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Conserved domains on  [gi|471434838|ref|NP_001264209|]
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ankyrin-1 isoform 3 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
UPA_2 pfam17809
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
1269-1398 4.90e-67

UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich structure.


:

Pssm-ID: 375346  Cd Length: 131  Bit Score: 221.96  E-value: 4.90e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  1269 VPYMAKFVIFAKMNDAREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMPLFAELSGNLVPVKKAAQQRSFHF 1348
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 471434838  1349 QSFRENRLAIPVKVRDSSREPGGFLSFLRKTMKYEDTQH-ILCHLNITMPP 1398
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSqPLCTLNIVLPQ 131
Death_ank1 cd08805
Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and ...
1434-1517 3.34e-51

Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and related proteins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. ANK-1, also called ankyrin-R (for restricted), is found in brain, muscle, and erythrocytes and is thought to function in linking integral membrane proteins to the underlying cytoskeleton. It plays a critical nonredundant role in erythroid development and is associated with hereditary spherocytosis (HS), a common disorder of the red cell membrane. The small alternatively-spliced variant, sANK-1, found in striated muscle and concentrated in the sarcoplasmic reticulum (SR) binds obscurin and titin, which facilitates the anchoring of the network SR to the contractile apparatus. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


:

Pssm-ID: 260067  Cd Length: 84  Bit Score: 174.78  E-value: 3.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838 1434 DRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1513
Cdd:cd08805     1 ERVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSTALLNLWVDREGENAKMEPLYPALYSIDRLTIV 80

                  ....
gi 471434838 1514 NMLE 1517
Cdd:cd08805    81 NILE 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
944-1048 2.30e-49

Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.


:

Pssm-ID: 128514  Cd Length: 104  Bit Score: 170.61  E-value: 2.30e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838    944 TGFLVSFMVDARGGSMRGSRhNGLRVVIPPRTCAAPTRITCRLVKPQKLNTPPPLAEEEGLASRIIALGPTGAQFLSPVI 1023
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79
                            90       100
                    ....*....|....*....|....*
gi 471434838   1024 VEIPHFASHGRGDRELVVLRSENGS 1048
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
Ank_2 super family cl39094
Ankyrin repeats (3 copies);
579-792 1.69e-39

Ankyrin repeats (3 copies);


The actual alignment was detected with superfamily member PHA03100:

Pssm-ID: 453966 [Multi-domain]  Cd Length: 422  Bit Score: 153.28  E-value: 1.69e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  579 YGKVRLAELLLEHDAHPNAAG-----KNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQI----- 648
Cdd:PHA03100    7 LTKSRIIKVKNIKYIIMEDDLndysyKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvk 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  649 EVARSLLQYGGSANAESVQGVTPLHLAAQE--GHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHV--PVADVLIKHG 724
Cdd:PHA03100   87 EIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  725 VTVDATTR----------------MGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLK 788
Cdd:PHA03100  167 VDINAKNRvnyllsygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246

                  ....
gi 471434838  789 NGAS 792
Cdd:PHA03100  247 NGPS 250
PHA02876 super family cl31517
ankyrin repeat protein; Provisional
123-468 8.10e-37

ankyrin repeat protein; Provisional


The actual alignment was detected with superfamily member PHA02876:

Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 149.83  E-value: 8.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  123 QDE--VVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLI-NY 199
Cdd:PHA02876  155 QDEllIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIdNR 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  200 GTKGKVRLPALHiAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLN-VAQLLLNRGASVNFTPQNGITPLHI 278
Cdd:PHA02876  235 SNINKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYL 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  279 ASRRG-NVIMVRLLLDRGAQIETRTKDELTPLHCAA---RNGHVRISeiLLDHGAPIQAKTKNGLSPIHMAAQGDHLDCV 354
Cdd:PHA02876  314 MAKNGyDTENIRTLIMLGADVNAADRLYITPLHQAStldRNKDIVIT--LLELGANVNARDYCDKTPIHYAAVRNNVVII 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  355 RLLLQYNAEIDDITLDHLTPLHVAAhCGH--HRVAKVLLDKGAKPNSRALNGFTPLHIACKKN-HIRVMELLLKTGASID 431
Cdd:PHA02876  392 NTLLDYGADIEALSQKIGTALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 471434838  432 AVTESGLTPLHVAsfMGHLPIVKNLLQRGASPNVSNV 468
Cdd:PHA02876  471 AINIQNQYPLLIA--LEYHGIVNILLHYGAELRDSRV 505
PHA02875 super family cl31516
ankyrin repeat protein; Provisional
415-625 7.57e-24

ankyrin repeat protein; Provisional


The actual alignment was detected with superfamily member PHA02875:

Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 106.23  E-value: 7.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  415 NHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKA 494
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  495 -KANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPL 573
Cdd:PHA02875   93 fADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 471434838  574 HVAAKYGKVRLAELLLEHDAHPNAAGKNG-LTPLHVAVHHNNLDIVKLLLPRG 625
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRG 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
49-140 3.35e-17

Ankyrin repeats (3 copies);


:

Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 78.24  E-value: 3.35e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838    49 FLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMvVELLHKEIILETTTkKGNTALHIAALAGQDEVVR 128
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEI-VKLLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 471434838   129 ELVNYGANVNAQ 140
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_4 pfam13637
Ankyrin repeats (many copies);
767-819 1.01e-06

Ankyrin repeats (many copies);


:

Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 1.01e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 471434838   767 GYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVL 819
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
 
Name Accession Description Interval E-value
UPA_2 pfam17809
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
1269-1398 4.90e-67

UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich structure.


Pssm-ID: 375346  Cd Length: 131  Bit Score: 221.96  E-value: 4.90e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  1269 VPYMAKFVIFAKMNDAREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMPLFAELSGNLVPVKKAAQQRSFHF 1348
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 471434838  1349 QSFRENRLAIPVKVRDSSREPGGFLSFLRKTMKYEDTQH-ILCHLNITMPP 1398
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSqPLCTLNIVLPQ 131
Death_ank1 cd08805
Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and ...
1434-1517 3.34e-51

Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and related proteins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. ANK-1, also called ankyrin-R (for restricted), is found in brain, muscle, and erythrocytes and is thought to function in linking integral membrane proteins to the underlying cytoskeleton. It plays a critical nonredundant role in erythroid development and is associated with hereditary spherocytosis (HS), a common disorder of the red cell membrane. The small alternatively-spliced variant, sANK-1, found in striated muscle and concentrated in the sarcoplasmic reticulum (SR) binds obscurin and titin, which facilitates the anchoring of the network SR to the contractile apparatus. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260067  Cd Length: 84  Bit Score: 174.78  E-value: 3.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838 1434 DRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1513
Cdd:cd08805     1 ERVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSTALLNLWVDREGENAKMEPLYPALYSIDRLTIV 80

                  ....
gi 471434838 1514 NMLE 1517
Cdd:cd08805    81 NILE 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
944-1048 2.30e-49

Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.


Pssm-ID: 128514  Cd Length: 104  Bit Score: 170.61  E-value: 2.30e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838    944 TGFLVSFMVDARGGSMRGSRhNGLRVVIPPRTCAAPTRITCRLVKPQKLNTPPPLAEEEGLASRIIALGPTGAQFLSPVI 1023
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79
                            90       100
                    ....*....|....*....|....*
gi 471434838   1024 VEIPHFASHGRGDRELVVLRSENGS 1048
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
PHA03100 PHA03100
ankyrin repeat protein; Provisional
579-792 1.69e-39

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 153.28  E-value: 1.69e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  579 YGKVRLAELLLEHDAHPNAAG-----KNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQI----- 648
Cdd:PHA03100    7 LTKSRIIKVKNIKYIIMEDDLndysyKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvk 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  649 EVARSLLQYGGSANAESVQGVTPLHLAAQE--GHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHV--PVADVLIKHG 724
Cdd:PHA03100   87 EIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  725 VTVDATTR----------------MGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLK 788
Cdd:PHA03100  167 VDINAKNRvnyllsygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246

                  ....
gi 471434838  789 NGAS 792
Cdd:PHA03100  247 NGPS 250
PHA02876 PHA02876
ankyrin repeat protein; Provisional
123-468 8.10e-37

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 149.83  E-value: 8.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  123 QDE--VVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLI-NY 199
Cdd:PHA02876  155 QDEllIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIdNR 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  200 GTKGKVRLPALHiAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLN-VAQLLLNRGASVNFTPQNGITPLHI 278
Cdd:PHA02876  235 SNINKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYL 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  279 ASRRG-NVIMVRLLLDRGAQIETRTKDELTPLHCAA---RNGHVRISeiLLDHGAPIQAKTKNGLSPIHMAAQGDHLDCV 354
Cdd:PHA02876  314 MAKNGyDTENIRTLIMLGADVNAADRLYITPLHQAStldRNKDIVIT--LLELGANVNARDYCDKTPIHYAAVRNNVVII 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  355 RLLLQYNAEIDDITLDHLTPLHVAAhCGH--HRVAKVLLDKGAKPNSRALNGFTPLHIACKKN-HIRVMELLLKTGASID 431
Cdd:PHA02876  392 NTLLDYGADIEALSQKIGTALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 471434838  432 AVTESGLTPLHVAsfMGHLPIVKNLLQRGASPNVSNV 468
Cdd:PHA02876  471 AINIQNQYPLLIA--LEYHGIVNILLHYGAELRDSRV 505
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
948-1044 3.59e-36

ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.


Pssm-ID: 425872  Cd Length: 96  Bit Score: 132.25  E-value: 3.59e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   948 VSFMVDARGGSMRGSrHNGLRVVIPPRTCAAPTRITCRLVKPQKLNTPPPLAEEEGLASRIIALGPTGAQFLSPVIVEIP 1027
Cdd:pfam00791    1 ASGLFDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIEIYLAVLRDDTSRPPLEEGETLLSPVVECGPPGLKFLKPVILEIP 79
                           90
                   ....*....|....*..
gi 471434838  1028 HFASHGRGDRELVVLRS 1044
Cdd:pfam00791   80 HCASLRPGDWEIVLKRS 96
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
567-724 3.69e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738 [Multi-domain]  Cd Length: 235  Bit Score: 102.98  E-value: 3.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  567 KKGFTPLHVAAKYGKVRLAELLLEH-DAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQ 645
Cdd:COG0666    37 KKLNLYLELALLPAASLSELLLKLIvDRHLAARDLDGRLPLHSAASKGDDKIVKLLLASGADVNAKDADGDTPLHLAALN 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  646 NQ-----IEVARSLLQYGGS---ANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVA 717
Cdd:COG0666   117 GNppegnIEVAKLLLEAGADldvNNLRDEDGNTPLHWAALNGDADIVELLLEAGADPNSRNSYGVTALDPAAKNGRIELV 196

                  ....*..
gi 471434838  718 DVLIKHG 724
Cdd:COG0666   197 KLLLDKG 203
PHA02875 PHA02875
ankyrin repeat protein; Provisional
415-625 7.57e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 106.23  E-value: 7.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  415 NHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKA 494
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  495 -KANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPL 573
Cdd:PHA02875   93 fADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 471434838  574 HVAAKYGKVRLAELLLEHDAHPNAAGKNG-LTPLHVAVHHNNLDIVKLLLPRG 625
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRG 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
374-583 2.57e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738 [Multi-domain]  Cd Length: 235  Bit Score: 100.67  E-value: 2.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  374 PLHVAAHCGHHRVAKVLLDKGA----KPNSRALNGFTPLHIACKKNHIrVMELLLKTGASIDAVTESGLTPLHVASFMGH 449
Cdd:COG0666     7 ALLLINKCFLDLLLVALLLLLSldlsNPSDKKLNLYLELALLPAASLS-ELLLKLIVDRHLAARDLDGRLPLHSAASKGD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  450 LPIVKNLLQRGASPNVSNVKVETPLHMAARAGHT-----EVAKYLLQNKAKANAKAKDD---QTPLHCAARIGHTGMVKL 521
Cdd:COG0666    86 DKIVKLLLASGADVNAKDADGDTPLHLAALNGNPpegniEVAKLLLEAGADLDVNNLRDedgNTPLHWAALNGDADIVEL 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 471434838  522 LLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEAsqACMTKKGFTPLHVAAKYGKVR 583
Cdd:COG0666   166 LLEAGADPNSRNSYGVTALDPAAKNGRIELVKLLLDKGL--HLSLLKFNLEGVANANVSKRN 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
441-531 2.19e-22

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 92.88  E-value: 2.19e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   441 LHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQnkAKANAKAKDDQTPLHCAARIGHTGMVK 520
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 471434838   521 LLLENGASPNL 531
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
82-172 3.92e-22

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 92.11  E-value: 3.92e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838    82 LHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYgANVNAQSQkGFTPLYMAAQENHLEVVK 161
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 471434838   162 FLLENGANQNV 172
Cdd:pfam12796   79 LLLEKGADINV 89
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
314-491 5.15e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738 [Multi-domain]  Cd Length: 235  Bit Score: 96.82  E-value: 5.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  314 RNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHL-TPLHVAAHCGHHRVAKVLLD 392
Cdd:COG0666    15 FLDLLLVALLLLLSLDLSNPSDKKLNLYLELALLPAASLSELLLKLIVDRHLAARDLDGrLPLHSAASKGDDKIVKLLLA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  393 KGAKPNSRALNGFTPLHIACKKNH-----IRVMELLLKTGASIDAVT---ESGLTPLHVASFMGHLPIVKNLLQRGASPN 464
Cdd:COG0666    95 SGADVNAKDADGDTPLHLAALNGNppegnIEVAKLLLEAGADLDVNNlrdEDGNTPLHWAALNGDADIVELLLEAGADPN 174
                         170       180
                  ....*....|....*....|....*..
gi 471434838  465 VSNVKVETPLHMAARAGHTEVAKYLLQ 491
Cdd:COG0666   175 SRNSYGVTALDPAAKNGRIELVKLLLD 201
Death pfam00531
Death domain;
1437-1517 2.51e-21

Death domain;


Pssm-ID: 425735  Cd Length: 83  Bit Score: 89.69  E-value: 2.51e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  1437 EMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNsLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIVNML 1516
Cdd:pfam00531    1 RKQLDRLLDPLGKDWRELARKLGLSENEIDEIESENPD-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAAEKI 79

                   .
gi 471434838  1517 E 1517
Cdd:pfam00531   80 Q 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
672-763 3.24e-21

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 89.80  E-value: 3.24e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   672 LHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHgVTVDATTRmGYTPLHVASHYGNIKLVK 751
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 471434838   752 FLLQHQADVNAK 763
Cdd:pfam12796   79 LLLEKGADINVK 90
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
1433-1519 3.41e-21

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 89.39  E-value: 3.41e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   1433 TDRVEMRMAVIREH-LGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSE 1511
Cdd:smart00005    1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80

                    ....*...
gi 471434838   1512 IVNMLEGS 1519
Cdd:smart00005   81 AVELLRSE 88
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
538-714 2.71e-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: 87.76  E-value: 2.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  538 TPLHTAAREGHVDTALALLEKEASQACMTKK-GFTPLHVAAKYGKVRLAELLLEhdAHPNAAGK-------NGLTPLHVA 609
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGAlGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  610 VHHNNLDIVKLLLPRGG--------------SPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLH-L 674
Cdd:cd22192    97 VVNQNLNLVRELIARGAdvvspratgtffrpGPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiL 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 471434838  675 AAQEGHT---EMVALLLSKQANGNLG------NKSGLTPLHLVSQEGHV 714
Cdd:cd22192   177 VLQPNKTfacQMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNI 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
49-140 3.35e-17

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 78.24  E-value: 3.35e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838    49 FLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMvVELLHKEIILETTTkKGNTALHIAALAGQDEVVR 128
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEI-VKLLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 471434838   129 ELVNYGANVNAQ 140
Cdd:pfam12796   79 LLLEKGADINVK 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
210-379 7.32e-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: 86.22  E-value: 7.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  210 LHIAARNDDTRTAAVLLQNdPNPDVLSK--TGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQN-----GITPLHIASRR 282
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKC-PSCDLFQRgaLGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyqGETALHIAVVN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  283 GNVIMVRLLLDRGAQIET---------RTKDELT-----PLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAA-- 346
Cdd:cd22192   100 QNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVlq 179
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 471434838  347 QGDHLDC--VRLLLQYNAEIDDITLDH------LTPLHVAA 379
Cdd:cd22192   180 PNKTFACqmYDLILSYDKEDDLQPLDLvpnnqgLTPFKLAA 220
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
47-176 3.20e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738 [Multi-domain]  Cd Length: 235  Bit Score: 74.09  E-value: 3.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   47 TSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVK-----MVVELLHKEIILETTT---KKGNTALHIA 118
Cdd:COG0666    75 LPLHSAASKGDDKIVKLLLASGADVNAKDADGDTPLHLAALNGNPPegnieVAKLLLEAGADLDVNNlrdEDGNTPLHWA 154
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 471434838  119 ALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATED 176
Cdd:COG0666   155 ALNGDADIVELLLEAGADPNSRNSYGVTALDPAAKNGRIELVKLLLDKGLHLSLLKFN 212
PHA02874 PHA02874
ankyrin repeat protein; Provisional
43-186 4.81e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.91  E-value: 4.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   43 ADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAG 122
Cdd:PHA02874  122 AELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYG 201
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 471434838  123 QDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHlEVVKFLLENgANQNVATEDGFTPLAVALQ 186
Cdd:PHA02874  202 DYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAIN 263
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
406-589 2.46e-10

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 65.42  E-value: 2.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  406 TPLHIACKKNHIRVMELLLKTgASIDAVTESGL--TPLHVASFMGHLPIVKNLLQrgASPNVSNVKV-------ETPLHM 476
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKC-PSCDLFQRGALgeTALHVAALYDNLEAAVVLME--AAPELVNEPMtsdlyqgETALHI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  477 AARAGHTEVAKYLLQNKAkanakakDDQTP---------------------LHCAARIGHTGMVKLLLENGASPNLATTA 535
Cdd:cd22192    96 AVVNQNLNLVRELIARGA-------DVVSPratgtffrpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSL 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 471434838  536 GHTPLH------TAAREGHVDTALALLEKEASQACM----TKKGFTPLHVAAKYGKVRLAELLL 589
Cdd:cd22192   169 GNTVLHilvlqpNKTFACQMYDLILSYDKEDDLQPLdlvpNNQGLTPFKLAAKEGNIVMFQHLV 232
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
139-359 1.15e-09

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: 63.18  E-value: 1.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   139 AQSQKGFTPlymAAQENHLEVVKFLLENGA--NQNVATEDGFTPLAVALQQG-HENVVAHLINYGTKGKVRLPALHIAAR 215
Cdd:TIGR00870   15 SDEEKAFLP---AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTLLHAISL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   216 ND--------------DTRTAAVLLQNDPNPDVLSKtGFTPLHIAAHYENLNVAQLLLNRGASVN-------FTPQNGIT 274
Cdd:TIGR00870   92 EYvdaveaillhllaaFRKSGPLELANDQYTSEFTP-GITALHLAAHRQNYEIVKLLLERGASVParacgdfFVKSQGVD 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   275 -------PLHIASRRGNVIMVRLLLDRGAQIETRtkDEL--TPLHCA-------ARNGHVRIS--EILLDHGAPIQAKTK 336
Cdd:TIGR00870  171 sfyhgesPLNAAACLGSPSIVALLSEDPADILTA--DSLgnTLLHLLvmenefkAEYEELSCQmyNFALSLLDKLRDSKE 248
                          250       260       270
                   ....*....|....*....|....*....|
gi 471434838   337 -------NGLSPIHMAAQGDHLDCVRLLLQ 359
Cdd:TIGR00870  249 levilnhQGLTPLKLAAKEGRIVLFRLKLA 278
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
646-808 3.50e-09

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: 61.64  E-value: 3.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   646 NQIEVARSLLQYGGSANAESVQ-------GVTPLHLAAQEG-HTEMVALLLSKQANGNLGNksglTPLHLVSQEGHVPVA 717
Cdd:TIGR00870   23 PAAERGDLASVYRDLEEPKKLNincpdrlGRSALFVAAIENeNLELTELLLNLSCRGAVGD----TLLHAISLEYVDAVE 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   718 DVLI-------KHGVTVDATTRM------GYTPLHVASHYGNIKLVKFLLQHQADVNAKTK--------------LGYSP 770
Cdd:TIGR00870   99 AILLhllaafrKSGPLELANDQYtseftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESP 178
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 471434838   771 LHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAK 808
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV 216
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
403-432 9.46e-07

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: 46.43  E-value: 9.46e-07
                            10        20        30
                    ....*....|....*....|....*....|
gi 471434838    403 NGFTPLHIACKKNHIRVMELLLKTGASIDA 432
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
767-819 1.01e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 1.01e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 471434838   767 GYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVL 819
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
733-762 1.70e-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: 45.66  E-value: 1.70e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 471434838    733 MGYTPLHVASHYGNIKLVKFLLQHQADVNA 762
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
502-531 2.36e-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: 42.57  E-value: 2.36e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 471434838    502 DDQTPLHCAARIGHTGMVKLLLENGASPNL 531
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
745-848 2.15e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  745 GNIKLVKFLLQHQAD-VNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGyisVTDVLKVVT 823
Cdd:PHA02874   12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIG---AHDIIKLLI 88
                          90       100
                  ....*....|....*....|....*...
gi 471434838  824 D---ETSVVLVSDKHRmsypETVDEILD 848
Cdd:PHA02874   89 DngvDTSILPIPCIEK----DMIKTILD 112
 
Name Accession Description Interval E-value
UPA_2 pfam17809
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
1269-1398 4.90e-67

UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich structure.


Pssm-ID: 375346  Cd Length: 131  Bit Score: 221.96  E-value: 4.90e-67
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  1269 VPYMAKFVIFAKMNDAREGRLRCYCMTDDKVDKTLEQHENFVEVARSRDIEVLEGMPLFAELSGNLVPVKKAAQQRSFHF 1348
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 471434838  1349 QSFRENRLAIPVKVRDSSREPGGFLSFLRKTMKYEDTQH-ILCHLNITMPP 1398
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSqPLCTLNIVLPQ 131
Death_ank1 cd08805
Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and ...
1434-1517 3.34e-51

Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and related proteins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. ANK-1, also called ankyrin-R (for restricted), is found in brain, muscle, and erythrocytes and is thought to function in linking integral membrane proteins to the underlying cytoskeleton. It plays a critical nonredundant role in erythroid development and is associated with hereditary spherocytosis (HS), a common disorder of the red cell membrane. The small alternatively-spliced variant, sANK-1, found in striated muscle and concentrated in the sarcoplasmic reticulum (SR) binds obscurin and titin, which facilitates the anchoring of the network SR to the contractile apparatus. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260067  Cd Length: 84  Bit Score: 174.78  E-value: 3.34e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838 1434 DRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1513
Cdd:cd08805     1 ERVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSTALLNLWVDREGENAKMEPLYPALYSIDRLTIV 80

                  ....
gi 471434838 1514 NMLE 1517
Cdd:cd08805    81 NILE 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
944-1048 2.30e-49

Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.


