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Conserved domains on  [gi|1907073017|ref|XP_036011415|]
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ankyrin-3 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
421-709 3.94e-63

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 218.67  E-value: 3.94e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  421 IRVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQAEVVRYLVQDGAQV 500
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  501 EAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLAAREGHEDVAAFLLDHGASLSITTKKGFTPLHVA 580
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  581 AKYGKLEVASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLLDQGASPHAAAKNGYTPLHIAAKKNQMDIATSLLE 660
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1907073017  661 YGADANAVTRQGIASVHLAAQEGHVDMVSLLLSRNANVNLSNKSGLTPL 709
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
256-544 1.07e-58

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.96  E-value: 1.07e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  256 INVATLLLNRAAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRSAPI 335
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  336 LSKTKNGLSPLHMATQGDHLNCVQLLLQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKASPNAKALNGFTPLHIA 415
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  416 CKKNRIRVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQAEVVRYLVQ 495
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1907073017  496 DGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPL 544
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
UPA_2 super family cl39303
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 1382-1511 1.31e-56

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


The actual alignment was detected with superfamily member pfam17809:

Pssm-ID: 375346  Cd Length: 131  Bit Score: 193.46  E-value: 1.31e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1382 VPYMAKFVVFAKTNDPVESSLRCFCMTDDRVDKTLEQQENFEEVARSKDIEVLEGKPIYVDCYGNLAPLTKGGQQLVFNF 1461
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1462 YSFKENRLPFSIKIRDTSQEPCGRLSFLKEPKTTKGLPQTAVCNLNITLP 1511
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-313 1.19e-52

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 188.62  E-value: 1.19e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017    1 MAHAASQLKKNRDLEINAEEETEKKRKHRKRSRDRKKKSDANASYLRAARAGHLEKALDYIKNGVDVNICNQNGLNALHL 80
Cdd:COG0666     14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHA 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   81 ASKEGHVEVVSELLQREANVDAATKKGNTALHIASLAGQAEVVKVLVTNGANVNAQSQNGFTPLYMAAQENHLEVVRFLL 160
Cdd:COG0666     94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  161 DNGASQSLATEDGFTPLAVALQQGHDQVVSLLLENdtkgkvrlpalhiaarkddtkaaalllqndtNADveskmvVNRAT 240
Cdd:COG0666    174 EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-------------------------------GAD------VNAKD 216

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907073017  241 ESGFTPLHIAAHYGNINVATLLLNRAAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPL 313
Cdd:COG0666    217 NDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Death_ank3 cd08803
Death domain of Ankyrin-3; Death Domain (DD) of the human protein ankyrin-3 (ANK-3) and ...
 4118-4201 1.25e-46

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: 163.31  E-value: 1.25e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 4118 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 4197
Cdd:cd08803      1 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 80


                   ....
gi 1907073017 4198 TLLE 4201
Cdd:cd08803     81 TLLE 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 1023-1160 9.11e-41

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


:

Pssm-ID: 128514  Cd Length: 104  Bit Score: 147.11  E-value: 9.11e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  1023 SRFLVSFMVDARGGSMRGSRHhGMRIIIPPRKCTAPTRITCRLVKRHKLANPPPMVEGEGLASRLVEMGPAGAQFLgklh 1102
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPRT-GVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFL---- 75

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907073017  1103 lpthpppvnegeslvsrilqlgpqgtkfiGPVIVEIPHFGSMRGKERELIVLRSENGE 1160
Cdd:smart00218   76 -----------------------------RPVILEVPHCASLRPRDWEIVLLRSENGG 104
PHA03100 super family cl39094
ankyrin repeat protein; Provisional
 608-817 9.52e-32

ankyrin repeat protein; Provisional


The actual alignment was detected with superfamily member PHA03100:

Pssm-ID: 476869 [Multi-domain]  Cd Length: 422  Bit Score: 131.71  E-value: 9.52e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  608 TPLHVAAHYDNQKVALLLLDQGASPHAAAKNGYTPLHIAA-----KKNQMDIATSLLEYGADANAVTRQGIASVHLAAQE 682
Cdd:PHA03100    37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISK 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  683 --GHVDMVSLLLSRNANVNLSNKSGLTPLHLAAQ--EDRVNVAEVLVNQGAHVDAQTKmgytplhvgchygnikiVNFLL 758
Cdd:PHA03100   117 ksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKGVDINAKNR-----------------VNYLL 179

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907073017  759 QHSAKVNAKTKNGYTALHQAAQQGHTHIINVLLQNNASPNELTVNGNTAL--AIARRLGYI 817
Cdd:PHA03100   180 SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLhiAILNNNKEI 240
Herpes_BLLF1 super family cl37540
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 1547-1954 3.53e-11

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


The actual alignment was detected with superfamily member pfam05109:

Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 69.95  E-value: 3.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1547 TEPSMKTVERSSGTArslpTTYSHKPFFSTRPYQSWTT---------APITVPGPAKSGSLSSSPSNTPSASPLKSIWSV 1617
Cdd:pfam05109  398 TAPKTLIITRTATNA----TTTTHKVIFSKAPESTTTSptlnttgfaAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADV 473

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1618 STPSPIKSTLGASTTSSVKS---------ISDVASPIRSfrtVSSPIKTVVSPSPY----NPQVASGTLGR--------- 1675
Cdd:pfam05109  474 TSPTPAGTTSGASPVTPSPSprdngteskAPDMTSPTSA---VTTPTPNATSPTPAvttpTPNATSPTLGKtsptsavtt 550

