87e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 9.87e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587278  258 LTDYGANVNQPNNSGFTPLHFAAasTHGAL-CLELLVNNGADVNIQSKDGKSPLHM 312
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAA--KYGALeIVRVLLAYGVDLNLKDEEGLTALDL 55
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 211-314 1.10e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 1.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  211 HAAASNGQINVvKHLLNLGVEIDEINVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFAAASTHGALcLE 290
Cdd:PTZ00322    88 QLAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV-VQ 165

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1333587278  291 LLV-------NNGADVNIQSKDGK------SPLHMTA 314
Cdd:PTZ00322   166 LLSrhsqchfELGANAKPDSFTGKppsledSPISSHH 202
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 624-708 1.60e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 1.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  624 LAAfKGHTECVEALINQGASIFVKDnVTKRTPLHASVINGHTLCLRLLLEIADNPEVVDvKDakGQTPLMLAVAYGHIDA 703
Cdd:PTZ00322    89 LAA-SGDAVGARILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLD-KD--GKTPLELAEENGFREV 163


                   ....*
gi 1333587278  704 VSLLL 708
Cdd:PTZ00322   164 VQLLS 168
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 850-1014 1.91e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.34  E-value: 1.91e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  850 VNCRDDKGRTPLHAAAFADHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVDILVNS----------------- 912
Cdd:PHA02874    28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNgvdtsilpipciekdmi 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  913 -----AQADLTVKDKDLNTPLHLASSKGHEKCALLILDKIQDeslINAKNNALQTPLHVAARNGLKVVVEELLAKGACVL 987
Cdd:PHA02874   108 ktildCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGAD---VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                          170       180
                   ....*....|....*....|....*..
gi 1333587278  988 AVDENGHTPALACAPNKDVAdCLALIL 1014
Cdd:PHA02874   185 VKDNNGESPLHNAAEYGDYA-CIKLLI 210
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 376-494 1.93e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 45.26  E-value: 1.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  376 LHLAALNAHS---DCCRKLLSSGQKYSIVSLFSNEHVLSAGFEidtpdkfGRTCLHAAAAGGNVECIKLLQSSGADFH-- 450
Cdd:cd21882     30 LHKAALNLNDgvnEAIMLLLEAAPDSGNPKELVNAPCTDEFYQ-------GQTALHIAIENRNLNLVRLLVENGADVSar 102

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333587278  451 ------KKDKC-----GRTPLHYAAANCHFHCIETLVTTG---ANVNETDDWGRTALH 494
Cdd:cd21882    103 atgrffRKSPGnlfyfGELPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLH 160
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 205-234 2.23e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 2.23e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1333587278   205 KGYTPLHAAASNGQINVVKHLLNLGVEIDE 234
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 856-971 2.30e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 45.13  E-value: 2.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  856 KGRTPLHAAAFADHVECLQLLLRHNAQVNAADNS--------------GKTALMMAAENGQAGAVDILVNSAQADLTVKD 921
Cdd:cd22194    140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQD 219

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1333587278  922 KDLNTPLHL-----ASSKGHEKCALLILDKI----QDESLINAKNNALQTPLHVAARNG 971
Cdd:cd22194    220 SRGNTVLHAlvtvaEDSKTQNDFVKRMYDMIllksENKNLETIRNNEGLTPLQLAAKMG 278
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 862-955 2.35e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 2.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  862 HAAAFADHVEcLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLASSKGHEKCAL 941
Cdd:PTZ00322    88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFREVVQ 165