Pssm-ID: 128514  Cd Length: 104  Bit Score: 170.61  E-value: 2.30e-49
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838    944 TGFLVSFMVDARGGSMRGSRhNGLRVVIPPRTCAAPTRITCRLVKPQKLNTPPPLAEEEGLASRIIALGPTGAQFLSPVI 1023
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFLRPVI 79
                            90       100
                    ....*....|....*....|....*
gi 471434838   1024 VEIPHFASHGRGDRELVVLRSENGS 1048
Cdd:smart00218   80 LEVPHCASLRPRDWEIVLLRSENGG 104
PHA03100 PHA03100
ankyrin repeat protein; Provisional
579-792 1.69e-39

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 153.28  E-value: 1.69e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  579 YGKVRLAELLLEHDAHPNAAG-----KNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQI----- 648
Cdd:PHA03100    7 LTKSRIIKVKNIKYIIMEDDLndysyKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvk 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  649 EVARSLLQYGGSANAESVQGVTPLHLAAQE--GHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHV--PVADVLIKHG 724
Cdd:PHA03100   87 EIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKG 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  725 VTVDATTR----------------MGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLK 788
Cdd:PHA03100  167 VDINAKNRvnyllsygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246

                  ....
gi 471434838  789 NGAS 792
Cdd:PHA03100  247 NGPS 250
PHA02876 PHA02876
ankyrin repeat protein; Provisional
123-468 8.10e-37

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 149.83  E-value: 8.10e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  123 QDE--VVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLI-NY 199
Cdd:PHA02876  155 QDEllIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIdNR 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  200 GTKGKVRLPALHiAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLN-VAQLLLNRGASVNFTPQNGITPLHI 278
Cdd:PHA02876  235 SNINKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYL 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  279 ASRRG-NVIMVRLLLDRGAQIETRTKDELTPLHCAA---RNGHVRISeiLLDHGAPIQAKTKNGLSPIHMAAQGDHLDCV 354
Cdd:PHA02876  314 MAKNGyDTENIRTLIMLGADVNAADRLYITPLHQAStldRNKDIVIT--LLELGANVNARDYCDKTPIHYAAVRNNVVII 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  355 RLLLQYNAEIDDITLDHLTPLHVAAhCGH--HRVAKVLLDKGAKPNSRALNGFTPLHIACKKN-HIRVMELLLKTGASID 431
Cdd:PHA02876  392 NTLLDYGADIEALSQKIGTALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 471434838  432 AVTESGLTPLHVAsfMGHLPIVKNLLQRGASPNVSNV 468
Cdd:PHA02876  471 AINIQNQYPLLIA--LEYHGIVNILLHYGAELRDSRV 505
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
948-1044 3.59e-36

ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.


Pssm-ID: 425872  Cd Length: 96  Bit Score: 132.25  E-value: 3.59e-36
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   948 VSFMVDARGGSMRGSrHNGLRVVIPPRTCAAPTRITCRLVKPQKLNTPPPLAEEEGLASRIIALGPTGAQFLSPVIVEIP 1027
Cdd:pfam00791    1 ASGLFDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIEIYLAVLRDDTSRPPLEEGETLLSPVVECGPPGLKFLKPVILEIP 79
                           90
                   ....*....|....*..
gi 471434838  1028 HFASHGRGDRELVVLRS 1044
Cdd:pfam00791   80 HCASLRPGDWEIVLKRS 96
PHA03100 PHA03100
ankyrin repeat protein; Provisional
225-462 5.52e-34

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 136.72  E-value: 5.52e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  225 LLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVI-----MVRLLLDRGAQIE 299
Cdd:PHA03100   21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVN 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  300 TRTKDELTPLHCAARN--GHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDH--LDCVRLLLQYNAEIDDITldhltpl 375
Cdd:PHA03100  101 APDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN------- 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  376 hvaahcghhRVaKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKN 455
Cdd:PHA03100  174 ---------RV-NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243

                  ....*..
gi 471434838  456 LLQRGAS 462
Cdd:PHA03100  244 LLNNGPS 250
PHA03100 PHA03100
ankyrin repeat protein; Provisional
273-491 3.22e-33

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 134.41  E-value: 3.22e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  273 ITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHV-----RISEILLDHGAPIQAKTKNGLSPIHMAAQ 347
Cdd:PHA03100   36 VLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIS 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  348 G--DHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHH--RVAKVLLDKGAKPNsralngftplhiacKKNHIrvmELL 423
Cdd:PHA03100  116 KksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDIN--------------AKNRV---NYL 178
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 471434838  424 LKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQ 491
Cdd:PHA03100  179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246
PHA03100 PHA03100
ankyrin repeat protein; Provisional
225-433 9.97e-33

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 133.25  E-value: 9.97e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  225 LLQNDPNPDVLSKTGFTPLHIAAHY-----ENLNVAQLLLNRGASVNFTPQNGITPLHIAS--RRGNVIMVRLLLDRGAQ 297
Cdd:PHA03100   54 LLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGAN 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  298 IETRTKDELTPLHCAARNGHV--RISEILLDHGAPIQAKTKnglspihmaaqgdhldcVRLLLQYNAEIDDITLDHLTPL 375
Cdd:PHA03100  134 VNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPL 196
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 471434838  376 HVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAV 433
Cdd:PHA03100  197 HYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254
PHA03095 PHA03095
ankyrin-like protein; Provisional
149-447 1.39e-32

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 133.61  E-value: 1.39e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  149 YMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVvahlinygtKGKVRLpalhiaarnddtrtaavLLQN 228
Cdd:PHA03095   19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKV---------KDIVRL-----------------LLEA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  229 DPNPDVLSKTGFTPLHIAAHYEN-LNVAQLLLNRGASVNFTPQNGITPLHI--ASRRGNVIMVRLLLDRGAQIETRTKDE 305
Cdd:PHA03095   73 GADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYG 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  306 LTPLHCAARNGHVRIS--EILLDHGAPIQAKTKNGLSPIHMAAQG--DHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHC 381
Cdd:PHA03095  153 MTPLAVLLKSRNANVEllRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATG 232
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 471434838  382 GHHRVAKV--LLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLhvaSFM 447
Cdd:PHA03095  233 SSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL---SLM 297
PHA03095 PHA03095
ankyrin-like protein; Provisional
252-558 1.28e-31

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 130.92  E-value: 1.28e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  252 LNVAQLLLNRGASVNFTPQNGITPLHIASRRGN---VIMVRLLLDRGAQIETRTKDELTPLHCAARNGHV-RISEILLDH 327
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  328 GAPIQAKTKNGLSPIHMAAQGD--HLDCVRLLLQYNAEIDDITLDHLTPLHVaaHCGHHRVA----KVLLDKGAKPNSRA 401
Cdd:PHA03095  107 GADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAV--LLKSRNANvellRLLIDAGADVYAVD 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  402 LNGFTPLHIACKKNHIR--VMELLLKTGASIDAVTESGLTPLHVASFMGHL--PIVKNLLQRGASPNVSNVKVETPLHMA 477
Cdd:PHA03095  185 DRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSSCkrSLVLPLLIAGISINARNRYGQTPLHYA 264
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  478 ARAGHTEVAKYLLQNkakanakakddqtplhcaarightgmvklllenGASPNLATTAGHTPLHTAAREGHVDTALALLE 557
Cdd:PHA03095  265 AVFNNPRACRRLIAL---------------------------------GADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311

                  .
gi 471434838  558 K 558
Cdd:PHA03095  312 K 312
PHA02875 PHA02875
ankyrin repeat protein; Provisional
246-465 2.02e-31

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 128.96  E-value: 2.02e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  246 AAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILL 325
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  326 DHGAPIQ-AKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNG 404
Cdd:PHA02875   89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 471434838  405 FTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLP-IVKNLLQRGASPNV 465
Cdd:PHA02875  169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIdIVRLFIKRGADCNI 230
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
1434-1517 2.35e-31

Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. Ankyrins function as adaptor proteins and they interact, through ANK repeats, with structurally diverse membrane proteins, including ion channels/pumps, calcium release channels, and cell adhesion molecules. They play critical roles in the proper expression and membrane localization of these proteins. In mammals, this family includes ankyrin-R for restricted (or ANK1), ankyrin-B for broadly expressed (or ANK2) and ankyrin-G for general or giant (or ANK3). They are expressed in different combinations in many tissues and play non-overlapping functions. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260029  Cd Length: 84  Bit Score: 118.14  E-value: 2.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838 1434 DRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1513
Cdd:cd08317     1 HRADLRLSDIANLLGSDWPELARELGVSEEDIDLIRSENPNSLAQQAMAMLRLWLEREGEKATGNALESALKKIGRDDIV 80

                  ....
gi 471434838 1514 NMLE 1517
Cdd:cd08317    81 EKCE 84
PHA02876 PHA02876
ankyrin repeat protein; Provisional
485-819 1.04e-29

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 127.49  E-value: 1.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  485 VAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASqac 564
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN--- 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  565 MTKKGFTPLHvAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLD-IVKLLLPRGGSPHSPAWNGYTPLHIAA 643
Cdd:PHA02876  237 INKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMA 315
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  644 KQN-QIEVARSLLQYGGSANAESVQGVTPLHLAAQ-EGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLI 721
Cdd:PHA02876  316 KNGyDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLL 395
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  722 KHGVTVDATTRMGYTPLHVASHYGNIKL-VKFLLQHQADVNAKTKLGYSPLHQAAQQG-HTDIVTLLLKNGASPNEVSSN 799
Cdd:PHA02876  396 DYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQ 475
                         330       340
                  ....*....|....*....|
gi 471434838  800 GTTPLAIAkrLGYISVTDVL 819
Cdd:PHA02876  476 NQYPLLIA--LEYHGIVNIL 493
PHA03095 PHA03095
ankyrin-like protein; Provisional
519-845 1.82e-29

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 124.37  E-value: 1.82e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  519 VKLLLENGASPNLATTAGHTPLHTAAREGH---VDTALALLEKEASQACMTKKGFTPLHVAAKYGKV-RLAELLLEHDAH 594
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGAD 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  595 PNAAGKNGLTPLHV--AVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVA--RSLLQYGGSANAESVQGVT 670
Cdd:PHA03095  110 VNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDAGADVYAVDDRFRS 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  671 PLHLAAQEGHT--EMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADV--LIKHGVTVDATTRMGYTPLHVASHYGN 746
Cdd:PHA03095  190 LLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNN 269
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  747 IKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNgttpLAIAKRLGYISVTD-----VLKV 821
Cdd:PHA03095  270 PRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAAT----LNTASVAGGDIPSDatrlcVAKV 345
                         330       340
                  ....*....|....*....|....
gi 471434838  822 VTDETSVVLvSDKHRMSYPETVDE 845
Cdd:PHA03095  346 VLRGAFSLL-PEPIRAYHADFIRE 368
PHA02878 PHA02878
ankyrin repeat protein; Provisional
233-512 1.92e-29

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 124.22  E-value: 1.92e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  233 DVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLdrGAQIETRTKDELTPLHCA 312
Cdd:PHA02878   31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI--RSINKCSVFYTLVAIKDA 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  313 ARNGHVRISE-ILLDHGAPIQAKTkngLSPIHMAAQGDHLDC--VRLLLQYNAEIDDITLDHL-TPLHVAAHCGHHRVAK 388
Cdd:PHA02878  109 FNNRNVEIFKiILTNRYKNIQTID---LVYIDKKSKDDIIEAeiTKLLLSYGADINMKDRHKGnTALHYATENKDQRLTE 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  389 VLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVA-SFMGHLPIVKNLLQRGASPNV-S 466
Cdd:PHA02878  186 LLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAkS 265
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 471434838  467 NVKVETPLHMAARAghTEVAKYLLQNKAKANAKAKDDQTPLHCAAR 512
Cdd:PHA02878  266 YILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA03100 PHA03100
ankyrin repeat protein; Provisional
82-300 2.46e-29

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 122.85  E-value: 2.46e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   82 LHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQD-----EVVRELVNYGANVNAQSQKGFTPLYMAAQE-- 154
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKks 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  155 NHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHE--NVVAHLINYGT----KGKVRLpalhiaarnddtrtaavLLQN 228
Cdd:PHA03100  119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVdinaKNRVNY-----------------LLSY 181
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 471434838  229 DPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIET 300
Cdd:PHA03100  182 GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
215-527 7.66e-29

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 124.79  E-value: 7.66e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  215 RNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVR----- 289
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidn 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  290 ------------------------LLLDRGAQIETRTKDELTPLHCAARNGHV-RISEILLDHGAPIQAKTKNGLSPIH- 343
Cdd:PHA02876  234 rsninkndlsllkairnedletslLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYl 313
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  344 MAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHR-VAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMEL 422
Cdd:PHA02876  314 MAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINT 393
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  423 LLKTGASIDAVTESGLTPLHVAsFMGHLPI--VKNLLQRGASPNVSNVKVETPLHMAARAG-HTEVAKYLLQNKAKANAK 499
Cdd:PHA02876  394 LLDYGADIEALSQKIGTALHFA-LCGTNPYmsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAI 472
                         330       340
                  ....*....|....*....|....*...
gi 471434838  500 AKDDQTPLHCAarIGHTGMVKLLLENGA 527
Cdd:PHA02876  473 NIQNQYPLLIA--LEYHGIVNILLHYGA 498
PHA02874 PHA02874
ankyrin repeat protein; Provisional
289-579 7.67e-29

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 121.61  E-value: 7.67e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  289 RLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLlqynaeIDDIT 368
Cdd:PHA02874   19 KIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLL------IDNGV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  369 LDHLTPLHvaahCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMG 448
Cdd:PHA02874   93 DTSILPIP----CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHN 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  449 HLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAarIGHTGMVKLLLENGAS 528
Cdd:PHA02874  169 FFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA--IIHNRSAIELLINNAS 246
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 471434838  529 PNLATTAGHTPLHTAAR-EGHVDTALALLEKEASQACMTKKGFTPLHVAAKY 579
Cdd:PHA02874  247 INDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTAFKY 298
PHA02876 PHA02876
ankyrin repeat protein; Provisional
250-593 5.04e-28

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 122.48  E-value: 5.04e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  250 ENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGA 329
Cdd:PHA02876  156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  330 PIQaktKNGLSPIHmAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGH-HRVAKVLLDKGAKPNSRALNGFTPL 408
Cdd:PHA02876  236 NIN---KNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  409 HIACKKNH-IRVMELLLKTGASIDAVTESGLTPLHVASFMG-HLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVA 486
Cdd:PHA02876  312 YLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVII 391
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  487 KYLLQNKAKANAKAKDDQTPLHCAARIGHTGM-VKLLLENGASPNLATTAGHTPLHTAAREG-HVDTALALLEKEASQAC 564
Cdd:PHA02876  392 NTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNA 471
                         330       340
                  ....*....|....*....|....*....
gi 471434838  565 MTKKGFTPLHVAAKYGKVrlAELLLEHDA 593
Cdd:PHA02876  472 INIQNQYPLLIALEYHGI--VNILLHYGA 498
PHA03095 PHA03095
ankyrin-like protein; Provisional
65-362 1.23e-27

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 118.59  E-value: 1.23e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   65 LRNGVDINTCNQNGLNGLH--LASKEGHVKMVVE-LLHKEIILETTTKKGNTALHIAALAGQDE-VVRELVNYGANVNAQ 140
Cdd:PHA03095   34 LAAGADVNFRGEYGKTPLHlyLHYSSEKVKDIVRlLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAK 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  141 SQKGFTPL--YMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENV--VAHLINYG----TKGKVRLPALHI 212
Cdd:PHA03095  114 DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGadvyAVDDRFRSLLHH 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  213 AARNDDTRTAAV--LLQNDPNPDVLSKTGFTPLHIAAHY---ENLNVAQLLLNrGASVNFTPQNGITPLHIASRRGNVIM 287
Cdd:PHA03095  194 HLQSFKPRARIVreLIRAGCDPAATDMLGNTPLHSMATGsscKRSLVLPLLIA-GISINARNRYGQTPLHYAAVFNNPRA 272
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 471434838  288 VRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQ--AKTKNGLSPihmAAQGDHLDCVRLLLQYNA 362
Cdd:PHA03095  273 CRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAEtvAATLNTASV---AGGDIPSDATRLCVAKVV 346
PHA02878 PHA02878
ankyrin repeat protein; Provisional
145-444 2.44e-27

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 118.06  E-value: 2.44e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  145 FTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRlpalhiaarnddtrtaav 224
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVF------------------ 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  225 llqndpNPDVLSKTGFtplhiaaHYENLNVAQLLLNRGASVNFTpqngITPLHIASRRGNVI----MVRLLLDRGAQIET 300
Cdd:PHA02878  100 ------YTLVAIKDAF-------NNRNVEIFKIILTNRYKNIQT----IDLVYIDKKSKDDIieaeITKLLLSYGADINM 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  301 RTKDEL-TPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVA- 378
Cdd:PHA02878  163 KDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISv 242
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 471434838  379 AHCGHHRVAKVLLDKGAKPNSRA-LNGFTPLHIACKKNhiRVMELLLKTGASIDAVTESGLTPLHVA 444
Cdd:PHA02878  243 GYCKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02878 PHA02878
ankyrin repeat protein; Provisional
539-812 4.53e-27

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 117.29  E-value: 4.53e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  539 PLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKY-GKVRLAELLLEHDahpNAAGKNGLTPLHVAVHHNNLDI 617
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpNKLGMKEMIRSIN---KCSVFYTLVAIKDAFNNRNVEI 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  618 VKLLLPRGGSphspawNGYT----PLHIAAKQNQIE--VARSLLQYGGSANAESV-QGVTPLHLAAQEGHTEMVALLLSK 690
Cdd:PHA02878  117 FKIILTNRYK------NIQTidlvYIDKKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSY 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  691 QANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHY-GNIKLVKFLLQHQADVNAK-TKLGY 768
Cdd:PHA02878  191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKsYILGL 270
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 471434838  769 SPLHQAAQQghTDIVTLLLKNGASPNEVSSNGTTPLAIA--KRLGY 812
Cdd:PHA02878  271 TALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAvkQYLCI 314
PHA02875 PHA02875
ankyrin repeat protein; Provisional
609-800 7.85e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 115.47  E-value: 7.85e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  609 AVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLL 688
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  689 --SKQANgNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKL 766
Cdd:PHA02875   89 dlGKFAD-DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167
                         170       180       190
                  ....*....|....*....|....*....|....
gi 471434838  767 GYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNG 800
Cdd:PHA02875  168 GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG 201
PHA02874 PHA02874
ankyrin repeat protein; Provisional
571-820 1.91e-26

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 114.68  E-value: 1.91e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  571 TPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHS---PAWNG------------ 635
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIlpiPCIEKdmiktildcgid 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  636 --------YTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHL 707
Cdd:PHA02874  117 vnikdaelKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  708 VSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYgNIKLVKFLLqHQADVNAKTKLGYSPLHQAAQQG-HTDIVTLL 786
Cdd:PHA02874  197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLI-NNASINDQDIDGSTPLHHAINPPcDIDIIDIL 274
                         250       260       270
                  ....*....|....*....|....*....|....
gi 471434838  787 LKNGASPNEVSSNGTTPLAIAKRlgYISVTDVLK 820
Cdd:PHA02874  275 LYHKADISIKDNKGENPIDTAFK--YINKDPVIK 306
PHA02875 PHA02875
ankyrin repeat protein; Provisional
576-794 2.78e-26

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 113.55  E-value: 2.78e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  576 AAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLL 655
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  656 QYGGSANAESVQ-GVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMG 734
Cdd:PHA02875   89 DLGKFADDVFYKdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 471434838  735 YTPLHVASHYGNIKLVKFLLQHQADVNAKTKLG-YSPLHQAAQQGHTDIVTLLLKNGASPN 794
Cdd:PHA02875  169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA03100 PHA03100
ankyrin repeat protein; Provisional
280-528 3.36e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 113.61  E-value: 3.36e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  280 SRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARngHVRIS--EILLDHGAPIQAKTKNGLSPIH-----MAAQGDHLD 352
Cdd:PHA03100   10 SRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKE--ARNIDvvKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  353 CVRLLLQYNAEIDDITLDHLTPLHVAA--HCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHI--RVMELLLKTGA 428
Cdd:PHA03100   88 IVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  429 SIDAVTEsgltplhvasfmghlpiVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLH 508
Cdd:PHA03100  168 DINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLH 230
                         250       260
                  ....*....|....*....|
gi 471434838  509 CAARIGHTGMVKLLLENGAS 528
Cdd:PHA03100  231 IAILNNNKEIFKLLLNNGPS 250
Death_ank3 cd08803
Death domain of Ankyrin-3; Death Domain (DD) of the human protein ankyrin-3 (ANK-3) and ...
1434-1517 2.66e-25

Death domain of Ankyrin-3; Death Domain (DD) of the human protein ankyrin-3 (ANK-3) and related proteins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. ANK-3, also called anykyrin-G (for general or giant), is found in neurons and at least one splice variant has been shown to be essential for propagation of action potentials as a binding partner to neurofascin and voltage-gated sodium channels. It is required for maintaining axo-dendritic polarity, and may be a genetic risk factor associated with bipolar disorder. ANK-3 may also play roles in other cell types. Mutations affecting ANK-3 pathways for Na channel localization are associated with Brugada syndrome, a potentially fatal arrythmia. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 176781  Cd Length: 84  Bit Score: 100.90  E-value: 2.66e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838 1434 DRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1513
Cdd:cd08803     1 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 80

                  ....
gi 471434838 1514 NMLE 1517
Cdd:cd08803    81 TLLE 84
PHA02875 PHA02875
ankyrin repeat protein; Provisional
481-696 4.59e-25

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 110.08  E-value: 4.59e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  481 GHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEA 560
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  561 -SQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPL 639
Cdd:PHA02875   93 fADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 471434838  640 HIAAKQNQIEVARSLLQYGGSANAESVQG-VTPLHLAAQEGHTEMVALLLSKQANGNL 696
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA02874 PHA02874
ankyrin repeat protein; Provisional
121-455 6.08e-25

