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Conserved domains on  [gi|530371153|ref|XP_005247005|]
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serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit B isoform X7 [Homo sapiens]

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 7.66e-52

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 184.00  E-value: 7.66e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  54 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSV 133
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 134 NVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 213
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 214 ASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALcLELLV 293
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 530371153 294 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 343
Cdd:COG0666  240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
510-767 2.52e-36

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 2.52e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 510 NAHDNSEELERARELKEKEATLCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEESDSGATksPL 589
Cdd:COG0666   14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT--LL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 590 HLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLR 669
Cdd:COG0666   92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVK 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 670 LLLEI-ADnpeaVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSIL 748
Cdd:COG0666  171 LLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
                        250
                 ....*....|....*....
gi 530371153 749 CKDSRGRTPLHYAAARGHA 767
Cdd:COG0666  247 AKDKDGLTALLLAAAAGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
668-993 5.74e-32

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 5.74e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 668 LRLLLEIADNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSI 747
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 748 LCKDSRGRTPLHYAAARGHATWLSELLQmalSEEDCCFKDNQGYTPLHWACYNGNENCIEVLLEQKcfrkfignpftplh 827
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-------------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 828 cAIINdhgncaslllgaidssivsCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVD 907
Cdd:COG0666  144 -ADVN-------------------AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 908 ILVNsAQADLTVKDKDLNTPLHLACSKGHEKCALLILDKIQDeslINEKNNALQTPLHVAARNGLKVVVEELLAKGACVL 987
Cdd:COG0666  204 LLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279

                 ....*.
gi 530371153 988 AVDENG 993
Cdd:COG0666  280 AALLDL 285
PHA03095 super family cl33707
ankyrin-like protein; Provisional
212-493 1.25e-24

ankyrin-like protein; Provisional


The actual alignment was detected with superfamily member PHA03095:

Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 108.57  E-value: 1.25e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 212 AAASNGQINVVKHLLNLGVEIDEINVYGNTALH--IACYNGQDA-VVNELIDYGANVNQPNNNGFTPLHFAAASTHGALC 288
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 289 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGH---ELLiNTLITSGA 363
Cdd:PHA03095 100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGA 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 364 DTAKCGIHSMFPLHLAALNAHSDccrkllssgqkYSIVslfsnEHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQ 443
Cdd:PHA03095 179 DVYAVDDRFRSLLHHHLQSFKPR-----------ARIV-----RELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLP 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530371153 444 --SSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTAL 493
Cdd:PHA03095 243 llIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 5.03e-06

Ankyrin repeats (many copies);


:

Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 5.03e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530371153   10 PPLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLI 61
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-343 7.66e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 184.00  E-value: 7.66e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  54 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSV 133
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 134 NVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 213
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 214 ASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALcLELLV 293
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 530371153 294 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 343
Cdd:COG0666  240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
22-310 7.62e-40

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 154.41  E-value: 7.62e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  22 EEIRMLIHKTEDVNTLDSEKRTPLHVaaFLG-----DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAV-QVLIK 95
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDViKLLIK 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  96 HSADVNARDKNWQTPLHVAAANKAVkcaeviipllssvnvsdrggrtalhhaalngHVEMVNLLLAKGANINAFDKKDRR 175
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 176 ALHwaAYMGH----LDVVALLINHGAEVTCKDKKGYTPLHAAASNGQIN--VVKHLLNLGVEIDEINVYGNTALHIACYN 249
Cdd:PHA03095 155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530371153 250 G--QDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLELLvNNGADVNIQSKDGKSPL 310
Cdd:PHA03095 233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGNTPL 294
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
510-767 2.52e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 2.52e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 510 NAHDNSEELERARELKEKEATLCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEESDSGATksPL 589
Cdd:COG0666   14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT--LL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 590 HLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLR 669
Cdd:COG0666   92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVK 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 670 LLLEI-ADnpeaVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSIL 748
Cdd:COG0666  171 LLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
                        250
                 ....*....|....*....
gi 530371153 749 CKDSRGRTPLHYAAARGHA 767
Cdd:COG0666  247 AKDKDGLTALLLAAAAGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
668-993 5.74e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 5.74e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 668 LRLLLEIADNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSI 747
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 748 LCKDSRGRTPLHYAAARGHATWLSELLQmalSEEDCCFKDNQGYTPLHWACYNGNENCIEVLLEQKcfrkfignpftplh 827
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-------------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 828 cAIINdhgncaslllgaidssivsCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVD 907
Cdd:COG0666  144 -ADVN-------------------AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 908 ILVNsAQADLTVKDKDLNTPLHLACSKGHEKCALLILDKIQDeslINEKNNALQTPLHVAARNGLKVVVEELLAKGACVL 987
Cdd:COG0666  204 LLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279

                 ....*.
gi 530371153 988 AVDENG 993
Cdd:COG0666  280 AALLDL 285
PHA03095 PHA03095
ankyrin-like protein; Provisional
212-493 1.25e-24

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 108.57  E-value: 1.25e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 212 AAASNGQINVVKHLLNLGVEIDEINVYGNTALH--IACYNGQDA-VVNELIDYGANVNQPNNNGFTPLHFAAASTHGALC 288
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 289 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGH---ELLiNTLITSGA 363
Cdd:PHA03095 100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGA 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 364 DTAKCGIHSMFPLHLAALNAHSDccrkllssgqkYSIVslfsnEHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQ 443
Cdd:PHA03095 179 DVYAVDDRFRSLLHHHLQSFKPR-----------ARIV-----RELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLP 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530371153 444 --SSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTAL 493
Cdd:PHA03095 243 llIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
355-682 1.60e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 98.94  E-value: 1.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 355 INTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRkllssgqkysIVSLfsnehVLSAGFEIDTPDKFGRTCLHAAAAGG 434
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKD----------IVRL-----LLEAGADVNAPERCGFTPLHLYLYNA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 435 NVE-CIKLLQSSGADFHKKDKCGRTPLH-YAA-ANCHFHCIETLVTTGANVNETDDWGRTALHyaaasdmdrnktILGNA 511
Cdd:PHA03095  95 TTLdVIKLLIKAGADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLA------------VLLKS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 512 HDNSEELerarelkekeatlcLEFLLQNDANPSIRDKEGYNSIHYAAAYGH--RQCLELLLERTNSGFEESDSGATksPL 589
Cdd:PHA03095 163 RNANVEL--------------LRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNT--PL 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 590 HLAAYNGHHQALEV--LLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLC 667
Cdd:PHA03095 227 HSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNTPLSLMVRNNNGRA 305
                        330
                 ....*....|....*
gi 530371153 668 LRLLLEIADNPEAVD 682
Cdd:PHA03095 306 VRAALAKNPSAETVA 320
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-269 3.41e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 3.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  177 LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNlGVEIDEINvYGNTALHIACYNGQDAVVN 256
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 530371153  257 ELIDYGANVNQPN 269
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
669-984 6.28e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 91.24  E-value: 6.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 669 RLLLEIADnpeaVDVKDAKGQTPLMLAVAYGH---IDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEE-CVQMLLEQE 744
Cdd:PHA03095  32 RLLAAGAD----VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 745 VSILCKDSRGRTPLH-YAA-ARGHATWLSELLQMALSEEDCcfkDNQGYTPLHwaCYNGNENC----IEVLLEQKCF--- 815
Cdd:PHA03095 108 ADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNAL---DLYGMTPLA--VLLKSRNAnvelLRLLIDAGADvya 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 816 RKFIGNpfTPLH--CAIINDHGNCASLLLGAIDSsiVSCRDDKGRTPLHAAAFADHVECLQL--LLRHSAPVNAVDNSGK 891
Cdd:PHA03095 183 VDDRFR--SLLHhhLQSFKPRARIVRELIRAGCD--PAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQ 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 892 TALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLACSKGHEKCALLILDKIQDESLINEKNNALQTPLHVAARNG 971
Cdd:PHA03095 259 TPLHYAAVFNNPRACRRLIA-LGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTASVAGGDIPSDA 337
                        330
                 ....*....|...
gi 530371153 972 LKVVVEELLAKGA 984
Cdd:PHA03095 338 TRLCVAKVVLRGA 350
Ank_2 pfam12796
Ankyrin repeats (3 copies);
622-718 5.88e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 5.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  622 LDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADnpeaVDVKDaKGQTPLMLAVAYGHI 701
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHL 74
                          90
                  ....*....|....*..
gi 530371153  702 DAVSLLLEKEANVDTVD 718
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
74-281 7.40e-17

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 85.45  E-value: 7.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  74 WLTPLHRAVASRSEEAVQVLIK-HSADVNARDKNWQTPLHVAAANKAVKCAEVII---PLLssVNV---SD-RGGRTALH 145
Cdd:cd22192   17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaaPEL--VNEpmtSDlYQGETALH 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 146 HAALNGHVEMVNLLLAKGANIN------AFDKKDRRAL-----H---WAAYMGHLDVVALLINHGAEVTCKDKKGYTPLH 211
Cdd:cd22192   95 IAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530371153 212 AAASNGQINVVKH----LLNLGVEIDEINVYgntalHIacyngqdavvnelidyganvnqPNNNGFTPLHFAAA 281
Cdd:cd22192  175 ILVLQPNKTFACQmydlILSYDKEDDLQPLD-----LV----------------------PNNQGLTPFKLAAK 221
Ank_2 pfam12796
Ankyrin repeats (3 copies);
861-949 2.04e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 2.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  861 LHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKdlnTPLHLACSKGHEKCA 940
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77

                  ....*....
gi 530371153  941 LLILDKIQD 949
Cdd:pfam12796  78 KLLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
427-500 6.33e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 6.33e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530371153  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 1.51e-11

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 68.57  E-value: 1.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153   49 AFLGDAEIIELLILSGARVNAK-------DNMWLTPLHRAVA-SRSEEAVQVLIKHSADVNARDknwqTPLHVAAANKAV 120
Cdd:TIGR00870  20 AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAISLEYVD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  121 KCAEVIIPLLSS---------VNVSDRG----GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRA----- 176
Cdd:TIGR00870  96 AVEAILLHLLAAfrksgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDsfyhg 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  177 ---LHWAAYMGHLDVVALLINHGAEVTCKDKKGytplhaaasngqiNVVKHLLNLGVEideiNVYGNTALHIACYngqda 253
Cdd:TIGR00870 176 espLNAAACLGSPSIVALLSEDPADILTADSLG-------------NTLLHLLVMENE----FKAEYEELSCQMY----- 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 530371153  254 vvNELIDYGANVNQ-------PNNNGFTPLHFAA 280
Cdd:TIGR00870 234 --NFALSLLDKLRDskeleviLNHQGLTPLKLAA 265
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
585-802 3.90e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 60.41  E-value: 3.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 585 TKSPLHLAAYNGHHQALEVLL-QSLVDLDIRDEKGRTALDLAAFKGHTECVEALInqgasifvkDNVTkrtplhasving 663
Cdd:cd22192   17 SESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLM---------EAAP------------ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 664 htlclrlllEIADNPEAVDVkdAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGcTALHRGI-------------- 729
Cdd:cd22192   76 ---------ELVNEPMTSDL--YQGETALHIAVVNQNLNLVRELIARGADVVSPRATG-TFFRPGPknliyygehplsfa 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 730 -MTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALSEE----DCCF---KDNQGYTPLHWACYNG 801
Cdd:cd22192  144 aCVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYDLILSYDkeddLQPLdlvPNNQGLTPFKLAAKEG 223

                 .
gi 530371153 802 N 802
Cdd:cd22192  224 N 224
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
274-461 3.47e-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: 3.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 274 TPLhFAAASTHGALCLE-LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGE-----IDCVDKDGNTPLHVAA 347
Cdd:cd22192   19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 348 RYGHELLINTLITSGADTAK---CGihSMFPLHLAALnahsdccrkllssgqkysivsLFSNEHVLSagfeidtpdkFgr 424
Cdd:cd22192   98 VNQNLNLVRELIARGADVVSpraTG--TFFRPGPKNL---------------------IYYGEHPLS----------F-- 142
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 530371153 425 tclhaAAAGGNVECIKLLQSSGADFHKKDKCGRTPLH 461
Cdd:cd22192  143 -----AACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
587-831 3.68e-08

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 57.40  E-value: 3.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  587 SPLHLAAYNGHHQALEVLLQSLvdlDIRDEKGRTALdLAAFKGHTECVEALIN--------QGASIFVKDNVTKR----- 653
Cdd:TIGR00870  54 SALFVAAIENENLELTELLLNL---SCRGAVGDTLL-HAISLEYVDAVEAILLhllaafrkSGPLELANDQYTSEftpgi 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  654 TPLHASVINGHTLCLRLLLEIADNPEA----VDVKDAKGQT-------PLMLAVAYGHIDAVSLLLEKEANVDTVDILGC 722
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPAracgDFFVKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  723 TALHRGIMtgheECVQMLLEQEVSILCKDSrgrtplhyaaarghATWLSELLQMALSEEDCCfkDNQGYTPLHWACYNGN 802
Cdd:TIGR00870 210 TLLHLLVM----ENEFKAEYEELSCQMYNF--------------ALSLLDKLRDSKELEVIL--NHQGLTPLKLAAKEGR 269
                         250       260       270
                  ....*....|....*....|....*....|
gi 530371153  803 ENCIEVLLEQKCF-RKFIGNPFTPLHCAII 831
Cdd:TIGR00870 270 IVLFRLKLAIKYKqKKFVAWPNGQQLLSLY 299
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
140-168 4.78e-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: 4.78e-06
                           10        20
                   ....*....|....*....|....*....
gi 530371153   140 GRTALHHAALNGHVEMVNLLLAKGANINA 168
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 5.03e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 5.03e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530371153   10 PPLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLI 61
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
738-944 6.92e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.08  E-value: 6.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  738 QMLLE-QEVSILCKDSRGRTPLHYAAARGHATWLSELLQmalseedccFKDNQGY---TPLHWACYNGNENCIEVLLEQK 813
Cdd:TIGR00870  35 RDLEEpKKLNINCPDRLGRSALFVAAIENENLELTELLL---------NLSCRGAvgdTLLHAISLEYVDAVEAILLHLL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  814 CFRKFIGNPF--------------TPLHCAIINDHGNCASLLL--GAIDSSIVSCRDDK----------GRTPLHAAAFA 867
Cdd:TIGR00870 106 AAFRKSGPLElandqytseftpgiTALHLAAHRQNYEIVKLLLerGASVPARACGDFFVksqgvdsfyhGESPLNAAACL 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  868 DHVECLQLLLRHSAPVNAVDNSGKTALMMA-------AENG------QAGAVDILvnsAQADLTVK-----DKDLNTPLH 929
Cdd:TIGR00870 186 GSPSIVALLSEDPADILTADSLGNTLLHLLvmenefkAEYEelscqmYNFALSLL---DKLRDSKElevilNHQGLTPLK 262
                         250
                  ....*....|....*
gi 530371153  930 LACSKGHEKCALLIL 944
Cdd:TIGR00870 263 LAAKEGRIVLFRLKL 277
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
792-982 1.82e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.47  E-value: 1.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 792 TPLHWACYNGNENCIEVLLEQK----CFRKFIGNpfTPLHCAIINDHGNCASLLLGAIDSSI---VSCRDDKGRTPLHAA 864
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCPscdlFQRGALGE--TALHVAALYDNLEAAVVLMEAAPELVnepMTSDLYQGETALHIA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 865 AFADHVECLQLLLRHSAPVNA-----------VDN---SGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHL 930
Cdd:cd22192   97 VVNQNLNLVRELIARGADVVSpratgtffrpgPKNliyYGEHPLSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVLHI 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530371153 931 ACSKGHEKCA------LLILDKIQDE-SLINEKNNALQTPLHVAARNGLKVVVEELLAK 982
Cdd:cd22192  176 LVLQPNKTFAcqmydlILSYDKEDDLqPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
456-484 7.79e-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: 37.57  E-value: 7.79e-04
                           10        20
                   ....*....|....*....|....*....
gi 530371153   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 ...
789-811 1.98e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 1.98e-03
                           10        20
                   ....*....|....*....|...
gi 530371153   789 QGYTPLHWACYNGNENCIEVLLE 811
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLD 23
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
332-494 3.50e-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: 3.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  332 IDCVDKDGNTPLHVAARYG-HELLINTLITSGA-----DTAkcgihsmfpLHLAALNAHSDC--CRKLLSSGQKYSIVSL 403
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISLEYVDAVeaILLHLLAAFRKSGPLE 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  404 FSNEHVLSAGFeidtpdkFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKC--------------GRTPLHYAAANCHF 469
Cdd:TIGR00870 116 LANDQYTSEFT-------PGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSP 188
                         170       180
                  ....*....|....*....|....*
gi 530371153  470 HCIETLVTTGANVNETDDWGRTALH 494
Cdd:TIGR00870 189 SIVALLSEDPADILTADSLGNTLLH 213
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
687-715 4.71e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 4.71e-03
                           10        20
                   ....*....|....*....|....*....
gi 530371153   687 KGQTPLMLAVAYGHIDAVSLLLEKEANVD 715
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-343 7.66e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 184.00  E-value: 7.66e-52
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  54 AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSV 133
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 134 NVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 213
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 214 ASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALcLELLV 293
Cdd:COG0666  161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|
gi 530371153 294 NNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 343
Cdd:COG0666  240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
11-276 4.43e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 175.91  E-value: 4.43e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  11 PLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAV 90
Cdd:COG0666   24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  91 QVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFD 170
Cdd:COG0666  104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 171 KKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNG 250
Cdd:COG0666  184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
                        250       260
                 ....*....|....*....|....*.
gi 530371153 251 QDAVVNELIDYGANVNQPNNNGFTPL 276
Cdd:COG0666  264 AALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-307 4.61e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 175.91  E-value: 4.61e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  22 EEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVN 101
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 102 ARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAA 181
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 182 YMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDY 261
Cdd:COG0666  162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 530371153 262 GANVNQPNNNGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGK 307
Cdd:COG0666  242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
8-243 4.46e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.88  E-value: 4.46e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153   8 DQPPLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSE 87
Cdd:COG0666   87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  88 EAVQVLIKHSADVNARDKNwqtplhvaaankavkcaeviipllssvnvsdrgGRTALHHAALNGHVEMVNLLLAKGANIN 167
Cdd:COG0666  167 EIVKLLLEAGADVNARDND---------------------------------GETPLHLAAENGHLEIVKLLLEAGADVN 213
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530371153 168 AFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTAL 243
Cdd:COG0666  214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
22-310 7.62e-40

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 154.41  E-value: 7.62e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  22 EEIRMLIHKTEDVNTLDSEKRTPLHVaaFLG-----DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAV-QVLIK 95
Cdd:PHA03095  28 EEVRRLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDViKLLIK 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  96 HSADVNARDKNWQTPLHVAAANKAVkcaeviipllssvnvsdrggrtalhhaalngHVEMVNLLLAKGANINAFDKKDRR 175
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMT 154
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 176 ALHwaAYMGH----LDVVALLINHGAEVTCKDKKGYTPLHAAASNGQIN--VVKHLLNLGVEIDEINVYGNTALHIACYN 249
Cdd:PHA03095 155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530371153 250 G--QDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLELLvNNGADVNIQSKDGKSPL 310
Cdd:PHA03095 233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLI-ALGADINAVSSDGNTPL 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
86-359 2.25e-39