                           90
                   ....*....|....
gi 1333587278  942 LILDKIQDESLINA 955
Cdd:PTZ00322   166 LLSRHSQCHFELGA 179
Ank_4 pfam13637
Ankyrin repeats (many copies);
532-570 2.36e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 2.36e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1333587278  532 CLEFLLQNEANPSIRDKEGYNSIHYAAAYGHRQCLELLL 570
Cdd:pfam13637   16 LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
674-726 2.44e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 2.44e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1333587278  674 IADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIMGCTALH 726
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 272-304 2.55e-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: 2.55e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1333587278  272 GFTPLHFAAASTHGALCLELLVNNGADVNIQSK 304
Cdd:pfam00023    2 GNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 687-718 3.13e-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: 3.13e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1333587278  687 KGQTPLMLAVA-YGHIDAVSLLLEKEANVDAVD 718
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
339-392 3.18e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 3.18e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1333587278  339 GNTPLHVAARYGHELLINTLITSGADTAKCGVHSMFPLHLAALNAHSDCCRKLL 392
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 236-313 3.48e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 43.82  E-value: 3.48e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  236 NVYGNTALHLACYNGQDAVVNeLTDYGANVNQ-PNNSGFTPLHFAAasTHGAL-CLELLVNNGADVNIQSKDGKSPLHMT 313
Cdd:PHA02884    68 NSKTNPLIYAIDCDNDDAAKL-LIRYGADVNRyAEEAKITPLYISV--LHGCLkCLEILLSYGADINIQTNDMVTPIELA 144
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 238-266 3.65e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 3.65e-04
                            10        20
                    ....*....|....*....|....*....
gi 1333587278   238 YGNTALHLACYNGQDAVVNELTDYGANVN 266
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
587-625 4.31e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 4.31e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1333587278  587 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLA 625
Cdd:pfam13857   18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 868-1014 4.50e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.47  E-value: 4.50e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  868 DHVECLQLLLRHNAQVNA-------ADNSGK-------TALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLASS 933
Cdd:PLN03192   489 DNVVILKNFLQHHKELHDlnvgdllGDNGGEhddpnmaSNLLTVASTGNAALLEELLK-AKLDPDIGDSKGRTPLHIAAS 567

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  934 KGHEKCALLILD-----KIQDES-------LINAKNNALQTPLH----------------VAARNGLKVVVEELLAKGAC 985
Cdd:PLN03192   568 KGYEDCVLVLLKhacnvHIRDANgntalwnAISAKHHKIFRILYhfasisdphaagdllcTAAKRNDLTAMKELLKQGLN 647

                          170       180
                   ....*....|....*....|....*....
gi 1333587278  986 VLAVDENGHTpALACAPNKDVADCLALIL 1014
Cdd:PLN03192   648 VDSEDHQGAT-ALQVAMAEDHVDMVRLLI 675
Ank_5 pfam13857
Ankyrin repeats (many copies);
236-279 4.58e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 4.58e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....
gi 1333587278  236 NVYGNTALHLACYNGQDAVVNELTDYGANVNQPNNSGFTPLHFA 279
Cdd:pfam13857   13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 213-350 5.83e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.98  E-value: 5.83e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  213 AASNGqinVVKHLLNlgVEIDEINVYGNTALHLACYNGQDAVVNELTDYGANVN--------QP--NNSGF----TPLHF 278
Cdd:cd22194    120 AEENG---ILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffNPkyKHEGFyfgeTPLAL 194

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  279 AAASTHGALcLELLVNNGADvNIQSKD--GKSPLHMTAVHGRFTRSQT-----------LIQNGGEIDCV-DKDGNTPLH 344
Cdd:cd22194    195 AACTNQPEI-VQLLMEKEST-DITSQDsrGNTVLHALVTVAEDSKTQNdfvkrmydmilLKSENKNLETIrNNEGLTPLQ 272


                   ....*.
gi 1333587278  345 VAARYG 350
Cdd:cd22194    273 LAAKMG 278
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 161-347 6.15e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.92  E-value: 6.15e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  161 AKGANINAFDKKDRRALHWAAYMG-HLDVVALLITHGAEVtckdKKGYTPLHAAaSNGQINVVKHLLNLGVEIDEinvyG 239
Cdd:TIGR00870   40 PKKLNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRG----AVGDTLLHAI-SLEYVDAVEAILLHLLAAFR----K 110