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 110.05  E-value: 6.08e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  121 AGQDEVVRELV-NYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINY 199
Cdd:PHA02874   11 SGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDN 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  200 GTKGKVrLPALHIaaRNDDTRTaavLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIA 279
Cdd:PHA02874   91 GVDTSI-LPIPCI--EKDMIKT---ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  280 SRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQgdHLDCVRLLLQ 359
Cdd:PHA02874  165 IKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLI 242
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  360 YNAEIDDITLDHLTPLHVAAH--CGHHrVAKVLLDKGAKPNSRALNGFTPLHIACKknHIRVMELLLKTGAsiDAVTESG 437
Cdd:PHA02874  243 NNASINDQDIDGSTPLHHAINppCDID-IIDILLYHKADISIKDNKGENPIDTAFK--YINKDPVIKDIIA--NAVLIKE 317
                         330
                  ....*....|....*...
gi 471434838  438 LTPLHVASFMGHLPIVKN 455
Cdd:PHA02874  318 ADKLKDSDFLEHIEIKDN 335
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
567-724 3.69e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738 [Multi-domain]  Cd Length: 235  Bit Score: 102.98  E-value: 3.69e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  567 KKGFTPLHVAAKYGKVRLAELLLEH-DAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQ 645
Cdd:COG0666    37 KKLNLYLELALLPAASLSELLLKLIvDRHLAARDLDGRLPLHSAASKGDDKIVKLLLASGADVNAKDADGDTPLHLAALN 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  646 NQ-----IEVARSLLQYGGS---ANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVA 717
Cdd:COG0666   117 GNppegnIEVAKLLLEAGADldvNNLRDEDGNTPLHWAALNGDADIVELLLEAGADPNSRNSYGVTALDPAAKNGRIELV 196

                  ....*..
gi 471434838  718 DVLIKHG 724
Cdd:COG0666   197 KLLLDKG 203
PHA02875 PHA02875
ankyrin repeat protein; Provisional
155-369 4.45e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 107.00  E-value: 4.45e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  155 NHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRLPA----LHIAARNDDTRTAAVLLQ-ND 229
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDieseLHDAVEEGDVKAVEELLDlGK 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  230 PNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPL 309
Cdd:PHA02875   93 FADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 471434838  310 HCAARNGHVRISEILLDHGAPIQAKTKNG-LSPIHMAAQGDHLDCVRLLLQYNAEIDDITL 369
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMFM 233
PHA02875 PHA02875
ankyrin repeat protein; Provisional
415-625 7.57e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 106.23  E-value: 7.57e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  415 NHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKA 494
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  495 -KANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPL 573
Cdd:PHA02875   93 fADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 471434838  574 HVAAKYGKVRLAELLLEHDAHPNAAGKNG-LTPLHVAVHHNNLDIVKLLLPRG 625
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRG 225
PHA02874 PHA02874
ankyrin repeat protein; Provisional
386-675 1.94e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 105.43  E-value: 1.94e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  386 VAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNV 465
Cdd:PHA02874   17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  466 SNVKvetplhmaarAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAR 545
Cdd:PHA02874   97 LPIP----------CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIK 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  546 EGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNlDIVKLLLpRG 625
Cdd:PHA02874  167 HNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI-NN 244
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 471434838  626 GSPHSPAWNGYTPLHIAAKQN-QIEVARSLLQYGGSANAESVQGVTPLHLA 675
Cdd:PHA02874  245 ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
374-583 2.57e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738 [Multi-domain]  Cd Length: 235  Bit Score: 100.67  E-value: 2.57e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  374 PLHVAAHCGHHRVAKVLLDKGA----KPNSRALNGFTPLHIACKKNHIrVMELLLKTGASIDAVTESGLTPLHVASFMGH 449
Cdd:COG0666     7 ALLLINKCFLDLLLVALLLLLSldlsNPSDKKLNLYLELALLPAASLS-ELLLKLIVDRHLAARDLDGRLPLHSAASKGD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  450 LPIVKNLLQRGASPNVSNVKVETPLHMAARAGHT-----EVAKYLLQNKAKANAKAKDD---QTPLHCAARIGHTGMVKL 521
Cdd:COG0666    86 DKIVKLLLASGADVNAKDADGDTPLHLAALNGNPpegniEVAKLLLEAGADLDVNNLRDedgNTPLHWAALNGDADIVEL 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 471434838  522 LLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEAsqACMTKKGFTPLHVAAKYGKVR 583
Cdd:COG0666   166 LLEAGADPNSRNSYGVTALDPAAKNGRIELVKLLLDKGL--HLSLLKFNLEGVANANVSKRN 225
Death_ank2 cd08804
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ...
1434-1517 3.13e-23

Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. Ankyrins are modular proteins comprising three conserved domains, an N-terminal membrane-binding domain containing ANK repeats, a spectrin-binding domain and a C-terminal DD. ANK-2, also called ankyrin-B (for broadly expressed), is required for proper function of the Na/Ca ion exchanger-1 in cardiomyocytes, and is thought to function in linking integral membrane proteins to the underlying cytoskeleton. Human ANK-2 is associated with "Ankyrin-B syndrome", an atypical arrythmia disorder with risk of sudden cardiac death. It also plays key roles in the brain and striated muscle. Loss of ANK-2 is associated with significant nervous system defects and sarcomere disorganization. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260066  Cd Length: 84  Bit Score: 95.15  E-value: 3.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838 1434 DRVEMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIV 1513
Cdd:cd08804     1 ERTEERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLTQCLTKINRMDIV 80

                  ....
gi 471434838 1514 NMLE 1517
Cdd:cd08804    81 HLME 84
PHA02878 PHA02878
ankyrin repeat protein; Provisional
405-708 6.13e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 104.58  E-value: 6.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  405 FTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSN--VKVETPLHMAaragH 482
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYtlVAIKDAFNNR----N 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  483 TEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTaghtplhtaareghvdtalallekeasq 562
Cdd:PHA02878  114 VEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDR---------------------------- 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  563 acmtKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIA 642
Cdd:PHA02878  166 ----HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 471434838  643 AKQ-NQIEVARSLLQYGGSANAES-VQGVTPLHLAAQEghTEMVALLLSKQANGNLGNKSGLTPLHLV 708
Cdd:PHA02878  242 VGYcKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
505-729 6.41e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 103.59  E-value: 6.41e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  505 TPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHV-----DTALALLEKEASQACMTKKGFTPLHVAA-- 577
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAIsk 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  578 KYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVH--HNNLDIVKLLLPRGgsphspawngytplhiaAKQNQIEVARSLL 655
Cdd:PHA03100  117 KSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKG-----------------VDINAKNRVNYLL 179
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 471434838  656 QYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDA 729
Cdd:PHA03100  180 SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
510-699 1.18e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738 [Multi-domain]  Cd Length: 235  Bit Score: 98.74  E-value: 1.18e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  510 AARIGHTGMVKLLLENGA----SPNLATTAGHTPLHTAAREGHVDTALALLEKEaSQACMTKKGFTPLHVAAKYGKVRLA 585
Cdd:COG0666    11 INKCFLDLLLVALLLLLSldlsNPSDKKLNLYLELALLPAASLSELLLKLIVDR-HLAARDLDGRLPLHSAASKGDDKIV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  586 ELLLEHDAHPNAAGKNGLTPLHVAVHHNNL-----DIVKLLLPRGGSPHSPAW---NGYTPLHIAAKQNQIEVARSLLQY 657
Cdd:COG0666    90 KLLLASGADVNAKDADGDTPLHLAALNGNPpegniEVAKLLLEAGADLDVNNLrdeDGNTPLHWAALNGDADIVELLLEA 169
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 471434838  658 GGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNK 699
Cdd:COG0666   170 GADPNSRNSYGVTALDPAAKNGRIELVKLLLDKGLHLSLLKF 211
Ank_2 pfam12796
Ankyrin repeats (3 copies);
441-531 2.19e-22

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 92.88  E-value: 2.19e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   441 LHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQnkAKANAKAKDDQTPLHCAARIGHTGMVK 520
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 471434838   521 LLLENGASPNL 531
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
82-172 3.92e-22

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 92.11  E-value: 3.92e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838    82 LHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYgANVNAQSQkGFTPLYMAAQENHLEVVK 161
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 471434838   162 FLLENGANQNV 172
Cdd:pfam12796   79 LLLEKGADINV 89
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
314-491 5.15e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738 [Multi-domain]  Cd Length: 235  Bit Score: 96.82  E-value: 5.15e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  314 RNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHL-TPLHVAAHCGHHRVAKVLLD 392
Cdd:COG0666    15 FLDLLLVALLLLLSLDLSNPSDKKLNLYLELALLPAASLSELLLKLIVDRHLAARDLDGrLPLHSAASKGDDKIVKLLLA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  393 KGAKPNSRALNGFTPLHIACKKNH-----IRVMELLLKTGASIDAVT---ESGLTPLHVASFMGHLPIVKNLLQRGASPN 464
Cdd:COG0666    95 SGADVNAKDADGDTPLHLAALNGNppegnIEVAKLLLEAGADLDVNNlrdEDGNTPLHWAALNGDADIVELLLEAGADPN 174
                         170       180
                  ....*....|....*....|....*..
gi 471434838  465 VSNVKVETPLHMAARAGHTEVAKYLLQ 491
Cdd:COG0666   175 SRNSYGVTALDPAAKNGRIELVKLLLD 201
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
215-427 6.35e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738 [Multi-domain]  Cd Length: 235  Bit Score: 96.43  E-value: 6.35e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  215 RNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRG-ASVNFTPQNGITPLHIASRRGNVIMVRLLLD 293
Cdd:COG0666    15 FLDLLLVALLLLLSLDLSNPSDKKLNLYLELALLPAASLSELLLKLIVdRHLAARDLDGRLPLHSAASKGDDKIVKLLLA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  294 RGAQIETRTKDELTPLHCAARNGHVRIseilldhgapiqaktknglspihmaaqgDHLDCVRLLLQYNAEIDDITL---D 370
Cdd:COG0666    95 SGADVNAKDADGDTPLHLAALNGNPPE----------------------------GNIEVAKLLLEAGADLDVNNLrdeD 146
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 471434838  371 HLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTG 427
Cdd:COG0666   147 GNTPLHWAALNGDADIVELLLEAGADPNSRNSYGVTALDPAAKNGRIELVKLLLDKG 203
Ank_2 pfam12796
Ankyrin repeats (3 copies);
507-597 6.96e-22

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 91.34  E-value: 6.96e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   507 LHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQacMTKKGFTPLHVAAKYGKVRLAE 586
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN--LKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 471434838   587 LLLEHDAHPNA 597
Cdd:pfam12796   79 LLLEKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
44-314 8.03e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 100.42  E-value: 8.03e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   44 DAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMV--------------VELLHKEII------ 103
Cdd:PHA02874   34 ETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIkllidngvdtsilpIPCIEKDMIktildc 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  104 ---LETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTP 180
Cdd:PHA02874  114 gidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  181 lavalqqghenvvahlinygtkgkvrlpaLHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYeNLNVAQLLLN 260
Cdd:PHA02874  194 -----------------------------LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLIN 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 471434838  261 rGASVNFTPQNGITPLHIASRRG-NVIMVRLLLDRGAQIETRTKDELTPLHCAAR 314
Cdd:PHA02874  244 -NASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
375-467 1.72e-21

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 90.57  E-value: 1.72e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   375 LHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASidAVTESGLTPLHVASFMGHLPIVK 454
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 471434838   455 NLLQRGASPNVSN 467
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
342-432 1.95e-21

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 90.18  E-value: 1.95e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   342 IHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKpnSRALNGFTPLHIACKKNHIRVME 421
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 471434838   422 LLLKTGASIDA 432
Cdd:pfam12796   79 LLLEKGADINV 89
Death pfam00531
Death domain;
1437-1517 2.51e-21

Death domain;


Pssm-ID: 425735  Cd Length: 83  Bit Score: 89.69  E-value: 2.51e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  1437 EMRMAVIREHLGLSWAELARELQFSVEDINRIRVENPNsLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIVNML 1516
Cdd:pfam00531    1 RKQLDRLLDPLGKDWRELARKLGLSENEIDEIESENPD-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAAEKI 79

                   .
gi 471434838  1517 E 1517
Cdd:pfam00531   80 Q 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
309-400 2.85e-21

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 89.80  E-value: 2.85e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   309 LHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEidDITLDHLTPLHVAAHCGHHRVAK 388
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 471434838   389 VLLDKGAKPNSR 400
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
672-763 3.24e-21

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 89.80  E-value: 3.24e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   672 LHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHgVTVDATTRmGYTPLHVASHYGNIKLVK 751
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 471434838   752 FLLQHQADVNAK 763
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
573-663 3.24e-21

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 89.80  E-value: 3.24e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   573 LHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSphSPAWNGYTPLHIAAKQNQIEVAR 652
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 471434838   653 SLLQYGGSANA 663
Cdd:pfam12796   79 LLLEKGADINV 89
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
1433-1519 3.41e-21

DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain present in a variety of proteins with apoptotic functions. Some (but not all) of these domains form homotypic and heterotypic dimers.


Pssm-ID: 214467 [Multi-domain]  Cd Length: 88  Bit Score: 89.39  E-value: 3.41e-21
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   1433 TDRVEMRMAVIREH-LGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSE 1511
Cdd:smart00005    1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80

                    ....*...
gi 471434838   1512 IVNMLEGS 1519
Cdd:smart00005   81 AVELLRSE 88
PHA02875 PHA02875
ankyrin repeat protein; Provisional
503-810 4.09e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 98.14  E-value: 4.09e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  503 DQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDtALALLEKEASQACMTKKGF-TPLHVAAKYGK 581
Cdd:PHA02875    2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSE-AIKLLMKHGAIPDVKYPDIeSELHDAVEEGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  582 VRLAELLLEHDAHPN-AAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGS 660
Cdd:PHA02875   81 VKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  661 ANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSG-LTPLHLVSQEGHVPVADVLIKHGVTVD-ATTRMG--YT 736
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNiMFMIEGeeCT 240
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 471434838  737 PLHVASHYgniklvkfllqhqaDVNAKTklgysplhQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRL 810
Cdd:PHA02875  241 ILDMICNM--------------CTNLES--------EAIDALIADIAIRIHKKTIRRDEGFKNNMSTIEDKEEF 292
Ank_2 pfam12796
Ankyrin repeats (3 copies);
705-794 4.34e-21

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 89.41  E-value: 4.34e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   705 LHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHqADVNAKTKlGYSPLHQAAQQGHTDIVT 784
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|
gi 471434838   785 LLLKNGASPN 794
Cdd:pfam12796   79 LLLEKGADIN 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
243-334 5.32e-21

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 89.03  E-value: 5.32e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   243 LHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQieTRTKDELTPLHCAARNGHVRISE 322
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 471434838   323 ILLDHGAPIQAK 334
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
115-440 6.84e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 98.03  E-value: 6.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  115 LHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQE-------------------------------NHLEVVKFL 163
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpnklgmkemirsinkcsvfytlvaikdafnnRNVEIFKII 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  164 LENGANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKVRL-----PALHIAARNDDTRTAAVLLQNDPNPDVLSKT 238
Cdd:PHA02878  121 LTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDrhkgnTALHYATENKDQRLTELLLSYGANVNIPDKT 200
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  239 GFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRgnvimvrlLLDrgaqietrtkdeltplhcaarnghV 318
Cdd:PHA02878  201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY--------CKD------------------------Y 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  319 RISEILLDHGAPIQAK-TKNGLSPIHMAAQGDhlDCVRLLLQYNAEIDDITLDHLTPLHVAA------HCGHHRVAKVLL 391
Cdd:PHA02878  249 DILKLLLEHGVDVNAKsYILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVkqylciNIGRILISNICL 326
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*....
gi 471434838  392 DKGAKPNSRALNGFTpLHIACKKNHIRVMELLLKTGASIDAVTESGLTP 440
Cdd:PHA02878  327 LKRIKPDIKNSEGFI-DNMDCITSNKRLNQIKDKCEDELNRLASIKITN 374
PHA02875 PHA02875
ankyrin repeat protein; Provisional
444-662 1.34e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 96.60  E-value: 1.34e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  444 ASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLL 523
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  524 ENGASPN-LATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNG 602
Cdd:PHA02875   89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 471434838  603 LTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNG-YTPLHIAAKQNQIEVARSLLQYGGSAN 662
Cdd:PHA02875  169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCN 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
115-200 2.22e-20

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 87.10  E-value: 2.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   115 LHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENgANQNVaTEDGFTPLAVALQQGHENVVA 194
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNL-KDNGRTALHYAARSGHLEIVK 78

                   ....*.
gi 471434838   195 HLINYG 200
Cdd:pfam12796   79 LLLEKG 84
PHA02878 PHA02878
ankyrin repeat protein; Provisional
341-610 6.61e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 94.95  E-value: 6.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  341 PIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLdkgAKPNSRAL-NGFTPLHIACKKNHIRV 419
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVfYTLVAIKDAFNNRNVEI 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  420 MELLLKTgaSIDAVTESGLTPLHVASFMGHL--PIVKNLLQRGASPN-VSNVKVETPLHMAARAGHTEVAKYLLQNKAKA 496
Cdd:PHA02878  117 FKIILTN--RYKNIQTIDLVYIDKKSKDDIIeaEITKLLLSYGADINmKDRHKGNTALHYATENKDQRLTELLLSYGANV 194
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  497 NAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTA-AREGHVDTALALLEKEAS-QACMTKKGFTPLH 574
Cdd:PHA02878  195 NIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDvNAKSYILGLTALH 274
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 471434838  575 VAAKygKVRLAELLLEHDAHPNAAGKNGLTPLHVAV 610
Cdd:PHA02878  275 SSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAV 308
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
1442-1517 6.78e-20

Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. Structural analysis of DD-DD complexes show that the domains interact with each other in many different ways. DD-containing proteins serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes. In mammals, they are prominent components of the programmed cell death (apoptosis) pathway and are found in a number of other signaling pathways. In invertebrates, they are involved in transcriptional regulation of zygotic patterning genes in insect embryogenesis, and are components of the ToII/NF-kappaB pathway, a conserved innate immune pathway in animal cells.


Pssm-ID: 260017 [Multi-domain]  Cd Length: 79  Bit Score: 85.41  E-value: 6.78e-20
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 471434838 1442 VIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIVNMLE 1517
Cdd:cd01670     4 LVAEELGRDWKKLARKLGLSEGDIDQIEEDNRDDLKEQAYQMLERWREREGDEATLGRLIQALREIGRRDLAEKLE 79
Ank_2 pfam12796
Ankyrin repeats (3 copies);
474-560 7.80e-20

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 85.56  E-value: 7.80e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   474 LHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASpnLATTAGHTPLHTAAREGHVDTAL 553
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                   ....*..
gi 471434838   554 ALLEKEA 560
Cdd:pfam12796   79 LLLEKGA 85
PHA02876 PHA02876
ankyrin repeat protein; Provisional
581-807 8.85e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 95.90  E-value: 8.85e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  581 KVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVAR-------- 652
Cdd:PHA02876  157 ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsn 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  653 -------------------SLLQY--GGSANAESVQGVTPLHLAAQEGH-TEMVALLLSKQANGNLGNKSGLTPLHLVSQ 710
Cdd:PHA02876  237 inkndlsllkairnedletSLLLYdaGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAK 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  711 EGH-VPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIK-LVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLK 788
Cdd:PHA02876  317 NGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
                         250
                  ....*....|....*....
gi 471434838  789 NGASPNEVSSNGTTPLAIA 807
Cdd:PHA02876  397 YGADIEALSQKIGTALHFA 415
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
448-663 9.37e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738 [Multi-domain]  Cd Length: 235  Bit Score: 90.27  E-value: 9.37e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  448 GHLPIVKNLLQRGASPNVSNVKVETPLH--MAARAGHTEVAKYLLQNKAKANAKAKDDQ-TPLHCAARIGHTGMVKLLLE 524
Cdd:COG0666    15 FLDLLLVALLLLLSLDLSNPSDKKLNLYleLALLPAASLSELLLKLIVDRHLAARDLDGrLPLHSAASKGDDKIVKLLLA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  525 NGASPNLATTAGHTPLHTAAREGHvdtalallekeasqacmtkkgftplhvaAKYGKVRLAELLLEHDAH---PNAAGKN 601
Cdd:COG0666    95 SGADVNAKDADGDTPLHLAALNGN----------------------------PPEGNIEVAKLLLEAGADldvNNLRDED 146
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 471434838  602 GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANA 663
Cdd:COG0666   147 GNTPLHWAALNGDADIVELLLEAGADPNSRNSYGVTALDPAAKNGRIELVKLLLDKGLHLSL 208
Ank_2 pfam12796
Ankyrin repeats (3 copies);
639-730 1.53e-19

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 84.79  E-value: 1.53e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   639 LHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKqANGNLGNKsGLTPLHLVSQEGHVPVAD 718
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 471434838   719 VLIKHGVTVDAT 730
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
210-301 2.56e-19

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 84.02  E-value: 2.56e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   210 LHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTpqNGITPLHIASRRGNVIMVR 289
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 471434838   290 LLLDRGAQIETR 301
Cdd:pfam12796   79 LLLEKGADINVK 90
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
670-820 3.48e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738 [Multi-domain]  Cd Length: 235  Bit Score: 88.73  E-value: 3.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  670 TPLHLAAQEGHTEmvaLLLSKQA--NGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGN- 746
Cdd:COG0666    43 LELALLPAASLSE---LLLKLIVdrHLAARDLDGRLPLHSAASKGDDKIVKLLLASGADVNAKDADGDTPLHLAALNGNp 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  747 ----IKLVKFLLQH---QADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVL 819
Cdd:COG0666   120 pegnIEVAKLLLEAgadLDVNNLRDEDGNTPLHWAALNGDADIVELLLEAGADPNSRNSYGVTALDPAAKNGRIELVKLL 199

                  .
gi 471434838  820 K 820
Cdd:COG0666   200 L 200
PHA02878 PHA02878
ankyrin repeat protein; Provisional
603-822 4.37e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 92.64  E-value: 4.37e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  603 LTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQ-NQI---EVARSLLQYGGSANAESVQGvtplhlAAQE 678
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpNKLgmkEMIRSINKCSVFYTLVAIKD------AFNN 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  679 GHTEMVALLLSKQANGNlgNKSGLTPLHLVSQEGHV--PVADVLIKHGVTVDATTR-MGYTPLHVASHYGNIKLVKFLLQ 755
Cdd:PHA02878  112 RNVEIFKIILTNRYKNI--QTIDLVYIDKKSKDDIIeaEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLS 189
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 471434838  756 HQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAkrLGYISVTDVLKVV 822
Cdd:PHA02878  190 YGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS--VGYCKDYDILKLL 254
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
210-337 2.14e-18