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 152.87  E-value: 2.25e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  86 SEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSS---VNVSDRGGRTALHHAALNGHVE-MVNLLLA 161
Cdd:PHA03095  26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAgadVNAPERCGFTPLHLYLYNATTLdVIKLLIK 105
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 162 KGANINAFDKKDRRALHwaAYMG----HLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINV--VKHLLNLGVEIDEI 235
Cdd:PHA03095 106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 236 NVYGNTALHIACYNGQD--AVVNELIDYGANVNQPNNNGFTPLHFAAA-STHGALCLELLVNNGADVNIQSKDGKSPLHM 312
Cdd:PHA03095 184 DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*..
gi 530371153 313 TAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLI 359
Cdd:PHA03095 264 AAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA03100 PHA03100
ankyrin repeat protein; Provisional
55-301 9.98e-37

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 144.04  E-value: 9.98e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  55 EIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAV-----KCAEVIIPL 129
Cdd:PHA03100  16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEY 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 130 LSSVNVSDRGGRTALHHAALN--GHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGH--LDVVALLINHGAEVTCKDKk 205
Cdd:PHA03100  96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNR- 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 206 gytplhaaasngqinvVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHG 285
Cdd:PHA03100 175 ----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK 238
                        250
                 ....*....|....*.
gi 530371153 286 ALcLELLVNNGADVNI 301
Cdd:PHA03100 239 EI-FKLLLNNGPSIKT 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
153-525 2.36e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 2.36e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 153 VEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEI 232
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 233 DEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALcLELLVNNGADVNIQskdgksplhm 312
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI-VKLLLEAGADVNAQ---------- 149
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 313 tavhgrftrsqtliqnggeidcvDKDGNTPLHVAARYGHELLINTLITSGADtakcgihsmfplhlaalnahsdccrkll 392
Cdd:COG0666  150 -----------------------DNDGNTPLHLAAANGNLEIVKLLLEAGAD---------------------------- 178
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 393 ssgqkysivslfsnehvlsagfeIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCI 472
Cdd:COG0666  179 -----------------------VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530371153 473 ETLVTTGANVNETDDWGRTALHYAAASDMDRNKTILGNAHDNSEELERARELK 525
Cdd:COG0666  236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
510-767 2.52e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 2.52e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 510 NAHDNSEELERARELKEKEATLCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEESDSGATksPL 589
Cdd:COG0666   14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNT--LL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 590 HLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLR 669
Cdd:COG0666   92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVK 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 670 LLLEI-ADnpeaVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSIL 748
Cdd:COG0666  171 LLLEAgAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
                        250
                 ....*....|....*....
gi 530371153 749 CKDSRGRTPLHYAAARGHA 767
Cdd:COG0666  247 AKDKDGLTALLLAAAAGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
533-813 7.08e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.08  E-value: 7.08e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 533 LEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEESDSGATKSPLHLAAYNGHHQALEVLLQSLVDLD 612
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 613 IRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEI-ADnpeaVDVKDAKGQTP 691
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAgAD----VNAQDNDGNTP 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 692 LMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLS 771
Cdd:COG0666  157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 530371153 772 ELLQMALSEEDccfKDNQGYTPLHWACYNGNENCIEVLLEQK 813
Cdd:COG0666  237 LLLEAGADLNA---KDKDGLTALLLAAAAGAALIVKLLLLAL 275
PHA02874 PHA02874
ankyrin repeat protein; Provisional
16-367 7.82e-34

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 135.86  E-value: 7.82e-34
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  16 IFSGDPEEIRMLI-HKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLI 94
Cdd:PHA02874   9 IYSGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  95 KHSADVNArdknwqtplhvaaankavkcaeVIIPLLSSvnvsdrggrtalhhaalnghvEMVNLLLAKGANINAFDKKDR 174
Cdd:PHA02874  89 DNGVDTSI----------------------LPIPCIEK---------------------DMIKTILDCGIDVNIKDAELK 125
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 175 RALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAV 254
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 255 VNELIDYGANVNQPNNNGFTPLHfaAASTHGALCLELLVNNgADVNIQSKDGKSPLHMtAVHGRFTRS--QTLIQNGGEI 332
Cdd:PHA02874 206 IKLLIDHGNHIMNKCKNGFTPLH--NAIIHNRSAIELLINN-ASINDQDIDGSTPLHH-AINPPCDIDiiDILLYHKADI 281
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|.
gi 530371153 333 DCVDKDGNTPLHVAARYGH------ELLINTLITSGADTAK 367
Cdd:PHA02874 282 SIKDNKGENPIDTAFKYINkdpvikDIIANAVLIKEADKLK 322
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
636-960 1.28e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.23  E-value: 1.28e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 636 ALINQGASIFVKDNVTKRTPLHASVINGHTLCLRLLLEIADNpeaVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVD 715
Cdd:COG0666    5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLA---LALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 716 TVDILGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQmalSEEDCCFKDNQGYTPLH 795
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE---AGADVNAQDNDGNTPLH 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 796 WACYNGNENCIEVLLEqkcfrkfignpftplHCAIINDhgncaslllgaidssivscRDDKGRTPLHAAAFADHVECLQL 875
Cdd:COG0666  159 LAAANGNLEIVKLLLE---------------AGADVNA-------------------RDNDGETPLHLAAENGHLEIVKL 204
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 876 LLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLACSKGHEKCALLILDKIQDESLINE 955
Cdd:COG0666  205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE-AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283

                 ....*
gi 530371153 956 KNNAL 960
Cdd:COG0666  284 DLLTL 288
PHA02876 PHA02876
ankyrin repeat protein; Provisional
26-364 2.42e-33

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 137.89  E-value: 2.42e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  26 MLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDK 105
Cdd:PHA02876 163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDL 242
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 106 NwqtpLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHV-EMVNLLLAKGANINAFDKKDRRALHWAAYMG 184
Cdd:PHA02876 243 S----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNG 318
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 185 H-LDVVALLINHGAEVTCKDKKGYTPLHAAAS-NGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYG 262
Cdd:PHA02876 319 YdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 263 ANVNQPNNNGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHG-RFTRSQTLIQNGGEIDCVDKDGNT 341
Cdd:PHA02876 399 ADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQY 478
                        330       340
                 ....*....|....*....|...
gi 530371153 342 PLHVAarYGHELLINTLITSGAD 364
Cdd:PHA02876 479 PLLIA--LEYHGIVNILLHYGAE 499
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
668-993 5.74e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 126.61  E-value: 5.74e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 668 LRLLLEIADNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSI 747
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 748 LCKDSRGRTPLHYAAARGHATWLSELLQmalSEEDCCFKDNQGYTPLHWACYNGNENCIEVLLEQKcfrkfignpftplh 827
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-------------- 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 828 cAIINdhgncaslllgaidssivsCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVD 907
Cdd:COG0666  144 -ADVN-------------------AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 908 ILVNsAQADLTVKDKDLNTPLHLACSKGHEKCALLILDKIQDeslINEKNNALQTPLHVAARNGLKVVVEELLAKGACVL 987
Cdd:COG0666  204 LLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279

                 ....*.
gi 530371153 988 AVDENG 993
Cdd:COG0666  280 AALLDL 285
PHA02876 PHA02876
ankyrin repeat protein; Provisional
56-385 1.24e-31

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 132.49  E-value: 1.24e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  56 IIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNV 135
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 136 SDrggrTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLD-VVALLINHGAEVTCKDKKGYTPLHAAA 214
Cdd:PHA02876 240 ND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMA 315
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 215 SNG-QINVVKHLLNLGVEIDEINVYGNTALHIACY--NGQDAVVNeLIDYGANVNQPNNNGFTPLHFAAAStHGALCLEL 291
Cdd:PHA02876 316 KNGyDTENIRTLIMLGADVNAADRLYITPLHQASTldRNKDIVIT-LLELGANVNARDYCDKTPIHYAAVR-NNVVIINT 393
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 292 LVNNGADVNIQSKDGKSPLHMtAVHGR--FTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHEL-LINTLITSGADTAKC 368
Cdd:PHA02876 394 LLDYGADIEALSQKIGTALHF-ALCGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAI 472
                        330
                 ....*....|....*..
gi 530371153 369 GIHSMFPLhLAALNAHS 385
Cdd:PHA02876 473 NIQNQYPL-LIALEYHG 488
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
289-622 4.37e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.91  E-value: 4.37e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 289 LELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKC 368
Cdd:COG0666    4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 369 GIHSMFPLHLAALNAHSDCCRKLLSsgqkysivslfsnehvlsAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGAD 448
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLE------------------AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD 145
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 449 FHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAASdmdrnktilgnahdNSEELerarelkeke 528
Cdd:COG0666  146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN--------------GHLEI---------- 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 529 atlcLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEESDSGATksPLHLAAYNGHHQALEVLLQSL 608
Cdd:COG0666  202 ----VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLT--ALLLAAAAGAALIVKLLLLAL 275
                        330
                 ....*....|....
gi 530371153 609 VDLDIRDEKGRTAL 622
Cdd:COG0666  276 LLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
492-758 6.05e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.83  E-value: 6.05e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 492 ALHYAAASDMDRNKTILGNAHDNSEELERARELKEKEATLCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLE 571
Cdd:COG0666   29 ALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 572 RTNSGFEESDSGATksPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvT 651
Cdd:COG0666  109 AGADVNARDKDGET--PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN-D 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 652 KRTPLHASVINGHTLCLRLLLE-IADnpeaVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIM 730
Cdd:COG0666  186 GETPLHLAAENGHLEIVKLLLEaGAD----VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261
                        250       260
                 ....*....|....*....|....*...
gi 530371153 731 TGHEECVQMLLEQEVSILCKDSRGRTPL 758
Cdd:COG0666  262 AGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
410-687 1.33e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 119.67  E-value: 1.33e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 410 LSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWG 489
Cdd:COG0666   41 LLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDG 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 490 RTALHYAAASdmdrnktilgnahdNSEELerarelkekeatlcLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELL 569
Cdd:COG0666  121 ETPLHLAAYN--------------GNLEI--------------VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 570 LERTNSGFEESDSGATksPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDN 649
Cdd:COG0666  173 LEAGADVNARDNDGET--PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 530371153 650 VTKRTPLHASVINGHTLCLRLLLEIADNPEAVDVKDAK 687
Cdd:COG0666  251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
403-725 1.70e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.59  E-value: 1.70e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 403 LFSNEHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANV 482
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 483 NETDDWGRTALHYAAAsdmdrnktilgnahDNSEELerarelkekeatlcLEFLLQNDANPSIRDKEGYNSIHYAAAYGH 562
Cdd:COG0666   81 NAKDDGGNTLLHAAAR--------------NGDLEI--------------VKLLLEAGADVNARDKDGETPLHLAAYNGN 132
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 563 RQCLELLLERTNSGFEESDSGATksPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGA 642
Cdd:COG0666  133 LEIVKLLLEAGADVNAQDNDGNT--PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 643 SIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADNPEAvdvKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGC 722
Cdd:COG0666  211 DVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGADLNA---KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286

                 ...
gi 530371153 723 TAL 725
Cdd:COG0666  287 TLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
123-483 2.39e-28

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 122.09  E-value: 2.39e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 123 AEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCK 202
Cdd:PHA02876 161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKN 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 203 DkkgyTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQ-DAVVNELIDYGANVNQPNNNGFTPLHFAAA 281
Cdd:PHA02876 241 D----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAK 316
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 282 STHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQ-TLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLIT 360
Cdd:PHA02876 317 NGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIViTLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 361 SGADtakcgihsmfplhLAALNahsdccrkllssgqkysivslfsnehvlsagfeidtpDKFGrTCLHAAAAGGN-VECI 439
Cdd:PHA02876 397 YGAD-------------IEALS-------------------------------------QKIG-TALHFALCGTNpYMSV 425
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|....*
gi 530371153 440 KLLQSSGADFHKKDKCGRTPLHYAAA-NCHFHCIETLVTTGANVN 483
Cdd:PHA02876 426 KTLIDRGANVNSKNKDLSTPLHYACKkNCKLDVIEMLLDNGADVN 470
PHA02876 PHA02876
ankyrin repeat protein; Provisional
12-265 2.59e-28

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 122.09  E-value: 2.59e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  12 LVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGD-AEIIELLILSGARVNAKDNMWLTPLH-RAVASRSEEA 89
Cdd:PHA02876 244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYlMAKNGYDTEN 323
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  90 VQVLIKHSADVNARDKNWQTPLHVAAANKAVKcaEVIIPLL---SSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANI 166
Cdd:PHA02876 324 IRTLIMLGADVNAADRLYITPLHQASTLDRNK--DIVITLLelgANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 167 NAFDKKDRRALHWAAY-MGHLDVVALLINHGAEVTCKDKKGYTPLH-AAASNGQINVVKHLLNLGVEIDEINVYGNTALH 244
Cdd:PHA02876 402 EALSQKIGTALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHyACKKNCKLDVIEMLLDNGADVNAINIQNQYPLL 481
                        250       260
                 ....*....|....*....|.
gi 530371153 245 IACynGQDAVVNELIDYGANV 265
Cdd:PHA02876 482 IAL--EYHGIVNILLHYGAEL 500
PHA02878 PHA02878
ankyrin repeat protein; Provisional
75-346 2.40e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 113.82  E-value: 2.40e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  75 LTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVA--AANKavkcaEVIIPLLSSVNVSDRG-GRTALHHAALNG 151
Cdd:PHA02878  38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckEPNK-----LGMKEMIRSINKCSVFyTLVAIKDAFNNR 112
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 152 HVEMVNLLLakganINAFDKK---DRRALHWAAYMGHLD--VVALLINHGAEVTCKDK-KGYTPLHAAASNGQINVVKHL 225
Cdd:PHA02878 113 NVEIFKIIL-----TNRYKNIqtiDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELL 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 226 LNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLELLVNNGADVNIQSK- 304
Cdd:PHA02878 188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYi 267
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 530371153 305 DGKSPLHMTAVHGRFTRsqTLIQNGGEIDCVDKDGNTPLHVA 346
Cdd:PHA02878 268 LGLTALHSSIKSERKLK--LLLEYGADINSLNSYKLTPLSSA 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
28-238 1.89e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 110.52  E-value: 1.89e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  28 IHKTEDVNT-LDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLH-----RAVASRSEEAVQVLIKHSADVN 101
Cdd:PHA03100  21 IIMEDDLNDySYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 102 ARDKNWQTPLHVAAANKavKCAEVIIPLLSS----VNVSDRGGRTALHHAALNGHV--EMVNLLLAKGANINAFDK---- 171
Cdd:PHA03100 101 APDNNGITPLLYAISKK--SNSYSIVEYLLDnganVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRvnyl 178
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530371153 172 ---------KDRR---ALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVY 238
Cdd:PHA03100 179 lsygvpiniKDVYgftPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA03100 PHA03100
ankyrin repeat protein; Provisional
192-483 3.74e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 109.37  E-value: 3.74e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 192 LINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIAC---YNGQDAV--VNELIDYGANVN 266
Cdd:PHA03100  21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikYNLTDVKeiVKLLLEYGANVN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 267 QPNNNGFTPLHFAAASTHGALCL-ELLVNNGADVNIQSKDGKSPLHMtavhgrFTRSqtliqnggeiDCVDKDgntplhv 345
Cdd:PHA03100 101 APDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHL------YLES----------NKIDLK------- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 346 aaryghelLINTLITSGADtakcgihsmfplhlaaLNAhsdCCRkllssgqkysiVSLFsnehvLSAGFEIDTPDKFGRT 425
Cdd:PHA03100 158 --------ILKLLIDKGVD----------------INA---KNR-----------VNYL-----LSYGVPINIKDVYGFT 194
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530371153 426 CLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVN 483
Cdd:PHA03100 195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA03095 PHA03095
ankyrin-like protein; Provisional
212-493 1.25e-24