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  240 NTALHLAcyNGQDavvneLTDYGAnvnqpnnsGFTPLHFAAaSTHGALCLELLVNNGADVNIQSKDG---KSPLHMTAVH 316
Cdd:TIGR00870  111 SGPLELA--NDQY-----TSEFTP--------GITALHLAA-HRQNYEIVKLLLERGASVPARACGDffvKSQGVDSFYH 174

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1333587278  317 GRFTRS-----------QTLIQNGGEIDCVDKDGNTPLHVAA 347
Cdd:TIGR00870  175 GESPLNaaaclgspsivALLSEDPADILTADSLGNTLLHLLV 216
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 456-487 6.17e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 6.17e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1333587278  456 GRTPLHYAAANC-HFHCIETLVTTGANVNETDD 487
Cdd:pfam00023    2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
274-326 6.20e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 6.20e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1333587278  274 TPLHFAAASTHGAlCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI 326
Cdd:pfam13637    3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 214-360 7.24e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 43.75  E-value: 7.24e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  214 ASNGQINVVKHLLNLGVEIDEINVYGNTALH--LACYNGQDAVVNELTDYGANVNQPNNSGFTPLHfaaaSTHGALCLEL 291
Cdd:PHA02716   292 ARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLH----TYLSMLSVVN 367

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1333587278  292 LVNNGADVNIqskdgksplhmtavhgRFTRSQTLIQNGGEIDCVDKDGNTPLH----VAARYGHELLINTLIT 360
Cdd:PHA02716   368 ILDPETDNDI----------------RLDVIQCLISLGADITAVNCLGYTPLTsyicTAQNYMYYDIIDCLIS 424
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 456-484 7.25e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 7.25e-04
                            10        20
                    ....*....|....*....|....*....
gi 1333587278   456 GRTPLHYAAANCHFHCIETLVTTGANVNE 484
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
706-761 8.02e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 8.02e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587278  706 LLLEKEANVDAVDIMGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYA 761
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
415-463 8.51e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 8.51e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1333587278  415 EIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYA 463
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 661-785 8.82e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 8.82e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  661 INGHTLCLRLLLEIADNP-------EVVDVKDAKgqtplMLAVAYGHIDA------VSLLLEKEANVDAVDIMGCTALHR 727
Cdd:PTZ00322    47 IDTHLEALEATENKDATPdhnltteEVIDPVVAH-----MLTVELCQLAAsgdavgARILLTGGADPNCRDYDGRTPLHI 121

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  728 GIMTGHEECVQMLLE--QEVSILCKDsrGRTPLHYAAARGhatwLSELLQIALSEEDCSF 785
Cdd:PTZ00322   122 ACANGHVQVVRVLLEfgADPTLLDKD--GKTPLELAEENG----FREVVQLLSRHSQCHF 175
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 892-986 9.25e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.08  E-value: 9.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  892 TALMMAAENGQAGAVDILVNSAQADLTVKDKDLNTPLHLASSKGHEKCALLILDkiQDESLIN-AKNNAL---QTPLHVA 967
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNePMTSDLyqgETALHIA 96

                           90
                   ....*....|....*....
gi 1333587278  968 ARNGLKVVVEELLAKGACV 986
Cdd:cd22192     97 VVNQNLNLVRELIARGADV 115
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 238-270 1.02e-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: 37.65  E-value: 1.02e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1333587278  238 YGNTALHLACY-NGQDAVVNELTDYGANVNQPNN 270
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 205-234 1.05e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 1.05e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1333587278  205 KGYTPLHAAASNGQINVVKHLLNLGVEIDE 234
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
65-114 1.05e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.05e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1333587278   65 ARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVA 114
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 856-885 1.11e-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: 37.18  E-value: 1.11e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1333587278   856 KGRTPLHAAAFADHVECLQLLLRHNAQVNA 885
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 586-637 1.12e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 1.12e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1333587278  586 KSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEAL 637
Cdd:PTZ00322   116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 409-466 1.18e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 1.18e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1333587278  409 VLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAAN 466
Cdd:PTZ00322   101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 423-576 1.18e-03