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1676 -VPTITEATP-IKGLAPNSTFSS--RTSPVTTAGSLLERSSITMTPPASPKSNITMYSSSLpfksiiTSATPLISSPLKS 1751
Cdd:pfam05109  551 pTPNATSPTPaVTTPTPNATIPTlgKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGG------TSSTPVVTSPPKN 624

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1752 VVSP-TKSAADVISTAKATMA---SSLS---SPLKQMSGHAEVALVNGSvsplkYPSSSALINGCKATATLQDKISTA-- 1822
Cdd:pfam05109  625 ATSAvTTGQHNITSSSTSSMSlrpSSISetlSPSTSDNSTSHMPLLTSA-----HPTGGENITQVTPASTSTHHVSTSsp 699

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1823 ------TNAVSSVVSAASDTVEKALSTTTAMPfsPLRSYVSAAPS----AFQSLRTPSASALYTSLG---------SSIA 1883
Cdd:pfam05109  700 aprpgtTSQASGPGNSSTSTKPGEVNVTKGTP--PKNATSPQAPSgqktAVPTVTSTGGKANSTTGGkhttghgarTSTE 777

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907073017 1884 ATTSSVTSSIITVPVYSVVNVLPEPALKKLPDSNSFTksaaallSPIKTLTTETRPQPhfnRTSSPVKSSL 1954
Cdd:pfam05109  778 PTTDYGGDSTTPRTRYNATTYLPPSTSSKLRPRWTFT-------SPPVTTAQATVPVP---PTSQPRFSNL 838
Adeno_L433K_22K super family cl12642
Adenovirus L4-33K/L4-22K; Adenoviruses express up to 20 distinct mRNAs from five major late ...
 3301-3417 7.03e-04

Adenovirus L4-33K/L4-22K; Adenoviruses express up to 20 distinct mRNAs from five major late transcription unit (MLTU) regions, L1 to L5. The L4 region expresses L4-33K and a related protein, L4-22K. L4-22K and L4-33K have complementary but not redundant functions that provide the normal pattern of mRNA production during the late phase of infection. L4-33K is an alternative RNA splicing factor that up-regulates several MLTU splice acceptor sites as the late phase progresses. L4-22K plays a role in genome packaging via its binding, in association with IVa2, to the A2 sequence within the packaging signal. Additionally, L4-22K plays an important role in the temporal switch from the early to late phase of infection by regulating both early and late gene expression.


The actual alignment was detected with superfamily member pfam11081:

Pssm-ID: 314108  Cd Length: 168  Bit Score: 43.46  E-value: 7.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 3301 IEFPPPPPLDADQMESDKKHQYLPErEVDMMEV--SLQDESDKYQLAE--PVIRVQPPSPVPPGAEASDSSDDESLYQPV 3376
Cdd:pfam11081    7 LQLPPPPPTDEEEYWDSQAEEVLDE-EEEMMEDwdSLDEASEAEEVSDetPSPSVAFPSPAPQKLATVPSIATTSAPQAP 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1907073017 3377 PVKKYTFKLKEVDEGQKDTAKSKTAATKASNQKEADGNGRE 3417
Cdd:pfam11081   86 PALPVRRPNRRWDTTGTRAGKSKQPPPLAQEQQQRQGYRSW 126
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
421-709 3.94e-63

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 218.67  E-value: 3.94e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  421 IRVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQAEVVRYLVQDGAQV 500
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  501 EAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLAAREGHEDVAAFLLDHGASLSITTKKGFTPLHVA 580
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  581 AKYGKLEVASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLLDQGASPHAAAKNGYTPLHIAAKKNQMDIATSLLE 660
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1907073017  661 YGADANAVTRQGIASVHLAAQEGHVDMVSLLLSRNANVNLSNKSGLTPL 709
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
256-544 1.07e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.96  E-value: 1.07e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  256 INVATLLLNRAAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRSAPI 335
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  336 LSKTKNGLSPLHMATQGDHLNCVQLLLQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKASPNAKALNGFTPLHIA 415
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  416 CKKNRIRVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQAEVVRYLVQ 495
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1907073017  496 DGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPL 544
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
UPA_2 pfam17809
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 1382-1511 1.31e-56

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: 193.46  E-value: 1.31e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1382 VPYMAKFVVFAKTNDPVESSLRCFCMTDDRVDKTLEQQENFEEVARSKDIEVLEGKPIYVDCYGNLAPLTKGGQQLVFNF 1461
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1462 YSFKENRLPFSIKIRDTSQEPCGRLSFLKEPKTTKGLPQTAVCNLNITLP 1511
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-313 1.19e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 188.62  E-value: 1.19e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017    1 MAHAASQLKKNRDLEINAEEETEKKRKHRKRSRDRKKKSDANASYLRAARAGHLEKALDYIKNGVDVNICNQNGLNALHL 80
Cdd:COG0666     14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHA 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   81 ASKEGHVEVVSELLQREANVDAATKKGNTALHIASLAGQAEVVKVLVTNGANVNAQSQNGFTPLYMAAQENHLEVVRFLL 160
Cdd:COG0666     94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  161 DNGASQSLATEDGFTPLAVALQQGHDQVVSLLLENdtkgkvrlpalhiaarkddtkaaalllqndtNADveskmvVNRAT 240
Cdd:COG0666    174 EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-------------------------------GAD------VNAKD 216