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 108.57  E-value: 1.25e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 212 AAASNGQINVVKHLLNLGVEIDEINVYGNTALH--IACYNGQDA-VVNELIDYGANVNQPNNNGFTPLHFAAASTHGALC 288
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 289 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGH---ELLiNTLITSGA 363
Cdd:PHA03095 100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGA 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 364 DTAKCGIHSMFPLHLAALNAHSDccrkllssgqkYSIVslfsnEHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQ 443
Cdd:PHA03095 179 DVYAVDDRFRSLLHHHLQSFKPR-----------ARIV-----RELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLP 242
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530371153 444 --SSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTAL 493
Cdd:PHA03095 243 llIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
PHA02878 PHA02878
ankyrin repeat protein; Provisional
22-295 1.74e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 102.27  E-value: 1.74e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  22 EEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIK------ 95
Cdd:PHA02878  18 KYIEYIDHTENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcs 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  96 ------------HSADVNA-------RDKNWQTP--LHVAAANKAVKCAEVIIPLL----SSVNVSDR-GGRTALHHAAL 149
Cdd:PHA02878  98 vfytlvaikdafNNRNVEIfkiiltnRYKNIQTIdlVYIDKKSKDDIIEAEITKLLlsygADINMKDRhKGNTALHYATE 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 150 NGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASN-GQINVVKHLLNL 228
Cdd:PHA02878 178 NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEH 257
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530371153 229 GVEID-EINVYGNTALHIACYNGQdaVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLELLVNN 295
Cdd:PHA02878 258 GVDVNaKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISN 323
PHA03095 PHA03095
ankyrin-like protein; Provisional
355-682 1.60e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 98.94  E-value: 1.60e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 355 INTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRkllssgqkysIVSLfsnehVLSAGFEIDTPDKFGRTCLHAAAAGG 434
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKD----------IVRL-----LLEAGADVNAPERCGFTPLHLYLYNA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 435 NVE-CIKLLQSSGADFHKKDKCGRTPLH-YAA-ANCHFHCIETLVTTGANVNETDDWGRTALHyaaasdmdrnktILGNA 511
Cdd:PHA03095  95 TTLdVIKLLIKAGADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLA------------VLLKS 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 512 HDNSEELerarelkekeatlcLEFLLQNDANPSIRDKEGYNSIHYAAAYGH--RQCLELLLERTNSGFEESDSGATksPL 589
Cdd:PHA03095 163 RNANVEL--------------LRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNT--PL 226
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 590 HLAAYNGHHQALEV--LLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLC 667
Cdd:PHA03095 227 HSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNTPLSLMVRNNNGRA 305
                        330
                 ....*....|....*
gi 530371153 668 LRLLLEIADNPEAVD 682
Cdd:PHA03095 306 VRAALAKNPSAETVA 320
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-269 3.41e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 3.41e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  177 LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNlGVEIDEINvYGNTALHIACYNGQDAVVN 256
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 530371153  257 ELIDYGANVNQPN 269
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
144-236 5.82e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 5.82e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  144 LHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHgAEVTCKDkKGYTPLHAAASNGQINVVK 223
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 530371153  224 HLLNLGVEIDEIN 236
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
323-625 1.06e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 96.19  E-value: 1.06e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 323 QTLIQNGGE-IDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGQKYSIV 401
Cdd:PHA02874  18 EKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 402 SL--FSNEHV---LSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLV 476
Cdd:PHA02874  98 PIpcIEKDMIktiLDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL 177
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 477 TTGANVNETDDWGRTALHYAAasdmdrnktilgnahdnseelerarelkEKEATLCLEFLLQNDANPSIRDKEGYNSIHY 556
Cdd:PHA02874 178 EKGAYANVKDNNGESPLHNAA----------------------------EYGDYACIKLLIDHGNHIMNKCKNGFTPLHN 229
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530371153 557 AAAYgHRQCLELLLerTNSGFEESD-SGATksPLHLA-AYNGHHQALEVLLQSLVDLDIRDEKGRTALDLA 625
Cdd:PHA02874 230 AIIH-NRSAIELLI--NNASINDQDiDGST--PLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA03095 PHA03095
ankyrin-like protein; Provisional
24-227 1.96e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 95.86  E-value: 1.96e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  24 IRMLIHKTEDVNTLDSEKRTPLHV--AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASR--SEEAVQVLIKHSAD 99
Cdd:PHA03095 100 IKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGAD 179
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 100 VNARDKNWQTPLHVAAAN--KAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNL--LLAKGANINAFDKKDRR 175
Cdd:PHA03095 180 VYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQT 259
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530371153 176 ALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLN 227
Cdd:PHA03095 260 PLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
PHA02875 PHA02875
ankyrin repeat protein; Provisional
48-266 2.51e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 94.67  E-value: 2.51e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  48 AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 127
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 128 PLLSSVN-VSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKG 206
Cdd:PHA02875  89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530371153 207 YTPLHAAASNGQINVVKHLLNLGVEIDEINVYGN-TALHIACYNGQDAVVNELIDYGANVN 266
Cdd:PHA02875 169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCN 229
PHA03100 PHA03100
ankyrin repeat protein; Provisional
397-682 9.02e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 93.19  E-value: 9.02e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 397 KYSIVSLFSNEHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHF--HCIET 474
Cdd:PHA03100   9 KSRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltDVKEI 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 475 ---LVTTGANVNETDDWGRTALHYAAASDMDRNKTIlgnahdnseelerarelkekeatlclEFLLQNDANPSIRDKEGY 551
Cdd:PHA03100  89 vklLLEYGANVNAPDNNGITPLLYAISKKSNSYSIV--------------------------EYLLDNGANVNIKNSDGE 142
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 552 NSIHYAAAYGHR--QCLELLLERTNsgfeesdsgatksplHLAAYNghhqALEVLLQSLVDLDIRDEKGRTALDLAAFKG 629
Cdd:PHA03100 143 NLLHLYLESNKIdlKILKLLIDKGV---------------DINAKN----RVNYLLSYGVPINIKDVYGFTPLHYAVYNN 203
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530371153 630 HTECVEALINQGASIFVKDNVTKrTPLHASVINGHTLCLRLLLEIADNPEAVD 682
Cdd:PHA03100 204 NPEFVKYLLDLGANPNLVNKYGD-TPLHIAILNNNKEIFKLLLNNGPSIKTII 255
PHA03095 PHA03095
ankyrin-like protein; Provisional
254-640 9.55e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 93.55  E-value: 9.55e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 254 VVNELIDYGANVNQPNNNGFTPLHFAAASTHGAL--CLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTR-SQTLIQNGG 330
Cdd:PHA03095  29 EVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDvIKLLIKAGA 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 331 EIDCVDKDGNTPLHVAAR--YGHELLINTLITSGADTAKCGIHSMFPLHLaalnahsdccrkLLSSgqkysivslfsneh 408
Cdd:PHA03095 109 DVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLAV------------LLKS-------------- 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 409 vlsagfeidtpdkfgrtclhaaaAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFH--CIETLVTTGANVNETD 486
Cdd:PHA03095 163 -----------------------RNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATD 219
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 487 DWGRTALHYAAASDMDRNKTILgnahdnseelerarelkekeatlcleFLLQNDANPSIRDKEGYnsihyaaayghrqcl 566
Cdd:PHA03095 220 MLGNTPLHSMATGSSCKRSLVL--------------------------PLLIAGISINARNRYGQ--------------- 258
                        330       340       350       360       370       380       390
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530371153 567 elllertnsgfeesdsgatkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQ 640
Cdd:PHA03095 259 --------------------TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
Ank_2 pfam12796
Ankyrin repeats (3 copies);
111-203 3.71e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.24  E-value: 3.71e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  111 LHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKgANINAFDkKDRRALHWAAYMGHLDVVA 190
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 530371153  191 LLINHGAEVTCKD 203
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
669-984 6.28e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 91.24  E-value: 6.28e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 669 RLLLEIADnpeaVDVKDAKGQTPLMLAVAYGH---IDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEE-CVQMLLEQE 744
Cdd:PHA03095  32 RLLAAGAD----VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 745 VSILCKDSRGRTPLH-YAA-ARGHATWLSELLQMALSEEDCcfkDNQGYTPLHwaCYNGNENC----IEVLLEQKCF--- 815
Cdd:PHA03095 108 ADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNAL---DLYGMTPLA--VLLKSRNAnvelLRLLIDAGADvya 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 816 RKFIGNpfTPLH--CAIINDHGNCASLLLGAIDSsiVSCRDDKGRTPLHAAAFADHVECLQL--LLRHSAPVNAVDNSGK 891
Cdd:PHA03095 183 VDDRFR--SLLHhhLQSFKPRARIVRELIRAGCD--PAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQ 258
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 892 TALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLACSKGHEKCALLILDKIQDESLINEKNNALQTPLHVAARNG 971
Cdd:PHA03095 259 TPLHYAAVFNNPRACRRLIA-LGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTASVAGGDIPSDA 337
                        330
                 ....*....|...
gi 530371153 972 LKVVVEELLAKGA 984
Cdd:PHA03095 338 TRLCVAKVVLRGA 350
Ank_2 pfam12796
Ankyrin repeats (3 copies);
210-302 9.17e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.09  E-value: 9.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  210 LHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYgANVNqPNNNGFTPLHFAAASTHGAlCL 289
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLE-IV 77
                          90
                  ....*....|...
gi 530371153  290 ELLVNNGADVNIQ 302
Cdd:pfam12796  78 KLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
622-718 5.88e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 5.88e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  622 LDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLEIADnpeaVDVKDaKGQTPLMLAVAYGHI 701
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHL 74
                          90
                  ....*....|....*..
gi 530371153  702 DAVSLLLEKEANVDTVD 718
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
45-170 1.80e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 1.80e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153   45 LHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHsADVNARDKnwqtplhvaaankavkcae 124
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN------------------- 60
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 530371153  125 viipllssvnvsdrgGRTALHHAALNGHVEMVNLLLAKGANINAFD 170
Cdd:pfam12796  61 ---------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
589-887 2.12e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 86.17  E-value: 2.12e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 589 LHLAAYNGHHQALEVLLQSLVD-LDIRDEKGRTALDLAAFKGHTECVEALINQGASI-FVKDNVTKrtPLHASVINGHTL 666
Cdd:PHA02874   5 LRMCIYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADInHINTKIPH--PLLTAIKIGAHD 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 667 CLRLLLE--------------------IADNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALH 726
Cdd:PHA02874  83 IIKLLIDngvdtsilpipciekdmiktILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIH 162
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 727 RGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALSEEDCCfkdNQGYTPLHWACYNgNENCI 806
Cdd:PHA02874 163 IAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKC---KNGFTPLHNAIIH-NRSAI 238
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 807 EVLLEQKCFRKFIGNPFTPLHCAIIN--DHGNCASLLLGAIDSSIvscRDDKGRTPLHAA-AFADHVECLQLLLRHSAPV 883
Cdd:PHA02874 239 ELLINNASINDQDIDGSTPLHHAINPpcDIDIIDILLYHKADISI---KDNKGENPIDTAfKYINKDPVIKDIIANAVLI 315

                 ....
gi 530371153 884 NAVD 887
Cdd:PHA02874 316 KEAD 319
PHA02874 PHA02874
ankyrin repeat protein; Provisional
150-563 5.77e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 84.63  E-value: 5.77e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 150 NGHVEMV-NLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNL 228
Cdd:PHA02874  11 SGDIEAIeKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 229 GVEideinvygNTALHIACYNGQdaVVNELIDYGANVNQPNNNGFTPLHFAAASthGAL-CLELLVNNGADVNIQSKDGK 307
Cdd:PHA02874  91 GVD--------TSILPIPCIEKD--MIKTILDCGIDVNIKDAELKTFLHYAIKK--GDLeSIKMLFEYGADVNIEDDNGC 158
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 308 SPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGhellintlitsgadtakcgihsmfplhlaalnahsdc 387
Cdd:PHA02874 159 YPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYG------------------------------------- 201
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 388 crkllssgqkysivslfsnehvlsagfeidtpdkfgrtclhaaaaggNVECIKLLQSSGADFHKKDKCGRTPLHYAAanC 467
Cdd:PHA02874 202 -----------------------------------------------DYACIKLLIDHGNHIMNKCKNGFTPLHNAI--I 232
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 468 HFHCIETLVTTGANVNETDDWGRTALHYAAASDMDRNktilgnahdnseelerarelkekeatlCLEFLLQNDANPSIRD 547
Cdd:PHA02874 233 HNRSAIELLINNASINDQDIDGSTPLHHAINPPCDID---------------------------IIDILLYHKADISIKD 285
                        410
                 ....*....|....*.
gi 530371153 548 KEGYNSIHYAAAYGHR 563
Cdd:PHA02874 286 NKGENPIDTAFKYINK 301
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
74-281 7.40e-17

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 85.45  E-value: 7.40e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  74 WLTPLHRAVASRSEEAVQVLIK-HSADVNARDKNWQTPLHVAAANKAVKCAEVII---PLLssVNV---SD-RGGRTALH 145
Cdd:cd22192   17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaaPEL--VNEpmtSDlYQGETALH 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 146 HAALNGHVEMVNLLLAKGANIN------AFDKKDRRAL-----H---WAAYMGHLDVVALLINHGAEVTCKDKKGYTPLH 211
Cdd:cd22192   95 IAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530371153 212 AAASNGQINVVKH----LLNLGVEIDEINVYgntalHIacyngqdavvnelidyganvnqPNNNGFTPLHFAAA 281
Cdd:cd22192  175 ILVLQPNKTFACQmydlILSYDKEDDLQPLD-----LV----------------------PNNQGLTPFKLAAK 221
Ank_2 pfam12796
Ankyrin repeats (3 copies);
589-682 8.15e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 8.15e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  589 LHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQgasIFVKDNVTKRTPLHASVINGHTLCL 668
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 530371153  669 RLLLEIADNPEAVD 682
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
861-949 2.04e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 2.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  861 LHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKdlnTPLHLACSKGHEKCA 940
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77

                  ....*....
gi 530371153  941 LLILDKIQD 949
Cdd:pfam12796  78 KLLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
656-751 2.45e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 2.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  656 LHASVINGHTLCLRLLLEiadNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKeANVDTVDiLGCTALHRGIMTGHEE 735
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE---NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLE 75
                          90
                  ....*....|....*.
gi 530371153  736 CVQMLLEQEVSILCKD 751
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
12-104 3.22e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.77  E-value: 3.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153   12 LVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLiLSGARVNAKDNMWlTPLHRAVASRSEEAVQ 91
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDNGR-TALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 530371153   92 VLIKHSADVNARD 104
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
20-170 5.76e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 81.85  E-value: 5.76e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  20 DPEEIRMLIHKTEDVNTLDSEK-RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSA 98
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530371153  99 DVNARDKNWQTPLHVAAAnkAVKCAEVIIPLL---SSVNV-SDRGGRTALHHAALNGHVemVNLLLAKGANINAFD 170
Cdd:PHA02878 226 STDARDKCGNTPLHISVG--YCKDYDILKLLLehgVDVNAkSYILGLTALHSSIKSERK--LKLLLEYGADINSLN 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
794-887 9.21e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 9.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  794 LHWACYNGNENCIEVLLEQKC-FRKFIGNPFTPLHCAIINDHGNCASLLLGAIDSSIvscrDDKGRTPLHAAAFADHVEC 872
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL----KDNGRTALHYAARSGHLEI 76
                          90
                  ....*....|....*
gi 530371153  873 LQLLLRHSAPVNAVD 887
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
602-984 1.65e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 81.26  E-value: 1.65e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 602 EVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGA--SIFVKDNVTkrtplhasvinghtlclrlLLEIADNPE 679
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGAdvNIIALDDLS-------------------VLECAVDSK 222
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 680 AVDVKDA---------KGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGH-EECVQMLLEQEVSILC 749
Cdd:PHA02876 223 NIDTIKAiidnrsninKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNA 302
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 750 KDSRGRTPLHYAAARGHATwlSELLQMALSEEDCCFKDNQGYTPLHWA-CYNGNENCIEVLLEqkcfrkfignpftplhc 828
Cdd:PHA02876 303 KNIKGETPLYLMAKNGYDT--ENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLE----------------- 363
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 829 aiindhgncasllLGAidssIVSCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMA-AENGQAGAVD 907
Cdd:PHA02876 364 -------------LGA----NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVK 426
                        330       340       350       360       370       380       390       400
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 908 ILVNSAqADLTVKDKDLNTPLHLACSKgheKCAL----LILDKIQDESLINEKNnalQTPLHVAArnGLKVVVEELLAKG 983
Cdd:PHA02876 427 TLIDRG-ANVNSKNKDLSTPLHYACKK---NCKLdvieMLLDNGADVNAINIQN---QYPLLIAL--EYHGIVNILLHYG 497

                 .
gi 530371153 984 A 984
Cdd:PHA02876 498 A 498
Ank_2 pfam12796
Ankyrin repeats (3 copies);
725-814 1.67e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 1.67e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  725 LHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALSEEdccfkDNQGYTPLHWACYNGNEN 804
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAARSGHLE 75
                          90
                  ....*....|
gi 530371153  805 CIEVLLEQKC 814
Cdd:pfam12796  76 IVKLLLEKGA 85
PHA02875 PHA02875
ankyrin repeat protein; Provisional
533-743 1.67e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.04  E-value: 1.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 533 LEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLerTNSGFEESDSGATKSPLHLAAYNGHHQALEVLLQS--LVD 610
Cdd:PHA02875  18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLM--KHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLgkFAD 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 611 lDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKdNVTKRTPLHASVINGHTLCLRLLLeiaDNPEAVDVKDAKGQT 690
Cdd:PHA02875  96 -DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP-NTDKFSPLHLAVMMGDIKGIELLI---DHKACLDIEDCCGCT 170
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 530371153 691 PLMLAVAYGHIDAVSLLLEKEANVDTVDILGC-TALHRGIMTGHEECVQMLLEQ 743
Cdd:PHA02875 171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKR 224
Ank_2 pfam12796
Ankyrin repeats (3 copies);
554-648 2.17e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 2.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  554 IHYAAAYGHRQCLELLLERTNSGFEESDSGATksPLHLAAYNGHHQALEVLLQSlVDLDIRDEkGRTALDLAAFKGHTEC 633
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRT--ALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEI 76
                          90
                  ....*....|....*
gi 530371153  634 VEALINQGASIFVKD 648
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA02798 PHA02798
ankyrin-like protein; Provisional
78-364 2.54e-15

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 79.88  E-value: 2.54e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  78 LHRAvaSRSEEAVQVLIKHSADVNARDKNWQTPLhvaaankavkCAeviipLLSsvNVSDrggrtalhhaaLNGHVEMVN 157
Cdd:PHA02798  44 LQRD--SPSTDIVKLFINLGANVNGLDNEYSTPL----------CT-----ILS--NIKD-----------YKHMLDIVK 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 158 LLLAKGANINAFDKKDRRALHWA---AYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNG---QINVVKHLLNLGVE 231
Cdd:PHA02798  94 ILIENGADINKKNSDGETPLYCLlsnGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVD 173
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 232 IDEI-NVYGNTALHiaCY-----NGQDA-VVNELIDYGANVNQPNNngftplhfAAASTHGALCLELLVNNG-------- 296
Cdd:PHA02798 174 INTHnNKEKYDTLH--CYfkyniDRIDAdILKLFVDNGFIINKENK--------SHKKKFMEYLNSLLYDNKrfkknild 243
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530371153 297 ---ADVNIQSKD--GKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGAD 364
Cdd:PHA02798 244 fifSYIDINQVDelGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
567-749 4.28e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 79.91  E-value: 4.28e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 567 ELLLERTnsgfEESDSGATKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFV 646
Cdd:PLN03192 511 DLLGDNG----GEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI 586
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 647 KDnVTKRTPLHASVINGHTLCLRLLLEIA--DNPEAvdvkdakGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTA 724
Cdd:PLN03192 587 RD-ANGNTALWNAISAKHHKIFRILYHFAsiSDPHA-------AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
                        170       180
                 ....*....|....*....|....*
gi 530371153 725 LHRGIMTGHEECVQMLLEQEVSILC 749
Cdd:PLN03192 659 LQVAMAEDHVDMVRLLIMNGADVDK 683
Ank_2 pfam12796
Ankyrin repeats (3 copies);
427-500 6.33e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 6.33e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530371153  427 LHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTgANVNETDDwGRTALHYAAASD 500
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSG 72
PHA03095 PHA03095
ankyrin-like protein; Provisional
17-168 7.40e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.14  E-value: 7.40e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  17 FSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVaaFLG----DAEIIELLILSGARVNAKDNMWLTPLHR-AVASRSEEAV- 90
Cdd:PHA03095 128 FNINPKVIRLLLRKGADVNALDLYGMTPLAV--LLKsrnaNVELLRLLIDAGADVYAVDDRFRSLLHHhLQSFKPRARIv 205
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  91 QVLIKHSADVNARDKNWQTPLHVAAANKAVKcAEVIIPLL---SSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANIN 167
Cdd:PHA03095 206 RELIRAGCDPAATDMLGNTPLHSMATGSSCK-RSLVLPLLiagISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284

                 .
gi 530371153 168 A 168
Cdd:PHA03095 285 A 285
PHA02875 PHA02875
ankyrin repeat protein; Provisional
173-408 1.12e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 77.34  E-value: 1.12e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 173 DRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVeIDEINVYG-NTALHIACYNGQ 251
Cdd:PHA02875   2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDiESELHDAVEEGD 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 252 DAVVNELIDYGANVNQP-NNNGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGG 330
Cdd:PHA02875  81 VKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDI-MKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530371153 331 EIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAAL-NAHSDCCRKLLSSGQKYSIVSLFSNEH 408
Cdd:PHA02875 160 CLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIeNNKIDIVRLFIKRGADCNIMFMIEGEE 238
PHA02875 PHA02875
ankyrin repeat protein; Provisional
9-167 1.29e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 77.34  E-value: 1.29e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153   9 QPPLVQAIFSGDPEEIRMLIHKTEDVNTLDSEK-RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSE 87
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  88 EAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVN-VSDRGGRTALHHAALNGHVEMVNLLLAKGANI 166
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGADC 228