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738 [Multi-domain]  Cd Length: 235  Bit Score: 86.42  E-value: 2.14e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  210 LHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLN-----VAQLLLNRGA-SVNFTPQN--GITPLHIASR 281
Cdd:COG0666    77 LHSAASKGDDKIVKLLLASGADVNAKDADGDTPLHLAALNGNPPegnieVAKLLLEAGAdLDVNNLRDedGNTPLHWAAL 156
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 471434838  282 RGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKN 337
Cdd:COG0666   157 NGDADIVELLLEAGADPNSRNSYGVTALDPAAKNGRIELVKLLLDKGLHLSLLKFN 212
Ank_2 pfam12796
Ankyrin repeats (3 copies);
408-491 2.75e-18

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 2.75e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   408 LHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKveTPLHMAARAGHTEVAK 487
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR--TALHYAARSGHLEIVK 78

                   ....
gi 471434838   488 YLLQ 491
Cdd:pfam12796   79 LLLE 82
PHA02875 PHA02875
ankyrin repeat protein; Provisional
52-296 3.24e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 89.28  E-value: 3.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   52 AARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELV 131
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  132 NYGANVN-AQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPlavalqqghenvvahlinygtkgkvrlpaL 210
Cdd:PHA02875   89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP-----------------------------L 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  211 HIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNG-ITPLHIASRRGNVIMVR 289
Cdd:PHA02875  140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVR 219

                  ....*..
gi 471434838  290 LLLDRGA 296
Cdd:PHA02875  220 LFIKRGA 226
PHA03095 PHA03095
ankyrin-like protein; Provisional
682-806 3.66e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 89.70  E-value: 3.66e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  682 EMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADV---LIKHGVTVDATTRMGYTPLHVASHYGN-IKLVKFLLQHQ 757
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAG 107
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 471434838  758 ADVNAKTKLGYSPLHQ--AAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAI 806
Cdd:PHA03095  108 ADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAV 158
PHA02875 PHA02875
ankyrin repeat protein; Provisional
351-566 6.32e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 88.12  E-value: 6.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  351 LDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASI 430
Cdd:PHA02875   15 LDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  431 DAVT-ESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHC 509
Cdd:PHA02875   95 DDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLII 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 471434838  510 AARIGHTGMVKLLLENGASPNLATTAGH-TPLHTAAREGHVDTALALLEKEASQACMT 566
Cdd:PHA02875  175 AMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIMF 232
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
538-714 2.71e-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: 87.76  E-value: 2.71e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  538 TPLHTAAREGHVDTALALLEKEASQACMTKK-GFTPLHVAAKYGKVRLAELLLEhdAHPNAAGK-------NGLTPLHVA 609
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGAlGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  610 VHHNNLDIVKLLLPRGG--------------SPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLH-L 674
Cdd:cd22192    97 VVNQNLNLVRELIARGAdvvspratgtffrpGPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiL 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 471434838  675 AAQEGHT---EMVALLLSKQANGNLG------NKSGLTPLHLVSQEGHV 714
Cdd:cd22192   177 VLQPNKTfacQMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNI 225
PHA02875 PHA02875
ankyrin repeat protein; Provisional
646-819 2.85e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 86.20  E-value: 2.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  646 NQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGV 725
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  726 TV-DATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPL 804
Cdd:PHA02875   93 FAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172
                         170
                  ....*....|....*
gi 471434838  805 AIAKRLGYISVTDVL 819
Cdd:PHA02875  173 IIAMAKGDIAICKML 187
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
604-788 2.91e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738 [Multi-domain]  Cd Length: 235  Bit Score: 82.95  E-value: 2.91e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  604 TPLHVAVHHNNLDIVKLLLPRGGSPHSP--AWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHT 681
Cdd:COG0666     7 ALLLINKCFLDLLLVALLLLLSLDLSNPsdKKLNLYLELALLPAASLSELLLKLIVDRHLAARDLDGRLPLHSAASKGDD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  682 EMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVP-----VADVLIKHGVTVDATTR---MGYTPLHVASHYGNIKLVKFL 753
Cdd:COG0666    87 KIVKLLLASGADVNAKDADGDTPLHLAALNGNPPegnieVAKLLLEAGADLDVNNLrdeDGNTPLHWAALNGDADIVELL 166
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 471434838  754 LQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLK 788
Cdd:COG0666   167 LEAGADPNSRNSYGVTALDPAAKNGRIELVKLLLD 201
Ank_2 pfam12796
Ankyrin repeats (3 copies);
49-140 3.35e-17

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 78.24  E-value: 3.35e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838    49 FLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMvVELLHKEIILETTTkKGNTALHIAALAGQDEVVR 128
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEI-VKLLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 471434838   129 ELVNYGANVNAQ 140
Cdd:pfam12796   79 LLLEKGADINVK 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
505-691 4.43e-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: 86.99  E-value: 4.43e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  505 TPLHCAARIGHTGMVKLLLENGASPNLATTA-GHTPLHTAAREGHVDTALALLE--KEASQACMTK---KGFTPLHVAAK 578
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGAlGETALHVAALYDNLEAAVVLMEaaPELVNEPMTSdlyQGETALHIAVV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  579 YGKVRLAELLLEHDA---HPNAAG-------KN----GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAK 644
Cdd:cd22192    99 NQNLNLVRELIARGAdvvSPRATGtffrpgpKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL 178
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 471434838  645 QNQIEVARS----LLQYGGSANAESV------QGVTPLHLAAQEGHTEMVALLLSKQ 691
Cdd:cd22192   179 QPNKTFACQmydlILSYDKEDDLQPLdlvpnnQGLTPFKLAAKEGNIVMFQHLVQKR 235
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
210-379 7.32e-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: 86.22  E-value: 7.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  210 LHIAARNDDTRTAAVLLQNdPNPDVLSK--TGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQN-----GITPLHIASRR 282
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKC-PSCDLFQRgaLGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyqGETALHIAVVN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  283 GNVIMVRLLLDRGAQIET---------RTKDELT-----PLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAA-- 346
Cdd:cd22192   100 QNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVlq 179
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 471434838  347 QGDHLDC--VRLLLQYNAEIDDITLDH------LTPLHVAA 379
Cdd:cd22192   180 PNKTFACqmYDLILSYDKEDDLQPLDLvpnnqgLTPFKLAA 220
Ank_2 pfam12796
Ankyrin repeats (3 copies);
738-819 1.72e-16

Ankyrin repeats (3 copies);


Pssm-ID: 432791 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 1.72e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   738 LHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASpnEVSSNGTTPLAIAKRLGYISVTD 817
Cdd:pfam12796    1 LMLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                   ..
gi 471434838   818 VL 819
Cdd:pfam12796   79 LL 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
52-200 2.50e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738 [Multi-domain]  Cd Length: 235  Bit Score: 80.25  E-value: 2.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   52 AARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQD-----EV 126
Cdd:COG0666    47 LLPAASLSELLLKLIVDRHLAARDLDGRLPLHSAASKGDDKIVKLLLASGADVNAKDADGDTPLHLAALNGNPpegniEV 126
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 471434838  127 VRELVNYGA---NVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYG 200
Cdd:COG0666   127 AKLLLEAGAdldVNNLRDEDGNTPLHWAALNGDADIVELLLEAGADPNSRNSYGVTALDPAAKNGRIELVKLLLDKG 203
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
43-266 2.36e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738 [Multi-domain]  Cd Length: 235  Bit Score: 77.56  E-value: 2.36e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   43 ADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEII---LETTTKKGNTALHIAA 119
Cdd:COG0666     2 KPSLSALLLINKCFLDLLLVALLLLLSLDLSNPSDKKLNLYLELALLPAASLSELLLKLIVdrhLAARDLDGRLPLHSAA 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  120 LAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHL-----EVVKFLLENGANQNVAT---EDGFTPLavalqqghen 191
Cdd:COG0666    82 SKGDDKIVKLLLASGADVNAKDADGDTPLHLAALNGNPpegniEVAKLLLEAGADLDVNNlrdEDGNTPL---------- 151
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 471434838  192 vvahlinygtkgkvrlpalHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVN 266
Cdd:COG0666   152 -------------------HWAALNGDADIVELLLEAGADPNSRNSYGVTALDPAAKNGRIELVKLLLDKGLHLS 207
PHA02876 PHA02876
ankyrin repeat protein; Provisional
644-810 2.16e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 78.57  E-value: 2.16e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  644 KQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKH 723
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  724 -----------------------------GVTVDATTRMGYTPLHVASHYGNI-KLVKFLLQHQADVNAKTKLGYSPLHQ 773
Cdd:PHA02876  234 rsninkndlsllkairnedletslllydaGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYL 313
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 471434838  774 AAQQGH-TDIVTLLLKNGASPNEVSSNGTTPLAIAKRL 810
Cdd:PHA02876  314 MAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTL 351
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
47-176 3.20e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 223738 [Multi-domain]  Cd Length: 235  Bit Score: 74.09  E-value: 3.20e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   47 TSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVK-----MVVELLHKEIILETTT---KKGNTALHIA 118
Cdd:COG0666    75 LPLHSAASKGDDKIVKLLLASGADVNAKDADGDTPLHLAALNGNPPegnieVAKLLLEAGADLDVNNlrdEDGNTPLHWA 154
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 471434838  119 ALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATED 176
Cdd:COG0666   155 ALNGDADIVELLLEAGADPNSRNSYGVTALDPAAKNGRIELVKLLLDKGLHLSLLKFN 212
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
110-261 7.46e-13

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: 73.64  E-value: 7.46e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  110 KGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGF--------------TPLYMAAQENHLEVVKFLLENGANqNVATE 175
Cdd:cd22194   140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKEST-DITSQ 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  176 DGFTplavalqqgheNVVAHlinygtkgkvrlpALHIAARNDDTRTAAV------LLQNDPNPD---VLSKTGFTPLHIA 246
Cdd:cd22194   219 DSRG-----------NTVLH-------------ALVTVAEDSKTQNDFVkrmydmILLKSENKNletIRNNEGLTPLQLA 274
                         170
                  ....*....|....*
gi 471434838  247 AHYENLNVAQLLLNR 261
Cdd:cd22194   275 AKMGKAEILKYILSR 289
Death_FADD cd08306
Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in ...
1442-1505 1.02e-12

Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in FAS-associated via death domain (FADD). FADD is a component of the death-inducing signaling complex (DISC) and serves as an adaptor in the signaling pathway of death receptor proteins. It modulates apoptosis as well as non-apoptotic processes such as cell cycle progression, survival, innate immune signaling, and hematopoiesis. FADD contains an N-terminal DED and a C-terminal DD. Its DD interacts with the DD of the activated death receptor, FAS, and its DED recruits the initiator caspases, caspase-8 and -10, to the DISC complex via a homotypic interaction with the N-terminal DED of the caspase. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and they can recruit other proteins into signaling complexes.


Pssm-ID: 260020  Cd Length: 85  Bit Score: 65.01  E-value: 1.02e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 471434838 1442 VIREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALR 1505
Cdd:cd08306     7 VICENLGRDWRQLARKLGLSETKIESISEAHPRNLREQVRQSLREWKKIKKAEATVADLIKALR 70
Ank_4 pfam13637
Ankyrin repeats (many copies);
571-622 2.38e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 63.06  E-value: 2.38e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 471434838   571 TPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLL 622
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
734-787 5.06e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 62.29  E-value: 5.06e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 471434838   734 GYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLL 787
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
583-825 6.68e-12

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 69.70  E-value: 6.68e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  583 RLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQ--IEVARSLLQYGGS 660
Cdd:PHA02946   53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAK 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  661 A-NAESVQGVTPLhLAAQEGHTEMVALLLSKQANGNLGNKSGLTPL--HLVSQEGHVPVADVLIKHGVTVDATTRMGYTP 737
Cdd:PHA02946  133 InNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTP 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  738 LHV--ASHYGNIKLVKFLLQhQADVNAKTKLGYSPLhqaaqqghtdivTLLLKNGASPNEVSSNGTTPLAIAKRLGYISV 815
Cdd:PHA02946  212 LHIvcSKTVKNVDIINLLLP-STDVNKQNKFGDSPL------------TLLIKTLSPAHLINKLLSTSNVITDQTVNICI 278
                         250
                  ....*....|....
gi 471434838  816 ----TDVLKVVTDE 825
Cdd:PHA02946  279 fydrDDVLEIINDK 292
Ank_4 pfam13637
Ankyrin repeats (many copies);
437-490 1.23e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.14  E-value: 1.23e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 471434838   437 GLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLL 490
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
111-164 1.78e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.75  E-value: 1.78e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 471434838   111 GNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLL 164
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
670-806 2.05e-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: 68.89  E-value: 2.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  670 TPLHLAAQEGHTEMVA-LLLSKQAN----GNLGNksglTPLHLVSQEGHVPVADVLIKHG---VTVDATTRM--GYTPLH 739
Cdd:cd22192    19 SPLLLAAKENDVQAIKkLLKCPSCDlfqrGALGE----TALHVAALYDNLEAAVVLMEAApelVNEPMTSDLyqGETALH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  740 VASHYGNIKLVKFLLQHQADV------------NAKTKLGYS--PLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLA 805
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVvspratgtffrpGPKNLIYYGehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174

                  .
gi 471434838  806 I 806
Cdd:cd22192   175 I 175
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
510-693 2.58e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 68.74  E-value: 2.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  510 AARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEkeasQACmtkkgftPLHVaakygkvrlaelll 589
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLK----HAC-------NVHI-------------- 586
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  590 eHDAHPNAAGKNGLTplhvAVHHNNLDIVkLLLPRGGSPHSpawnGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGV 669
Cdd:PLN03192  587 -RDANGNTALWNAIS----AKHHKIFRIL-YHFASISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656
                         170       180
                  ....*....|....*....|....
gi 471434838  670 TPLHLAAQEGHTEMVALLLSKQAN 693
Cdd:PLN03192  657 TALQVAMAEDHVDMVRLLIMNGAD 680
Ank_4 pfam13637
Ankyrin repeats (many copies);
406-457 2.74e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 2.74e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 471434838   406 TPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLL 457
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02989 PHA02989
ankyrin repeat protein; Provisional
253-524 4.74e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 67.46  E-value: 4.74e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  253 NVAQLLLNRGASVNFTPQ-NGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDElTPLHCAARNGHV------RISEILL 325
Cdd:PHA02989   17 NALEFLLRTGFDVNEEYRgNSILLLYLKRKDVKIKIVKLLIDNGADVNYKGYIE-TPLCAVLRNREItsnkikKIVKLLL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  326 DHGAPIQAKTKNGLSPIHMAAQGDH---LDCVRLLLQYNAEIDDI-TLDHLTPLHVAAHCGHHR--VAKVLLDKGAKP-N 398
Cdd:PHA02989   96 KFGADINLKTFNGVSPIVCFIYNSNinnCDMLRFLLSKGINVNDVkNSRGYNLLHMYLESFSVKkdVIKILLSFGVNLfE 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  399 SRALNGFTPLHIACKKN----HIRVMELLLKTGASI---DAVTESGLTplhvaSFMGHLPI-------VKNLLQRGASPN 464
Cdd:PHA02989  176 KTSLYGLTPMNIYLRNDidviSIKVIKYLIKKGVNIetnNNGSESVLE-----SFLDNNKIlskkefkVLNFILKYIKIN 250
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  465 VSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLE 524
Cdd:PHA02989  251 KKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
PHA02874 PHA02874
ankyrin repeat protein; Provisional
43-186 4.81e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.91  E-value: 4.81e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   43 ADAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAG 122
Cdd:PHA02874  122 AELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYG 201
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 471434838  123 QDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHlEVVKFLLENgANQNVATEDGFTPLAVALQ 186
Cdd:PHA02874  202 DYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAIN 263
Ank_4 pfam13637
Ankyrin repeats (many copies);
371-424 5.54e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.21  E-value: 5.54e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 471434838   371 HLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLL 424
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
607-797 6.25e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.59  E-value: 6.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  607 HVAVHhnNLDIVKLLLPRGGSpHSPAWNGYTPLHIAAKQNQiEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVAL 686
Cdd:PLN03192  501 HKELH--DLNVGDLLGDNGGE-HDDPNMASNLLTVASTGNA-ALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLV 576
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  687 LLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTrmGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKL 766
Cdd:PLN03192  577 LLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQ 654
                         170       180       190
                  ....*....|....*....|....*....|.
gi 471434838  767 GYSPLHQAAQQGHTDIVTLLLKNGASPNEVS 797
Cdd:PLN03192  655 GATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
Ank_4 pfam13637
Ankyrin repeats (many copies);
241-292 1.10e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 1.10e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 471434838   241 TPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLL 292
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
57-202 1.33e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.24  E-value: 1.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   57 NLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIaALAGQDEV--VRELVNYG 134
Cdd:PHA02876  354 NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHF-ALCGTNPYmsVKTLIDRG 432
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 471434838  135 ANVNAQSQKGFTPLYMAAQEN-HLEVVKFLLENGANQNVATEDGFTPLAVALqqGHENVVAHLINYGTK 202
Cdd:PHA02876  433 ANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAE 499
Ank_4 pfam13637
Ankyrin repeats (many copies);
305-358 1.66e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 1.66e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 471434838   305 ELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLL 358
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
338-391 1.81e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.67  E-value: 1.81e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 471434838   338 GLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLL 391
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
406-589 2.46e-10

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 65.42  E-value: 2.46e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  406 TPLHIACKKNHIRVMELLLKTgASIDAVTESGL--TPLHVASFMGHLPIVKNLLQrgASPNVSNVKV-------ETPLHM 476
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKC-PSCDLFQRGALgeTALHVAALYDNLEAAVVLME--AAPELVNEPMtsdlyqgETALHI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  477 AARAGHTEVAKYLLQNKAkanakakDDQTP---------------------LHCAARIGHTGMVKLLLENGASPNLATTA 535
Cdd:cd22192    96 AVVNQNLNLVRELIARGA-------DVVSPratgtffrpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSL 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 471434838  536 GHTPLH------TAAREGHVDTALALLEKEASQACM----TKKGFTPLHVAAKYGKVRLAELLL 589
Cdd:cd22192   169 GNTVLHilvlqpNKTFACQMYDLILSYDKEDDLQPLdlvpNNQGLTPFKLAAKEGNIVMFQHLV 232
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
82-294 3.02e-10

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 65.03  E-value: 3.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   82 LHLASKEGHVKMVVELL-HKEIILETTTKKGNTALHIAALAGQDEV-------VRELVNygANVNAQSQKGFTPLYMAAQ 153
Cdd:cd22192    21 LLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAavvlmeaAPELVN--EPMTSDLYQGETALHIAVV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  154 ENHLEVVKFLLENGANQNVATEDG--FT------------PLAVALQQGHENVVAHLINYGTkgkvrlpalhiAARNDDT 219
Cdd:cd22192    99 NQNLNLVRELIARGADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEIVRLLIEHGA-----------DIRAQDS 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  220 RtaavllqndpnpdvlsktGFTPLHIAAHYENLNVA----QLLLNRGASVNFTP------QNGITPLHIASRRGNVIMVR 289
Cdd:cd22192   168 L------------------GNTVLHILVLQPNKTFAcqmyDLILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQ 229

                  ....*
gi 471434838  290 LLLDR 294
Cdd:cd22192   230 HLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
472-523 3.59e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.90  E-value: 3.59e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 471434838   472 TPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLL 523
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
46-200 3.98e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.89  E-value: 3.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   46 ATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDE 125
Cdd:PLN03192  526 ASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHK 605
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 471434838  126 VVRELVNYGANVNAQSqkGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLINYG 200
Cdd:PLN03192  606 IFRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNG 678
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
312-467 4.22e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.89  E-value: 4.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  312 AARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQY--NAEIDDITLDhlTPLHVAAHCGHHRVAKV 389
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHacNVHIRDANGN--TALWNAISAKHHKIFRI 609
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 471434838  390 LLDKGAKPNSRAlnGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSN 467
Cdd:PLN03192  610 LYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02798 PHA02798
ankyrin-like protein; Provisional
231-477 6.57e-10

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 63.70  E-value: 6.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  231 NPDVLSKTgFTPLHIAAHYEN--LNVAQLLLNRGASVNFTPQNGITPL-----HIASRRGNVIMVRLLLDRGAQIETRTK 303
Cdd:PHA02798   29 NPNEIVNE-YSIFQKYLQRDSpsTDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNS 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  304 DELTPLHCAARNGHVRISEILL---DHGAPIQAKTKNGLSPIHMAAQGDH---LDCVRLLLQYNAEIDDIT-LDHLTPLH 376
Cdd:PHA02798  108 DGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNnKEKYDTLH 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  377 VAAHCGHHR----VAKVLLDKG---AKPN----SRALNGFTPLHIACKKNHIRVMELLLKTgASIDAVTESGLTPLHVAS 445
Cdd:PHA02798  188 CYFKYNIDRidadILKLFVDNGfiiNKENkshkKKFMEYLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLYYSV 266
                         250       260       270
                  ....*....|....*....|....*....|..
gi 471434838  446 FMGHLPIVKNLLQRGASPNVSNVKVETPLHMA 477
Cdd:PHA02798  267 SHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
125-468 9.55e-10

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 63.39  E-value: 9.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  125 EVVRELVNYGANVNAQSQKGFTPL--YMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGhENVVAHLINY--- 199
Cdd:PHA02716  193 DILEWLCNNGVNVNLQNNHLITPLhtYLITGNVCASVIKKIIELGGDMDMKCVNGMSPIMTYIINI-DNINPEITNIyie 271
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  200 ---GTKGKVRLPALHI---AARNDDTRTAAVLLQNDPNPDVLSKTGFTPLH--IAAHYENLNVAQLLLNRGASVNFTPQN 271
Cdd:PHA02716  272 sldGNKVKNIPMILHSyitLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNI 351
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  272 GITPLHIASRRGNVI--------------MVRLLLDRGAQIETRTKDELTPLH---CAARN-GHVRISEILldhgapIQA 333
Cdd:PHA02716  352 GNTVLHTYLSMLSVVnildpetdndirldVIQCLISLGADITAVNCLGYTPLTsyiCTAQNyMYYDIIDCL------ISD 425
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  334 KTKNGLSpiHMAAQG-----DHLDCV--RLLLQYNAEIDDITLDH----LTPLHVAAHCGhhrvakvlLDKGAKPNSRAL 402
Cdd:PHA02716  426 KVLNMVK--HRILQDllirvDDTPCIihHIIAKYNIPTDLYTDEYepydSTKIHDVYHCA--------IIERYNNAVCET 495
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 471434838  403 NGFTPLHIA--CKKNHIRVME---LLLKTGASIDAVTESGLTPLHVA----SFMGHLP-IVKNLLQRgaSPNVSNV 468
Cdd:PHA02716  496 SGMTPLHVSiiSHTNANIVMDsfvYLLSIQYNINIPTKNGVTPLMLTmrnnRLSGHQWyIVKNILDK--RPNVDIV 569
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
139-359 1.15e-09