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907073017  241 ESGFTPLHIAAHYGNINVATLLLNRAAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPL 313
Cdd:COG0666    217 NDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Death_ank3 cd08803
Death domain of Ankyrin-3; Death Domain (DD) of the human protein ankyrin-3 (ANK-3) and ...
 4118-4201 1.25e-46

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: 163.31  E-value: 1.25e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 4118 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 4197
Cdd:cd08803      1 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 80


                   ....
gi 1907073017 4198 TLLE 4201
Cdd:cd08803     81 TLLE 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 1023-1160 9.11e-41

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 147.11  E-value: 9.11e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  1023 SRFLVSFMVDARGGSMRGSRHhGMRIIIPPRKCTAPTRITCRLVKRHKLANPPPMVEGEGLASRLVEMGPAGAQFLgklh 1102
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPRT-GVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFL---- 75

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907073017  1103 lpthpppvnegeslvsrilqlgpqgtkfiGPVIVEIPHFGSMRGKERELIVLRSENGE 1160
Cdd:smart00218   76 -----------------------------RPVILEVPHCASLRPRDWEIVLLRSENGG 104
PHA03095 PHA03095
ankyrin-like protein; Provisional
 377-665 1.25e-38

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 153.26  E-value: 1.25e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  377 TALHVAAHCGHYKVAKV---LLDKKASPNAKALNGFTPLHI-ACKKNRIRVMELLLKHGASIQAVTESGLTPIHV--AAF 450
Cdd:PHA03095    49 TPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGF 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  451 MGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQA--EVVRYLVQDGAQVEAKAKDDQTPLHISARLGK--ADIVQQL 526
Cdd:PHA03095   129 NINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNAnvELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVREL 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  527 LQQGASPNAATTSGYTPLHLAAREGHED--VAAFLLDHGASLSITTKKGFTPLHVAAKYGKLEVASLLLQKSASPDAAGK 604
Cdd:PHA03095   209 IRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS 288

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907073017  605 SGLTPLHVAAHYDNQKVALLLLDQGASPHAAAK-------NGYTPLhIAAKKNQMdiATSLLEYGADA 665
Cdd:PHA03095   289 DGNTPLSLMVRNNNGRAVRAALAKNPSAETVAAtlntasvAGGDIP-SDATRLCV--AKVVLRGAFSL 353
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 1027-1157 1.18e-34

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


Pssm-ID: 459941  Cd Length: 97  Bit Score: 129.57  E-value: 1.18e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1027 VSFMVDARGGSMRGSrHHGMRIIIPPRKCTAPTRITCRLVKRHKLANPPPMVEGEGLASRLVEMGPAGAQFLgklhlpth 1106
Cdd:pfam00791    1 VSGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFL-------- 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907073017 1107 pppvnegeslvsrilqlgpqgtkfiGPVIVEIPHFGSMRGKERELIVLRSE 1157
Cdd:pfam00791   72 -------------------------KPVILEVPHCASLRPEEWEIVLKRSD 97
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 252-502 4.00e-32

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 132.87  E-value: 4.00e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  252 HYGNINVATL--LLNRAAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQ-----V 324
Cdd:PHA03100     9 KSRIIKVKNIkyIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeI 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  325 VEMLLDRSAPILSKTKNGLSPLHMA--TQGDHLNCVQLLLQHNVPVDDVTNDYLTALHVAAHCGHY--KVAKVLLDKKAS 400
Cdd:PHA03100    89 VKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVD 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  401 PNAkalngftplhiackKNRIrvmELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHM 480
Cdd:PHA03100   169 INA--------------KNRV---NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI 231

                          250       260
                   ....*....|....*....|..
gi 1907073017  481 AARSGQAEVVRYLVQDGAQVEA 502
Cdd:PHA03100   232 AILNNNKEIFKLLLNNGPSIKT 253
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 608-817 9.52e-32

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 131.71  E-value: 9.52e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  608 TPLHVAAHYDNQKVALLLLDQGASPHAAAKNGYTPLHIAA-----KKNQMDIATSLLEYGADANAVTRQGIASVHLAAQE 682
Cdd:PHA03100    37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISK 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  683 --GHVDMVSLLLSRNANVNLSNKSGLTPLHLAAQ--EDRVNVAEVLVNQGAHVDAQTKmgytplhvgchygnikiVNFLL 758
Cdd:PHA03100   117 ksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKGVDINAKNR-----------------VNYLL 179

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907073017  759 QHSAKVNAKTKNGYTALHQAAQQGHTHIINVLLQNNASPNELTVNGNTAL--AIARRLGYI 817
Cdd:PHA03100   180 SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLhiAILNNNKEI 240
PHA03095 PHA03095
ankyrin-like protein; Provisional
 60-335 2.55e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 116.28  E-value: 2.55e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   60 YIKNGVDVNICNQNGLNALHLASKEGH---VEVVSELLQREANVDAATKKGNTALHI-ASLAGQAEVVKVLVTNGANVNA 135
Cdd:PHA03095    33 LLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNA 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  136 QSQNGFTPL--YMAAQENHLEVVRFLLDNGASQSLATEDGFTPLAVALQQGH--DQVVSLLLEND----TKGKVRLPALH 207
Cdd:PHA03095   113 KDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGadvyAVDDRFRSLLH 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  208 IaarkddtkaaalLLQN-DTNADVESKMVV-----NRATESGFTPLHIAAHYG---NINVATLLLNrAAAVDFTARNDIT 278
Cdd:PHA03095   193 H------------HLQSfKPRARIVRELIRagcdpAATDMLGNTPLHSMATGSsckRSLVLPLLIA-GISINARNRYGQT 259