                 .
gi 530371153 167 N 167
Cdd:PHA02875 229 N 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
692-766 1.38e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 1.38e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 530371153  692 LMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEvsILCKDSRGRTPLHYAAARGH 766
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA--DVNLKDNGRTALHYAARSGH 73
Ank_2 pfam12796
Ankyrin repeats (3 copies);
376-486 1.81e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.76  E-value: 1.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  376 LHLAALNAHSDCCRKLLSSGqkysivslfsnehvlsagFEIDTPDKFGRTCLHAAAAGGNVECIKLLqSSGADFHKKDKc 455
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG------------------ADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDN- 60
                          90       100       110
                  ....*....|....*....|....*....|.
gi 530371153  456 GRTPLHYAAANCHFHCIETLVTTGANVNETD 486
Cdd:pfam12796  61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
701-993 2.58e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.60  E-value: 2.58e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 701 IDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEEC---VQMLLEQEVSILCKDSRGRTPLHYaaarghatwlseLLQMA 777
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHL------------YLYNA 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 778 LSEE----------DCCFKDNQGYTPLHwACYNG---NENCIEVLLEQKcfrkfignpftplhcAIINDhgncaslllga 844
Cdd:PHA03095  95 TTLDvikllikagaDVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKG---------------ADVNA----------- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 845 idssivscRDDKGRTPLHA---AAFADhVECLQLLLRHSAPVNAVDNSGKTALMMAAEN--GQAGAVDILVnSAQADLTV 919
Cdd:PHA03095 148 --------LDLYGMTPLAVllkSRNAN-VELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELI-RAGCDPAA 217
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530371153 920 KDKDLNTPLHLACSKGHEKcALLILDKIQDESLINEKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVDENG 993
Cdd:PHA03095 218 TDMLGNTPLHSMATGSSCK-RSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDG 290
Ank_2 pfam12796
Ankyrin repeats (3 copies);
894-990 8.37e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.83  E-value: 8.37e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  894 LMMAAENGQAGAVDILVNSaQADLTVKDKDLNTPLHLACSKGHEKCALLILDKIQdeslINEKNNAlQTPLHVAARNGLK 973
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD----VNLKDNG-RTALHYAARSGHL 74
                          90
                  ....*....|....*..
gi 530371153  974 VVVEELLAKGACVLAVD 990
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
738-991 1.30e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 75.10  E-value: 1.30e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 738 QMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMAlseEDCCFKDNQGYTPLHWACYNGNENCIEVLLEQkcfRK 817
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYG---ADVNIIALDDLSVLECAVDSKNIDTIKAIIDN---RS 235
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 818 FIGNPFTPLHCAIINDHGNCASLLLGAIDSsiVSCRDDKGRTPLHAAAFADHVECL-QLLLRHSAPVNAVDNSGKTALMM 896
Cdd:PHA02876 236 NINKNDLSLLKAIRNEDLETSLLLYDAGFS--VNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYL 313
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 897 AAENGQAGAVDILVNSAQADLTVKDKDLNTPLHLACSKGHEKCALLILdkIQDESLINEKNNALQTPLHVAARNGLKVVV 976
Cdd:PHA02876 314 MAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITL--LELGANVNARDYCDKTPIHYAAVRNNVVII 391
                        250
                 ....*....|....*
gi 530371153 977 EELLAKGACVLAVDE 991
Cdd:PHA02876 392 NTLLDYGADIEALSQ 406
PHA03100 PHA03100
ankyrin repeat protein; Provisional
656-926 1.32e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.93  E-value: 1.32e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 656 LHASVINGHTLCLRLLLE--IADNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGH 733
Cdd:PHA03100   1 LYSYIVLTKSRIIKVKNIkyIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKY 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 734 E-----ECVQMLLEQEVSILCKDSRGRTPLHYAAAR--GHATWLSELLQMALSEEDccfKDNQGYTPLHWA--CYNGNEN 804
Cdd:PHA03100  81 NltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNI---KNSDGENLLHLYleSNKIDLK 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 805 CIEVLLEqkcfrkfignpftplHCAIINDHGNCASLL-LGA-IDSsivscRDDKGRTPLHAAAFADHVECLQLLLRHSAP 882
Cdd:PHA03100 158 ILKLLID---------------KGVDINAKNRVNYLLsYGVpINI-----KDVYGFTPLHYAVYNNNPEFVKYLLDLGAN 217
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|.
gi 530371153 883 VNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTV-------KDKDLNT 926
Cdd:PHA03100 218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIietllyfKDKDLNT 268
PHA02798 PHA02798
ankyrin-like protein; Provisional
55-266 2.18e-13

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 73.72  E-value: 2.18e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  55 EIIELLILSGARVNAKDNMWLTPLHRAVASRSE-----EAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPL 129
Cdd:PHA02798  52 DIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFM 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 130 L---SSVNVSDRGGRTALHHAALNGH---VEMVNLLLAKGANINAFDKKDR-RALHwaAYMGH------LDVVALLINHG 196
Cdd:PHA02798 132 IengADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNNKEKyDTLH--CYFKYnidridADILKLFVDNG 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 197 ---------------------------------------AEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINV 237
Cdd:PHA02798 210 fiinkenkshkkkfmeylnsllydnkrfkknildfifsyIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITE 289
                        250       260
                 ....*....|....*....|....*....
gi 530371153 238 YGNTALHIACYNGQDAVVNELIDYGANVN 266
Cdd:PHA02798 290 LGNTCLFTAFENESKFIFNSILNKKPNKN 318
PHA02876 PHA02876
ankyrin repeat protein; Provisional
585-926 2.23e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 74.33  E-value: 2.23e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 585 TKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKD---------------- 648
Cdd:PHA02876 178 CITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDlsllkairnedletsl 257
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 649 ------------NVTKRTPLHASVingHTLCL-RLLLEIADNPEAVDVKDAKGQTPLMLAVAYGH-IDAVSLLLEKEANV 714
Cdd:PHA02876 258 llydagfsvnsiDDCKNTPLHHAS---QAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADV 334
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 715 DTVDILGCTALHRG-IMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALSEEDCCFKDNqgyTP 793
Cdd:PHA02876 335 NAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG---TA 411
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 794 LHWACYNgnencievlleqkcfrkfiGNPFTPLHCAIinDHGncaslllgaidsSIVSCRDDKGRTPLHAAAFAD-HVEC 872
Cdd:PHA02876 412 LHFALCG-------------------TNPYMSVKTLI--DRG------------ANVNSKNKDLSTPLHYACKKNcKLDV 458
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530371153 873 LQLLLRHSAPVNAVDNSGKTALMMAAenGQAGAVDILVNSAQA--DLTVKDKDLNT 926
Cdd:PHA02876 459 IEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAElrDSRVLHKSLND 512
PHA02875 PHA02875
ankyrin repeat protein; Provisional
254-483 3.79e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 72.72  E-value: 3.79e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 254 VVNELIDYGANVNQPNNNGFTPLHFAAaSTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI- 332
Cdd:PHA02875  17 IARRLLDIGINPNFEIYDGISPIKLAM-KFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAd 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 333 DCVDKDGNTPLHVAARYGHELLINTLITSGADTakcgihsmfplhlaalnahsdccrkllssgqkysivslfsnehvlsa 412
Cdd:PHA02875  96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADP----------------------------------------------- 128
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530371153 413 gfEIDTPDKFgrTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVN 483
Cdd:PHA02875 129 --DIPNTDKF--SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
Ank_2 pfam12796
Ankyrin repeats (3 copies);
758-842 4.88e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 4.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  758 LHYAAARGHATWLSELLQmalSEEDCCFKDNQGYTPLHWACYNGNENCIEVLLEQKCFRKFiGNPFTPLHCAIINDHGNC 837
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE---NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-DNGRTALHYAARSGHLEI 76

                  ....*
gi 530371153  838 ASLLL 842
Cdd:pfam12796  77 VKLLL 81
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
48-201 9.81e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 72.59  E-value: 9.81e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  48 AAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 127
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530371153 128 PLLSSVNVSDRGgrTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTC 201
Cdd:PLN03192 612 HFASISDPHAAG--DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
Ank_2 pfam12796
Ankyrin repeats (3 copies);
532-615 1.01e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 1.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  532 CLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSgfEESDSGATksPLHLAAYNGHHQALEVLLQSLVDL 611
Cdd:pfam12796  12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRT--ALHYAARSGHLEIVKLLLEKGADI 87

                  ....
gi 530371153  612 DIRD 615
Cdd:pfam12796  88 NVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
233-568 1.64e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.06  E-value: 1.64e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 233 DEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLELL-VNNGADVNIQSKDGKSPLH 311
Cdd:PHA02878  31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIrSINKCSVFYTLVAIKDAFN 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 312 MTAVH-------GRFTRSQTLiqNGGEIDCVDKDGNTPLHVaaryghellINTLITSGADTAKCGIHSM-FPLHLAALNA 383
Cdd:PHA02878 111 NRNVEifkiiltNRYKNIQTI--DLVYIDKKSKDDIIEAEI---------TKLLLSYGADINMKDRHKGnTALHYATENK 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 384 HSDCCRKLLSSGQkysivslfsnehvlsagfEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYA 463
Cdd:PHA02878 180 DQRLTELLLSYGA------------------NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 464 AANC-HFHCIETLVTTGANVN-ETDDWGRTALHYAAASDmDRNKTILG-----NAHDNSEELERARELKEKEATLCLEFL 536
Cdd:PHA02878 242 VGYCkDYDILKLLLEHGVDVNaKSYILGLTALHSSIKSE-RKLKLLLEygadiNSLNSYKLTPLSSAVKQYLCINIGRIL 320
                        330       340       350
                 ....*....|....*....|....*....|....*..
gi 530371153 537 -----LQNDANPSIRDKEGYnSIHYAAAYGHRQCLEL 568
Cdd:PHA02878 321 isnicLLKRIKPDIKNSEGF-IDNMDCITSNKRLNQI 356
PHA02878 PHA02878
ankyrin repeat protein; Provisional
309-628 2.51e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 70.29  E-value: 2.51e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 309 PLHMtAVHGR-FTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSgadTAKCGIHSmfplhlaALNAHSDC 387
Cdd:PHA02878  40 PLHQ-AVEARnLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS---INKCSVFY-------TLVAIKDA 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 388 CRKLLSSGQKYSIVSLFSNEHVLSAgFEIDTPDKFGRTclhaaaaggNVECIKLLQSSGADFHKKDK-CGRTPLHYAAAN 466
Cdd:PHA02878 109 FNNRNVEIFKIILTNRYKNIQTIDL-VYIDKKSKDDII---------EAEITKLLLSYGADINMKDRhKGNTALHYATEN 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 467 CHFHCIETLVTTGANVNETDDWGRTALHYAAASdmdRNKTIlgnahdnseelerarelkekeatlcLEFLLQNDANPSIR 546
Cdd:PHA02878 179 KDQRLTELLLSYGANVNIPDKTNNSPLHHAVKH---YNKPI-------------------------VHILLENGASTDAR 230
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 547 DKEGYNSIHYAAAY-GHRQCLELLLERTNSGFEESdSGATKSPLHLAAYNghHQALEVLLQSLVDLDIRDEKGRTALDLA 625
Cdd:PHA02878 231 DKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKS-YILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307

                 ...
gi 530371153 626 AFK 628
Cdd:PHA02878 308 VKQ 310
PHA02876 PHA02876
ankyrin repeat protein; Provisional
407-761 5.29e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.71  E-value: 5.29e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 407 EHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNetd 486
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN--- 238
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 487 dwgrtalhyaaasdmdRNKTILGNAHDNsEELERArelkekeatlclefLLQNDANPSIRDKEGYNSihyaaayghrqcl 566
Cdd:PHA02876 239 ----------------KNDLSLLKAIRN-EDLETS--------------LLLYDAGFSVNSIDDCKN------------- 274
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 567 elllertnsgfeesdsgatkSPLHLAAYNGHHQAL-EVLLQSLVDLDIRDEKGRTALDLAAFKGH-TECVEALINQGASI 644
Cdd:PHA02876 275 --------------------TPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADV 334
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 645 FVKDNVTKrTPLH-ASVINGHTLCLRLLLEIADNpeaVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCT 723
Cdd:PHA02876 335 NAADRLYI-TPLHqASTLDRNKDIVITLLELGAN---VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGT 410
                        330       340       350
                 ....*....|....*....|....*....|....*....
gi 530371153 724 ALHRGIM-TGHEECVQMLLEQEVSILCKDSRGRTPLHYA 761
Cdd:PHA02876 411 ALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
Ank_4 pfam13637
Ankyrin repeats (many copies);
140-193 5.94e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.14  E-value: 5.94e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530371153  140 GRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLI 193
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
174-226 1.22e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 1.22e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530371153  174 RRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLL 226
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
343-453 1.51e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 1.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  343 LHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGQKYSIVSlfsnehvlsagfeidtpdkf 422
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN-------------------- 60
                          90       100       110
                  ....*....|....*....|....*....|.
gi 530371153  423 GRTCLHAAAAGGNVECIKLLQSSGADFHKKD 453
Cdd:pfam12796  61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
49-280 1.51e-11

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 68.57  E-value: 1.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153   49 AFLGDAEIIELLILSGARVNAK-------DNMWLTPLHRAVA-SRSEEAVQVLIKHSADVNARDknwqTPLHVAAANKAV 120
Cdd:TIGR00870  20 AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAISLEYVD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  121 KCAEVIIPLLSS---------VNVSDRG----GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRA----- 176
Cdd:TIGR00870  96 AVEAILLHLLAAfrksgplelANDQYTSeftpGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDsfyhg 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  177 ---LHWAAYMGHLDVVALLINHGAEVTCKDKKGytplhaaasngqiNVVKHLLNLGVEideiNVYGNTALHIACYngqda 253
Cdd:TIGR00870 176 espLNAAACLGSPSIVALLSEDPADILTADSLG-------------NTLLHLLVMENE----FKAEYEELSCQMY----- 233
                         250       260       270
                  ....*....|....*....|....*....|....
gi 530371153  254 vvNELIDYGANVNQ-------PNNNGFTPLHFAA 280
Cdd:TIGR00870 234 --NFALSLLDKLRDskeleviLNHQGLTPLKLAA 265
Ank_2 pfam12796
Ankyrin repeats (3 copies);
276-364 2.02e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.90  E-value: 2.02e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  276 LHFAAASTHgALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNgGEIDCVDkDGNTPLHVAARYGHELLI 355
Cdd:pfam12796   1 LHLAAKNGN-LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                  ....*....
gi 530371153  356 NTLITSGAD 364
Cdd:pfam12796  78 KLLLEKGAD 86
Ank_4 pfam13637
Ankyrin repeats (many copies);
423-476 2.36e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.60  E-value: 2.36e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530371153  423 GRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLV 476
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
183-374 2.43e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.97  E-value: 2.43e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 183 MGHLDVVALLINHGAEVTckDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYG 262
Cdd:PLN03192 504 LHDLNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 263 ANVNQPNNNGFTPLHFAAASTHGALcLELLVNNGADVNIQSkdGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTP 342
Cdd:PLN03192 582 CNVHIRDANGNTALWNAISAKHHKI-FRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
                        170       180       190
                 ....*....|....*....|....*....|..
gi 530371153 343 LHVAARYGHELLINTLITSGADTAKCGIHSMF 374
Cdd:PLN03192 659 LQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
PHA02878 PHA02878
ankyrin repeat protein; Provisional
166-463 5.39e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.06  E-value: 5.39e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 166 INAFDKKDRRA----------LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEI 235
Cdd:PHA02878  20 IEYIDHTENYStsaslipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVF 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 236 NVYgnTALHIACYNGQDAVVNELIdyganVNQPNNNGFTPLHFAAASTHG----ALCLELLVNNGADVNIQSKD-GKSPL 310
Cdd:PHA02878 100 YTL--VAIKDAFNNRNVEIFKIIL-----TNRYKNIQTIDLVYIDKKSKDdiieAEITKLLLSYGADINMKDRHkGNTAL 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 311 HMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAAlnahsdccrk 390
Cdd:PHA02878 173 HYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV---------- 242
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530371153 391 llSSGQKYSIVSLfsnehVLSAGFEIDTPDKF-GRTCLHAAAAGGNVecIKLLQSSGADFHKKDKCGRTPLHYA 463
Cdd:PHA02878 243 --GYCKDYDILKL-----LLEHGVDVNAKSYIlGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
PHA02878 PHA02878
ankyrin repeat protein; Provisional
459-696 6.04e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.06  E-value: 6.04e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 459 PLHYAAANCHFHCIETLVTTGANVNETDDWGRTALH--------------------------YAAASDMDRN------KT 506
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHiickepnklgmkemirsinkcsvfytLVAIKDAFNNrnveifKI 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 507 ILGNAHDNSEELErARELKEKEATLCLE-----FLLQNDANPSIRDKEGYNS-IHYAAAYGHRQCLELLLERtnsGFE-E 579
Cdd:PHA02878 120 ILTNRYKNIQTID-LVYIDKKSKDDIIEaeitkLLLSYGADINMKDRHKGNTaLHYATENKDQRLTELLLSY---GANvN 195
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 580 SDSGATKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLA-AFKGHTECVEALINQGASIFVKDNVTKRTPLHA 658
Cdd:PHA02878 196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILGLTALHS 275
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 530371153 659 SVINGHTlcLRLLLEIADNPEAVdvkDAKGQTPLMLAV 696
Cdd:PHA02878 276 SIKSERK--LKLLLEYGADINSL---NSYKLTPLSSAV 308
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
107-359 6.60e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 66.19  E-value: 6.60e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 107 WQTPLHVAAANKAVKCaevIIPLL--SSVNVSDRG--GRTALHHAALNGHVEMVNLLLakganinafdkkdrralhwaay 182
Cdd:cd22192   17 SESPLLLAAKENDVQA---IKKLLkcPSCDLFQRGalGETALHVAALYDNLEAAVVLM---------------------- 71
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 183 mghlDVVALLINHgaEVTCkdkkgytplhaaasngqinvvkhllnlgveideiNVY-GNTALHIACYNGQDAVVNELIDY 261
Cdd:cd22192   72 ----EAAPELVNE--PMTS----------------------------------DLYqGETALHIAVVNQNLNLVRELIAR 111
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 262 GANVNQPNNNG--FT------------PLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI- 326
Cdd:cd22192  112 GADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEI-VRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYd 190
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 530371153 327 --------QNGGEIDCV-DKDGNTPLHVAARYGHELLINTLI 359
Cdd:cd22192  191 lilsydkeDDLQPLDLVpNNQGLTPFKLAAKEGNIVMFQHLV 232
PHA02859 PHA02859
ankyrin repeat protein; Provisional
150-275 7.62e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 62.91  E-value: 7.62e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 150 NGHVEMVNLLLAKGANINAFDKKDRRAL--HWAAYMGHL--DVVALLINHGAEVTCKDKKGYTPLHAAASNG--QINVVK 223
Cdd:PHA02859  63 KVNVEILKFLIENGADVNFKTRDNNLSAlhHYLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHMYMCNFnvRINVIK 142
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530371153 224 HLLNLGVEIDEINVYGNTALH-IACYNGQDAVVNELIDYGANVNQPNNNGFTP 275
Cdd:PHA02859 143 LLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
PHA03100 PHA03100
ankyrin repeat protein; Provisional
634-813 9.63e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.07  E-value: 9.63e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 634 VEALINQGASIFVKDNvTKRTPLHASVINGHTLclRLLLEIAD----NPEAVDVKDAKGQTPLMLAVAY--GHIDAVSLL 707
Cdd:PHA03100  51 VKILLDNGADINSSTK-NNSTPLHYLSNIKYNL--TDVKEIVKllleYGANVNAPDNNGITPLLYAISKksNSYSIVEYL 127
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 708 LEKEANVDTVDILGCTALH------------------RGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATW 769
Cdd:PHA03100 128 LDNGANVNIKNSDGENLLHlylesnkidlkilkllidKGVDINAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEF 207
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 530371153 770 LSELLQMALSEEDCcfkDNQGYTPLHWACYNGNENCIEVLLEQK 813
Cdd:PHA03100 208 VKYLLDLGANPNLV---NKYGDTPLHIAILNNNKEIFKLLLNNG 248
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
147-276 1.14e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 65.66  E-value: 1.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 147 AALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPL---------------- 210
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrily 611
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 211 --------HA-------AASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPN-NNGFT 274
Cdd:PLN03192 612 hfasisdpHAagdllctAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDDDFS 691