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 42.92  E-value: 1.18e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  423 GRTCLHAAAAGGNVECIKLLQSSGADFH----------KKDKC---GRTPLHYAAANCHFHCIETLVTTG---ANVNETD 486
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGADVHaracgrffqkKQGTCfyfGELPLSLAACTKQWDVVNYLLENPhqpASLQAQD 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  487 DWGRTALHYAAasdmdrnkTILGNAHENSEELERA-RELKEKEAASCLEFLLQneanpSIRDKEGYNSIHYAAAYGHRQC 565
Cdd:cd22197    174 SLGNTVLHALV--------MIADNSPENSALVIKMyDGLLQAGARLCPTVQLE-----EISNHEGLTPLKLAAKEGKIEI 240

                          170
                   ....*....|.
gi 1333587278  566 LELLLERTNSG 576
Cdd:cd22197    241 FRHILQREFSG 251
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 40-180 1.33e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.56  E-value: 1.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   40 EKRTPLHVAAFLGDAEIIELLILSGARVNAKDN-------------MWLTPLHRAVASRSEEAVQVLIKHSAD---VNAR 103
Cdd:cd21882     72 QGQTALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQ 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  104 DKNWQTPLH--VAAANKAVKCAEVII--------------PLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANiN 167
Cdd:cd21882    152 DSLGNTVLHalVLQADNTPENSAFVCqmynlllsygahldPTQQLEEIPNHQGLTPLKLAAVEGKIVMFQHILQREFS-G 230

                          170
                   ....*....|...
gi 1333587278  168 AFDKKDRRALHWA 180
Cdd:cd21882    231 PYQPLSRKFTEWT 243
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 423-572 1.43e-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: 42.82  E-value: 1.43e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  423 GRTCLHAAAAGGNVECIKLLQSSGAD---------FHKKDK-----CGRTPLHYAAANCHFHCIETLVTTGA-NVNETDD 487
Cdd:cd22194    141 GQTALNIAIERRQGDIVKLLIAKGADvnahakgvfFNPKYKhegfyFGETPLALAACTNQPEIVQLLMEKEStDITSQDS 220

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  488 WGRTALH--YAAASDMDRNKTILGNAHEnseELERARELKEKEAasclefllqneanpsIRDKEGYNSIHYAAAYGHRQC 565
Cdd:cd22194    221 RGNTVLHalVTVAEDSKTQNDFVKRMYD---MILLKSENKNLET---------------IRNNEGLTPLQLAAKMGKAEI 282


                   ....*..
gi 1333587278  566 LELLLER 572
Cdd:cd22194    283 LKYILSR 289
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 189-318 1.48e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 1.48e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  189 VALLITHGAEVTCKDKKGYTPLHAAASNGQIN-VVKHLLNlgVEIDEINVYGntalhlacyngqDAV-VNELTDYGANVN 266
Cdd:PTZ00322    44 IARIDTHLEALEATENKDATPDHNLTTEEVIDpVVAHMLT--VELCQLAASG------------DAVgARILLTGGADPN 109

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1333587278  267 QPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGR 318
Cdd:PTZ00322   110 CRDYDGRTPLHIACANGHVQV-VRVLLEFGADPTLLDKDGKTPLELAEENGF 160
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 42-72 1.55e-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: 1.55e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1333587278   42 RTPLHVAA-FLGDAEIIELLILSGARVNAKDN 72
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 140-280 1.66e-03

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 42.53  E-value: 1.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  140 GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRALhwaaYMGHLdvvallithgaevtckdkkgytPLHAA 213
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGADVHAracgrfFQKKQGTCF----YFGEL----------------------PLSLA 147

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  214 ASNGQINVVKHLLNLGVE---IDEINVYGNTALHLACYNGQDAVVN---------ELTDYGANVNQ-------PNNSGFT 274
Cdd:cd22197    148 ACTKQWDVVNYLLENPHQpasLQAQDSLGNTVLHALVMIADNSPENsalvikmydGLLQAGARLCPtvqleeiSNHEGLT 227