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907073017  279 PLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRSAPI 335
Cdd:PHA03095   260 PLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSA 316
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 4117-4203 5.88e-26

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: 104.42  E-value: 5.88e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  4117 CERTDIRMAIVADH-LGLSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDALTSVLTKINRID 4195
Cdd:smart00005    1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80


                    ....*...
gi 1907073017  4196 IVTLLEGP 4203
Cdd:smart00005   81 AVELLRSE 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
78-165 8.35e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.57  E-value: 8.35e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   78 LHLASKEGHVEVVSELLQREANVDAATKKGNTALHIASLAGQAEVVKVLVTNgANVNAQSqNGFTPLYMAAQENHLEVVR 157
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*...
gi 1907073017  158 FLLDNGAS 165
Cdd:pfam12796   79 LLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
478-569 4.49e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 4.49e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  478 LHMAARSGQAEVVRYLVQDGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASpnAATTSGYTPLHLAAREGHEDVAA 557
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1907073017  558 FLLDHGASLSIT 569
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
677-767 1.91e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.72  E-value: 1.91e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  677 HLAAQEGHVDMVSLLLSRNANVNLSNKSGLTPLHLAAQEDRVNVAEVLVNQgAHVDAQTKmGYTPLHVGCHYGNIKIVNF 756
Cdd:pfam12796    2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|.
gi 1907073017  757 LLQHSAKVNAK 767
Cdd:pfam12796   80 LLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
346-436 7.47e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.79  E-value: 7.47e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  346 LHMATQGDHLNCVQLLLQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDkKASPNAKaLNGFTPLHIACKKNRIRVME 425
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLK-DNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 1907073017  426 LLLKHGASIQA 436
Cdd:pfam12796   79 LLLEKGADINV 89
Death pfam00531
Death domain;
4123-4201 8.74e-18

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 80.87  E-value: 8.74e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 4123 RMAIVADH---LGLSWTELARELNFSVDEINQIRVENPNsLISQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTL 4199
Cdd:pfam00531    3 QLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAAEK 81


                   ..
gi 1907073017 4200 LE 4201
Cdd:pfam00531   82 IQ 83
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 575-759 1.85e-15

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 83.52  E-value: 1.85e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  575 TPLHVAAKYGKLE-VASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLLDqgASPH-------AAAKNGYTPLHIA 646
Cdd:cd22192     19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPElvnepmtSDLYQGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  647 AKKNQMDIATSLLEYGADANA--VT----RQGIAS--------VHLAAQEGHVDMVSLLLSRNANVNLSNKSGLTPLH-L 711
Cdd:cd22192     97 VVNQNLNLVRELIARGADVVSprATgtffRPGPKNliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiL 176

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907073017  712 AAQEDRVNVAEV---LVNQGAHVDAQT------KMGYTPLHVGCHYGNIKIVNFLLQ 759
Cdd:cd22192    177 VLQPNKTFACQMydlILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQHLVQ 233
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 385-594 6.18e-13

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: 75.50  E-value: 6.18e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  385 CGHYKVAKVLLDKKASPNAKALN-------GFTPLHIACKKNRIR-VMELLLKHGASIqavtESGLTPIHVAAfMGHVNI 456
Cdd:TIGR00870   22 LPAAERGDLASVYRDLEEPKKLNincpdrlGRSALFVAAIENENLeLTELLLNLSCRG----AVGDTLLHAIS-LEYVDA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  457 VSQLM-----HHGASPNTTNV---------RGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDD--------------Q 508
Cdd:TIGR00870   97 VEAILlhllaAFRKSGPLELAndqytseftPGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgE 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  509 TPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLAAREGHEDVA---------AFLLDHGASLS-------ITTKK 572
Cdd:TIGR00870  177 SPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKAEyeelscqmyNFALSLLDKLRdskelevILNHQ 256

                          250       260
                   ....*....|....*....|..
gi 1907073017  573 GFTPLHVAAKYGKLEVASLLLQ 594
Cdd:TIGR00870  257 GLTPLKLAAKEGRIVLFRLKLA 278
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 106-265 3.29e-12

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: 73.25  E-value: 3.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  106 KGNTALHIASLAGQAEVVKVLVTNGANVNAQSQNGF--------------TPLYMAAQENHLEVVRFLLDNGasqslate 171
Cdd:cd22194    140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKE-------- 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  172 dgftPLAVALQqghdqvvslllenDTKGKVRLPALHIAArkDDTKAaalllQNDTNADVESKMVVNRATES--------G 243
Cdd:cd22194    212 ----STDITSQ-------------DSRGNTVLHALVTVA--EDSKT-----QNDFVKRMYDMILLKSENKNletirnneG 267

                          170       180
                   ....*....|....*....|..
gi 1907073017  244 FTPLHIAAHYGNINVATLLLNR 265
Cdd:cd22194    268 LTPLQLAAKMGKAEILKYILSR 289
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 1547-1954 3.53e-11

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 69.95  E-value: 3.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1547 TEPSMKTVERSSGTArslpTTYSHKPFFSTRPYQSWTT---------APITVPGPAKSGSLSSSPSNTPSASPLKSIWSV 1617
Cdd:pfam05109  398 TAPKTLIITRTATNA----TTTTHKVIFSKAPESTTTSptlnttgfaAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADV 473