                 ..
gi 530371153 275 PL 276
Cdd:PLN03192 692 PT 693
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
761-930 2.29e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.89  E-value: 2.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 761 AAARGHATWLSELLQMALSEEdccFKDNQGYTPLHWACYNGNENCIEVLLEQKC---FRKFIGNpfTPLHCAIINDHGNC 837
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPD---IGDSKGRTPLHIAASKGYEDCVLVLLKHACnvhIRDANGN--TALWNAISAKHHKI 606
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 838 ASLLLGAIDSSIVSCRDDKgrtpLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILV-NSAQAD 916
Cdd:PLN03192 607 FRILYHFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLImNGADVD 682
                        170
                 ....*....|....
gi 530371153 917 LTVKDKDLnTPLHL 930
Cdd:PLN03192 683 KANTDDDF-SPTEL 695
Ank_2 pfam12796
Ankyrin repeats (3 copies);
310-400 3.73e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.43  E-value: 3.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  310 LHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGAdtAKCGIHSMFPLHLAALNAHSDCCR 389
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|.
gi 530371153  390 KLLSSGQKYSI 400
Cdd:pfam12796  79 LLLEKGADINV 89
Ank_4 pfam13637
Ankyrin repeats (many copies);
690-741 5.23e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 5.23e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530371153  690 TPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLL 741
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
791-992 7.36e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 62.38  E-value: 7.36e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 791 YTPLHWACYNGNENCIEVLLEQKCF-RKFIGNPFTPLH-----CAIINDHGNCASLLL--GAIDSSIvscrDDKGRTPLH 862
Cdd:PHA03100  36 VLPLYLAKEARNIDVVKILLDNGADiNSSTKNNSTPLHylsniKYNLTDVKEIVKLLLeyGANVNAP----DNNGITPLL 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 863 AAAFA--DHVECLQLLLRHSAPVNAVDNSGKTALMMAAENG------------------QAGAVDILVNSAqADLTVKDK 922
Cdd:PHA03100 112 YAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNkidlkilkllidkgvdinAKNRVNYLLSYG-VPINIKDV 190
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 923 DLNTPLHLACSKGHEKCALLILDKIQDESLINEKNNalqTPLHVAARNGLKVVVEELLAKGACVLAVDEN 992
Cdd:PHA03100 191 YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD---TPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02989 PHA02989
ankyrin repeat protein; Provisional
20-317 1.03e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 62.07  E-value: 1.03e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  20 DPEEIRMLIHKTEDVN-TLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMwLTPL-----HRAVAS-RSEEAVQV 92
Cdd:PHA02989  15 DKNALEFLLRTGFDVNeEYRGNSILLLYLKRKDVKIKIVKLLIDNGADVNYKGYI-ETPLcavlrNREITSnKIKKIVKL 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  93 LIKHSADVNARDKNWQTPlhvaaankavkcaevIIPLLSSVNVSDrggrtalhhaalnghVEMVNLLLAKGANINafDKK 172
Cdd:PHA02989  94 LLKFGADINLKTFNGVSP---------------IVCFIYNSNINN---------------CDMLRFLLSKGINVN--DVK 141
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 173 DRRA---LH--WAAYMGHLDVVALLINHGAEV-TCKDKKGYTP----LHAAASNGQINVVKHLLNLGVEIDEINVYGNTA 242
Cdd:PHA02989 142 NSRGynlLHmyLESFSVKKDVIKILLSFGVNLfEKTSLYGLTPmniyLRNDIDVISIKVIKYLIKKGVNIETNNNGSESV 221
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 243 L------HIACYNGQDAVVNELIDYgANVNQPNNNGFTPLhFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVH 316
Cdd:PHA02989 222 LesfldnNKILSKKEFKVLNFILKY-IKINKKDKKGFNPL-LISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKH 299

                 .
gi 530371153 317 G 317
Cdd:PHA02989 300 G 300
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
144-226 1.38e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.84  E-value: 1.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 144 LHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQINVVK 223
Cdd:PTZ00322  86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                 ...
gi 530371153 224 HLL 226
Cdd:PTZ00322 166 LLS 168
PHA02878 PHA02878
ankyrin repeat protein; Provisional
3-114 1.67e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.43  E-value: 1.67e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153   3 VLKLTDQPPLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVA-AFLGDAEIIELLILSGARVNAKDNMW-LTPLHR 80
Cdd:PHA02878 196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILgLTALHS 275
                         90       100       110
                 ....*....|....*....|....*....|....
gi 530371153  81 AVasRSEEAVQVLIKHSADVNARDKNWQTPLHVA 114
Cdd:PHA02878 276 SI--KSERKLKLLLEYGADINSLNSYKLTPLSSA 307
Ank_4 pfam13637
Ankyrin repeats (many copies);
587-638 1.92e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 1.92e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530371153  587 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALI 638
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
653-765 2.88e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 2.88e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 653 RTPLHASVINGHTLCLRLLLEIadNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTG 732
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLDL--GKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146
                         90       100       110
                 ....*....|....*....|....*....|...
gi 530371153 733 HEECVQMLLEQEVSILCKDSRGRTPLHYAAARG 765
Cdd:PHA02875 147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
585-802 3.90e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 60.41  E-value: 3.90e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 585 TKSPLHLAAYNGHHQALEVLL-QSLVDLDIRDEKGRTALDLAAFKGHTECVEALInqgasifvkDNVTkrtplhasving 663
Cdd:cd22192   17 SESPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLM---------EAAP------------ 75
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 664 htlclrlllEIADNPEAVDVkdAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGcTALHRGI-------------- 729
Cdd:cd22192   76 ---------ELVNEPMTSDL--YQGETALHIAVVNQNLNLVRELIARGADVVSPRATG-TFFRPGPknliyygehplsfa 143
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 730 -MTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALSEE----DCCF---KDNQGYTPLHWACYNG 801
Cdd:cd22192  144 aCVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYDLILSYDkeddLQPLdlvPNNQGLTPFKLAAKEG 223

                 .
gi 530371153 802 N 802
Cdd:cd22192  224 N 224
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
108-282 4.81e-09

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 60.28  E-value: 4.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 108 QTPLHVAAANKAVKCAEVIIPLLSSVNVSDRG--------------GRTALHHAALNGHVEMVNLLLAKGANINA----- 168
Cdd:cd21882   27 KTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAratgr 106
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 169 FDKKDRR--------ALHWAAYMGHLDVVALLINHGAE---VTCKDKKGYTPLHAAasngqinvvkhllnlgVEIDEiNV 237
Cdd:cd21882  107 FFRKSPGnlfyfgelPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHAL----------------VLQAD-NT 169
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530371153 238 YGNTALHIACYNGqdavvneLIDYGANVNQ-------PNNNGFTPLHFAAAS 282
Cdd:cd21882  170 PENSAFVCQMYNL-------LLSYGAHLDPtqqleeiPNHQGLTPLKLAAVE 214
PHA02946 PHA02946
ankyin-like protein; Provisional
323-571 5.04e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 59.68  E-value: 5.04e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 323 QTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHL-------------------AALNA 383
Cdd:PHA02946  56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsgtddevierinllvqygAKINN 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 384 HSD--CCRKLLSSGQKYSIVSlfsnEHVLSAGFEIDTPDKFGRTCLHAAAAGGN--VECIKLLQSSGADFHKKDKCGRTP 459
Cdd:PHA02946 136 SVDeeGCGPLLACTDPSERVF----KKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHDGNTP 211
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 460 LHYAAANCHFHC-IETLVTTGANVNETDDWGRTALHYAAASdmdrnktiLGNAHDNSEELERARELKEKEATLCLeFLLQ 538
Cdd:PHA02946 212 LHIVCSKTVKNVdIINLLLPSTDVNKQNKFGDSPLTLLIKT--------LSPAHLINKLLSTSNVITDQTVNICI-FYDR 282
                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 530371153 539 NDANPSIRDK-EGYNSIHY--AAAYGHRQCLELLLE 571
Cdd:PHA02946 283 DDVLEIINDKgKQYDSTDFkmAVEVGSIRCVKYLLD 318
PHA02874 PHA02874
ankyrin repeat protein; Provisional
792-993 8.99e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.82  E-value: 8.99e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 792 TPLHWACYNGNENCIEVLLEQKCFRKFIG-NPFTPLHCAI-INDHGNCASLLLGAIDSSI-------------------- 849
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINtKIPHPLLTAIkIGAHDIIKLLIDNGVDTSIlpipciekdmiktildcgid 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 850 VSCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLH 929
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLH 195
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530371153 930 LACSKGHEKCALLILDkiqDESLINEKNNALQTPLHVAARNGLKVVveELLAKGACVLAVDENG 993
Cdd:PHA02874 196 NAAEYGDYACIKLLID---HGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDG 254
PHA02946 PHA02946
ankyin-like protein; Provisional
53-312 1.31e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 58.53  E-value: 1.31e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  53 DAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKavkcAEVIipllss 132
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTD----DEVI------ 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 133 vnvsdrggrtalhhaalnghvEMVNLLLAKGANINafdkkdrralhwaaymghldvvallinhgaevTCKDKKGYTPLHA 212
Cdd:PHA02946 121 ---------------------ERINLLVQYGAKIN--------------------------------NSVDEEGCGPLLA 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 213 AASNGQiNVVKHLLNLGVEIDEINVYGNTAL--HIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALCLE 290
Cdd:PHA02946 148 CTDPSE-RVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKNVDII 226
                        250       260
                 ....*....|....*....|..
gi 530371153 291 LLVNNGADVNIQSKDGKSPLHM 312
Cdd:PHA02946 227 NLLLPSTDVNKQNKFGDSPLTL 248
PHA02875 PHA02875
ankyrin repeat protein; Provisional
587-757 1.49e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 1.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 587 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGAsiFVKDNVTKR--TPLHASVINGH 664
Cdd:PHA02875  37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK--FADDVFYKDgmTPLHLATILKK 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 665 TLCLRLLLEIADNPeavDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQE 744
Cdd:PHA02875 115 LDIMKLLIARGADP---DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
                        170
                 ....*....|...
gi 530371153 745 VSIlckDSRGRTP 757
Cdd:PHA02875 192 ANI---DYFGKNG 201
PHA03095 PHA03095
ankyrin-like protein; Provisional
20-164 1.67e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.11  E-value: 1.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  20 DPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGD--AEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHS 97
Cdd:PHA03095 201 RARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530371153  98 ADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRggrtALHHAALNGHV-------EMVNLLLAKGA 164
Cdd:PHA03095 281 ADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA----TLNTASVAGGDipsdatrLCVAKVVLRGA 350
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
429-644 1.91e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.34  E-value: 1.91e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 429 AAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAASDMDRNKTIL 508
Cdd:PLN03192 531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 509 gnahdnseelerarelkekeatlclefllqndanpsirdkegynsIHYAAAyghrqclelllertnsgfeeSDSGATKSP 588
Cdd:PLN03192 611 ---------------------------------------------YHFASI--------------------SDPHAAGDL 625
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 530371153 589 LHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASI 644
Cdd:PLN03192 626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PHA02874 PHA02874
ankyrin repeat protein; Provisional
11-147 2.28e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.67  E-value: 2.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  11 PLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVA-SRSeeA 89
Cdd:PHA02874 160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIhNRS--A 237
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530371153  90 VQVLIkHSADVNARDKNWQTPLHVAAankAVKCAEVIIPLL----SSVNVSDRGGRTALHHA 147
Cdd:PHA02874 238 IELLI-NNASINDQDIDGSTPLHHAI---NPPCDIDIIDILlyhkADISIKDNKGENPIDTA 295
Ank_4 pfam13637
Ankyrin repeats (many copies);
456-498 2.36e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 2.36e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 530371153  456 GRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAA 498
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAAS 43
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
556-775 2.47e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 57.72  E-value: 2.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 556 YAAAYGHRQCLELLL--ERTNSgFEESDSGATKspLHLAAYNGHHQALEVLLQS---LVDLDIRDE--KGRTALDLAAFK 628
Cdd:cd22192   23 LAAKENDVQAIKKLLkcPSCDL-FQRGALGETA--LHVAALYDNLEAAVVLMEAapeLVNEPMTSDlyQGETALHIAVVN 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 629 GHTECVEALINQGAsifvkDNVTKRTPLHASVINGHTLCLRllleiadnpeavdvkdakGQTPLMLAVAYGHIDAVSLLL 708
Cdd:cd22192  100 QNLNLVRELIARGA-----DVVSPRATGTFFRPGPKNLIYY------------------GEHPLSFAACVGNEEIVRLLI 156
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530371153 709 EKEANVDTVDILGCTALHRGIMTGHEECV-QM---LLEQEVSI------LCKDSRGRTPLHYAAARGHATWLSELLQ 775
Cdd:cd22192  157 EHGADIRAQDSLGNTVLHILVLQPNKTFAcQMydlILSYDKEDdlqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
Ank_4 pfam13637
Ankyrin repeats (many copies);
206-259 3.01e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 3.01e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530371153  206 GYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELI 259
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
274-461 3.47e-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: 3.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 274 TPLhFAAASTHGALCLE-LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGE-----IDCVDKDGNTPLHVAA 347
Cdd:cd22192   19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 348 RYGHELLINTLITSGADTAK---CGihSMFPLHLAALnahsdccrkllssgqkysivsLFSNEHVLSagfeidtpdkFgr 424
Cdd:cd22192   98 VNQNLNLVRELIARGADVVSpraTG--TFFRPGPKNL---------------------IYYGEHPLS----------F-- 142
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 530371153 425 tclhaAAAGGNVECIKLLQSSGADFHKKDKCGRTPLH 461
Cdd:cd22192  143 -----AACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
PHA02859 PHA02859
ankyrin repeat protein; Provisional
77-250 3.62e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 54.83  E-value: 3.62e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  77 PLHRAVASRSEEAVQVLIKHSADVNardKNWQTPLHVAAANKAV--KCAEVIIPLLSSVNVSDRG-GRTALHH-AALNGH 152
Cdd:PHA02859  24 PLFYYVEKDDIEGVKKWIKFVNDCN---DLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRDnNLSALHHyLSFNKN 100
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 153 V--EMVNLLLAKGANINAFDKKDRRALHwaAYMGH----LDVVALLINHGAEVTCKDKKGYTPLHA-AASNGQINVVKHL 225
Cdd:PHA02859 101 VepEILKILIDSGSSITEEDEDGKNLLH--MYMCNfnvrINVIKLLIDSGVSFLNKDFDNNNILYSyILFHSDKKIFDFL 178
                        170       180
                 ....*....|....*....|....*
gi 530371153 226 LNLGVEIDEINVYGNTALHIACYNG 250
Cdd:PHA02859 179 TSLGIDINETNKSGYNCYDLIKFRN 203
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
587-831 3.68e-08

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 57.40  E-value: 3.68e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  587 SPLHLAAYNGHHQALEVLLQSLvdlDIRDEKGRTALdLAAFKGHTECVEALIN--------QGASIFVKDNVTKR----- 653
Cdd:TIGR00870  54 SALFVAAIENENLELTELLLNL---SCRGAVGDTLL-HAISLEYVDAVEAILLhllaafrkSGPLELANDQYTSEftpgi 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  654 TPLHASVINGHTLCLRLLLEIADNPEA----VDVKDAKGQT-------PLMLAVAYGHIDAVSLLLEKEANVDTVDILGC 722
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPAracgDFFVKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  723 TALHRGIMtgheECVQMLLEQEVSILCKDSrgrtplhyaaarghATWLSELLQMALSEEDCCfkDNQGYTPLHWACYNGN 802
Cdd:TIGR00870 210 TLLHLLVM----ENEFKAEYEELSCQMYNF--------------ALSLLDKLRDSKELEVIL--NHQGLTPLKLAAKEGR 269
                         250       260       270
                  ....*....|....*....|....*....|
gi 530371153  803 ENCIEVLLEQKCF-RKFIGNPFTPLHCAII 831
Cdd:TIGR00870 270 IVLFRLKLAIKYKqKKFVAWPNGQQLLSLY 299
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
340-494 4.02e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 57.33  E-value: 4.02e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 340 NTPLHVAARYGHELLINTLITS-GADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSgqkysiVSLFSNEHVLSAGFEidt 418
Cdd:cd22192   18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEA------APELVNEPMTSDLYQ--- 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 419 pdkfGRTCLHAAAAGGNVECIKLLQSSGAD----------FHKKDKC----GRTPLHYAAANCHFHCIETLVTTGANVNE 484
Cdd:cd22192   89 ----GETALHIAVVNQNLNLVRELIARGADvvspratgtfFRPGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRA 164
                        170
                 ....*....|
gi 530371153 485 TDDWGRTALH 494
Cdd:cd22192  165 QDSLGNTVLH 174
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
45-326 4.04e-08

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 57.23  E-value: 4.04e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  45 LHvaAFLG----DAEIIELLILSGARVNAKDNMWLTPLHRAV--ASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANK 118
Cdd:PHA02716 181 LH--AYLGnmyvDIDILEWLCNNGVNVNLQNNHLITPLHTYLitGNVCASVIKKIIELGGDMDMKCVNGMSPIMTYIINI 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 119 AVKCAEVI----------------------IPLLSSVNVS---------------DRGGRTALHHAAL--NGHVEMVNLL 159
Cdd:PHA02716 259 DNINPEITniyiesldgnkvknipmilhsyITLARNIDISvvysflqpgvklhykDSAGRTCLHQYILrhNISTDIIKLL 338
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 160 LAKGANINAFDKKDRRALHwaAYMG----------------HLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQ----- 218
Cdd:PHA02716 339 HEYGNDLNEPDNIGNTVLH--TYLSmlsvvnildpetdndiRLDVIQCLISLGADITAVNCLGYTPLTSYICTAQnymyy 416
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 219 -----------INVVKH--LLNLGVEIDE--------INVYG-NTALHIACYNGQDAVVNELIDYGANVNQPNNN----- 271
Cdd:PHA02716 417 diidclisdkvLNMVKHriLQDLLIRVDDtpciihhiIAKYNiPTDLYTDEYEPYDSTKIHDVYHCAIIERYNNAvcets 496
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530371153 272 GFTPLHFAAASTHGAL----CLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI 326
Cdd:PHA02716 497 GMTPLHVSIISHTNANivmdSFVYLLSIQYNINIPTKNGVTPLMLTMRNNRLSGHQWYI 555
Ank_4 pfam13637
Ankyrin repeats (many copies);
109-160 4.08e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 4.08e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530371153  109 TPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLL 160
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
857-910 4.82e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 4.82e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530371153  857 GRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILV 910
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
74-127 4.91e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 4.91e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530371153   74 WLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 127
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
689-910 5.05e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.54  E-value: 5.05e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 689 QTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHAT 768
Cdd:PHA02875   3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 769 WLSELLQMALSEEDCCFKDnqGYTPLHWACYNGNENCIEVLLEQKCFRKFIG-NPFTPLHCAIINDHGNCASLLLGaiDS 847
Cdd:PHA02875  83 AVEELLDLGKFADDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNtDKFSPLHLAVMMGDIKGIELLID--HK 158
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530371153 848 SIVSCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALM-MAAENGQAGAVDILV 910
Cdd:PHA02875 159 ACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFI 222
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
12-97 6.59e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 6.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  12 LVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQ 91
Cdd:PTZ00322  86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                 ....*.
gi 530371153  92 VLIKHS 97
Cdd:PTZ00322 166 LLSRHS 171
PHA02859 PHA02859
ankyrin repeat protein; Provisional
209-368 6.71e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 54.05  E-value: 6.71e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 209 PLHAAASNGQINVVKHLLNLgveIDEINVYGNTALHiACYNGQDAVVNE---LIDYGANVN-QPNNNGFTPLHFAAASTH 284
Cdd:PHA02859  24 PLFYYVEKDDIEGVKKWIKF---VNDCNDLYETPIF-SCLEKDKVNVEIlkfLIENGADVNfKTRDNNLSALHHYLSFNK 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 285 GAL--CLELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLI-NTLI 359
Cdd:PHA02859 100 NVEpeILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKKIfDFLT 179