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: 63.18  E-value: 1.15e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   139 AQSQKGFTPlymAAQENHLEVVKFLLENGA--NQNVATEDGFTPLAVALQQG-HENVVAHLINYGTKGKVRLPALHIAAR 215
Cdd:TIGR00870   15 SDEEKAFLP---AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTLLHAISL 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   216 ND--------------DTRTAAVLLQNDPNPDVLSKtGFTPLHIAAHYENLNVAQLLLNRGASVN-------FTPQNGIT 274
Cdd:TIGR00870   92 EYvdaveaillhllaaFRKSGPLELANDQYTSEFTP-GITALHLAAHRQNYEIVKLLLERGASVParacgdfFVKSQGVD 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   275 -------PLHIASRRGNVIMVRLLLDRGAQIETRtkDEL--TPLHCA-------ARNGHVRIS--EILLDHGAPIQAKTK 336
Cdd:TIGR00870  171 sfyhgesPLNAAACLGSPSIVALLSEDPADILTA--DSLgnTLLHLLvmenefkAEYEELSCQmyNFALSLLDKLRDSKE 248
                          250       260       270
                   ....*....|....*....|....*....|
gi 471434838   337 -------NGLSPIHMAAQGDHLDCVRLLLQ 359
Cdd:TIGR00870  249 levilnhQGLTPLKLAAKEGRIVLFRLKLA 278
Ank_4 pfam13637
Ankyrin repeats (many copies);
635-688 1.20e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 1.20e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 471434838   635 GYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLL 688
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
266-363 1.23e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 1.23e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  266 NFTPQNGITP--LHIA-------SRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTK 336
Cdd:PTZ00322   67 NLTTEEVIDPvvAHMLtvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDK 146
                          90       100
                  ....*....|....*....|....*..
gi 471434838  337 NGLSPIHMAAQGDHLDCVRLLLQYNAE 363
Cdd:PTZ00322  147 DGKTPLELAEENGFREVVQLLSRHSQC 173
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
571-807 1.67e-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: 62.72  E-value: 1.67e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  571 TPLHVAAKYGKVR-LAELLLEHDAHPNAAGKNGLTPLHVAVHHNNLDIVKLLLprggsphspawngytplhiaakqnqiE 649
Cdd:cd22192    19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLM--------------------------E 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  650 VARSLLQYggSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTplhlvsqegHVPVADVLIKHGvtvda 729
Cdd:cd22192    73 AAPELVNE--PMTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTF---------FRPGPKNLIYYG----- 136
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  730 ttrmgYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVT----LLL-----KNGASPNEVSSN- 799
Cdd:cd22192   137 -----EHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACqmydLILsydkeDDLQPLDLVPNNq 211

                  ....*...
gi 471434838  800 GTTPLAIA 807
Cdd:cd22192   212 GLTPFKLA 219
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
50-261 1.85e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 62.34  E-value: 1.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   50 LRAARSGNLDkALDHLRNGVDINTCnQNGLNG---LHLASKEGHVKMVVELLH--KEIILETTTK---KGNTALHIAALA 121
Cdd:cd22192    22 LLAAKENDVQ-AIKKLLKCPSCDLF-QRGALGetaLHVAALYDNLEAAVVLMEaaPELVNEPMTSdlyQGETALHIAVVN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  122 GQDEVVRELVNYGANVNAQSQKG--FT------------PLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQ 187
Cdd:cd22192   100 QNLNLVRELIARGADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQ 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  188 GHENVVAHLINygtkgkvrlpalhiaarnddtrtaaVLLQNDPNPD------VLSKTGFTPLHIAAHYENLNVAQLLLNR 261
Cdd:cd22192   180 PNKTFACQMYD-------------------------LILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
274-325 2.86e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 2.86e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 471434838   274 TPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILL 325
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
536-694 3.10e-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: 61.82  E-value: 3.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  536 GHTPLHTAA---REGHVDTALALLE--------KEASQACMTK---KGFTPLHVAAKYGKVRLAELLLEH--DAHPNAAG 599
Cdd:cd21882    26 GKTCLHKAAlnlNDGVNEAIMLLLEaapdsgnpKELVNAPCTDefyQGQTALHIAIENRNLNLVRLLVENgaDVSARATG 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  600 KN-----------GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWN---GYTPLHIAAKQNQIEVARS---------LLQ 656
Cdd:cd21882   106 RFfrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHALVLQADNTPENSafvcqmynlLLS 185
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 471434838  657 YGGSANA----ESV---QGVTPLHLAAQEGHTEMVALLLSKQANG 694
Cdd:cd21882   186 YGAHLDPtqqlEEIpnhQGLTPLKLAAVEGKIVMFQHILQREFSG 230
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
646-808 3.50e-09

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: 61.64  E-value: 3.50e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   646 NQIEVARSLLQYGGSANAESVQ-------GVTPLHLAAQEG-HTEMVALLLSKQANGNLGNksglTPLHLVSQEGHVPVA 717
Cdd:TIGR00870   23 PAAERGDLASVYRDLEEPKKLNincpdrlGRSALFVAAIENeNLELTELLLNLSCRGAVGD----TLLHAISLEYVDAVE 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   718 DVLI-------KHGVTVDATTRM------GYTPLHVASHYGNIKLVKFLLQHQADVNAKTK--------------LGYSP 770
Cdd:TIGR00870   99 AILLhllaafrKSGPLELANDQYtseftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESP 178
                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 471434838   771 LHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAK 808
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV 216
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
206-327 4.52e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.45  E-value: 4.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  206 RLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNvAQLLLNRGASVNFTPQNGITPLHIASRRGNV 285
Cdd:PTZ00322   50 HLEALEATENKDATPDHNLTTEEVIDPVVAHMLTVELCQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHV 128
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 471434838  286 IMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEILLDH 327
Cdd:PTZ00322  129 QVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
569-772 4.83e-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: 61.05  E-value: 4.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  569 GFTPLHVAAKY---GKVRLAELLLEHDAHPNAAGK-----------NGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPA-- 632
Cdd:cd21882    26 GKTCLHKAALNlndGVNEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSARAtg 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  633 -----------WNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQ---GVTPLH-LAAQEGHTEMVALLLSKQANGNLG 697
Cdd:cd21882   106 rffrkspgnlfYFGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHaLVLQADNTPENSAFVCQMYNLLLS 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  698 NKSGLTPLhlvsqeghVPVADVlikhgvtvdaTTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAK------TKLGYSPL 771
Cdd:cd21882   186 YGAHLDPT--------QQLEEI----------PNHQGLTPLKLAAVEGKIVMFQHILQREFSGPYQplsrkfTEWTYGPV 247

                  .
gi 471434838  772 H 772
Cdd:cd21882   248 T 248
Ank_5 pfam13857
Ankyrin repeats (many copies);
390-444 5.25e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.50  E-value: 5.25e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 471434838   390 LLDKG-AKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVA 444
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
420-573 5.87e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.04  E-value: 5.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  420 MELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAK 499
Cdd:PLN03192  541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH 620
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 471434838  500 AKDDqtpLHC-AARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACM-TKKGFTPL 573
Cdd:PLN03192  621 AAGD---LLCtAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAnTDDDFSPT 693
PHA02798 PHA02798
ankyrin-like protein; Provisional
125-368 6.36e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 60.62  E-value: 6.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  125 EVVRELVNYGANVNAQSQKGFTPL-----YMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLIny 199
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILL-- 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  200 gtkgkvrlpalhiaarnddtrtaaVLLQNDPNPDVLSKTGFTPLHI---AAHYENLNVAQLLLNRGASVN-FTPQNGITP 275
Cdd:PHA02798  130 ------------------------FMIENGADTTLLDKDGFTMLQVylqSNHHIDIEIIKLLLEKGVDINtHNNKEKYDT 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  276 LHIASR----RGNVIMVRLLLDRGAQIETRTK-------DELTPLHCAARNGHVRISEILLDHgAPIQAKTKNGLSPIHM 344
Cdd:PHA02798  186 LHCYFKynidRIDADILKLFVDNGFIINKENKshkkkfmEYLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLYY 264
                         250       260
                  ....*....|....*....|....
gi 471434838  345 AAQGDHLDCVRLLLQYNAEIDDIT 368
Cdd:PHA02798  265 SVSHNNRKIFEYLLQLGGDINIIT 288
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
387-457 6.70e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.68  E-value: 6.70e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 471434838  387 AKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLL 457
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
225-370 7.83e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 60.65  E-value: 7.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  225 LLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKD 304
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG 623
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 471434838  305 ELtpLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLD 370
Cdd:PLN03192  624 DL--LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
514-602 8.15e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.30  E-value: 8.15e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  514 GHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDA 593
Cdd:PTZ00322   93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172

                  ....*....
gi 471434838  594 HPNAAGKNG 602
Cdd:PTZ00322  173 CHFELGANA 181
PHA02946 PHA02946
ankyin-like protein; Provisional
92-276 9.36e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 59.68  E-value: 9.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   92 KMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYM--AAQENHLEVVKFLLENGAN 169
Cdd:PHA02946   53 RFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAK 132
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  170 -QNVATEDGFTPLaVALQQGHENVVAHLINYGTKGKV------RLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTP 242
Cdd:PHA02946  133 iNNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIvdkfgkNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTP 211
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 471434838  243 LHI--AAHYENLNVAQLLLnrgASVNFTPQN--GITPL 276
Cdd:PHA02946  212 LHIvcSKTVKNVDIINLLL---PSTDVNKQNkfGDSPL 246
Death_NMPP84 cd08318
Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix ...
1439-1516 9.56e-09

Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix Protein P84 (also known as HPR1 or THOC1). HPR1/p84 resides in the nuclear matrix and is part of the THO complex, also called TREX (transcription/export) complex, which functions in mRNP biogenesis at the interface between transcription and export of mRNA from the nucleus. Mice lacking THOC1 have abnormal testis development and are sterile. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260030  Cd Length: 86  Bit Score: 54.06  E-value: 9.56e-09
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 471434838 1439 RMAVIREHLGLSWAELARELQFSVEDINRIRvENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNIDRSEIVNML 1516
Cdd:cd08318     9 QIDVLANKLGEQWKTLAPYLEMKDKDIRQIE-SDSEDMKMRAKQLLVTWQDREGAQATPEILMTALNAAGLNEIAENL 85
Ank_4 pfam13637
Ankyrin repeats (many copies);
668-721 9.71e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 9.71e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 471434838   668 GVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLI 721
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
701-754 1.14e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 1.14e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 471434838   701 GLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLL 754
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
753-807 1.44e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.35  E-value: 1.44e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 471434838   753 LLQH-QADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIA 807
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
146-197 1.57e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 1.57e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 471434838   146 TPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAHLI 197
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
505-556 2.28e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 2.28e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 471434838   505 TPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALALL 556
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
68-187 2.50e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.35  E-value: 2.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   68 GVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQD-EVVRELVNYGANVNAQSQ-KGF 145
Cdd:PHA02878  191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGL 270
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 471434838  146 TPLYMAAQENhlEVVKFLLENGANQNVATEDGFTPLAVALQQ 187
Cdd:PHA02878  271 TALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
206-259 2.53e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 2.53e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 471434838   206 RLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLL 259
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
44-174 2.56e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 2.56e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   44 DAATSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQ 123
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 471434838  124 DEVVRELVNYGANVNAQSQKG-FTPLYMAAQENHLEVVKFLLENGANQNVAT 174
Cdd:PHA02875  181 IAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
510-678 3.75e-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: 58.17  E-value: 3.75e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   510 AARIGHTGMVKLLLENGAS--PNLATTAGHTPLHTAAREGHVDTALALLEKEASQACMtkkGFTPLHVAAKyGKVRLAEL 587
Cdd:TIGR00870   24 AAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENENLELTELLLNLSCRGAV---GDTLLHAISL-EYVDAVEA 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   588 LLEH--DAHP--------NAAGKN----GLTPLHVAVHHNNLDIVKLLLPRGG-------------SPHSP-AWNGYTPL 639
Cdd:TIGR00870  100 ILLHllAAFRksgplelaNDQYTSeftpGITALHLAAHRQNYEIVKLLLERGAsvparacgdffvkSQGVDsFYHGESPL 179
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 471434838   640 HIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQE 678
Cdd:TIGR00870  180 NAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVME 218
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
118-265 3.92e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.34  E-value: 3.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  118 AALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENV----- 192
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIfrily 611
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 471434838  193 -VAHLINYGTKGKVrlpaLHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASV 265
Cdd:PLN03192  612 hFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_5 pfam13857
Ankyrin repeats (many copies);
130-184 6.70e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 6.70e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 471434838   130 LVNYG-ANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVA 184
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
125-367 7.17e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 57.15  E-value: 7.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  125 EVVRELVNYGANVNAQSQKGFTPLYMAAQE---NHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHenvvahlinygt 201
Cdd:PHA02798   90 DIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNH------------ 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  202 kgkvrlpalHIaarndDTRTAAVLLQNDPNPDVLS-KTGFTPLHIAAHYE----NLNVAQLLLNRGASVN----FTPQNG 272
Cdd:PHA02798  158 ---------HI-----DIEIIKLLLEKGVDINTHNnKEKYDTLHCYFKYNidriDADILKLFVDNGFIINkenkSHKKKF 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  273 I---TPLHIASRRGNVIMVRLLLdrgAQIETRTKDEL--TPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQ 347
Cdd:PHA02798  224 MeylNSLLYDNKRFKKNILDFIF---SYIDINQVDELgfNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFE 300
                         250       260
                  ....*....|....*....|
gi 471434838  348 GDHLDCVRLLLQYNAEIDDI 367
Cdd:PHA02798  301 NESKFIFNSILNKKPNKNTI 320
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
422-490 7.34e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 7.34e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 471434838  422 LLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLL 490
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
720-774 8.23e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 8.23e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 471434838   720 LIKHG-VTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQA 774
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
257-312 8.90e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.04  E-value: 8.90e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 471434838   257 LLLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCA 312
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
618-689 9.24e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 9.24e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 471434838  618 VKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLS 689
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
343-425 9.48e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 9.48e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  343 HMAAQGDHLDcVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMEL 422
Cdd:PTZ00322   88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                  ...
gi 471434838  423 LLK 425
Cdd:PTZ00322  167 LSR 169
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
675-851 1.10e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.80  E-value: 1.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  675 AAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLL 754
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  755 QHQADVNAKTklGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVLkvVTDETSVVLVSDK 834
Cdd:PLN03192  612 HFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL--IMNGADVDKANTD 687
                         170
                  ....*....|....*..
gi 471434838  835 HRMSyPETVDEILDVSE 851
Cdd:PLN03192  688 DDFS-PTELRELLQKRE 703
Ank_5 pfam13857
Ankyrin repeats (many copies);
567-609 1.15e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.04  E-value: 1.15e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 471434838   567 KKGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVA 609
Cdd:pfam13857   14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
536-589 1.20e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 1.20e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 471434838   536 GHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLL 589
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
538-635 1.69e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 1.69e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  538 TPLHTAAREGHVDTALA---------------------LLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLEHDAHPN 596
Cdd:PTZ00322   63 TPDHNLTTEEVIDPVVAhmltvelcqlaasgdavgariLLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPT 142
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 471434838  597 AAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNG 635
Cdd:PTZ00322  143 LLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANA 181
Ank_4 pfam13637
Ankyrin repeats (many copies);
602-655 1.76e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 1.76e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 471434838   602 GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQIEVARSLL 655
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02989 PHA02989
ankyrin repeat protein; Provisional
516-817 2.04e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 55.52  E-value: 2.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  516 TGMVKLLLENGASPNlattaghtplhtaaREGHVDTAL-ALLEKEASQACMTKKgftplhvaakygkvrLAELLLEHDAH 594
Cdd:PHA02989   50 IKIVKLLIDNGADVN--------------YKGYIETPLcAVLRNREITSNKIKK---------------IVKLLLKFGAD 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  595 PNAAGKNGLTPLHVAVHH---NNLDIVKLLLPRGGSPHS-PAWNGYTPLHIAAKQNQI--EVARSLLQYGgsanaesvqg 668
Cdd:PHA02989  101 INLKTFNGVSPIVCFIYNsniNNCDMLRFLLSKGINVNDvKNSRGYNLLHMYLESFSVkkDVIKILLSFG---------- 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  669 VTPLHLAAQEGHTEMvalllskqaNGNLGNKsgltpLHLVSqeghVPVADVLIKHGVTVDATTRMGYTPL------HVAS 742
Cdd:PHA02989  171 VNLFEKTSLYGLTPM---------NIYLRND-----IDVIS----IKVIKYLIKKGVNIETNNNGSESVLesfldnNKIL 232
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 471434838  743 HYGNIKLVKFLLQHqADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTD 817
Cdd:PHA02989  233 SKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLN 306
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
157-341 2.14e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 2.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  157 LEVVKFLLENGAnQNVATEDGFTPLAVAlQQGHENVVAHLINYG-------TKGKVrlpALHIAARNDDTRTAAVLLQND 229
Cdd:PLN03192  507 LNVGDLLGDNGG-EHDDPNMASNLLTVA-STGNAALLEELLKAKldpdigdSKGRT---PLHIAASKGYEDCVLVLLKHA 581
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  230 PNPDVLSKTGFTPLH---IAAHYENLNVaqllLNRGASVNfTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDEL 306
Cdd:PLN03192  582 CNVHIRDANGNTALWnaiSAKHHKIFRI----LYHFASIS-DPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 471434838  307 TPLHCAARNGHVRISEILLDHGAPI-QAKTKNGLSP 341
Cdd:PLN03192  657 TALQVAMAEDHVDMVRLLIMNGADVdKANTDDDFSP 692
Ank_5 pfam13857
Ankyrin repeats (many copies);
588-642 2.37e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 2.37e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 471434838   588 LLEHD-AHPNAAGKNGLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIA 642
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
325-596 3.36e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 55.09  E-value: 3.36e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   325 LDHGAPIQAKTKN--GLSPIHMAA-QGDHLDCVRLLLQYNAEIDdiTLDHLtpLHVAAHCGHHRVAKVLLDKGAKP---- 397
Cdd:TIGR00870   37 LEEPKKLNINCPDrlGRSALFVAAiENENLELTELLLNLSCRGA--VGDTL--LHAISLEYVDAVEAILLHLLAAFrksg 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   398 -----NSRALNGFTPlhiackknhirvmelllktgasidavtesGLTPLHVASFMGHLPIVKNLLQRGASPNVS---NVK 469
Cdd:TIGR00870  113 plelaNDQYTSEFTP-----------------------------GITALHLAAHRQNYEIVKLLLERGASVPARacgDFF 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   470 VETPLHMAARAGhtevakyllqnkakanakakddQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHV 549
Cdd:TIGR00870  164 VKSQGVDSFYHG----------------------ESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEF 221
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   550 ------------DTALALLEKEAS----QACMTKKGFTPLHVAAKYGKVRLAELLL-------EHDAHPN 596
Cdd:TIGR00870  222 kaeyeelscqmyNFALSLLDKLRDskelEVILNHQGLTPLKLAAKEGRIVLFRLKLaikykqkKFVAWPN 291
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
673-756 3.86e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 3.86e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  673 HLAAQeGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKF 752
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                  ....
gi 471434838  753 LLQH 756
Cdd:PTZ00322  167 LSRH 170
PHA02859 PHA02859
ankyrin repeat protein; Provisional
736-835 4.48e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 52.51  E-value: 4.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  736 TPLH--VASHYGNIKLVKFLLQHQADVNAKTK-LGYSPLH---QAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIakR 809
Cdd:PHA02859   53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRdNNLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLLHM--Y 130
                          90       100
                  ....*....|....*....|....*..
gi 471434838  810 LGYISV-TDVLKVVTDETSVVLVSDKH 835
Cdd:PHA02859  131 MCNFNVrINVIKLLIDSGVSFLNKDFD 157
Ank_5 pfam13857
Ankyrin repeats (many copies);
225-279 5.35e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 5.35e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 471434838   225 LLQNDP-NPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIA 279
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
49-326 5.69e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 54.32  E-value: 5.69e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838    49 FLRAARSGNLDKALDHLRNG--VDINTCNQNGLNGLHLASKEGHVKMVVELLHKeiiLETTTKKGNTALHIAALAGQDeV 126
Cdd:TIGR00870   21 FLPAAERGDLASVYRDLEEPkkLNINCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISLEYVD-A 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   127 VRELVNYGAN----------VNAQS----QKGFTPLYMAAQENHLEVVKFLLENGANQNV-ATEDGFTplavaLQQGHEn 191
Cdd:TIGR00870   97 VEAILLHLLAafrksgplelANDQYtsefTPGITALHLAAHRQNYEIVKLLLERGASVPArACGDFFV-----KSQGVD- 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   192 vvahLINYGtkgkvRLPaLHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPLHIA-------AHYENL-----NVAQLLL 259
Cdd:TIGR00870  171 ----SFYHG-----ESP-LNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLvmenefkAEYEELscqmyNFALSLL 240
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 471434838   260 NRGAS-------VNFtpqNGITPLHIASRRGNVIMVRLLLdrgaQIETRTKDeltplHCAARNGHVRISEILLD 326
Cdd:TIGR00870  241 DKLRDskeleviLNH---QGLTPLKLAAKEGRIVLFRLKL----AIKYKQKK-----FVAWPNGQQLLSLYWLE 302
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
100-269 6.08e-07