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1618 STPSPIKSTLGASTTSSVKS---------ISDVASPIRSfrtVSSPIKTVVSPSPY----NPQVASGTLGR--------- 1675
Cdd:pfam05109  474 TSPTPAGTTSGASPVTPSPSprdngteskAPDMTSPTSA---VTTPTPNATSPTPAvttpTPNATSPTLGKtsptsavtt 550

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1676 -VPTITEATP-IKGLAPNSTFSS--RTSPVTTAGSLLERSSITMTPPASPKSNITMYSSSLpfksiiTSATPLISSPLKS 1751
Cdd:pfam05109  551 pTPNATSPTPaVTTPTPNATIPTlgKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGG------TSSTPVVTSPPKN 624

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1752 VVSP-TKSAADVISTAKATMA---SSLS---SPLKQMSGHAEVALVNGSvsplkYPSSSALINGCKATATLQDKISTA-- 1822
Cdd:pfam05109  625 ATSAvTTGQHNITSSSTSSMSlrpSSISetlSPSTSDNSTSHMPLLTSA-----HPTGGENITQVTPASTSTHHVSTSsp 699

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1823 ------TNAVSSVVSAASDTVEKALSTTTAMPfsPLRSYVSAAPS----AFQSLRTPSASALYTSLG---------SSIA 1883
Cdd:pfam05109  700 aprpgtTSQASGPGNSSTSTKPGEVNVTKGTP--PKNATSPQAPSgqktAVPTVTSTGGKANSTTGGkhttghgarTSTE 777

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907073017 1884 ATTSSVTSSIITVPVYSVVNVLPEPALKKLPDSNSFTksaaallSPIKTLTTETRPQPhfnRTSSPVKSSL 1954
Cdd:pfam05109  778 PTTDYGGDSTTPRTRYNATTYLPPSTSSKLRPRWTFT-------SPPVTTAQATVPVP---PTSQPRFSNL 838
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 135-450 1.25e-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: 58.17  E-value: 1.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  135 AQSQNGFTPlymAAQENHLEVVRFLLDNGASQSLATED--GFTPLAVALQQG-HDQVVSLLLENDTKGKVRLPALHIAAR 211
Cdd:TIGR00870   15 SDEEKAFLP---AAERGDLASVYRDLEEPKKLNINCPDrlGRSALFVAAIENeNLELTELLLNLSCRGAVGDTLLHAISL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  212 --KDDTKAAALLLQNDTNADVESKMVVNRATeSGFTPlhiaahygninvatlllnraaavdftarnDITPLHVASKRGNA 289
Cdd:TIGR00870   92 eyVDAVEAILLHLLAAFRKSGPLELANDQYT-SEFTP-----------------------------GITALHLAAHRQNY 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  290 NMVKLLLDRGAKIDAKT--------------RDGLTPLHCGARSGHEQVVEMLLDRSAPILSKTKNGLSPLHMAtqgdhl 355
Cdd:TIGR00870  142 EIVKLLLERGASVPARAcgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLL------ 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  356 ncvqlllqhnVPVDDVTNDYLTalhVAAHCghYKVAKVLLDKKASPNAKAL----NGFTPLHIACKKNRIRVMELLLKHG 431
Cdd:TIGR00870  216 ----------VMENEFKAEYEE---LSCQM--YNFALSLLDKLRDSKELEVilnhQGLTPLKLAAKEGRIVLFRLKLAIK 280

                          330
                   ....*....|....*....
gi 1907073017  432 ASIQAVTESGLTPIHVAAF 450
Cdd:TIGR00870  281 YKQKKFVAWPNGQQLLSLY 299
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 278-495 8.54e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 55.40  E-value: 8.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  278 TPLHVASKRGNANMVKLLLdRGAKIDAKTRDGL--TPLHCGARSGHEQVVEMLLDRSA-----PILSKTKNGLSPLHMAT 350
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLL-KCPSCDLFQRGALgeTALHVAALYDNLEAAVVLMEAAPelvnePMTSDLYQGETALHIAV 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  351 QGDHLNCVQLLLQHNVpvdDVTNdyltalhvAAHCGHYkvakvlldkkASPNAKALNGFTPlHI----ACKKNRIRVmEL 426
Cdd:cd22192     98 VNQNLNLVRELIARGA---DVVS--------PRATGTF----------FRPGPKNLIYYGE-HPlsfaACVGNEEIV-RL 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907073017  427 LLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMH---------HGASPNT-TNVRGETALHMAARSGQAEVVRYLVQ 495
Cdd:cd22192    155 LIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYDlilsydkedDLQPLDLvPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 54-265 1.53e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 54.70  E-value: 1.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   54 LEKALDYIKNGVDVnicnqnGLNALHLASKEgHVEVVSELLQREANVDAATK--------------KGNTALHIASLAGQ 119
Cdd:TIGR00870   68 LTELLLNLSCRGAV------GDTLLHAISLE-YVDAVEAILLHLLAAFRKSGplelandqytseftPGITALHLAAHRQN 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  120 AEVVKVLVTNGANVNA----------QSQNGF----TPLYMAAQENHLEVVRFLLDNGASQSLATEDGFTPLavalqqgH 185
Cdd:TIGR00870  141 YEIVKLLLERGASVPAracgdffvksQGVDSFyhgeSPLNAAACLGSPSIVALLSEDPADILTADSLGNTLL-------H 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  186 DQVVslllENDTKGKVRLPALHIaarKDdtkaaaLLLQNDTNAD--VESKMVVNRAtesGFTPLHIAAHYGNINVATLLL 263
Cdd:TIGR00870  214 LLVM----ENEFKAEYEELSCQM---YN------FALSLLDKLRdsKELEVILNHQ---GLTPLKLAAKEGRIVLFRLKL 277