                 ....*....
gi 530371153 360 TSGADTAKC 368
Cdd:PHA02859 180 SLGIDINET 188
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
898-993 8.59e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 8.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 898 AENGQAGAVDILVNSAqADLTVKDKDLNTPLHLACSKGHEKCALLILDKIQDESLINEKNNalqTPLHVAARNGLKVVVE 977
Cdd:PTZ00322  90 AASGDAVGARILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK---TPLELAEENGFREVVQ 165
                         90
                 ....*....|....*.
gi 530371153 978 ELLAKGACVLAVDENG 993
Cdd:PTZ00322 166 LLSRHSQCHFELGANA 181
PHA02878 PHA02878
ankyrin repeat protein; Provisional
7-114 1.34e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.27  E-value: 1.34e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153   7 TDQPPLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVAS-R 85
Cdd:PHA02878 167 KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcK 246
                         90       100       110
                 ....*....|....*....|....*....|
gi 530371153  86 SEEAVQVLIKHSADVNARDKNWQ-TPLHVA 114
Cdd:PHA02878 247 DYDILKLLLEHGVDVNAKSYILGlTALHSS 276
PHA02859 PHA02859
ankyrin repeat protein; Provisional
11-171 1.35e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 53.28  E-value: 1.35e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  11 PLVQAIFSGDPEEIRMLIHKTEDVNTLDsekRTPLH--VAAFLGDAEIIELLILSGARVNAK---DNmwLTPLHRAVA-- 83
Cdd:PHA02859  24 PLFYYVEKDDIEGVKKWIKFVNDCNDLY---ETPIFscLEKDKVNVEILKFLIENGADVNFKtrdNN--LSALHHYLSfn 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  84 -SRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAevIIPLLSSVNVS----DRGGRTALH-HAALNGHVEMVN 157
Cdd:PHA02859  99 kNVEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRIN--VIKLLIDSGVSflnkDFDNNNILYsYILFHSDKKIFD 176
                        170
                 ....*....|....
gi 530371153 158 LLLAKGANINAFDK 171
Cdd:PHA02859 177 FLTSLGIDINETNK 190
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
281-350 1.67e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 1.67e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 281 ASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYG 350
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
PHA02878 PHA02878
ankyrin repeat protein; Provisional
710-990 1.70e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.89  E-value: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 710 KEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGHATWLSELLQMALseedccfKDNQ 789
Cdd:PHA02878  26 TENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSIN-------KCSV 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 790 GYT--PLHWACYNGNENCIEVLLeqkcFRKFIGNPFTPLH--CAIINDHGNCASL--LLGAIDSSIVSCRDDKGRTPLHA 863
Cdd:PHA02878  99 FYTlvAIKDAFNNRNVEIFKIIL----TNRYKNIQTIDLVyiDKKSKDDIIEAEItkLLLSYGADINMKDRHKGNTALHY 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 864 AAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLACSKGHEKCALLI 943
Cdd:PHA02878 175 ATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHISVGYCKDYDILKL 253
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*...
gi 530371153 944 LdkIQDESLINEKNNALQ-TPLHVAARNGLKVVVeeLLAKGACVLAVD 990
Cdd:PHA02878 254 L--LEHGVDVNAKSYILGlTALHSSIKSERKLKL--LLEYGADINSLN 297
Ank_5 pfam13857
Ankyrin repeats (many copies);
192-246 2.00e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 2.00e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530371153  192 LINHG-AEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIA 246
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
723-766 2.22e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 2.22e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 530371153  723 TALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYAAARGH 766
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
Ank_4 pfam13637
Ankyrin repeats (many copies);
239-293 2.27e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 2.27e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530371153  239 GNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGAlCLELLV 293
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
69-198 3.23e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 3.23e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  69 AKDNMWLTPLHRAVasrSEEAVQVLIKHSADVNArdknwqtpLHVAAANKAVKcAEVIIPLLSSVNVSDRGGRTALHHAA 148
Cdd:PTZ00322  56 ATENKDATPDHNLT---TEEVIDPVVAHMLTVEL--------CQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIAC 123
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 530371153 149 LNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAE 198
Cdd:PTZ00322 124 ANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173
Ank_4 pfam13637
Ankyrin repeats (many copies);
42-94 4.24e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 4.24e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530371153   42 RTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLI 94
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
840-916 4.40e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 4.40e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530371153 840 LLLGAIDSSivsCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILVNSAQAD 916
Cdd:PTZ00322 101 LLTGGADPN---CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCH 174
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
325-493 8.03e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.33  E-value: 8.03e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 325 LIQNGGEIDCVDKDGNtpLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGQKYSIVSLF 404
Cdd:PLN03192 513 LGDNGGEHDDPNMASN--LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDAN 590
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 405 SNE---HVLSAG----FEI-------DTPDKFGrTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFH 470
Cdd:PLN03192 591 GNTalwNAISAKhhkiFRIlyhfasiSDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVD 669
                        170       180
                 ....*....|....*....|....*.
gi 530371153 471 CIETLVTTGANV---NETDDWGRTAL 493
Cdd:PLN03192 670 MVRLLIMNGADVdkaNTDDDFSPTEL 695
PHA02874 PHA02874
ankyrin repeat protein; Provisional
690-993 9.90e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.27  E-value: 9.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 690 TPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEV--SILckdsrgrtPLHYAAARGHA 767
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVdtSIL--------PIPCIEKDMIK 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 768 TWLSellqmalSEEDCCFKDNQGYTPLHWACYNGNENCIEVLLEQKcfrkfignpftplhcaiindhgncaslllgaids 847
Cdd:PHA02874 109 TILD-------CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYG---------------------------------- 147
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 848 SIVSCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTP 927
Cdd:PHA02874 148 ADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG-NHIMNKCKNGFTP 226
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 530371153 928 LHLACSKGHEKCALLIldkiqDESLINEKNNALQTPLHVAARNGLKV-VVEELLAKGACVLAVDENG 993
Cdd:PHA02874 227 LHNAIIHNRSAIELLI-----NNASINDQDIDGSTPLHHAINPPCDIdIIDILLYHKADISIKDNKG 288
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
835-990 1.21e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 835 GNCA---SLLLGAIDSSIvscRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILVN 911
Cdd:PLN03192 536 GNAAlleELLKAKLDPDI---GDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYH 612
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 912 SAQADLTVKDKDLntpLHLACSKGHekcaLLILDKIQDESL-INEKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVD 990
Cdd:PLN03192 613 FASISDPHAAGDL---LCTAAKRND----LTAMKELLKQGLnVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
189-261 1.42e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 1.42e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530371153 189 VALLINHGAEVTCKDKKGYTPLHAAASNGQINVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDY 261
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
407-528 2.17e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.79  E-value: 2.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 407 EHVLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPL-------HYAAANCHFHC-------- 471
Cdd:PLN03192 542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHHKIFRILYHFasisdpha 621
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 472 ----------------IETLVTTGANVNETDDWGRTALHYAAASD---------MDRNKTILGNAHDNSEELERARELKE 526
Cdd:PLN03192 622 agdllctaakrndltaMKELLKQGLNVDSEDHQGATALQVAMAEDhvdmvrlliMNGADVDKANTDDDFSPTELRELLQK 701

                 ..
gi 530371153 527 KE 528
Cdd:PLN03192 702 RE 703
PHA02878 PHA02878
ankyrin repeat protein; Provisional
587-813 2.26e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.42  E-value: 2.26e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 587 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKgrTALDLAAFKGHTECVEA-LINQGASIFVKDNVTKRTPLHASVINghT 665
Cdd:PHA02878  72 TPLHIICKEPNKLGMKEMIRSINKCSVFYTL--VAIKDAFNNRNVEIFKIiLTNRYKNIQTIDLVYIDKKSKDDIIE--A 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 666 LCLRLLLEIADNPEAVDvkDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEV 745
Cdd:PHA02878 148 EITKLLLSYGADINMKD--RHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 746 SILCKDSRGRTPLHYAAARGHATwlsELLQMALSEEDCCFKDN--QGYTPLHWACYngNENCIEVLLEQK 813
Cdd:PHA02878 226 STDARDKCGNTPLHISVGYCKDY---DILKLLLEHGVDVNAKSyiLGLTALHSSIK--SERKLKLLLEYG 290
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
289-493 2.44e-06

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 51.45  E-value: 2.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 289 LELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRS--QTLIQNGGEIDCVDKDGNTPLH---VAARYGHELLINTLITSGA 363
Cdd:PHA02716 195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASviKKIIELGGDMDMKCVNGMSPIMtyiINIDNINPEITNIYIESLD 274
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 364 DTAKCGIHSMFPLHLAalnahsdccrklLSSGQKYSIVslfsnEHVLSAGFEIDTPDKFGRTCLHAAAAGGNV--ECIKL 441
Cdd:PHA02716 275 GNKVKNIPMILHSYIT------------LARNIDISVV-----YSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKL 337
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530371153 442 LQSSGADFHKKDKCGRTPLH-YAAANCHFH-------------CIETLVTTGANVNETDDWGRTAL 493
Cdd:PHA02716 338 LHEYGNDLNEPDNIGNTVLHtYLSMLSVVNildpetdndirldVIQCLISLGADITAVNCLGYTPL 403
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
431-500 3.99e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 3.99e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 431 AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYAAASD 500
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
Ank_4 pfam13637
Ankyrin repeats (many copies);
754-810 4.34e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 4.34e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 530371153  754 GRTPLHYAAARGHatwlSELLQMAL-SEEDCCFKDNQGYTPLHWACYNGNENCIEVLL 810
Cdd:pfam13637   1 ELTALHAAAASGH----LELLRLLLeKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
308-359 4.70e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 4.70e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530371153  308 SPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLI 359
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
140-168 4.78e-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: 4.78e-06
                           10        20
                   ....*....|....*....|....*....
gi 530371153   140 GRTALHHAALNGHVEMVNLLLAKGANINA 168
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-61 5.03e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 5.03e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 530371153   10 PPLVQAIFSGDPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLI 61
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
20-210 5.06e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 50.05  E-value: 5.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  20 DPEEIRMLIHKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSE--EAVQVLIKHS 97
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEviERINLLVQYG 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  98 ADV-NARDKNWQTPLhVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAAL--NGHVEMVNLLLAKGANINAFDKKDR 174
Cdd:PHA02946 131 AKInNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMsdNPKASTISWMMKLGISPSKPDHDGN 209
                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 530371153 175 RALH--WAAYMGHLDVVALLINhGAEVTCKDKKGYTPL 210
Cdd:PHA02946 210 TPLHivCSKTVKNVDIINLLLP-STDVNKQNKFGDSPL 246
PHA02878 PHA02878
ankyrin repeat protein; Provisional
705-897 5.50e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.26  E-value: 5.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 705 SLLLEKEANVDTVDILG-CTALHRGIMtgHEECVQMLLEQEVSILCKD-SRGRTPLHYAAARGHaTWLSELLQMALSEED 782
Cdd:PHA02878 119 IILTNRYKNIQTIDLVYiDKKSKDDII--EAEITKLLLSYGADINMKDrHKGNTALHYATENKD-QRLTELLLSYGANVN 195
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 783 CCFKDNQgyTPLHWACYNGNENCIEVLLEQKCF---RKFIGNpfTPLHCA-----------IINDHGNCASlllgaIDSS 848
Cdd:PHA02878 196 IPDKTNN--SPLHHAVKHYNKPIVHILLENGAStdaRDKCGN--TPLHISvgyckdydilkLLLEHGVDVN-----AKSY 266
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 530371153 849 IvscrddKGRTPLHAAAFADHVecLQLLLRHSAPVNAVDNSGKTALMMA 897
Cdd:PHA02878 267 I------LGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
Ank_5 pfam13857
Ankyrin repeats (many copies);
158-213 6.50e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 6.50e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530371153  158 LLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 213
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
738-944 6.92e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.08  E-value: 6.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  738 QMLLE-QEVSILCKDSRGRTPLHYAAARGHATWLSELLQmalseedccFKDNQGY---TPLHWACYNGNENCIEVLLEQK 813
Cdd:TIGR00870  35 RDLEEpKKLNINCPDRLGRSALFVAAIENENLELTELLL---------NLSCRGAvgdTLLHAISLEYVDAVEAILLHLL 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  814 CFRKFIGNPF--------------TPLHCAIINDHGNCASLLL--GAIDSSIVSCRDDK----------GRTPLHAAAFA 867
Cdd:TIGR00870 106 AAFRKSGPLElandqytseftpgiTALHLAAHRQNYEIVKLLLerGASVPARACGDFFVksqgvdsfyhGESPLNAAACL 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  868 DHVECLQLLLRHSAPVNAVDNSGKTALMMA-------AENG------QAGAVDILvnsAQADLTVK-----DKDLNTPLH 929
Cdd:TIGR00870 186 GSPSIVALLSEDPADILTADSLGNTLLHLLvmenefkAEYEelscqmYNFALSLL---DKLRDSKElevilNHQGLTPLK 262
                         250
                  ....*....|....*
gi 530371153  930 LACSKGHEKCALLIL 944
Cdd:TIGR00870 263 LAAKEGRIVLFRLKL 277
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
534-711 7.28e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.01  E-value: 7.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 534 EFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNSGFEE---SDSGATKSPLHLAAYNGHHQALEVLLQSLVD 610
Cdd:cd22192   35 KLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtSDLYQGETALHIAVVNQNLNLVRELIARGAD 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 611 LD--------IRDEK------GRTALDLAAFKGHTECVEALINQGASIFVKDNVTKrTPLHASVINGHTL--C----LRL 670
Cdd:cd22192  115 VVspratgtfFRPGPknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN-TVLHILVLQPNKTfaCqmydLIL 193
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 530371153 671 LLEIADNPEAVD-VKDAKGQTPLMLAVAYGHIDAVSLLLEKE 711
Cdd:cd22192  194 SYDKEDDLQPLDlVPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
PHA03100 PHA03100
ankyrin repeat protein; Provisional
799-993 9.19e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 9.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 799 YNGNENCIEVLLEQKCFRKFIGN------PFTPLHCAIindHGNCASLLLGAIDSSI-VSCRDDKGRTPLHAAAFADHV- 870
Cdd:PHA03100   6 VLTKSRIIKVKNIKYIIMEDDLNdysykkPVLPLYLAK---EARNIDVVKILLDNGAdINSSTKNNSTPLHYLSNIKYNl 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 871 ----ECLQLLLRHSAPVNAVDNSGKTALMMAAEN--GQAGAVDILVNSAqADLTVKDKDLNTPLHLACSKGHEK---CAL 941
Cdd:PHA03100  83 tdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDlkiLKL 161
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530371153 942 LILDK------------IQDESLINEKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVDENG 993
Cdd:PHA03100 162 LIDKGvdinaknrvnylLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYG 225
Ank_4 pfam13637
Ankyrin repeats (many copies);
375-442 9.61e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 9.61e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 530371153  375 PLHLAALNAHSDCCRKLLSSGqkysivslfsnehvlsagFEIDTPDKFGRTCLHAAAAGGNVECIKLL 442
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKG------------------ADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
140-171 1.09e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.05  E-value: 1.09e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 530371153  140 GRTALHHAAL-NGHVEMVNLLLAKGANINAFDK 171
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
618-672 1.09e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 1.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 530371153  618 GRTALDLAAFKGHTECVEALINQGASIFVKDNvTKRTPLHASVINGHTLCLRLLL 672
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
140-282 1.14e-05

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 49.42  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 140 GRTALHHAALN---GHVEMVNLLL---AKGANINAF------DK--KDRRALHWAAYMGHLDVVALLINHGAEVTC---- 201
Cdd:cd22196   47 GKTCLLKAMLNlhnGQNDTISLLLdiaEKTGNLKEFvnaaytDSyyKGQTALHIAIERRNMHLVELLVQNGADVHArasg 126
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 202 ------KDKKGY----TPLHAAASNGQINVVKHLLN---LGVEIDEINVYGNTALH----IAcYNGQD------AVVNEL 258
Cdd:cd22196  127 effkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLHalveVA-DNTPEntkfvtKMYNEI 205
                        170       180       190
                 ....*....|....*....|....*....|.
gi 530371153 259 IDYGANVNQ-------PNNNGFTPLHFAAAS 282
Cdd:cd22196  206 LILGAKIRPllkleeiTNKKGLTPLKLAAKT 236
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
561-798 1.18e-05

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 49.11  E-value: 1.18e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 561 GHRQCLELLLerTNSGFEESDSGatKSPLHLAAYNGHHQALE---VLLQS---------LVDLDIRDE--KGRTALDLAA 626
Cdd:cd21882    6 GLLECLRWYL--TDSAYQRGATG--KTCLHKAALNLNDGVNEaimLLLEAapdsgnpkeLVNAPCTDEfyQGQTALHIAI 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 627 FKGHTECVEALINQGASIFVKDNVT--KRTPLHASVINGHTLCL----------RLLLEIADNPEAVDVKDAKGQTPLml 694
Cdd:cd21882   82 ENRNLNLVRLLVENGADVSARATGRffRKSPGNLFYFGELPLSLaactnqeeivRLLLENGAQPAALEAQDSLGNTVL-- 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 695 avaygHIdavslLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEqEVSilckDSRGRTPLHYAAARGHATWLSELL 774
Cdd:cd21882  160 -----HA-----LVLQADNTPENSAFVCQMYNLLLSYGAHLDPTQQLE-EIP----NHQGLTPLKLAAVEGKIVMFQHIL 224
                        250       260
                 ....*....|....*....|....
gi 530371153 775 QMALSEEdcCFKDNQGYTplHWAC 798
Cdd:cd21882  225 QREFSGP--YQPLSRKFT--EWTY 244
PHA03095 PHA03095
ankyrin-like protein; Provisional
850-994 1.32e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.87  E-value: 1.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 850 VSCRDDKGRTPLHA---AAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQ-AGAVDILVnSAQADLTVKDKDLN 925
Cdd:PHA03095  40 VNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLI-KAGADVNAKDKVGR 118
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 530371153 926 TPLHlACSKGHEkcallildkiqdeslINEKnnalqtplhvaarnglkvVVEELLAKGACVLAVDENGC 994
Cdd:PHA03095 119 TPLH-VYLSGFN---------------INPK------------------VIRLLLRKGADVNALDLYGM 153
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
213-350 1.49e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 48.99  E-value: 1.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 213 AASNGqinVVKHLLNlgVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVN--------QP--NNNGF----TPLHF 278
Cdd:cd22194  120 AEENG---ILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffNPkyKHEGFyfgeTPLAL 194
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 279 AAASTHGALcLELLVNNGADvNIQSKD--GKSPLHMTAVHGRFTRSQT-----------LIQNGGEIDCV-DKDGNTPLH 344
Cdd:cd22194  195 AACTNQPEI-VQLLMEKEST-DITSQDsrGNTVLHALVTVAEDSKTQNdfvkrmydmilLKSENKNLETIrNNEGLTPLQ 272