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: 54.12  E-value: 6.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  100 KEIILETTTK---KGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGF-------------TPLYMAAQENHLEVVKFL 163
Cdd:cd21882    59 KELVNAPCTDefyQGQTALHIAIENRNLNLVRLLVENGADVSARATGRFfrkspgnlfyfgeLPLSLAACTNQEEIVRLL 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  164 LENGANqnvatedgftPLAVALQQGHENVVAHLINYGTKGKVRLPALHIAARNDDTRTAAVLLQNDPNPDVLSKTGFTPL 243
Cdd:cd21882   139 LENGAQ----------PAALEAQDSLGNTVLHALVLQADNTPENSAFVCQMYNLLLSYGAHLDPTQQLEEIPNHQGLTPL 208
                         170       180
                  ....*....|....*....|....*.
gi 471434838  244 HIAAHYENLNVAQLLLNRGASVNFTP 269
Cdd:cd21882   209 KLAAVEGKIVMFQHILQREFSGPYQP 234
PHA02736 PHA02736
Viral ankyrin protein; Provisional
336-431 6.17e-07

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 50.65  E-value: 6.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  336 KNGLSPIHMAAQGDHLDC---VRLLLQYNAEID-DITLDHLTPLHVAAHCGHHRVAKVLLDKgAKPNSRALNGF--TPLH 409
Cdd:PHA02736   53 RHGKQCVHIVSNPDKADPqekLKLLMEWGADINgKERVFGNTPLHIAVYTQNYELATWLCNQ-PGVNMEILNYAfkTPYY 131
                          90       100
                  ....*....|....*....|..
gi 471434838  410 IACKKNHIRVMELLLKTGASID 431
Cdd:PHA02736  132 VACERHDAKMMNILRAKGAQCK 153
PHA02798 PHA02798
ankyrin-like protein; Provisional
581-807 7.97e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 53.69  E-value: 7.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  581 KVRLAELLLEHDAHPNAAGKNGLTPL-----HVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQ---NQIEVAR 652
Cdd:PHA02798   50 STDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILL 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  653 SLLQYGGSANAESVQGVTPLHLAAQEGHT---EMVALLLSKQANGNL-GNKSGLTPLHLVSQEG----HVPVADVLIKHG 724
Cdd:PHA02798  130 FMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNidriDADILKLFVDNG 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  725 VTV---DATTRMGYTPLHVASHYGNIK----LVKFLLQHqADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVS 797
Cdd:PHA02798  210 FIInkeNKSHKKKFMEYLNSLLYDNKRfkknILDFIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIIT 288
                         250
                  ....*....|
gi 471434838  798 SNGTTPLAIA 807
Cdd:PHA02798  289 ELGNTCLFTA 298
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
734-765 8.42e-07

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: 425426 [Multi-domain]  Cd Length: 34  Bit Score: 46.90  E-value: 8.42e-07
                           10        20        30
                   ....*....|....*....|....*....|...
gi 471434838   734 GYTPLHVAS-HYGNIKLVKFLLQHQADVNAKTK 765
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
403-432 9.46e-07

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: 46.43  E-value: 9.46e-07
                            10        20        30
                    ....*....|....*....|....*....|
gi 471434838    403 NGFTPLHIACKKNHIRVMELLLKTGASIDA 432
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
767-819 1.01e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 1.01e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 471434838   767 GYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVL 819
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Death_RAIDD cd08319
Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) ...
1433-1508 1.15e-06

Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) of RAIDD (RIP-associated ICH-1 homologous protein with a death domain), also known as CRADD (Caspase and RIP adaptor). RAIDD is an adaptor protein that together with the p53-inducible protein PIDD and caspase-2, forms the PIDDosome complex, which is required for caspase-2 activation and plays a role in mediating stress-induced apoptosis. RAIDD contains an N-terminal Caspase Activation and Recruitment Domain (CARD), which interacts with the caspase-2 CARD, and a C-terminal DD, which interacts with the DD of PIDD. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD, DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260031  Cd Length: 83  Bit Score: 48.09  E-value: 1.15e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 471434838 1433 TDRVEMRMAvirEHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNID 1508
Cdd:cd08319     1 TDRQLNKLA---QRLGPEWEQVLLDLGLSKADIYRCKADHPYNVQSQIVEALVKWKQRQGKKATVQSLIQSLKAVE 73
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
632-754 1.23e-06

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: 53.22  E-value: 1.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  632 AWNGYTPLHIAAKQNQIEVARSLLQYGGSANAESvQGV---------------TPLHLAAQEGHTEMVALLLSK-QANGN 695
Cdd:cd22194   138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHA-KGVffnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKeSTDIT 216
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 471434838  696 LGNKSGLTPLHLVsqeghVPVAD---------------VLIKHGVTVDATTR--MGYTPLHVASHYGNIKLVKFLL 754
Cdd:cd22194   217 SQDSRGNTVLHAL-----VTVAEdsktqndfvkrmydmILLKSENKNLETIRnnEGLTPLQLAAKMGKAEILKYIL 287
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
116-199 1.27e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 1.27e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  116 HIAAlAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENVVAH 195
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                  ....
gi 471434838  196 LINY 199
Cdd:PTZ00322  167 LSRH 170
PHA02946 PHA02946
ankyin-like protein; Provisional
258-441 1.28e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 52.75  E-value: 1.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  258 LLNRGASVNFTPQNGITPLHIASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAARNGHVRISEI--LLDHGAPIQAKT 335
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERInlLVQYGAKINNSV 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  336 -KNGLSPIHMAAQGDHLDCVRLL-LQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIACK 413
Cdd:PHA02946  138 dEEGCGPLLACTDPSERVFKKIMsIGFEARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCS 217
                         170       180       190
                  ....*....|....*....|....*....|
gi 471434838  414 KN--HIRVMELLLKTgASIDAVTESGLTPL 441
Cdd:PHA02946  218 KTvkNVDIINLLLPS-TDVNKQNKFGDSPL 246
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
58-261 1.34e-06

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: 53.27  E-value: 1.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   58 LDKALDHLRNGVdintcNQNGLNGLHLASKEGHVKMVVELLHKEiiletTTKKGNTALHIAALAGQDEVVRELVNYGANV 137
Cdd:cd22196    51 LLKAMLNLHNGQ-----NDTISLLLDIAEKTGNLKEFVNAAYTD-----SYYKGQTALHIAIERRNMHLVELLVQNGADV 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  138 NA----------QSQKGF----TPLYMAAQENHLEVVKFLLENGANQ-NVATEDGFTplavalqqgheNVVAHlinygtk 202
Cdd:cd22196   121 HArasgeffkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLENPHSPaDISARDSMG-----------NTVLH------- 182
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 471434838  203 gkvrlpALHIAARNDDTRTAAV--------LLQNDPNP-----DVLSKTGFTPLHIAAHYENLNVAQLLLNR 261
Cdd:cd22196   183 ------ALVEVADNTPENTKFVtkmyneilILGAKIRPllkleEITNKKGLTPLKLAAKTGKIGIFAYILGR 248
Ank_5 pfam13857
Ankyrin repeats (many copies);
654-708 1.37e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 1.37e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 471434838   654 LLQYGG-SANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLV 708
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
733-762 1.70e-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: 45.66  E-value: 1.70e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 471434838    733 MGYTPLHVASHYGNIKLVKFLLQHQADVNA 762
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
475-556 1.74e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 1.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  475 HMAArAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTAAREGHVDTALA 554
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                  ..
gi 471434838  555 LL 556
Cdd:PTZ00322  167 LS 168
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
111-294 1.96e-06

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 52.57  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  111 GNTALHIAALAGQD----------EVVRELVNYGANVNAQSQ----KGFTPLYMAAQENHLEVVKFLLENGAN-QNVATE 175
Cdd:cd21882    26 GKTCLHKAALNLNDgvneaimlllEAAPDSGNPKELVNAPCTdefyQGQTALHIAIENRNLNLVRLLVENGADvSARATG 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  176 DGFT------------PLAVALQQGHENVVAHLINYGTKgkvrlPAlHIAARND--DTRTAAVLLQNDPNPDvlsKTGFt 241
Cdd:cd21882   106 RFFRkspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQ-----PA-ALEAQDSlgNTVLHALVLQADNTPE---NSAF- 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  242 plhiAAHYENlnvaqLLLNRGASVNFTPQ-------NGITPLHIASRRGNVIMVRLLLDR 294
Cdd:cd21882   176 ----VCQMYN-----LLLSYGAHLDPTQQleeipnhQGLTPLKLAAVEGKIVMFQHILQR 226
PHA02989 PHA02989
ankyrin repeat protein; Provisional
125-294 2.26e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 52.05  E-value: 2.26e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  125 EVVRELVNYGANVNA-QSQKGFTPLYMAAQENHL--EVVKFLLENGANQNVATE-DGFTPLAVALQQGHENVVAHLINYG 200
Cdd:PHA02989  125 DMLRFLLSKGINVNDvKNSRGYNLLHMYLESFSVkkDVIKILLSFGVNLFEKTSlYGLTPMNIYLRNDIDVISIKVIKYL 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  201 TKGKVRLP---ALHIAARNDDTRTAAVLLQND----------PNPDVLSKTGFTPLHIAAHYENLNVAQLLLNRGASVNF 267
Cdd:PHA02989  205 IKKGVNIEtnnNGSESVLESFLDNNKILSKKEfkvlnfilkyIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYN 284
                         170       180
                  ....*....|....*....|....*..
gi 471434838  268 TPQNGITPLHIASRRGNVIMVRLLLDR 294
Cdd:PHA02989  285 VSKDGDTVLTYAIKHGNIDMLNRILQL 311
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
734-762 2.56e-06

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


Pssm-ID: 404492 [Multi-domain]  Cd Length: 30  Bit Score: 45.33  E-value: 2.56e-06
                           10        20
                   ....*....|....*....|....*....
gi 471434838   734 GYTPLHVASHYGNIKLVKFLLQHQADVNA 762
Cdd:pfam13606    2 GNTPLHLAARNGNLEIVKLLLERGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
143-172 2.60e-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: 45.27  E-value: 2.60e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 471434838    143 KGFTPLYMAAQENHLEVVKFLLENGANQNV 172
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
417-598 3.54e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.79  E-value: 3.54e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  417 IRVMELLLK-TGASIDAVTESGLtpLHVASfMGHLPIVKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAK 495
Cdd:PLN03192  507 LNVGDLLGDnGGEHDDPNMASNL--LTVAS-TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN 583
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  496 ANAKAKDDQTPLHCAARIGHTGMVKLLLENGASPNlaTTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKGFTPLHV 575
Cdd:PLN03192  584 VHIRDANGNTALWNAISAKHHKIFRILYHFASISD--PHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQV 661
                         170       180
                  ....*....|....*....|...
gi 471434838  576 AAKYGKVRLAELLLEHDAHPNAA 598
Cdd:PLN03192  662 AMAEDHVDMVRLLIMNGADVDKA 684
PHA02859 PHA02859
ankyrin repeat protein; Provisional
241-338 4.18e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 49.43  E-value: 4.18e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  241 TPLH--IAAHYENLNVAQLLLNRGASVNF-TPQNGITPLH---IASRRGNVIMVRLLLDRGAQIETRTKDELTPLHCAAR 314
Cdd:PHA02859   53 TPIFscLEKDKVNVEILKFLIENGADVNFkTRDNNLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLLHMYMC 132
                          90       100
                  ....*....|....*....|....*.
gi 471434838  315 NGHVRIS--EILLDHGAPIQAKTKNG 338
Cdd:PHA02859  133 NFNVRINviKLLIDSGVSFLNKDFDN 158
Ank_5 pfam13857
Ankyrin repeats (many copies);
422-477 4.63e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 4.63e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 471434838   422 LLLKTGASIDAVTESGLTPLHVASFMGHLPIVKNLLQRGASPNVSNVKVETPLHMA 477
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
234-573 4.74e-06

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 51.45  E-value: 4.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  234 VLSKTGFTPLH--IAAHYENLNVAQLLLNRGASVNFTPQNGITPLHIASRRGNVI--MVRLLLDRGAQIETRTKDELTPL 309
Cdd:PHA02716  172 VCKKTGYGILHayLGNMYVDIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNVCasVIKKIIELGGDMDMKCVNGMSPI 251
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  310 HCAARNGHVRISEILLDHGAPIQA-KTKNGLSPIHM---AAQGDHLDCVRLLLQYNAEIDDITLDHLTPLH--VAAHCGH 383
Cdd:PHA02716  252 MTYIINIDNINPEITNIYIESLDGnKVKNIPMILHSyitLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNIS 331
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  384 HRVAKVLLDKGAKPNSRALNGFTPLHIACKK------------NHIR--VMELLLKTGASIDAVTESGLTPL-----HVA 444
Cdd:PHA02716  332 TDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMlsvvnildpetdNDIRldVIQCLISLGADITAVNCLGYTPLtsyicTAQ 411
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  445 SFMGHLPI-------VKNLLQRGASPNVSNVKVETPlhmaaRAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAArigHTG 517
Cdd:PHA02716  412 NYMYYDIIdclisdkVLNMVKHRILQDLLIRVDDTP-----CIIHHIIAKYNIPTDLYTDEYEPYDSTKIHDVY---HCA 483
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 471434838  518 MVKLLlengaSPNLATTAGHTPLHTAAREGH-----VDTALALLEKEASQACMTKKGFTPL 573
Cdd:PHA02716  484 IIERY-----NNAVCETSGMTPLHVSIISHTnanivMDSFVYLLSIQYNINIPTKNGVTPL 539
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
502-533 4.92e-06

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


Pssm-ID: 425426 [Multi-domain]  Cd Length: 34  Bit Score: 44.59  E-value: 4.92e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 471434838   502 DDQTPLHCAA-RIGHTGMVKLLLENGASPNLAT 533
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02798 PHA02798
ankyrin-like protein; Provisional
149-444 5.05e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 50.99  E-value: 5.05e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  149 YMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALqqghenvvAHLINYGTKGKVRLpalhiaarnddtrtaaVLLQN 228
Cdd:PHA02798   43 YLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLCTIL--------SNIKDYKHMLDIVK----------------ILIEN 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  229 DPNPDVLSKTGFTPLHIAAHYENLNVAQLLL---NRGASVNFTPQNGITPLHIASRRGNVI---MVRLLLDRGAQIETRT 302
Cdd:PHA02798   99 GADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDINTHN 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  303 KDE-LTPLHCAARNGHVRIS----EILLDHGAPIQAKTKNGLSPIhmaaqgdhLDCVRLLLQYNAEIDDITLDhltplhv 377
Cdd:PHA02798  179 NKEkYDTLHCYFKYNIDRIDadilKLFVDNGFIINKENKSHKKKF--------MEYLNSLLYDNKRFKKNILD------- 243
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 471434838  378 aahcghhrvakvLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVA 444
Cdd:PHA02798  244 ------------FIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
Ank_5 pfam13857
Ankyrin repeats (many copies);
635-675 5.16e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 5.16e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 471434838   635 GYTPLHIAAKQNQIEVARSLLQYGGSANAESVQGVTPLHLA 675
Cdd:pfam13857   16 GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
568-691 6.50e-06

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: 50.91  E-value: 6.50e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  568 KGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKN--------------GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPAW 633
Cdd:cd22194   140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQD 219
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 471434838  634 N-GYTPLH---IAAKQNQ------IEVARSLLQYGGSANAESV---QGVTPLHLAAQEGHTEMVALLLSKQ 691
Cdd:cd22194   220 SrGNTVLHalvTVAEDSKtqndfvKRMYDMILLKSENKNLETIrnnEGLTPLQLAAKMGKAEILKYILSRE 290
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
403-435 7.42e-06

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


Pssm-ID: 425426 [Multi-domain]  Cd Length: 34  Bit Score: 44.20  E-value: 7.42e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 471434838   403 NGFTPLHIACKK-NHIRVMELLLKTGASIDAVTE 435
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
664-812 7.85e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.83  E-value: 7.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  664 ESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVASH 743
Cdd:PHA02876  141 ESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVD 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  744 YGNIKLVKFLLQHQADVNA--------------KTKL-----GYS----------PLHQAAQQGH-TDIVTLLLKNGASP 793
Cdd:PHA02876  221 SKNIDTIKAIIDNRSNINKndlsllkairnedlETSLllydaGFSvnsiddckntPLHHASQAPSlSRLVPKLLERGADV 300
                         170
                  ....*....|....*....
gi 471434838  794 NEVSSNGTTPLAIAKRLGY 812
Cdd:PHA02876  301 NAKNIKGETPLYLMAKNGY 319
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
110-140 8.77e-06

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


Pssm-ID: 425426 [Multi-domain]  Cd Length: 34  Bit Score: 43.82  E-value: 8.77e-06
                           10        20        30
                   ....*....|....*....|....*....|..
gi 471434838   110 KGNTALHIAAL-AGQDEVVRELVNYGANVNAQ 140
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
110-261 8.82e-06

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: 50.56  E-value: 8.82e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  110 KGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGF--------------TPLYMAAQENHLEVVKFLLENganqnvate 175
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLEN--------- 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  176 dGFTPLAVALQQGHENVVAHlinygtkgkvrlpALHIAARNDDTRTAAV------LLQNDPN--PDV-----LSKTGFTP 242
Cdd:cd22193   146 -EHQPADIEAQDSRGNTVLH-------------ALVTVADNTKENTKFVtrmydmILIRGAKlcPTVeleeiRNNDGLTP 211
                         170
                  ....*....|....*....
gi 471434838  243 LHIAAHYENLNVAQLLLNR 261
Cdd:cd22193   212 LQLAAKMGKIEILKYILQR 230
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
110-139 9.65e-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: 43.73  E-value: 9.65e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 471434838    110 KGNTALHIAALAGQDEVVRELVNYGANVNA 139
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
291-345 1.12e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 1.12e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 471434838   291 LLDRG-AQIETRTKDELTPLHCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMA 345
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
640-723 1.16e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  640 HIAAKQNQIEvARSLLQYGGSANAESVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADV 719
Cdd:PTZ00322   88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                  ....
gi 471434838  720 LIKH 723
Cdd:PTZ00322  167 LSRH 170
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
546-691 1.21e-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: 50.19  E-value: 1.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  546 EGHVDTALALLE--------KEASQACMTK---KGFTPLHVAAKYGKVRLAELLLEHDAHPNAA----------GKNGL- 603
Cdd:cd22196    60 NGQNDTISLLLDiaektgnlKEFVNAAYTDsyyKGQTALHIAIERRNMHLVELLVQNGADVHARasgeffkkkkGGPGFy 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  604 ---TPLHVAVHHNNLDIVKLLLPrggSPHSPA------WNGYTPLH--IAAKQNQIEVAR-------SLLQYGG----SA 661
Cdd:cd22196   140 fgeLPLSLAACTNQLDIVKFLLE---NPHSPAdisardSMGNTVLHalVEVADNTPENTKfvtkmynEILILGAkirpLL 216
                         170       180       190
                  ....*....|....*....|....*....|...
gi 471434838  662 NAESV---QGVTPLHLAAQEGHTEMVALLLSKQ 691
Cdd:cd22196   217 KLEEItnkKGLTPLKLAAKTGKIGIFAYILGRE 249
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
201-462 1.40e-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: 49.88  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  201 TKGKVRLPALHIAARNDDTR---TAAVLLQNDPNPDVLSKTGFTPLhIAAHYEnlnvaqlllnrgasvnftpqnGITPLH 277
Cdd:cd21882    21 QRGATGKTCLHKAALNLNDGvneAIMLLLEAAPDSGNPKELVNAPC-TDEFYQ---------------------GQTALH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  278 IASRRGNVIMVRLLLDRGAQIETRTKdeltplhcaarnghvriseilldhGAPIQAKTKNGL----SPIHMAAQGDHLDC 353
Cdd:cd21882    79 IAIENRNLNLVRLLVENGADVSARAT------------------------GRFFRKSPGNLFyfgeLPLSLAACTNQEEI 134
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  354 VRLLLQYNAEIDDITL-DHL--TPLHvaahcghhrvAKVLLDKGAKPNSRalngftplhIACKknhirVMELLLKTGA-- 428
Cdd:cd21882   135 VRLLLENGAQPAALEAqDSLgnTVLH----------ALVLQADNTPENSA---------FVCQ-----MYNLLLSYGAhl 190
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 471434838  429 ----SIDAVT-ESGLTPLHVASFMGHLPIVKNLLQRGAS 462
Cdd:cd21882   191 dptqQLEEIPnHQGLTPLKLAAVEGKIVMFQHILQREFS 229
PHA03100 PHA03100
ankyrin repeat protein; Provisional
65-139 1.50e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 49.28  E-value: 1.50e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 471434838   65 LRNGVDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNA 139
Cdd:PHA03100  179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
750-819 1.50e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 1.50e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  750 VKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGYISVTDVL 819
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_4 pfam13637
Ankyrin repeats (many copies);
82-131 1.55e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 1.55e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 471434838    82 LHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIAALAGQDEVVRELV 131
Cdd:pfam13637    5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
601-629 1.56e-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: 42.96  E-value: 1.56e-05
                            10        20
                    ....*....|....*....|....*....
gi 471434838    601 NGLTPLHVAVHHNNLDIVKLLLPRGGSPH 629
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
437-467 1.71e-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: 425426 [Multi-domain]  Cd Length: 34  Bit Score: 43.05  E-value: 1.71e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 471434838   437 GLTPLHVASFM-GHLPIVKNLLQRGASPNVSN 467
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
97-151 2.12e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 2.12e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 471434838    97 LLHKEIILETTTKKGNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMA 151
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
614-837 2.16e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 49.53  E-value: 2.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  614 NLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQI--EVARSLLQYGGSANAESVQGVTPL--HLAAQEGHTEMVALLLS 689
Cdd:PHA02716  191 DIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNVcaSVIKKIIELGGDMDMKCVNGMSPImtYIINIDNINPEITNIYI 270
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  690 KQANGNlgnKSGLTP--LHL---VSQEGHVPVADVLIKHGVTVDATTRMGYTPLH--VASHYGNIKLVKFLLQHQADVNA 762
Cdd:PHA02716  271 ESLDGN---KVKNIPmiLHSyitLARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNE 347
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  763 KTKLGYSPLH--------------QAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLA----IAKRLGYISVTDVLkvVTD 824
Cdd:PHA02716  348 PDNIGNTVLHtylsmlsvvnildpETDNDIRLDVIQCLISLGADITAVNCLGYTPLTsyicTAQNYMYYDIIDCL--ISD 425
                         250
                  ....*....|...
gi 471434838  825 EtsvVLVSDKHRM 837
Cdd:PHA02716  426 K---VLNMVKHRI 435
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
502-531 2.36e-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: 42.57  E-value: 2.36e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 471434838    502 DDQTPLHCAARIGHTGMVKLLLENGASPNL 531
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
734-804 2.36e-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: 49.03  E-value: 2.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  734 GYTPLHVASHYGNIKLVKFLLQHQADVNA--------KTK------LGYSPLHQAAQQGHTDIVTLLLKNGASPNEVS-- 797
Cdd:cd22196    94 GQTALHIAIERRNMHLVELLVQNGADVHArasgeffkKKKggpgfyFGELPLSLAACTNQLDIVKFLLENPHSPADISar 173