                   ..
gi 1907073017  264 NR 265
Cdd:TIGR00870  278 AI 279
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 407-434 3.19e-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: 46.43  E-value: 3.19e-06
                            10        20
                    ....*....|....*....|....*...
gi 1907073017   407 NGFTPLHIACKKNRIRVMELLLKHGASI 434
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 540-568 1.05e-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: 44.89  E-value: 1.05e-05
                            10        20
                    ....*....|....*....|....*....
gi 1907073017   540 GYTPLHLAAREGHEDVAAFLLDHGASLSI 568
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 139-165 2.65e-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: 43.73  E-value: 2.65e-05
                            10        20
                    ....*....|....*....|....*..
gi 1907073017   139 NGFTPLYMAAQENHLEVVRFLLDNGAS 165
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 737-766 1.14e-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: 41.80  E-value: 1.14e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1907073017   737 MGYTPLHVGCHYGNIKIVNFLLQHSAKVNA 766
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 630-791 4.72e-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: 46.29  E-value: 4.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  630 ASPHAAAKNGYTPLHIAAKKNQMDIATSLLEYGADANAVTRQ--------------GIASVHLAAQEGHVDMVSLLLSRN 695
Cdd:cd22194    132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKE 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  696 ANVNLSNKS-GLTPLHLAaqedrVNVAEVLVNQGAHVdaqtkmgytplhvgchygnIKIVNFLLQHSAKVNAKT---KNG 771
Cdd:cd22194    212 STDITSQDSrGNTVLHAL-----VTVAEDSKTQNDFV-------------------KRMYDMILLKSENKNLETirnNEG 267

                          170       180
                   ....*....|....*....|
gi 1907073017  772 YTALHQAAQQGHTHIINVLL 791
Cdd:cd22194    268 LTPLQLAAKMGKAEILKYIL 287
Adeno_L433K_22K pfam11081
Adenovirus L4-33K/L4-22K; Adenoviruses express up to 20 distinct mRNAs from five major late ...
 3301-3417 7.03e-04

Adenovirus L4-33K/L4-22K; Adenoviruses express up to 20 distinct mRNAs from five major late transcription unit (MLTU) regions, L1 to L5. The L4 region expresses L4-33K and a related protein, L4-22K. L4-22K and L4-33K have complementary but not redundant functions that provide the normal pattern of mRNA production during the late phase of infection. L4-33K is an alternative RNA splicing factor that up-regulates several MLTU splice acceptor sites as the late phase progresses. L4-22K plays a role in genome packaging via its binding, in association with IVa2, to the A2 sequence within the packaging signal. Additionally, L4-22K plays an important role in the temporal switch from the early to late phase of infection by regulating both early and late gene expression.


Pssm-ID: 314108  Cd Length: 168  Bit Score: 43.46  E-value: 7.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 3301 IEFPPPPPLDADQMESDKKHQYLPErEVDMMEV--SLQDESDKYQLAE--PVIRVQPPSPVPPGAEASDSSDDESLYQPV 3376
Cdd:pfam11081    7 LQLPPPPPTDEEEYWDSQAEEVLDE-EEEMMEDwdSLDEASEAEEVSDetPSPSVAFPSPAPQKLATVPSIATTSAPQAP 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1907073017 3377 PVKKYTFKLKEVDEGQKDTAKSKTAATKASNQKEADGNGRE 3417
Cdd:pfam11081   86 PALPVRRPNRRWDTTGTRAGKSKQPPPLAQEQQQRQGYRSW 126
COG5099 COG5099
RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal ...
 1682-1960 1.57e-03

RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227430 [Multi-domain]  Cd Length: 777  Bit Score: 44.74  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1682 ATPIKGLAPNSTFSSRTSPVTTAGSLleRSSITMTPPASPKSN--ITMYSSSLPFKSIITSATPLISSPLKSVVSPTKSA 1759
Cdd:COG5099     27 STTSQELMNGNSTPNSFSPIPSKASS--SATFTLNLPINNSVNhkITSSSSSRRKPSGSWSVAISSSTSGSQSLLMELPS 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1760 AdviSTAKATMASSLSSPLkqmsgHAEVALVNGSVSPLKYPSSSAlinGCKATATLQDKISTATNavSSVVSAASDTVEK 1839
Cdd:COG5099    105 S---SFNPSTSSRNKSNSA-----LSSTQQGNANSSVTLSSSTAS---SMFNSNKLPLPNPNHSN--SATTNQSGSSFIN 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1840 ALSTTTampFSPLRSYVSAAPSAFQSLRTPSASALYTSLGSSIAATTSSVTSSIIT-VPVYSVVNVLPEPALKKLPDSNS 1918
Cdd:COG5099    172 TPASSS---SQPLTNLVVSSIKRFPYLTSLSPFFNYLIDPSSDSATASADTSPSFNpPPNLSPNNLFSTSDLSPLPDTQS 248