                 ....*.
gi 530371153 345 VAARYG 350
Cdd:cd22194  273 LAAKMG 278
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
211-314 1.65e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 1.65e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 211 HAAASNGQINVvKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFAAASTHGALcLE 290
Cdd:PTZ00322  88 QLAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV-VQ 165
                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 530371153 291 LLV-------NNGADVNIQSKDGK------SPLHMTA 314
Cdd:PTZ00322 166 LLSrhsqchfELGANAKPDSFTGKppsledSPISSHH 202
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
792-982 1.82e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.47  E-value: 1.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 792 TPLHWACYNGNENCIEVLLEQK----CFRKFIGNpfTPLHCAIINDHGNCASLLLGAIDSSI---VSCRDDKGRTPLHAA 864
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCPscdlFQRGALGE--TALHVAALYDNLEAAVVLMEAAPELVnepMTSDLYQGETALHIA 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 865 AFADHVECLQLLLRHSAPVNA-----------VDN---SGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHL 930
Cdd:cd22192   97 VVNQNLNLVRELIARGADVVSpratgtffrpgPKNliyYGEHPLSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVLHI 175
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530371153 931 ACSKGHEKCA------LLILDKIQDE-SLINEKNNALQTPLHVAARNGLKVVVEELLAK 982
Cdd:cd22192  176 LVLQPNKTFAcqmydlILSYDKEDDLqPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
550-605 2.35e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 2.35e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530371153  550 GYNSIHYAAAYGHRQCLELLLERTNSGFEESDSGATksPLHLAAYNGHHQALEVLL 605
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGET--ALHFAASNGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
140-168 2.61e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.86  E-value: 2.61e-05
                          10        20
                  ....*....|....*....|....*....
gi 530371153  140 GRTALHHAALNGHVEMVNLLLAKGANINA 168
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
132-180 3.13e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.13e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 530371153  132 SVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWA 180
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
93-147 3.16e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.16e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530371153   93 LIKH-SADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHA 147
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
258-312 3.22e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.22e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530371153  258 LIDYG-ANVNQPNNNGFTPLHFAAasTHGAL-CLELLVNNGADVNIQSKDGKSPLHM 312
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAA--KYGALeIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank_5 pfam13857
Ankyrin repeats (many copies);
29-81 3.29e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.29e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530371153   29 HKTEDVNTLDSEKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRA 81
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
236-279 3.55e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.55e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 530371153  236 NVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTPLHFA 279
Cdd:pfam13857  13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
46-117 3.70e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 3.70e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530371153  46 HVAAFlGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAAN 117
Cdd:PTZ00322  88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
Ank_4 pfam13637
Ankyrin repeats (many copies);
653-708 4.00e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 4.00e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530371153  653 RTPLHASVINGHTLCLRLLLEiadNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLL 708
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLE---KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
875-931 4.20e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 4.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 530371153  875 LLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLA 931
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
PHA02791 PHA02791
ankyrin-like protein; Provisional
768-963 4.56e-05

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 46.57  E-value: 4.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 768 TWLSELLQMALSEEDCCFKDNQGYTPLHWACYNGNENCIEVLLEQKCFRKFIGNPFtPLH-CAIINDHGNCASLLLGAID 846
Cdd:PHA02791   8 TWKSKQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF-PLHqAATLEDTKIVKILLFSGMD 86
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 847 SSIVscrDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSG-KTALMMAAENGQAGAVDILVNSAQA--DLTVkdkd 923
Cdd:PHA02791  87 DSQF---DDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPStfDLAI---- 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 530371153 924 LNTPLHLACSKGHEKCALLILDKIQDeslINEKNNALQTP 963
Cdd:PHA02791 160 LLSCIHITIKNGHVDMMILLLDYMTS---TNTNNSLLFIP 196
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
856-888 4.85e-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: 4.85e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 530371153  856 KGRTPLHAAA-FADHVECLQLLLRHSAPVNAVDN 888
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
238-266 4.89e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.03  E-value: 4.89e-05
                           10        20
                   ....*....|....*....|....*....
gi 530371153   238 YGNTALHIACYNGQDAVVNELIDYGANVN 266
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
441-496 5.11e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 5.11e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530371153  441 LLQSSGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYA 496
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
824-877 6.73e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 6.73e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530371153  824 TPLHCAIINDHGNCASLLLGAidSSIVSCRDDKGRTPLHAAAFADHVECLQLLL 877
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEK--GADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
790-842 7.00e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 7.00e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530371153  790 GYTPLHWACYNGNENCIEVLLEQK-CFRKFIGNPFTPLHCAIINDHGNCASLLL 842
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGaDINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
662-741 7.91e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 7.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 662 NGHTLCLRLLLEIADNPeavDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLL 741
Cdd:PTZ00322  92 SGDAVGARILLTGGADP---NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
624-708 7.98e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 7.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 624 LAAfKGHTECVEALINQGASIFVKDnVTKRTPLHASVINGHTLCLRLLLEIADNPEAVDvKDakGQTPLMLAVAYGHIDA 703
Cdd:PTZ00322  89 LAA-SGDAVGARILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLD-KD--GKTPLELAEENGFREV 163

                 ....*
gi 530371153 704 VSLLL 708
Cdd:PTZ00322 164 VQLLS 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
310-399 8.26e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 8.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 310 LHMTAVH-------GRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALN 382
Cdd:PTZ00322  79 AHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
                         90
                 ....*....|....*..
gi 530371153 383 AHSDCCRKLLSSGQKYS 399
Cdd:PTZ00322 159 GFREVVQLLSRHSQCHF 175
PHA02884 PHA02884
ankyrin repeat protein; Provisional
236-313 9.31e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 45.74  E-value: 9.31e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 236 NVYGNTALHIACYNGQDAVVNeLIDYGANVNQPNNNG-FTPLHFAAasTHGAL-CLELLVNNGADVNIQSKDGKSPLHMT 313
Cdd:PHA02884  68 NSKTNPLIYAIDCDNDDAAKL-LIRYGADVNRYAEEAkITPLYISV--LHGCLkCLEILLSYGADINIQTNDMVTPIELA 144
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
271-304 9.46e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 9.46e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 530371153  271 NGFTPLHFAAASTHGALCLELLVNNGADVNIQSK 304
Cdd:pfam00023   1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
PHA02946 PHA02946
ankyin-like protein; Provisional
156-442 1.03e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.82  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 156 VNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLH-AAASNGQInvvkhllnlgveIDE 234
Cdd:PHA02946  55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYyLSGTDDEV------------IER 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 235 INVygntalhiacyngqdavvneLIDYGANVNQP-NNNGFTPLhfAAASTHGALCLELLVNNGADVNIQSKDGKSPLH-- 311
Cdd:PHA02946 123 INL--------------------LVQYGAKINNSvDEEGCGPL--LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHrh 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 312 MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLH-VAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALN-AHSDCCR 389
Cdd:PHA02946 181 LMSDNPKASTISWMMKLGISPSKPDHDGNTPLHiVCSKTVKNVDIINLLLPSTDVNKQNKFGDSPLTLLIKTlSPAHLIN 260
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 390 KLLSSG-----QKYSIVSLFSNEHVLsagfEI--DTPDKFGRTCLHAAAAGGNVECIKLL 442
Cdd:PHA02946 261 KLLSTSnvitdQTVNICIFYDRDDVL----EIinDKGKQYDSTDFKMAVEVGSIRCVKYL 316
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
238-270 1.04e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 1.04e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 530371153  238 YGNTALHIACY-NGQDAVVNELIDYGANVNQPNN 270
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
140-280 1.18e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 45.90  E-value: 1.18e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 140 GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRR--------ALHWAAYMGHLDVVALLINHGAE-VTCKDK 204
Cdd:cd22194  141 GQTALNIAIERRQGDIVKLLIAKGADVNAhakgvfFNPKYKHegfyfgetPLALAACTNQPEIVQLLMEKESTdITSQDS 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 205 KGYTPLHAAA-----SNGQINVVKHLLnlgveiDEI-NVYGNTALhiacyngqdavvnELIdyganvnqPNNNGFTPLHF 278
Cdd:cd22194  221 RGNTVLHALVtvaedSKTQNDFVKRMY------DMIlLKSENKNL-------------ETI--------RNNEGLTPLQL 273

                 ..
gi 530371153 279 AA 280
Cdd:cd22194  274 AA 275
Ank_4 pfam13637
Ankyrin repeats (many copies);
339-392 1.45e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 1.45e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530371153  339 GNTPLHVAARYGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLL 392
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
376-494 1.77e-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: 1.77e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 376 LHLAALNAHS---DCCRKLLSSGQKYSIVSLFSNEHVLSAGFEidtpdkfGRTCLHAAAAGGNVECIKLLQSSGADFH-- 450
Cdd:cd21882   30 LHKAALNLNDgvnEAIMLLLEAAPDSGNPKELVNAPCTDEFYQ-------GQTALHIAIENRNLNLVRLLVENGADVSar 102
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530371153 451 ------KKDKC-----GRTPLHYAAANCHFHCIETLVTTG---ANVNETDDWGRTALH 494
Cdd:cd21882  103 atgrffRKSPGnlfyfGELPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLH 160
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
862-951 1.96e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 1.96e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 862 HAAAFADHVEcLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLACSKGHEKCAL 941
Cdd:PTZ00322  88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFREVVQ 165
                         90
                 ....*....|
gi 530371153 942 LILDKIQDES 951
Cdd:PTZ00322 166 LLSRHSQCHF 175
Ank_5 pfam13857
Ankyrin repeats (many copies);
674-726 2.09e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 2.09e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530371153  674 IADNPEAVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALH 726
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
532-570 2.13e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 2.13e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 530371153  532 CLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLL 570
Cdd:pfam13637  16 LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
205-234 2.42e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 2.42e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 530371153   205 KGYTPLHAAASNGQINVVKHLLNLGVEIDE 234
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
631-900 2.84e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.44  E-value: 2.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 631 TECVEALINQGASIFVKDNvTKRTPLHA--SVINGHTLCLRLLLEIADNPEAVDVKDAKGQTPLMLAVAYGHIDA---VS 705
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDN-EYSTPLCTilSNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNleiLL 129
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 706 LLLEKEANVDTVDILGCTALHRGIMTGHE---ECVQMLLEQEVSIlckdsrgrtplhyaaaRGHATWlsellqmalseed 782
Cdd:PHA02798 130 FMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDI----------------NTHNNK------------- 180
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 783 ccfkdnQGYTPLHwaCY-NGNENCIEVLLEQ---------KCFRKFIGNPFTPLHCAIINDHGNCASLLLGAIDSSI-VS 851
Cdd:PHA02798 181 ------EKYDTLH--CYfKYNIDRIDADILKlfvdngfiiNKENKSHKKKFMEYLNSLLYDNKRFKKNILDFIFSYIdIN 252
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*....
gi 530371153 852 CRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAEN 900
Cdd:PHA02798 253 QVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFEN 301
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
214-360 2.90e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 44.90  E-value: 2.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 214 ASNGQINVVKHLLNLGVEIDEINVYGNTALH--IACYNGQDAVVNELIDYGANVNQPNNNGFTPLHfaaaSTHGALCLEL 291
Cdd:PHA02716 292 ARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLH----TYLSMLSVVN 367
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530371153 292 LVNNGADVNIqskdgksplhmtavhgRFTRSQTLIQNGGEIDCVDKDGNTPLH----VAARYGHELLINTLIT 360
Cdd:PHA02716 368 ILDPETDNDI----------------RLDVIQCLISLGADITAVNCLGYTPLTsyicTAQNYMYYDIIDCLIS 424
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
140-282 2.91e-04

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 44.79  E-value: 2.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 140 GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRA--------LHWAAYMGHLDVVALLINHG---AEVTCK 202
Cdd:cd22193   76 GQTALHIAIERRQGDIVALLVENGADVHAhakgrfFQPKYQGEgfyfgelpLSLAACTNQPDIVQYLLENEhqpADIEAQ 155
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 203 DKKGYTPLHAAasngqinvvkhllnlgVEIDEiNVYGNTALHIACYNGqdavvneLIDYGANVNQP-------NNNGFTP 275
Cdd:cd22193  156 DSRGNTVLHAL----------------VTVAD-NTKENTKFVTRMYDM-------ILIRGAKLCPTveleeirNNDGLTP 211

                 ....*..
gi 530371153 276 LHFAAAS 282
Cdd:cd22193  212 LQLAAKM 218
PHA02875 PHA02875
ankyrin repeat protein; Provisional
857-994 3.17e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.21  E-value: 3.17e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 857 GRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKDLNTPLHLACSKGH 936
Cdd:PHA02875  35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKK 114
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530371153 937 EKCALLILDKIQDESLINEKNNalqTPLHVAARNGLKVVVEELLAKGACVLAVDENGC 994
Cdd:PHA02875 115 LDIMKLLIARGADPDIPNTDKF---SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGC 169
PHA02798 PHA02798
ankyrin-like protein; Provisional
436-729 3.46e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.44  E-value: 3.46e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 436 VECIKLLQSSGADFHKKDKCGRTPL-----HYAAANCHFHCIETLVTTGANVNETDDWGRTALHyaaasdmdrnkTILGN 510
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLY-----------CLLSN 119
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 511 AHDNSEELerarelkekeatlcLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLlertnsgfeesdsgatksplh 590
Cdd:PHA02798 120 GYINNLEI--------------LLFMIENGADTTLLDKDGFTMLQVYLQSNHHIDIEII--------------------- 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 591 laaynghhqalEVLLQSLVDLD-IRDEKGRTALDlAAFKGHTECVEA-----LINQGASIFVKDNVTKRTPLH--ASVI- 661
Cdd:PHA02798 165 -----------KLLLEKGVDINtHNNKEKYDTLH-CYFKYNIDRIDAdilklFVDNGFIINKENKSHKKKFMEylNSLLy 232
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 530371153 662 ---NGHTLCLRLLLEIADnpeaVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVDILGCTALHRGI 729
Cdd:PHA02798 233 dnkRFKKNILDFIFSYID----INQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAF 299
Ank_5 pfam13857
Ankyrin repeats (many copies);
706-761 4.03e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 4.03e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530371153  706 LLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLEQEVSILCKDSRGRTPLHYA 761
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
587-625 4.07e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 4.07e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 530371153  587 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLA 625
Cdd:pfam13857  18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
423-576 4.33e-04

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 44.08  E-value: 4.33e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 423 GRTCLHAAAAGGNVECIKLLQSSGADFH----------KKDKC---GRTPLHYAAANCHFHCIETLVTTG---ANVNETD 486
Cdd:cd22197   94 GHSALHIAIEKRSLQCVKLLVENGADVHaracgrffqkKQGTCfyfGELPLSLAACTKQWDVVNYLLENPhqpASLQAQD 173
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 487 DWGRTALH--YAAASDMDRNKTILGNAHDnseelerarELKEKEATLCLEFLLQndanpSIRDKEGYNSIHYAAAYGHRQ 564
Cdd:cd22197  174 SLGNTVLHalVMIADNSPENSALVIKMYD---------GLLQAGARLCPTVQLE-----EISNHEGLTPLKLAAKEGKIE 239
                        170
                 ....*....|..
gi 530371153 565 CLELLLERTNSG 576
Cdd:cd22197  240 IFRHILQREFSG 251
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
423-572 4.52e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.98  E-value: 4.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 423 GRTCLHAAAAGGNVECIKLLQSSGAD---------FHKKDK-----CGRTPLHYAAANCHFHCIETLVTTGA-NVNETDD 487
Cdd:cd22194  141 GQTALNIAIERRQGDIVKLLIAKGADvnahakgvfFNPKYKhegfyFGETPLALAACTNQPEIVQLLMEKEStDITSQDS 220
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 488 WGRTALH--YAAASDMDRNKTILGNAHDnseELERARELKEKEAtlclefllqndanpsIRDKEGYNSIHYAAAYGHRQC 565
Cdd:cd22194  221 RGNTVLHalVTVAEDSKTQNDFVKRMYD---MILLKSENKNLET---------------IRNNEGLTPLQLAAKMGKAEI 282