                  ....*...
gi 471434838  798 -SNGTTPL 804
Cdd:cd22196   174 dSMGNTVL 181
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
1450-1517 2.64e-05

Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin receptor (p75NTR, NGFR, TNFRSF16). p75NTR binds members of the neurotrophin (NT) family including nerve growth factor (NGF), brain-derived neurotrophic factor (BDNF), and NT3, among others. It contains an NT-binding extracellular region that bears four cysteine-rich repeats, a transmembrane domain, and an intracellular DD. p75NTR plays roles in the immune, vascular, and nervous systems, and has been shown to promote cell death or survival, and to induce neurite outgrowth or collapse depending on its ligands and co-receptors. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260025  Cd Length: 80  Bit Score: 43.81  E-value: 2.64e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 471434838 1450 SWAELARELQFSVEDINRI-RVENPnslldqSTALLTLWVDREGenAKMENLYTALRNIDRSEIVNMLE 1517
Cdd:cd08311    20 DWRALAGELGYSAEEIDSFaREADP------CRALLTDWSAQDG--ATLGVLLTALRKIGRDDIVEILQ 80
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
602-720 2.78e-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: 49.03  E-value: 2.78e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  602 GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPA--------------WNGYTPLHIAAKQNQIEVARSLLQYGGSA---NAE 664
Cdd:cd22196    94 GQTALHIAIERRNMHLVELLVQNGADVHARAsgeffkkkkggpgfYFGELPLSLAACTNQLDIVKFLLENPHSPadiSAR 173
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 471434838  665 SVQGVTPLH-LAAQEGHTEMVALLLSKQANG---------------NLGNKSGLTPLHLVSQEGHVPV-ADVL 720
Cdd:cd22196   174 DSMGNTVLHaLVEVADNTPENTKFVTKMYNEililgakirpllkleEITNKKGLTPLKLAAKTGKIGIfAYIL 246
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
239-266 2.98e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 2.98e-05
                            10        20
                    ....*....|....*....|....*...
gi 471434838    239 GFTPLHIAAHYENLNVAQLLLNRGASVN 266
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
324-378 3.05e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 3.05e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 471434838   324 LLDHG-APIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVA 378
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
717-800 3.07e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 3.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  717 ADVLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEV 796
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177

                  ....
gi 471434838  797 SSNG 800
Cdd:PTZ00322  178 GANA 181
Ank_5 pfam13857
Ankyrin repeats (many copies);
504-543 3.30e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 3.30e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 471434838   504 QTPLHCAARIGHTGMVKLLLENGASPNLATTAGHTPLHTA 543
Cdd:pfam13857   17 YTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
271-303 3.57e-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: 425426 [Multi-domain]  Cd Length: 34  Bit Score: 42.28  E-value: 3.57e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 471434838   271 NGITPLHIAS-RRGNVIMVRLLLDRGAQIETRTK 303
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
271-299 4.04e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.80  E-value: 4.04e-05
                            10        20
                    ....*....|....*....|....*....
gi 471434838    271 NGITPLHIASRRGNVIMVRLLLDRGAQIE 299
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
686-741 4.22e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 4.22e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 471434838   686 LLLSKQANGNLGNKSGLTPLHLVSQEGHVPVADVLIKHGVTVDATTRMGYTPLHVA 741
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
143-175 4.79e-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: 425426 [Multi-domain]  Cd Length: 34  Bit Score: 41.89  E-value: 4.79e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 471434838   143 KGFTPLYMAA-QENHLEVVKFLLENGANQNVATE 175
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
110-139 4.81e-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: 404492 [Multi-domain]  Cd Length: 30  Bit Score: 41.86  E-value: 4.81e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 471434838   110 KGNTALHIAALAGQDEVVRELVNYGANVNA 139
Cdd:pfam13606    1 DGNTPLHLAARNGNLEIVKLLLERGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
354-490 5.40e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 47.83  E-value: 5.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  354 VRLLLQY-----------NAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRA----------LNGF----TPL 408
Cdd:cd22194   113 VRILLAFaeengildrfiNAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykHEGFyfgeTPL 192
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  409 HIACKKNHIRVMELLLKTGASIDAVTES-GLTPLH----VA-SFMGHLPIVKNL----LQRGASPN---VSNVKVETPLH 475
Cdd:cd22194   193 ALAACTNQPEIVQLLMEKESTDITSQDSrGNTVLHalvtVAeDSKTQNDFVKRMydmiLLKSENKNletIRNNEGLTPLQ 272
                         170
                  ....*....|....*
gi 471434838  476 MAARAGHTEVAKYLL 490
Cdd:cd22194   273 LAAKMGKAEILKYIL 287
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
403-432 5.46e-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.


Pssm-ID: 404492 [Multi-domain]  Cd Length: 30  Bit Score: 41.48  E-value: 5.46e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 471434838   403 NGFTPLHIACKKNHIRVMELLLKTGASIDA 432
Cdd:pfam13606    1 DGNTPLHLAARNGNLEIVKLLLERGADINA 30
PHA02884 PHA02884
ankyrin repeat protein; Provisional
218-314 5.57e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 46.90  E-value: 5.57e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  218 DTRTAAVLLQNDPN-PDVLSKTGFT-PLHIAAHYENLNVAQLLLNRGASVN-FTPQNGITPLHIASRRGNVIMVRLLLDR 294
Cdd:PHA02884   47 DIIDAILKLGADPEaPFPLSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNrYAEEAKITPLYISVLHGCLKCLEILLSY 126
                          90       100
                  ....*....|....*....|
gi 471434838  295 GAQIETRTKDELTPLHCAAR 314
Cdd:PHA02884  127 GADINIQTNDMVTPIELALM 146
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
502-530 5.63e-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: 404492 [Multi-domain]  Cd Length: 30  Bit Score: 41.48  E-value: 5.63e-05
                           10        20
                   ....*....|....*....|....*....
gi 471434838   502 DDQTPLHCAARIGHTGMVKLLLENGASPN 530
Cdd:pfam13606    1 DGNTPLHLAARNGNLEIVKLLLERGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
337-366 5.64e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 5.64e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 471434838    337 NGLSPIHMAAQGDHLDCVRLLLQYNAEIDD 366
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
324-491 5.70e-05

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 47.87  E-value: 5.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  324 LLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQY-----------NAEIDDITLDHLTPLHVAAHCGHHRVAKVLLD 392
Cdd:cd22193    18 LTDSEFTESSTGKTCLMKALLNLNPGTNDTIRILLDIaektdnlkrfiNAEYTDEYYEGQTALHIAIERRQGDIVALLVE 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  393 KGAKPNSRALNGF--------------TPLHIACKKNHIRVMELLLK---TGASIDAVTESGLTPLH----VA-SFMGHL 450
Cdd:cd22193    98 NGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLHalvtVAdNTKENT 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 471434838  451 PIVKN----LLQRGAS-------PNVSNVKVETPLHMAARAGHTEVAKYLLQ 491
Cdd:cd22193   178 KFVTRmydmILIRGAKlcptvelEEIRNNDGLTPLQLAAKMGKIEILKYILQ 229
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
1443-1517 5.87e-05

Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD (p53-induced protein with a death domain) and similar proteins. PIDD is a component of the PIDDosome complex, which is an oligomeric caspase-activating complex involved in caspase-2 activation and plays a role in mediating stress-induced apoptosis. The PIDDosome complex is composed of three components, PIDD, RAIDD and caspase-2, which interact through their DDs and DD-like domains. The DD of PIDD interacts with the DD of RAIDD, which also contains a Caspase Activation and Recruitment Domain (CARD) that interacts with the caspase-2 CARD. Autoproteolysis of PIDD determines the downstream signaling event, between pro-survival NF-kB or pro-death caspase-2 activation. In general, DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD, DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260049  Cd Length: 86  Bit Score: 43.07  E-value: 5.87e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 471434838 1443 IREHLGLSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENA-KMENLYTALRNIDRSEIVNMLE 1517
Cdd:cd08779     8 LAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAKTLPTSPdKVGLLVTALSKSGRSDLAEELR 83
Ank_5 pfam13857
Ankyrin repeats (many copies);
356-411 6.57e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 6.57e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 471434838   356 LLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGFTPLHIA 411
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
370-400 7.52e-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: 425426 [Multi-domain]  Cd Length: 34  Bit Score: 41.12  E-value: 7.52e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 471434838   370 DHLTPLHVAA-HCGHHRVAKVLLDKGAKPNSR 400
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
276-491 7.70e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.38  E-value: 7.70e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   276 LHIASRRGNVIMVRLLLDRGAQIETrtkdELTPLHcAARNGHVRISEILLDHGAPIQAKTKNglspihmaaqgdhldcvr 355
Cdd:TIGR00870   57 FVAAIENENLELTELLLNLSCRGAV----GDTLLH-AISLEYVDAVEAILLHLLAAFRKSGP------------------ 113
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   356 LLLQYNAEIDDITLDHlTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNGF--------------TPLHIACKKNHIRVME 421
Cdd:TIGR00870  114 LELANDQYTSEFTPGI-TALHLAAHRQNYEIVKLLLERGASVPARACGDFfvksqgvdsfyhgeSPLNAAACLGSPSIVA 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   422 LLLKTGASIDAVTESGLTPLH----VASF--------MGHLPIVKNLLQRGASPN----VSNVKVETPLHMAARAGHTEV 485
Cdd:TIGR00870  193 LLSEDPADILTADSLGNTLLHllvmENEFkaeyeelsCQMYNFALSLLDKLRDSKelevILNHQGLTPLKLAAKEGRIVL 272

                   ....*.
gi 471434838   486 AKYLLQ 491
Cdd:TIGR00870  273 FRLKLA 278
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
239-266 7.98e-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: 425426 [Multi-domain]  Cd Length: 34  Bit Score: 41.12  E-value: 7.98e-05
                           10        20
                   ....*....|....*....|....*....
gi 471434838   239 GFTPLHIAA-HYENLNVAQLLLNRGASVN 266
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
Death_DRs cd08784
Death Domain of Death Receptors; Death domain (DD) found in death receptor proteins. Death ...
1449-1508 8.25e-05

Death Domain of Death Receptors; Death domain (DD) found in death receptor proteins. Death receptors are members of the tumor necrosis factor (TNF) receptor superfamily, characterized by having a cytoplasmic DD. Known members of the family are Fas (CD95/APO-1), TNF-receptor 1 (TNFR1/TNFRSF1A/p55/CD120a), TNF-related apoptosis-inducing ligand receptor 1 (TRAIL-R1 /DR4), and receptor 2 (TRAIL-R2/DR5/APO-2/KILLER), as well as Death Receptor 3 (DR3/APO-3/TRAMP/WSL-1/LARD). They are involved in apoptosis signaling pathways. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260054  Cd Length: 80  Bit Score: 42.56  E-value: 8.25e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838 1449 LSWAELARELQFSVEDINRIRVENPNSLLDQSTALLTLWVDREGENAKMENLYTALRNID 1508
Cdd:cd08784    12 SQWKGFVRKLGLNEAEIDEIKNDNVQDTAEAKYQMLRNWHQLTGRKAAYDTLIKDLKKMN 71
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
767-794 1.14e-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: 425426 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 1.14e-04
                           10        20
                   ....*....|....*....|....*....
gi 471434838   767 GYSPLHQAAQQ-GHTDIVTLLLKNGASPN 794
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
660-806 1.16e-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: 46.80  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  660 SANAESVQGVTPLHLAA---QEGHTEMVALLLskQANGNLGNksgltPLHLVSQeghvPVADVLIKhgvtvdattrmGYT 736
Cdd:cd21882    18 SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLL--EAAPDSGN-----PKELVNA----PCTDEFYQ-----------GQT 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  737 PLHVASHYGNIKLVKFLLQHQADVNAKTK-------------LGYSPLHQAAQQGHTDIVTLLLKNGASPNEVS---SNG 800
Cdd:cd21882    76 ALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQPAALEaqdSLG 155

                  ....*.
gi 471434838  801 TTPLAI 806
Cdd:cd21882   156 NTVLHA 161
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
370-398 1.19e-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: 40.65  E-value: 1.19e-04
                            10        20
                    ....*....|....*....|....*....
gi 471434838    370 DHLTPLHVAAHCGHHRVAKVLLDKGAKPN 398
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
437-465 1.34e-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: 40.65  E-value: 1.34e-04
                            10        20
                    ....*....|....*....|....*....
gi 471434838    437 GLTPLHVASFMGHLPIVKNLLQRGASPNV 465
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
453-523 1.45e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 1.45e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 471434838  453 VKNLLQRGASPNVSNVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDDQTPLHCAARIGHTGMVKLLL 523
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
596-757 1.57e-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: 46.39  E-value: 1.57e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  596 NAAGKN----GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPA-------------WNGYTPLHIAAKQNQIEVARSLLQyg 658
Cdd:cd22197    84 NAQCTDeyyrGHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqkkqgtcfYFGELPLSLAACTKQWDVVNYLLE-- 161
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  659 gsanaesvQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHlvsqeghvpvaDVLIKHGVTVDATTRM----- 733
Cdd:cd22197   162 --------NPHQPASLQAQDSLGNTVLHALVMIADNSPENSALVIKMY-----------DGLLQAGARLCPTVQLeeisn 222
                         170       180
                  ....*....|....*....|....*.
gi 471434838  734 --GYTPLHVASHYGNIKLVKFLLQHQ 757
Cdd:cd22197   223 heGLTPLKLAAKEGKIEIFRHILQRE 248
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
271-300 1.59e-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: 404492 [Multi-domain]  Cd Length: 30  Bit Score: 40.32  E-value: 1.59e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 471434838   271 NGITPLHIASRRGNVIMVRLLLDRGAQIET 300
Cdd:pfam13606    1 DGNTPLHLAARNGNLEIVKLLLERGADINA 30
PHA02795 PHA02795
ankyrin-like protein; Provisional
125-188 1.61e-04

ankyrin-like protein; Provisional


Pssm-ID: 165157  Cd Length: 437  Bit Score: 46.14  E-value: 1.61e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 471434838  125 EVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQG 188
Cdd:PHA02795  202 EIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRG 265
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
338-459 1.64e-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: 46.39  E-value: 1.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  338 GLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHL-------------TPLHVAAHCGHHRVAKVLLDKGAKPNS---RA 401
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVENGADVHARACGRFfqkkqgtcfyfgeLPLSLAACTKQWDVVNYLLENPHQPASlqaQD 173
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 471434838  402 LNGFTPLH----IA--CKKNH---IRVMELLLKTGASIDA-------VTESGLTPLHVASFMGHLPIVKNLLQR 459
Cdd:cd22197   174 SLGNTVLHalvmIAdnSPENSalvIKMYDGLLQAGARLCPtvqleeiSNHEGLTPLKLAAKEGKIEIFRHILQR 247
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
568-600 1.68e-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: 425426 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 1.68e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 471434838   568 KGFTPLHVAA-KYGKVRLAELLLEHDAHPNAAGK 600
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
634-663 1.69e-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: 40.26  E-value: 1.69e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 471434838    634 NGYTPLHIAAKQNQIEVARSLLQYGGSANA 663
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
379-466 1.70e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.20  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  379 AHCG----HHRVAKVLLDKGAKPNSRALNGFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVASFMGHLPI-- 452
Cdd:PHA02946   43 AYCGikglDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIer 122
                          90
                  ....*....|....
gi 471434838  453 VKNLLQRGASPNVS 466
Cdd:PHA02946  123 INLLVQYGAKINNS 136
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
304-336 1.82e-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: 425426 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 1.82e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 471434838   304 DELTPLHCAA-RNGHVRISEILLDHGAPIQAKTK 336
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
111-164 1.83e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 1.83e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 471434838  111 GNTALHIAALAGQDEVVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLL 164
Cdd:PTZ00322  115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02884 PHA02884
ankyrin repeat protein; Provisional
606-710 1.84e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 45.36  E-value: 1.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  606 LHVAVHHNNLDIVKLLLPRGGSPHSP---AWNGYT-PLHIAAKQNQIEVARSLLQYGGSANAESVQGV-TPLHLAAQEGH 680
Cdd:PHA02884   37 LYSSIKFHYTDIIDAILKLGADPEAPfplSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGC 116
                          90       100       110
                  ....*....|....*....|....*....|
gi 471434838  681 TEMVALLLSKQANGNLGNKSGLTPLHLVSQ 710
Cdd:PHA02884  117 LKCLEILLSYGADINIQTNDMVTPIELALM 146
PHA02736 PHA02736
Viral ankyrin protein; Provisional
660-791 1.97e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 43.71  E-value: 1.97e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  660 SANAESVQGVTPLHLAAQEGhtEMVALLLSKQA----NGNLG---NKSGLTPLHLVSQEGHV-PVADV--LIKHGVTVDA 729
Cdd:PHA02736    9 FASEPDIEGENILHYLCRNG--GVTDLLAFKNAisdeNRYLVleyNRHGKQCVHIVSNPDKAdPQEKLklLMEWGADING 86
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 471434838  730 TTRM-GYTPLHVASHYGNIKLVKFLL-QHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGA 791
Cdd:PHA02736   87 KERVfGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
767-795 2.36e-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: 39.88  E-value: 2.36e-04
                            10        20
                    ....*....|....*....|....*....
gi 471434838    767 GYSPLHQAAQQGHTDIVTLLLKNGASPNE 795
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
601-629 2.37e-04

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


Pssm-ID: 425426 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 2.37e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 471434838   601 NGLTPLHVAV-HHNNLDIVKLLLPRGGSPH 629
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
667-699 2.57e-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: 425426 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 2.57e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 471434838   667 QGVTPLHLAA-QEGHTEMVALLLSKQANGNLGNK 699
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA03095 PHA03095
ankyrin-like protein; Provisional
747-804 2.62e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.40  E-value: 2.62e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 471434838  747 IKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGH---TDIVTLLLKNGASPNEVSSNGTTPL 804
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPL 87
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
404-612 2.73e-04

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 45.62  E-value: 2.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  404 GFTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLH--VASFMGHLpivknllqrgaspnvsnvkvetPLHMAARAG 481
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVENGADVHARACGRFFQKKqgTCFYFGEL----------------------PLSLAACTK 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  482 HTEVAKYLLQNKAKANAKAKDD---QTPLHCAARIGH---------TGMVKLLLENGA--SPNL-----ATTAGHTPLHT 542
Cdd:cd22197   152 QWDVVNYLLENPHQPASLQAQDslgNTVLHALVMIADnspensalvIKMYDGLLQAGArlCPTVqleeiSNHEGLTPLKL 231
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  543 AAREGHVDTALALLEKEASQAC------MTKKGFTPLHVAA-------KYGKVRLAELLLEHDAHPNAAGKNGLTPLHVA 609
Cdd:cd22197   232 AAKEGKIEIFRHILQREFSGPYqhlsrkFTEWCYGPVRVSLydlssvdSWEKNSVLEIIAFHSKSPNRHRMVVLEPLNKL 311

                  ...
gi 471434838  610 VHH 612
Cdd:cd22197   312 LQE 314
PHA02946 PHA02946
ankyin-like protein; Provisional
119-292 2.94e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.43  E-value: 2.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  119 ALAGQDE-VVRELVNYGANVNAQSQKGFTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQQGHENV--VAH 195
Cdd:PHA02946   46 GIKGLDErFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  196 LINYGTKgkvrlpalhIAARNDDTRTAAVLLQNDPNPDVLSKT-----------GFTPLHIAAHYENLN----VAQLLLN 260
Cdd:PHA02946  126 LVQYGAK---------INNSVDEEGCGPLLACTDPSERVFKKImsigfearivdKFGKNHIHRHLMSDNpkasTISWMMK 196
                         170       180       190
                  ....*....|....*....|....*....|....
gi 471434838  261 RGASVNFTPQNGITPLHIASRR--GNVIMVRLLL 292
Cdd:PHA02946  197 LGISPSKPDHDGNTPLHIVCSKtvKNVDIINLLL 230
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
503-656 2.97e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 45.46  E-value: 2.97e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   503 DQTPLHCAARIGHTGMVKLLLENGASPNLATTAGhtplhtaareghvdtalallekeasqACMTKKGFT-------PLHV 575
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARACGD--------------------------FFVKSQGVDsfyhgesPLNA 181
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   576 AAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVHHNNL------------DIVKLLLPRGGSP----HSPAWNGYTPL 639
Cdd:TIGR00870  182 AACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFkaeyeelscqmyNFALSLLDKLRDSkeleVILNHQGLTPL 261
                          170
                   ....*....|....*..
gi 471434838   640 HIAAKQNQIEVARSLLQ 656
Cdd:TIGR00870  262 KLAAKEGRIVLFRLKLA 278
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
568-691 3.13e-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: 45.56  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  568 KGFTPLHVAAKYGKVRLAELLLEHDAHPNAAGKN--------------GLTPLHVAVHHNNLDIVKLLLPrggSPHSPA- 632
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLE---NEHQPAd 151
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  633 -----WNGYTPLH----IA--AKQNQIEVAR---SLLQYGG----SANAESV---QGVTPLHLAAQEGHTEMVALLLSKQ 691
Cdd:cd22193   152 ieaqdSRGNTVLHalvtVAdnTKENTKFVTRmydMILIRGAklcpTVELEEIrnnDGLTPLQLAAKMGKIEILKYILQRE 231
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
568-597 3.43e-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: 404492 [Multi-domain]  Cd Length: 30  Bit Score: 39.17  E-value: 3.43e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 471434838   568 KGFTPLHVAAKYGKVRLAELLLEHDAHPNA 597
Cdd:pfam13606    1 DGNTPLHLAARNGNLEIVKLLLERGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
767-795 3.93e-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: 404492 [Multi-domain]  Cd Length: 30  Bit Score: 39.17  E-value: 3.93e-04
                           10        20
                   ....*....|....*....|....*....
gi 471434838   767 GYSPLHQAAQQGHTDIVTLLLKNGASPNE 795
Cdd:pfam13606    2 GNTPLHLAARNGNLEIVKLLLERGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
568-597 4.22e-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: 4.22e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 471434838    568 KGFTPLHVAAKYGKVRLAELLLEHDAHPNA 597
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02884 PHA02884
ankyrin repeat protein; Provisional
124-186 4.33e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 44.20  E-value: 4.33e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 471434838  124 DEVVRELVNYGANVNAQSQKG-FTPLYMAAQENHLEVVKFLLENGANQNVATEDGFTPLAVALQ 186
Cdd:PHA02884   83 DDAAKLLIRYGADVNRYAEEAkITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
143-172 4.64e-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: 404492 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 4.64e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 471434838   143 KGFTPLYMAAQENHLEVVKFLLENGANQNV 172
Cdd:pfam13606    1 DGNTPLHLAARNGNLEIVKLLLERGADINA 30
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
568-694 4.70e-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: 44.85  E-value: 4.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  568 KGFTPLHVAAKYGKVRLAELLLEH--DAHPNAAG----KN-------GLTPLHVAVHHNNLDIVKLLLPRggsPHSPAW- 633
Cdd:cd22197    93 RGHSALHIAIEKRSLQCVKLLVENgaDVHARACGrffqKKqgtcfyfGELPLSLAACTKQWDVVNYLLEN---PHQPASl 169
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  634 -----NGYTPLH----IA--AKQNQIEVAR---SLLQYGGSANAE-------SVQGVTPLHLAAQEGHTEMVALLLSKQA 692
Cdd:cd22197   170 qaqdsLGNTVLHalvmIAdnSPENSALVIKmydGLLQAGARLCPTvqleeisNHEGLTPLKLAAKEGKIEIFRHILQREF 249