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1907073017 1919 FTKSAAALLS-PIKTLTTETRPQPHF-NRTSSPVKSSLFLASSA 1960
Cdd:COG5099    249 VENNIILNSSsSINELTSIYGSVPSIrNLRGLNSALVSFLNVSS 292
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 639-819 4.25e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.53  E-value: 4.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  639 GYTPLHIAAKKNQMDIATSLLEYGADANAVtrqGIASVHLAAqEGHVDMVSLLLS-------RNANVNLSNKS------- 704
Cdd:TIGR00870   52 GRSALFVAAIENENLELTELLLNLSCRGAV---GDTLLHAIS-LEYVDAVEAILLhllaafrKSGPLELANDQytseftp 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  705 GLTPLHLAAQEDRVNVAEVLVNQGAHVDAQTKMG---YTPlHVGCHY------------GNIKIVNFLLQHSAKVNAKTK 769
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARACGDffvKSQ-GVDSFYhgesplnaaaclGSPSIVALLSEDPADILTADS 206

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907073017  770 NGYTALHQAAQQGH---------THIINVLLQNNA---SPNELTV----NGNTALAIARRLGYISV 819
Cdd:TIGR00870  207 LGNTLLHLLVMENEfkaeyeelsCQMYNFALSLLDklrDSKELEVilnhQGLTPLKLAAKEGRIVL 272
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
421-709 3.94e-63

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 218.67  E-value: 3.94e-63
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  421 IRVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQAEVVRYLVQDGAQV 500
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  501 EAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLAAREGHEDVAAFLLDHGASLSITTKKGFTPLHVA 580
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  581 AKYGKLEVASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLLDQGASPHAAAKNGYTPLHIAAKKNQMDIATSLLE 660
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1907073017  661 YGADANAVTRQGIASVHLAAQEGHVDMVSLLLSRNANVNLSNKSGLTPL 709
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
389-674 1.10e-62

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 217.51  E-value: 1.10e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  389 KVAKVLLDKKASPNAKALNGFTPLHIACKKNRIRVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPN 468
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  469 TTNVRGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLAA 548
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  549 REGHEDVAAFLLDHGASLSITTKKGFTPLHVAAKYGKLEVASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLLDQ 628
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1907073017  629 GASPHAAAKNGYTPLHIAAKKNQMDIATSLLEYGADANAVTRQGIA 674
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
360-643 1.25e-62

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 217.13  E-value: 1.25e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  360 LLLQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKASPNAKALNGFTPLHIACKKNRIRVMELLLKHGASIQAVTE 439
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  440 SGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDDQTPLHISARLGK 519
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  520 ADIVQQLLQQGASPNAATTSGYTPLHLAAREGHEDVAAFLLDHGASLSITTKKGFTPLHVAAKYGKLEVASLLLQKSASP 599
Cdd:COG0666    166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1907073017  600 DAAGKSGLTPLHVAAHYDNQKVALLLLDQGASPHAAAKNGYTPL 643
Cdd:COG0666    246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
553-824 2.10e-61

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 213.66  E-value: 2.10e-61
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  553 EDVAAFLLDHGASLSITTKKGFTPLHVAAKYGKLEVASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLLDQGASP 632
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  633 HAAAKNGYTPLHIAAKKNQMDIATSLLEYGADANAVTRQGIASVHLAAQEGHVDMVSLLLSRNANVNLSNKSGLTPLHLA 712
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  713 AQEDRVNVAEVLVNQGAHVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTALHQAAQQGHTHIINVLLQ 792
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270
                   ....*....|....*....|....*....|..
gi 1907073017  793 NNASPNELTVNGNTALAIARRLGYISVVDTLK 824
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
520-808 2.29e-60

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 210.97  E-value: 2.29e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  520 ADIVQQLLQQGASPNAATTSGYTPLHLAAREGHEDVAAFLLDHGASLSITTKKGFTPLHVAAKYGKLEVASLLLQKSASP 599
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  600 DAAGKSGLTPLHVAAHYDNQKVALLLLDQGASPHAAAKNGYTPLHIAAKKNQMDIATSLLEYGADANAVTRQGIASVHLA 679
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  680 AQEGHVDMVSLLLSRNANVNLSNKSGLTPLHLAAQEDRVNVAEVLVNQGAHVDAQTKMGYTPLHVGCHYGNIKIVNFLLQ 759
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1907073017  760 HSAKVNAKTKNGYTALHQAAQQGHTHIINVLLQNNASPNELTVNGNTAL 808
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
324-610 3.74e-60