                   ....*.
gi 1333587278  275 PLHFAA 280
Cdd:cd22197    228 PLKLAA 233
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 687-716 1.73e-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: 1.73e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1333587278  687 KGQTPLMLAVAYGHIDAVSLLLEKEANVDA 716
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 647-759 1.74e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 42.48  E-value: 1.74e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  647 KDNVTKRTPLHASVIN---GHTLCLRLLLEIAD---------NPEVVDVKdAKGQTPLMLAVAYGHIDAVSLLLEKEANV 714
Cdd:cd22193     24 TESSTGKTCLMKALLNlnpGTNDTIRILLDIAEktdnlkrfiNAEYTDEY-YEGQTALHIAIERRQGDIVALLVENGADV 102

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1333587278  715 DAVD--------------IMGCTALHRGIMTGHEECVQMLLE---QEVSILCKDSRGRTPLH 759
Cdd:cd22193    103 HAHAkgrffqpkyqgegfYFGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLH 164
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 789-811 1.86e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 1.86e-03
                            10        20
                    ....*....|....*....|...
gi 1333587278   789 QGYTPLHWACYNGNENCIEVLLE 811
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLD 23
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 617-649 2.42e-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: 2.42e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1333587278  617 KGRTALDLAAFK-GHTECVEALINQGASIFVKDN 649
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02795 PHA02795
ankyrin-like protein; Provisional
 124-201 2.45e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 41.52  E-value: 2.45e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  124 EVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMG--------HLDVVALLITH 195
Cdd:PHA02795   205 KLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHLKILEILLRE 284


                   ....*.
gi 1333587278  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 ...
 338-364 2.55e-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: 2.55e-03
                            10        20
                    ....*....|....*....|....*..
gi 1333587278   338 DGNTPLHVAARYGHELLINTLITSGAD 364
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 423-451 2.58e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 2.58e-03
                            10        20
                    ....*....|....*....|....*....
gi 1333587278   423 GRTCLHAAAAGGNVECIKLLQSSGADFHK 451
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 43-121 2.66e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.99  E-value: 2.66e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   43 TPLHVAAFLGDAEIIELLILSGARVNAKDN--MWLT------------PLHRAVASRSEEAVQVLIKHSADVNARDKNWQ 108
Cdd:TIGR00870  130 TALHLAAHRQNYEIVKLLLERGASVPARACgdFFVKsqgvdsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209

                           90
                   ....*....|...
gi 1333587278  109 TPLHVAAANKAVK 121
Cdd:TIGR00870  210 TLLHLLVMENEFK 222
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 140-282 2.81e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 41.70  E-value: 2.81e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  140 GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRA--------LHWAAYMGHLDVVALLITHG---AEVTCK 202
Cdd:cd22193     76 GQTALHIAIERRQGDIVALLVENGADVHAhakgrfFQPKYQGEgfyfgelpLSLAACTNQPDIVQYLLENEhqpADIEAQ 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  203 DKKGYTPLHAAasngqinvvkhllnlgVEIDEiNVYGNTALHLACYNGqdavvneLTDYGANVNQP-------NNSGFTP 275
Cdd:cd22193    156 DSRGNTVLHAL----------------VTVAD-NTKENTKFVTRMYDM-------ILIRGAKLCPTveleeirNNDGLTP 211


                   ....*..
gi 1333587278  276 LHFAAAS 282
Cdd:cd22193    212 LQLAAKM 218
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 687-716 3.05e-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: 3.05e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1333587278   687 KGQTPLMLAVAYGHIDAVSLLLEKEANVDA 716
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
925-971 3.34e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 3.34e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1333587278  925 NTPLHLASSKGHEKCALLILDKIQDeslINAKNNALQTPLHVAARNG 971
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNG 45
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 868-1003 3.65e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.20  E-value: 3.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  868 DHVECLQLLLRHNAQVNAADNSGKTALMMAAENGQAGAVDILVnSAQADL-------------TVKDKDLNTPLHLASSK 934
Cdd:PHA02876   156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLL-SYGADVniialddlsvlecAVDSKNIDTIKAIIDNR 234