                  ..
gi 471434838  693 NG 694
Cdd:cd22197   250 SG 251
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
601-629 4.74e-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: 404492 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 4.74e-04
                           10        20
                   ....*....|....*....|....*....
gi 471434838   601 NGLTPLHVAVHHNNLDIVKLLLPRGGSPH 629
Cdd:pfam13606    1 DGNTPLHLAARNGNLEIVKLLLERGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
667-693 4.89e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 4.89e-04
                            10        20
                    ....*....|....*....|....*..
gi 471434838    667 QGVTPLHLAAQEGHTEMVALLLSKQAN 693
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank_4 pfam13637
Ankyrin repeats (many copies);
47-98 4.97e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 4.97e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 471434838    47 TSFLRAARSGNLDKALDHLRNGVDINTCNQNGLNGLHLASKEGHVKMVVELL 98
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
602-716 5.50e-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: 5.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  602 GLTPLHVAVHHNNLDIVKLLLPRGGSPHSPA--------------WNGYTPLHIAAKQNQIEVARSLLQYG---GSANAE 664
Cdd:cd22193    76 GQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLAACTNQPDIVQYLLENEhqpADIEAQ 155
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 471434838  665 SVQGVTPLHLAAQEGH---------TEMVALLLSKQAN-------GNLGNKSGLTPLHLVSQEGHVPV 716
Cdd:cd22193   156 DSRGNTVLHALVTVADntkentkfvTRMYDMILIRGAKlcptvelEEIRNNDGLTPLQLAAKMGKIEI 223
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
239-266 5.54e-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: 404492 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 5.54e-04
                           10        20
                   ....*....|....*....|....*...
gi 471434838   239 GFTPLHIAAHYENLNVAQLLLNRGASVN 266
Cdd:pfam13606    2 GNTPLHLAARNGNLEIVKLLLERGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
337-368 6.22e-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: 425426 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 6.22e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 471434838   337 NGLSPIHMAA-QGDHLDCVRLLLQYNAEIDDIT 368
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02736 PHA02736
Viral ankyrin protein; Provisional
196-297 6.72e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 41.79  E-value: 6.72e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  196 LINYGTKGKvrlPALHIAARND--DTRTAAVLLQN---DPNPDVlSKTGFTPLHIAAHYENLNVAQLLLNRGA----SVN 266
Cdd:PHA02736   48 VLEYNRHGK---QCVHIVSNPDkaDPQEKLKLLMEwgaDINGKE-RVFGNTPLHIAVYTQNYELATWLCNQPGvnmeILN 123
                          90       100       110
                  ....*....|....*....|....*....|.
gi 471434838  267 FTPQngiTPLHIASRRGNVIMVRLLLDRGAQ 297
Cdd:PHA02736  124 YAFK---TPYYVACERHDAKMMNILRAKGAQ 151
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
351-606 8.39e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 44.10  E-value: 8.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  351 LDCVRLLLQYNAEIDDITLDhlTPLHVAA---HCGHHRVAKVLLDKGAKPNSRA-----------LNGFTPLHIACKKNH 416
Cdd:cd21882     8 LECLRWYLTDSAYQRGATGK--TCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKelvnapctdefYQGQTALHIAIENRN 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  417 IRVMELLLKTGASIDAVTESgltplhvASFMGHlpiVKNLLQRGaspnvsnvkvETPLHMAARAGHTEVAKYLLQNKAKA 496
Cdd:cd21882    86 LNLVRLLVENGADVSARATG-------RFFRKS---PGNLFYFG----------ELPLSLAACTNQEEIVRLLLENGAQP 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  497 NAKAKDD---QTPLHCAARIGH---------TGMVKLLLENGASPN-------LATTAGHTPLHTAAREGHVDTALALLE 557
Cdd:cd21882   146 AALEAQDslgNTVLHALVLQADntpensafvCQMYNLLLSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQ 225
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 471434838  558 KEASQACM------TKKGFTPLHVAA-------KYGKVRLAELLLEHDAHPNAAGKNGLTPL 606
Cdd:cd21882   226 REFSGPYQplsrkfTEWTYGPVTSSLydlseidSWEKNSVLELIAFSKKREARHQMLVQEPL 287
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
634-663 8.46e-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: 404492 [Multi-domain]  Cd Length: 30  Bit Score: 38.40  E-value: 8.46e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 471434838   634 NGYTPLHIAAKQNQIEVARSLLQYGGSANA 663
Cdd:pfam13606    1 DGNTPLHLAARNGNLEIVKLLLERGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
437-465 8.97e-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: 404492 [Multi-domain]  Cd Length: 30  Bit Score: 38.01  E-value: 8.97e-04
                           10        20
                   ....*....|....*....|....*....
gi 471434838   437 GLTPLHVASFMGHLPIVKNLLQRGASPNV 465
Cdd:pfam13606    2 GNTPLHLAARNGNLEIVKLLLERGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
58-300 9.05e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.67  E-value: 9.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   58 LDKALDHLRNGVDINTCNQNGLNGLHLaskeghvkmvveLLHKEIIletttkkgntalhiaalaGQDEVVRELVNYGANV 137
Cdd:PHA02798   89 LDIVKILIENGADINKKNSDGETPLYC------------LLSNGYI------------------NNLEILLFMIENGADT 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  138 NAQSQKGFTPLYMAAQENH---LEVVKFLLENGANQNV-ATEDGFTPLAVALQQGHE----NVVAHLINYG--------- 200
Cdd:PHA02798  139 TLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNIDridaDILKLFVDNGfiinkenks 218
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  201 TKGKVR--LPALHIAARNDDTRTAAVLLQ--NDPNPDVLsktGFTPLHIAAHYENLNVAQLLLNRGASVNFTPQNGITPL 276
Cdd:PHA02798  219 HKKKFMeyLNSLLYDNKRFKKNILDFIFSyiDINQVDEL---GFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCL 295
                         250       260
                  ....*....|....*....|....
gi 471434838  277 HIASRRGNVIMVRLLLDRGAQIET 300
Cdd:PHA02798  296 FTAFENESKFIFNSILNKKPNKNT 319
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
467-590 9.23e-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: 9.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  467 NVKVETPLHMAARAGHTEVAKYLLQNKAKANAKAKDD--------------QTPLHCAARIGHTGMVKLLLENGASP-NL 531
Cdd:cd22194   138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIVQLLMEKESTDiTS 217
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 471434838  532 ATTAGHTPLH---TAAR--EGHV-------DTALALLEKEASQACMTKKGFTPLHVAAKYGKVRLAELLLE 590
Cdd:cd22194   218 QDSRGNTVLHalvTVAEdsKTQNdfvkrmyDMILLKSENKNLETIRNNEGLTPLQLAAKMGKAEILKYILS 288
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
370-398 9.42e-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: 404492 [Multi-domain]  Cd Length: 30  Bit Score: 38.01  E-value: 9.42e-04
                           10        20
                   ....*....|....*....|....*....
gi 471434838   370 DHLTPLHVAAHCGHHRVAKVLLDKGAKPN 398
Cdd:pfam13606    1 DGNTPLHLAARNGNLEIVKLLLERGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
307-331 1.04e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 1.04e-03
                            10        20
                    ....*....|....*....|....*
gi 471434838    307 TPLHCAARNGHVRISEILLDHGAPI 331
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLDKGADI 28
Ank_5 pfam13857
Ankyrin repeats (many copies);
65-118 1.27e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 1.27e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 471434838    65 LRNG-VDINTCNQNGLNGLHLASKEGHVKMVVELLHKEIILETTTKKGNTALHIA 118
Cdd:pfam13857    2 LEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
634-663 1.58e-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: 425426 [Multi-domain]  Cd Length: 34  Bit Score: 37.65  E-value: 1.58e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 471434838   634 NGYTPLHIAAKQ-NQIEVARSLLQYGGSANA 663
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNA 31
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
504-656 1.88e-03

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 42.92  E-value: 1.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  504 QTPLHCAARIGHTGMVKLLLENGASPNLATTA-------------GHTPLHTAAREGHVDTALALLEKEASQACMTKK-- 568
Cdd:cd22197    95 HSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELPLSLAACTKQWDVVNYLLENPHQPASLQAQds 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  569 -GFTPLHvaakygkvrlAELLLEHDAHPNAAgkngltpLHVAVHHNNLDIVKLLLPRGGSPHSPAWNGYTPLHIAAKQNQ 647
Cdd:cd22197   175 lGNTVLH----------ALVMIADNSPENSA-------LVIKMYDGLLQAGARLCPTVQLEEISNHEGLTPLKLAAKEGK 237

                  ....*....
gi 471434838  648 IEVARSLLQ 656
Cdd:cd22197   238 IEIFRHILQ 246
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
239-377 2.10e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.82  E-value: 2.10e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  239 GFTPLHIAAHYENLNVAQLLLNRGASVN-------FTPQN-------GITPLHIASRRGNVIMVRLLLDRGAQIETrTKD 304
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNahakgvfFNPKYkhegfyfGETPLALAACTNQPEIVQLLMEKESTDIT-SQD 219
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  305 EL--TPLHC---AARNGHVRIS-------EILLDHGAPIQAKTKN--GLSPIHMAAQGDHLDCVRLLLqyNAEIDDITLD 370
Cdd:cd22194   220 SRgnTVLHAlvtVAEDSKTQNDfvkrmydMILLKSENKNLETIRNneGLTPLQLAAKMGKAEILKYIL--SREIKEKPNR 297

                  ....*..
gi 471434838  371 HLTPLHV 377
Cdd:cd22194   298 SLSRKFT 304
PHA02874 PHA02874
ankyrin repeat protein; Provisional
745-848 2.15e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 2.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  745 GNIKLVKFLLQHQAD-VNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSSNGTTPLAIAKRLGyisVTDVLKVVT 823
Cdd:PHA02874   12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIG---AHDIIKLLI 88
                          90       100
                  ....*....|....*....|....*...
gi 471434838  824 D---ETSVVLVSDKHRmsypETVDEILD 848
Cdd:PHA02874   89 DngvDTSILPIPCIEK----DMIKTILD 112
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
701-732 2.32e-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: 425426 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 2.32e-03
                           10        20        30
                   ....*....|....*....|....*....|...
gi 471434838   701 GLTPLHL-VSQEGHVPVADVLIKHGVTVDATTR 732
Cdd:pfam00023    2 GNTPLHLaAGRRGNLEIVKLLLSKGADVNARDK 34
PHA02736 PHA02736
Viral ankyrin protein; Provisional
71-205 2.44e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 40.24  E-value: 2.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   71 INTCNQN--GLNGLHLASKEGHVkmvVELL-HKEIILETT-------TKKGNTALHIAALAGQ---DEVVRELVNYGANV 137
Cdd:PHA02736    8 IFASEPDieGENILHYLCRNGGV---TDLLaFKNAISDENrylvleyNRHGKQCVHIVSNPDKadpQEKLKLLMEWGADI 84
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  138 NAQSQK-GFTPLYMAAQENHLEVVKFLLEN-GANQNVATEDGFTPLAVALQQGHENVVAHLINYGTKGKV 205
Cdd:PHA02736   85 NGKERVfGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCKV 154
PHA02791 PHA02791
ankyrin-like protein; Provisional
532-727 3.09e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.57  E-value: 3.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  532 ATTAGHTPLHTAAREGHVDTALALLEKEASQACMTKKgfTPLHVAAKYGKVRLAELLLEHDAHPNAAGKNGLTPLHVAVH 611
Cdd:PHA02791   26 ADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVD 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  612 HNNLDIVKLLLPRGGSPHSPAWNGY-TPLHIAAKQNQIEVARSLLQYGGSANAESVQgVTPLHLAAQEGHTEMVALLLSK 690
Cdd:PHA02791  104 SGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLSEIPSTFDLAIL-LSCIHITIKNGHVDMMILLLDY 182
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 471434838  691 QANGNLGNKSGLTP-LHLVSQEGHVPVADVLIKHGVTV 727
Cdd:PHA02791  183 MTSTNTNNSLLFIPdIKLAIDNKDLEMLQALFKYDINI 220
PHA02859 PHA02859
ankyrin repeat protein; Provisional
125-200 3.74e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 3.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  125 EVVRELVNYGANVNAQSQ-KGFTPL--YMAAQEN-HLEVVKFLLENGANQNVATEDGFTPLAVALQQGHEN--VVAHLIN 198
Cdd:PHA02859   67 EILKFLIENGADVNFKTRdNNLSALhhYLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRinVIKLLID 146

                  ..
gi 471434838  199 YG 200
Cdd:PHA02859  147 SG 148
PHA02795 PHA02795
ankyrin-like protein; Provisional
719-813 3.99e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157  Cd Length: 437  Bit Score: 41.52  E-value: 3.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  719 VLIKHGVTVDATTRMGYTPLHVASHYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNEVSS 798
Cdd:PHA02795  173 IPDENDVKLDLYKIIQYTRGFLVDEPTVLEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMS 252
                          90
                  ....*....|....*
gi 471434838  799 NGTTPLAIAKRLGYI 813
Cdd:PHA02795  253 NGYTCLDVAVDRGSV 267
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
472-491 4.13e-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: 4.13e-03
                            10        20
                    ....*....|....*....|
gi 471434838    472 TPLHMAARAGHTEVAKYLLQ 491
Cdd:smart00248    4 TPLHLAAENGNLEVVKLLLD 23
PHA02791 PHA02791
ankyrin-like protein; Provisional
634-798 4.25e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.18  E-value: 4.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  634 NGYTPLHIAAKQNQIEVARSLLQYGGSANAesVQGVTPLHLAAQEGHTEMVALLLSKQANGNLGNKSGLTPLHLVSQEGH 713
Cdd:PHA02791   29 HGHSALYYAIADNNVRLVCTLLNAGALKNL--LENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGN 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  714 VPVADVLIKHGVTVDATTRMGY-TPLHVASHYGNIKLVKFLLqhqADVNAKTKLG--YSPLHQAAQQGHTDIVTLLLKNG 790
Cdd:PHA02791  107 MQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFL---SEIPSTFDLAilLSCIHITIKNGHVDMMILLLDYM 183

                  ....*...
gi 471434838  791 ASPNEVSS 798
Cdd:PHA02791  184 TSTNTNNS 191
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
716-807 4.71e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 4.71e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  716 VADVLIKHGVTvDATTRMGYTPLHVAShYGNIKLVKFLLQHQADVNAKTKLGYSPLHQAAQQGHTDIVTLLLKNGASPNE 795
Cdd:PLN03192  509 VGDLLGDNGGE-HDDPNMASNLLTVAS-TGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI 586
                          90
                  ....*....|....
gi 471434838  796 VSSNGTTPL--AIA 807
Cdd:PLN03192  587 RDANGNTALwnAIS 600
PHA02884 PHA02884
ankyrin repeat protein; Provisional
371-445 5.90e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.74  E-value: 5.90e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 471434838  371 HLTPLHVAAHCGHHRVAKVLLDKGAKPNSRALNG-FTPLHIACKKNHIRVMELLLKTGASIDAVTESGLTPLHVAS 445
Cdd:PHA02884   70 KTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELAL 145
PHA02741 PHA02741
hypothetical protein; Provisional
75-192 6.43e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 39.26  E-value: 6.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838   75 NQNGLNGLHLASKEGHVKMVVELL------HKEIILETTTKKGNTALHIAALAGQD----EVVRELVNYGANVNAQ-SQK 143
Cdd:PHA02741   18 NSEGENFFHEAARCGCFDIIARFTpfirgdCHAAALNATDDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQeMLE 97
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 471434838  144 GFTPLYMAAQENHLEVVKFLL-ENGANQNVATEDGFTPLAVAlqQGHENV 192
Cdd:PHA02741   98 GDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPFELA--IDNEDV 145
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
106-294 7.39e-03

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 40.99  E-value: 7.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  106 TTTKKGNTALHIAALAGQD----------EVVRELVNYGANVNAQSQ----KGFTPLYMAAQENHLEVVKFLLENGANQN 171
Cdd:cd22197    42 TEGSTGKTCLMKAVLNLQDgvnacimpllEIDKDSGNPKPLVNAQCTdeyyRGHSALHIAIEKRSLQCVKLLVENGADVH 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  172 VATEDGFTplavalqQGHENVVAHlinYGtkgkvRLPaLHIAARNDDTRTAAVLLQNDPNPDVLSKT---GFTPLH---- 244
Cdd:cd22197   122 ARACGRFF-------QKKQGTCFY---FG-----ELP-LSLAACTKQWDVVNYLLENPHQPASLQAQdslGNTVLHalvm 185
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 471434838  245 IAAHYENlNVAQL------LLNRGASVNFTPQ-------NGITPLHIASRRGNVIMVRLLLDR 294
Cdd:cd22197   186 IADNSPE-NSALVikmydgLLQAGARLCPTVQleeisnhEGLTPLKLAAKEGKIEIFRHILQR 247
PHA02859 PHA02859
ankyrin repeat protein; Provisional
386-463 7.76e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.80  E-value: 7.76e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  386 VAKVLLDKGAKPNSRAL-NGFTPLH--IACKKN-HIRVMELLLKTGASIDAVTESGLTPLHV--ASFMGHLPIVKNLLQR 459
Cdd:PHA02859   68 ILKFLIENGADVNFKTRdNNLSALHhyLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLIDS 147

                  ....
gi 471434838  460 GASP 463
Cdd:PHA02859  148 GVSF 151
PHA02946 PHA02946
ankyin-like protein; Provisional
310-476 7.89e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.81  E-value: 7.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  310 HCAARNGHVRISEILLDHGAPIQAKTKNGLSPIHMAAQGDHLDCVRLLLQYNAEIDDITLDHLTPLHVAAHCGHHRVAKV 389
Cdd:PHA02946   44 YCGIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERI 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  390 --LLDKGAK-PNSRALNGFTPLhIACKKNHIRVMELLLKTGASIDAVTESGLTPLHvASFMGHLP---IVKNLLQRGASP 463
Cdd:PHA02946  124 nlLVQYGAKiNNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIH-RHLMSDNPkasTISWMMKLGISP 201
                         170
                  ....*....|...
gi 471434838  464 NVSNVKVETPLHM 476
Cdd:PHA02946  202 SKPDHDGNTPLHI 214
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
337-365 9.69e-03

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


Pssm-ID: 404492 [Multi-domain]  Cd Length: 30  Bit Score: 35.32  E-value: 9.69e-03
                           10        20
                   ....*....|....*....|....*....
gi 471434838   337 NGLSPIHMAAQGDHLDCVRLLLQYNAEID 365
Cdd:pfam13606    1 DGNTPLHLAARNGNLEIVKLLLERGADIN 29
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
361-491 9.74e-03

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: 40.56  E-value: 9.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  361 NAEIDDITLDHLTPLHVAAHCGHHRVAKVLLDKGAKPNSRAL----------NGF----TPLHIACKKNHIRVMELLLK- 425
Cdd:cd22196    84 NAAYTDSYYKGQTALHIAIERRNMHLVELLVQNGADVHARASgeffkkkkggPGFyfgeLPLSLAACTNQLDIVKFLLEn 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 471434838  426 --TGASIDAVTESGLTPLH----VA-------SFMGHLpiVKNLLQRGASPN-------VSNVKVETPLHMAARAGHTEV 485
Cdd:cd22196   164 phSPADISARDSMGNTVLHalveVAdntpentKFVTKM--YNEILILGAKIRpllkleeITNKKGLTPLKLAAKTGKIGI 241

                  ....*.
gi 471434838  486 AKYLLQ 491
Cdd:cd22196   242 FAYILG 247
Death_TRAILR_DR4_DR5 cd08315
Death domain of Tumor necrosis factor-Related Apoptosis-Inducing Ligand Receptors; Death ...
1450-1508 9.79e-03

Death domain of Tumor necrosis factor-Related Apoptosis-Inducing Ligand Receptors; Death Domain (DD) found in Tumor necrosis factor-Related Apoptosis-Inducing Ligand (TRAIL) Receptors. In mammals, this family includes TRAILR1 (also called DR4 or TNFRSF10A) and TRAILR2 (also called DR5, TNFRSF10B, or KILLER). They function as receptors for the cytokine TRAIL and are involved in apoptosis signaling pathways. TRAIL preferentially induces apoptosis in cancer cells while exhibiting little toxicity in normal cells. DDs are protein-protein interaction domains found in a variety of domain architectures. Their common feature is that they form homodimers by self-association or heterodimers by associating with other members of the DD superfamily including CARD (Caspase activation and recruitment domain), DED (Death Effector Domain), and PYRIN. They serve as adaptors in signaling pathways and can recruit other proteins into signaling complexes.


Pssm-ID: 260027  Cd Length: 88  Bit Score: 36.86  E-value: 9.79e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 471434838 1450 SWAELARELQFSVEDINRIRVENPNSLlDQSTALLTLWVDREGENAKMENLYTALRNID 1508
Cdd:cd08315    13 SWKRLMRALGLSDNEIKLAEANDPGSQ-EPLYQMLNKWLNKTGRKASVNTLLDALEDLG 70
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.20
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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