                 ....*..
gi 530371153 566 LELLLER 572
Cdd:cd22194  283 LKYILSR 289
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
201-347 4.77e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.92  E-value: 4.77e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  201 CKDKKGYTPL-HAAASNGQINVVKHLLNLGVEIDEinvyGNTALHIACYNGQDAVvNELIDY-----GANVNQPNNN--- 271
Cdd:TIGR00870  47 CPDRLGRSALfVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLEYVDAV-EAILLHllaafRKSGPLELANdqy 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  272 ------GFTPLHFAAaSTHGALCLELLVNNGADVNIQSKDG---KSPLHMTAVHGRFTRS-----------QTLIQNGGE 331
Cdd:TIGR00870 122 tseftpGITALHLAA-HRQNYEIVKLLLERGASVPARACGDffvKSQGVDSFYHGESPLNaaaclgspsivALLSEDPAD 200
                         170
                  ....*....|....*.
gi 530371153  332 IDCVDKDGNTPLHVAA 347
Cdd:TIGR00870 201 ILTADSLGNTLLHLLV 216
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
856-971 4.84e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.98  E-value: 4.84e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 856 KGRTPLHAAAFADHVECLQLLLRHSAPVNA---------VDNS-----GKTALMMAAENGQAGAVDILVNSAQADLTVKD 921
Cdd:cd22194  140 EGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQD 219
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 530371153 922 KDLNTPLHLAC-----SKGHEKCALLILDKI----QDESLINEKNNALQTPLHVAARNG 971
Cdd:cd22194  220 SRGNTVLHALVtvaedSKTQNDFVKRMYDMIllksENKNLETIRNNEGLTPLQLAAKMG 278
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
55-227 5.41e-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: 5.41e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  55 EIIELLI-----------LSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKN-WQTPLHvaaankavkc 122
Cdd:cd22194  111 EIVRILLafaeengildrFINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvFFNPKY---------- 180
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 123 aeviipllssvnvSDRG---GRTALHHAALNGHVEMVNLLLAKGANINAF-DKKDRRALHwAAYM------GHLDVV--- 189
Cdd:cd22194  181 -------------KHEGfyfGETPLALAACTNQPEIVQLLMEKESTDITSqDSRGNTVLH-ALVTvaedskTQNDFVkrm 246
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 530371153 190 --ALLINHGAEV--TCKDKKGYTPLHAAASNGQINVVKHLLN 227
Cdd:cd22194  247 ydMILLKSENKNleTIRNNEGLTPLQLAAKMGKAEILKYILS 288
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
892-986 5.90e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.85  E-value: 5.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 892 TALMMAAENGQAGAVDILVNSAQADLTVKDKDLNTPLHLACSKGHEKCALLILDkiQDESLINEK-NNAL---QTPLHVA 967
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPmTSDLyqgETALHIA 96
                         90
                 ....*....|....*....
gi 530371153 968 ARNGLKVVVEELLAKGACV 986
Cdd:cd22192   97 VVNQNLNLVRELIARGADV 115
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
456-487 6.56e-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: 6.56e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 530371153  456 GRTPLHYAAANC-HFHCIETLVTTGANVNETDD 487
Cdd:pfam00023   2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
274-326 6.79e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 6.79e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 530371153  274 TPLHFAAASTHGAlCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI 326
Cdd:pfam13637   3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
189-318 7.21e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 7.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 189 VALLINHGAEVTCKDKKGYTPLHAAASNGQIN-VVKHLLNlgVEIDEINVYGntalhiacyngqDAV-VNELIDYGANVN 266
Cdd:PTZ00322  44 IARIDTHLEALEATENKDATPDHNLTTEEVIDpVVAHMLT--VELCQLAASG------------DAVgARILLTGGADPN 109
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530371153 267 QPNNNGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGR 318
Cdd:PTZ00322 110 CRDYDGRTPLHIACANGHVQV-VRVLLEFGADPTLLDKDGKTPLELAEENGF 160
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
238-266 7.36e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 7.36e-04
                          10        20
                  ....*....|....*....|....*....
gi 530371153  238 YGNTALHIACYNGQDAVVNELIDYGANVN 266
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
844-897 7.42e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 7.42e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 530371153  844 AIDSSIVSCRDDKGRTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMA 897
Cdd:pfam13857   3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
456-484 7.79e-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: 37.57  E-value: 7.79e-04
                           10        20
                   ....*....|....*....|....*....
gi 530371153   456 GRTPLHYAAANCHFHCIETLVTTGANVNE 484
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
415-463 7.80e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 7.80e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 530371153  415 EIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYA 463
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
669-801 8.08e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.21  E-value: 8.08e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 669 RLLLEIADNPEAVDV--------KDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDTVD--------------ILGCTALH 726
Cdd:cd22194  114 RILLAFAEENGILDRfinaeyteEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykhegfYFGETPLA 193
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 727 RGIMTGHEECVQMLLEQE-VSILCKDSRGRTPLHYAA-----ARGHATWLSELLQMAL----SEEDCCFKDNQGYTPLHW 796
Cdd:cd22194  194 LAACTNQPEIVQLLMEKEsTDITSQDSRGNTVLHALVtvaedSKTQNDFVKRMYDMILlkseNKNLETIRNNEGLTPLQL 273

                 ....*
gi 530371153 797 ACYNG 801
Cdd:cd22194  274 AAKMG 278
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
140-280 8.35e-04

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 43.30  E-value: 8.35e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 140 GRTALHHAALNGHVEMVNLLLAKGANINA------FDKKDRRALhwaaYMGHLdvvallinhgaevtckdkkgytPLHAA 213
Cdd:cd22197   94 GHSALHIAIEKRSLQCVKLLVENGADVHAracgrfFQKKQGTCF----YFGEL----------------------PLSLA 147
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 214 ASNGQINVVKHLLNLGVE---IDEINVYGNTALHIACYNGQDAVVN---------ELIDYGANVNQ-------PNNNGFT 274
Cdd:cd22197  148 ACTKQWDVVNYLLENPHQpasLQAQDSLGNTVLHALVMIADNSPENsalvikmydGLLQAGARLCPtvqleeiSNHEGLT 227

                 ....*.
gi 530371153 275 PLHFAA 280
Cdd:cd22197  228 PLKLAA 233
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
40-226 8.73e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 43.33  E-value: 8.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  40 EKRTPLHVAAFLGDAEIIELLILSGARVNAKDN-------------MWLTPLHRAVASRSEEAVQVLIKHSAD---VNAR 103
Cdd:cd21882   72 QGQTALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQ 151
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 104 DKNWQTPLH--VAAANKAVKCAEVIIpllssvnvsdrggrtalhhaalnghvEMVNLLLAKGANINafdkkdrralhwaa 181
Cdd:cd21882  152 DSLGNTVLHalVLQADNTPENSAFVC--------------------------QMYNLLLSYGAHLD-------------- 191
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 530371153 182 ymgHLDVVALLINHgaevtckdkKGYTPLHAAASNGQINVVKHLL 226
Cdd:cd21882  192 ---PTQQLEEIPNH---------QGLTPLKLAAVEGKIVMFQHIL 224
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
586-637 9.56e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 9.56e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 530371153 586 KSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEAL 637
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
409-466 1.01e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 1.01e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530371153 409 VLSAGFEIDTPDKFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAAN 466
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
Ank_5 pfam13857
Ankyrin repeats (many copies);
65-114 1.01e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.01e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 530371153   65 ARVNAKDNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVA 114
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
205-234 1.18e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.18e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 530371153  205 KGYTPLHAAASNGQINVVKHLLNLGVEIDE 234
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
693-785 1.23e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 693 MLAVAYGHIDA------VSLLLEKEANVDTVDILGCTALHRGIMTGHEECVQMLLE--QEVSILCKDsrGRTPLHYAAAR 764
Cdd:PTZ00322  81 MLTVELCQLAAsgdavgARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEfgADPTLLDKD--GKTPLELAEEN 158
                         90       100
                 ....*....|....*....|.
gi 530371153 765 GhatwLSELLQMALSEEDCCF 785
Cdd:PTZ00322 159 G----FREVVQLLSRHSQCHF 175
Ank_4 pfam13637
Ankyrin repeats (many copies);
925-971 1.43e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 1.43e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 530371153  925 NTPLHLACSKGHEKCALLILDKIQDeslINEKNNALQTPLHVAARNG 971
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNG 45
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
42-72 1.64e-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: 1.64e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 530371153   42 RTPLHVAA-FLGDAEIIELLILSGARVNAKDN 72
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
687-718 1.67e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 1.67e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 530371153  687 KGQTPLMLAVA-YGHIDAVSLLLEKEANVDTVD 718
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02795 PHA02795
ankyrin-like protein; Provisional
124-201 1.83e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 41.90  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 124 EVIIPLLSSVNVSDRGGRTALHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMG--------HLDVVALLINH 195
Cdd:PHA02795 205 KLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHLKILEILLRE 284

                 ....*.
gi 530371153 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 ...
789-811 1.98e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 1.98e-03
                           10        20
                   ....*....|....*....|...
gi 530371153   789 QGYTPLHWACYNGNENCIEVLLE 811
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLD 23
PHA02791 PHA02791
ankyrin-like protein; Provisional
144-275 2.00e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.18  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 144 LHHAALNGHVEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGY-TPLHAAASNGQINVV 222
Cdd:PHA02791  65 LHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIV 144
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 530371153 223 KHLLNLGVEIDEINVYgNTALHIACYNGQDAVVNELIDYGANVNQPNNNGFTP 275
Cdd:PHA02791 145 SYFLSEIPSTFDLAIL-LSCIHITIKNGHVDMMILLLDYMTSTNTNNSLLFIP 196
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
176-204 2.27e-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: 2.27e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 530371153  176 ALHWAAYM-GHLDVVALLINHGAEVTCKDK 204
Cdd:pfam00023   5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
43-121 2.43e-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: 2.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153   43 TPLHVAAFLGDAEIIELLILSGARVNAKDN--MWLT------------PLHRAVASRSEEAVQVLIKHSADVNARDKNWQ 108
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPARACgdFFVKsqgvdsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209
                          90
                  ....*....|...
gi 530371153  109 TPLHVAAANKAVK 121
Cdd:TIGR00870 210 TLLHLLVMENEFK 222
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
617-649 2.55e-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: 36.50  E-value: 2.55e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 530371153  617 KGRTALDLAAFK-GHTECVEALINQGASIFVKDN 649
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
856-885 2.61e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 2.61e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 530371153   856 KGRTPLHAAAFADHVECLQLLLRHSAPVNA 885
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
338-364 2.74e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 2.74e-03
                           10        20
                   ....*....|....*....|....*..
gi 530371153   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 2.80e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 2.80e-03
                           10        20
                   ....*....|....*....|....*....
gi 530371153   423 GRTCLHAAAAGGNVECIKLLQSSGADFHK 451
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02791 PHA02791
ankyrin-like protein; Provisional
40-237 2.80e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.80  E-value: 2.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  40 EKRTPLHVAAFLGDAEIIELLILSGARVNAKDNMWLTPLHRAVASRSEEAVQVLIKhsadvnardKNWQTPLHvaaanka 119
Cdd:PHA02791  60 ENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVK---------KNWRLMFY------- 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 120 vkcaeviipllssvnvSDRGGRTALHHAALNGHVEMVNLLLAKGAniNAFDKKDRRA-LHWAAYMGHLDVVALLINHGAE 198
Cdd:PHA02791 124 ----------------GKTGWKTSFYHAVMLNDVSIVSYFLSEIP--STFDLAILLScIHITIKNGHVDMMILLLDYMTS 185
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 530371153 199 VTCKDKKGYTP-LHAAASNGQINVVKHLLNLGVEIDEINV 237
Cdd:PHA02791 186 TNTNNSLLFIPdIKLAIDNKDLEMLQALFKYDINIYSVNL 225
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
687-716 2.91e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.08  E-value: 2.91e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 530371153  687 KGQTPLMLAVAYGHIDAVSLLLEKEANVDT 716
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
332-494 3.50e-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: 3.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  332 IDCVDKDGNTPLHVAARYG-HELLINTLITSGA-----DTAkcgihsmfpLHLAALNAHSDC--CRKLLSSGQKYSIVSL 403
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISLEYVDAVeaILLHLLAAFRKSGPLE 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  404 FSNEHVLSAGFeidtpdkFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKC--------------GRTPLHYAAANCHF 469
Cdd:TIGR00870 116 LANDQYTSEFT-------PGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSP 188
                         170       180
                  ....*....|....*....|....*
gi 530371153  470 HCIETLVTTGANVNETDDWGRTALH 494
Cdd:TIGR00870 189 SIVALLSEDPADILTADSLGNTLLH 213
PHA02989 PHA02989
ankyrin repeat protein; Provisional
214-496 3.94e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 40.88  E-value: 3.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 214 ASNGQINVVKHLLNLGVEIDEinVY-GNTAL--HIACYNGQDAVVNELIDYGANVNQpnnNGF--TPL-----HFAAAST 283
Cdd:PHA02989  11 SDTVDKNALEFLLRTGFDVNE--EYrGNSILllYLKRKDVKIKIVKLLIDNGADVNY---KGYieTPLcavlrNREITSN 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 284 HGALCLELLVNNGADVNIQSKDGKSPLhMTAVHG---------RFtrsqtLIQNGGEIDCV-DKDGNTPLHVaarYGHEL 353
Cdd:PHA02989  86 KIKKIVKLLLKFGADINLKTFNGVSPI-VCFIYNsninncdmlRF-----LLSKGINVNDVkNSRGYNLLHM---YLESF 156
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 354 LINT-----LITSGADTAKCGIHsmfpLHLAALNAHSDccrkllssgQKYSIVSLFSNEHVLSAGFEIDTPDKFGRTCLH 428
Cdd:PHA02989 157 SVKKdvikiLLSFGVNLFEKTSL----YGLTPMNIYLR---------NDIDVISIKVIKYLIKKGVNIETNNNGSESVLE 223
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 530371153 429 AAAAGGNV---ECIKLLQS--SGADFHKKDKCGRTPLHYAAANCHFHCIETLVTTGANVNETDDWGRTALHYA 496
Cdd:PHA02989 224 SFLDNNKIlskKEFKVLNFilKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296
PHA02989 PHA02989
ankyrin repeat protein; Provisional
188-356 4.33e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 40.88  E-value: 4.33e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 188 VVALLINHGAEVTCKDKKGYTPLHAAASNGQIN---VVKHLLNLGVEIDEI-NVYGNTALHI---ACYNGQDaVVNELID 260
Cdd:PHA02989  90 IVKLLLKFGADINLKTFNGVSPIVCFIYNSNINncdMLRFLLSKGINVNDVkNSRGYNLLHMyleSFSVKKD-VIKILLS 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 261 YGANVNQPNN-NGFTPLHFAAASTHGALCLEL---LVNNGAD-------------------------------------- 298
Cdd:PHA02989 169 FGVNLFEKTSlYGLTPMNIYLRNDIDVISIKVikyLIKKGVNietnnngsesvlesfldnnkilskkefkvlnfilkyik 248
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530371153 299 VNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARYGHELLIN 356
Cdd:PHA02989 249 INKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLN 306
PHA02875 PHA02875
ankyrin repeat protein; Provisional
858-994 4.58e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.74  E-value: 4.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 858 RTPLHAAAFADHVECLQLLLRHSAPVNAV-DNSGKTALMMAAENGQAGAVDILVnSAQADLTVKDKDLNTPLHLACSKGH 936
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLI-ARGADPDIPNTDKFSPLHLAVMMGD 147
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 530371153 937 EKCALLILDKiqdESLINEKNNALQTPLHVAARNGLKVVVEELLAKGACVLAVDENGC 994
Cdd:PHA02875 148 IKGIELLIDH---KACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGC 202
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
176-201 4.71e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 4.71e-03
                           10        20
                   ....*....|....*....|....*.
gi 530371153   176 ALHWAAYMGHLDVVALLINHGAEVTC 201
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
687-715 4.71e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 4.71e-03
                           10        20
                   ....*....|....*....|....*....
gi 530371153   687 KGQTPLMLAVAYGHIDAVSLLLEKEANVD 715
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
647-759 4.92e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.55  E-value: 4.92e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 647 KDNVTKRTPLHASVIN---GHTLCLRLLLEIAD---------NPEAVDVKdAKGQTPLMLAVAYGHIDAVSLLLEKEANV 714
Cdd:cd22193   24 TESSTGKTCLMKALLNlnpGTNDTIRILLDIAEktdnlkrfiNAEYTDEY-YEGQTALHIAIERRQGDIVALLVENGADV 102
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 530371153 715 D--------------TVDILGCTALHRGIMTGHEECVQMLLE---QEVSILCKDSRGRTPLH 759
Cdd:cd22193  103 HahakgrffqpkyqgEGFYFGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLH 164
Ank_5 pfam13857
Ankyrin repeats (many copies);
291-346 5.43e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 5.43e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 530371153  291 LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVA 346
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
830-994 5.65e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 5.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 830 IINDHGNCASLllgAIDSSIvscrddkgrTPLHAAAFADHVECLQLLLRHSAPVNAVDNSGKTALMMAAENGQAGAVDIL 909
Cdd:PHA02874  20 IIKNKGNCINI---SVDETT---------TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 910 VNSAQADLTVKDKDLNtplhlacskghEKCALLILDKIQDeslINEKNNALQTPLHVAARNGLKVVVEELLAKGACVLAV 989
Cdd:PHA02874  88 IDNGVDTSILPIPCIE-----------KDMIKTILDCGID---VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIE 153

                 ....*
gi 530371153 990 DENGC 994
Cdd:PHA02874 154 DDNGC 158
PHA02743 PHA02743
Viral ankyrin protein; Provisional
153-268 5.95e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 38.64  E-value: 5.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 153 VEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVV---ALLINHGAEVTCKDKK-GYTPLHAAASNGQINVVKHLL-N 227
Cdd:PHA02743  37 MEVAPFISGDGHLLHRYDHHGRQCTHMVAWYDRANAVmkiELLVNMGADINARELGtGNTLLHIAASTKNYELAEWLCrQ 116
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 530371153 228 LGVEIDEINVYGNTALHIAcYNGQDAVVNE-LIDYGANVNQP 268
Cdd:PHA02743 117 LGVNLGAINYQHETAYHIA-YKMRDRRMMEiLRANGAVCDDP 157
PHA02884 PHA02884
ankyrin repeat protein; Provisional
55-195 7.32e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.58  E-value: 7.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153  55 EIIELLILSGARVNAK----DNMWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQ-TPLHVAAANKAVKCAEVIIPL 129
Cdd:PHA02884  47 DIIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSY 126
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 530371153 130 LSSVNVSDRGGRTALHHAALNGHVEMVNLLlaKGANINAFDKKDRRalhwaaYMGHLDVVALLINH 195
Cdd:PHA02884 127 GADINIQTNDMVTPIELALMICNNFLAFMI--CDNEISNFYKHPKK------ILINFDILKILVSH 184
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
423-454 7.53e-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: 7.53e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 530371153  423 GRTCLHAAAA-GGNVECIKLLQSSGADFHKKDK 454
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
617-646 7.93e-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: 7.93e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 530371153   617 KGRTALDLAAFKGHTECVEALINQGASIFV 646
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
76-105 7.99e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 7.99e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 530371153   76 TPLHRAVASR-SEEAVQVLIKHSADVNARDK 105
Cdd:pfam00023   4 TPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
455-484 8.35e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 8.35e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 530371153  455 CGRTPLHYAAANCHFHCIETLVTTGANVNE 484
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02791 PHA02791
ankyrin-like protein; Provisional
517-716 9.40e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 39.25  E-value: 9.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 517 ELERARELKEKEATlclEFLLQNDANPSirDKEGYNSIHYAAAYGHRQCLELLLertnsgfeesDSGATKS------PLH 590
Cdd:PHA02791   2 DLSRINTWKSKQLK---SFLSSKDAFKA--DVHGHSALYYAIADNNVRLVCTLL----------NAGALKNllenefPLH 66
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 591 LAAYNGHHQALEVLLQSLVDLDIRDEKGRTALDLAAFKGHTECVEALINQGASIFVKDNVTKRTPL-HASVINGHTLCLR 669
Cdd:PHA02791  67 QAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWKTSFyHAVMLNDVSIVSY 146
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 530371153 670 LLLEIadnPEAVDVkdAKGQTPLMLAVAYGHIDAVSLLLEKEANVDT 716
Cdd:PHA02791 147 FLSEI---PSTFDL--AILLSCIHITIKNGHVDMMILLLDYMTSTNT 188
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
239-350 9.66e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 39.78  E-value: 9.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 530371153 239 GNTALHIACYNGQDAVVNELIDYGANVN--------QPNNN------GFTPLHFAAASTHGALCLELLVNNGADVNIQSK 304
Cdd:cd22193   76 GQTALHIAIERRQGDIVALLVENGADVHahakgrffQPKYQgegfyfGELPLSLAACTNQPDIVQYLLENEHQPADIEAQ 155
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 530371153 305 D--GKSPLHMTAVHGRFTRSQT---------LIQNGGEI-------DCVDKDGNTPLHVAARYG 350
Cdd:cd22193  156 DsrGNTVLHALVTVADNTKENTkfvtrmydmILIRGAKLcptveleEIRNNDGLTPLQLAAKMG 219
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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