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  935 GH-EKCALLILDKIQDESL------------INAKNNALQTPLHVAARN-GLKVVVEELLAKGACVLAVDENGHTPALAC 1000
Cdd:PHA02876   235 SNiNKNDLSLLKAIRNEDLetslllydagfsVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLM 314


                   ...
gi 1333587278 1001 APN 1003
Cdd:PHA02876   315 AKN 317
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 176-204 3.77e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 3.77e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1333587278  176 ALHWAAYM-GHLDVVALLITHGAEVTCKDK 204
Cdd:pfam00023    5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 332-494 3.83e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.22  E-value: 3.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  332 IDCVDKDGNTPLHVAARYG-HELLINTLITSGA-----DTAkcgvhsmfpLHLAALNAHSDC--CRKLLSSGQKYSIVSL 403
Cdd:TIGR00870   45 INCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISLEYVDAVeaILLHLLAAFRKSGPLE 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278  404 FSNEHVLSAGFeidtpdkFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKC--------------GRTPLHYAAANCHF 469
Cdd:TIGR00870  116 LANDQYTSEFT-------PGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSP 188

                          170       180
                   ....*....|....*....|....*
gi 1333587278  470 HCIETLVTTGANVNETDDWGRTALH 494
Cdd:TIGR00870  189 SIVALLSEDPADILTADSLGNTLLH 213
Ank_5 pfam13857
Ankyrin repeats (many copies);
291-346 5.87e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 5.87e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587278  291 LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVA 346
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 55-195 6.76e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.97  E-value: 6.76e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   55 EIIELLILSGARVNAK----DNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQ-TPLHVAAANKAVKCAEVIIPL 129
Cdd:PHA02884    47 DIIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSY 126

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1333587278  130 LSSVNVSDRGGRTALHHAALNGHVEMVNLLlaKGANINAFDKKDRRalhwaaYMGHLDVVALLITH 195
Cdd:PHA02884   127 GADINIQTNDMVTPIELALMICNNFLAFMI--CDNEISNFYKHPKK------ILINFDILKILVSH 184
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 423-454 7.15e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 7.15e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1333587278  423 GRTCLHAAAA-GGNVECIKLLQSSGADFHKKDK 454
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA02791 PHA02791
ankyrin-like protein; Provisional
 40-160 7.33e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 39.64  E-value: 7.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1333587278   40 EKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKN-WQTPL-HVAAAN 117
Cdd:PHA02791    60 ENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTgWKTSFyHAVMLN 139

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1333587278  118 KAVKCAEVIIPLLSSVNVSDRggRTALHHAALNGHVEMVNLLL 160
Cdd:PHA02791   140 DVSIVSYFLSEIPSTFDLAIL--LSCIHITIKNGHVDMMILLL 180
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 76-105 7.51e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 7.51e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1333587278   76 TPLHRAVASR-SEEAVQVLIKHSADVNARDK 105
Cdd:pfam00023    4 TPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 617-646 7.53e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 7.53e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1333587278   617 KGRTALDLAAFKGHTECVEALINQGASIFV 646
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 455-484 7.69e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 7.69e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1333587278  455 CGRTPLHYAAANCHFHCIETLVTTGANVNE 484
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
745-797 8.21e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 8.21e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1333587278  745 VSILCKDSRGRTPLHYAAARGHATWLSELLqiaLSEEDCSFKDNQGYTPLHWA 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 ...
 176-201 8.56e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 8.56e-03
                            10        20
                    ....*....|....*....|....*.
gi 1333587278   176 ALHWAAYMGHLDVVALLITHGAEVTC 201
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 238-266 8.74e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 8.74e-03
                           10        20
                   ....*....|....*....|....*....
gi 1333587278  238 YGNTALHLACYNGQDAVVNELTDYGANVN 266
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
 
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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