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 210.20  E-value: 3.74e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  324 VVEMLLDRSAPILSKTKNGLSPLHMATQGDHLNCVQLLLQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKASPNA 403
Cdd:COG0666      3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  404 KALNGFTPLHIACKKNRIRVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAAR 483
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  484 SGQAEVVRYLVQDGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLAAREGHEDVAAFLLDHG 563
Cdd:COG0666    163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1907073017  564 ASLSITTKKGFTPLHVAAKYGKLEVASLLLQKSASPDAAGKSGLTPL 610
Cdd:COG0666    243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
487-775 2.97e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 207.50  E-value: 2.97e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  487 AEVVRYLVQDGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLAAREGHEDVAAFLLDHGASL 566
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  567 SITTKKGFTPLHVAAKYGKLEVASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLLDQGASPHAAAKNGYTPLHIA 646
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  647 AKKNQMDIATSLLEYGADANAVTRQGIASVHLAAQEGHVDMVSLLLSRNANVNLSNKSGLTPLHLAAQEDRVNVAEVLVN 726
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1907073017  727 QGAHVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTAL 775
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
256-544 1.07e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.96  E-value: 1.07e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  256 INVATLLLNRAAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRSAPI 335
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  336 LSKTKNGLSPLHMATQGDHLNCVQLLLQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKASPNAKALNGFTPLHIA 415
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  416 CKKNRIRVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQAEVVRYLVQ 495
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1907073017  496 DGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPL 544
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
289-564 1.19e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 205.96  E-value: 1.19e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  289 ANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRSAPILSKTKNGLSPLHMATQGDHLNCVQLLLQHNVPV 368
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  369 DDVTNDYLTALHVAAHCGHYKVAKVLLDKKASPNAKALNGFTPLHIACKKNRIRVMELLLKHGASIQAVTESGLTPIHVA 448
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  449 AFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDDQTPLHISARLGKADIVQQLLQ 528
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1907073017  529 QGASPNAATTSGYTPLHLAAREGHEDVAAFLLDHGA 564
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
454-742 5.48e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 204.03  E-value: 5.48e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  454 VNIVSQLMHHGASPNTTNVRGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASP 533
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  534 NAATTSGYTPLHLAAREGHEDVAAFLLDHGASLSITTKKGFTPLHVAAKYGKLEVASLLLQKSASPDAAGKSGLTPLHVA 613
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  614 AHYDNQKVALLLLDQGASPHAAAKNGYTPLHIAAKKNQMDIATSLLEYGADANAVTRQGIASVHLAAQEGHVDMVSLLLS 693
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1907073017  694 RNANVNLSNKSGLTPLHLAAQEDRVNVAEVLVNQGAHVDAQTKMGYTPL 742
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
227-511 3.38e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 201.72  E-value: 3.38e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  227 NADVESKMVVNRATESGFTPLHIAAHYGNINVATLLLNRAAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKT 306
Cdd:COG0666      5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  307 RDGLTPLHCGARSGHEQVVEMLLDRSAPILSKTKNGLSPLHMATQGDHLNCVQLLLQHNVPVDDVTNDYLTALHVAAHCG 386
Cdd:COG0666     85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  387 HYKVAKVLLDKKASPNAKALNGFTPLHIACKKNRIRVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGAS 466
Cdd:COG0666    165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1907073017  467 PNTTNVRGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDDQTPL 511
Cdd:COG0666    245 LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
UPA_2 pfam17809
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 1382-1511 1.31e-56

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: 193.46  E-value: 1.31e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1382 VPYMAKFVVFAKTNDPVESSLRCFCMTDDRVDKTLEQQENFEEVARSKDIEVLEGKPIYVDCYGNLAPLTKGGQQLVFNF 1461
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1462 YSFKENRLPFSIKIRDTSQEPCGRLSFLKEPKTTKGLPQTAVCNLNITLP 1511
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
191-478 3.00e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 199.02  E-value: 3.00e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  191 LLLENDTKGKVRLPALHIAARKDDTKAAALLLQNDTNADVESKMVVNRATESGFTPLHIAAHYGNINVATLLLNRAAAVD 270
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  271 FTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRSAPILSKTKNGLSPLHMAT 350
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  351 QGDHLNCVQLLLQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKASPNAKALNGFTPLHIACKKNRIRVMELLLKH 430
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1907073017  431 GASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETAL 478
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-313 1.19e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 188.62  E-value: 1.19e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017    1 MAHAASQLKKNRDLEINAEEETEKKRKHRKRSRDRKKKSDANASYLRAARAGHLEKALDYIKNGVDVNICNQNGLNALHL 80
Cdd:COG0666     14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHA 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   81 ASKEGHVEVVSELLQREANVDAATKKGNTALHIASLAGQAEVVKVLVTNGANVNAQSQNGFTPLYMAAQENHLEVVRFLL 160
Cdd:COG0666     94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  161 DNGASQSLATEDGFTPLAVALQQGHDQVVSLLLENdtkgkvrlpalhiaarkddtkaaalllqndtNADveskmvVNRAT 240
Cdd:COG0666    174 EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA-------------------------------GAD------VNAKD 216

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907073017  241 ESGFTPLHIAAHYGNINVATLLLNRAAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPL 313
Cdd:COG0666    217 NDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-379 1.66e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 188.24  E-value: 1.66e-52
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   54 LEKALDYIKNGVDVNICNQNGLNALHLASKEGHVEVVSELLQREANVDAATKKGNTALHIASLAGQAEVVKVLVTNGANV 133
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  134 NAQSQNGFTPLYMAAQENHLEVVRFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLLENdtkgkvrlpalhiaarkd 213
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA------------------ 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  214 dtkaaalllqndtNADveskmvVNRATESGFTPLHIAAHYGNINVATLLLNRAAAVDFTARNDITPLHVASKRGNANMVK 293
Cdd:COG0666    143 -------------GAD------VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  294 LLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRSAPILSKTKNGLSPLHMATQGDHLNCVQLLLQHNVPVDDVTN 373
Cdd:COG0666    204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283


                   ....*.
gi 1907073017  374 DYLTAL 379
Cdd:COG0666    284 DLLTLL 289
Death_ank3 cd08803
Death domain of Ankyrin-3; Death Domain (DD) of the human protein ankyrin-3 (ANK-3) and ...
 4118-4201 1.25e-46

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: 163.31  E-value: 1.25e-46
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 4118 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 4197
Cdd:cd08803      1 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 80


                   ....
gi 1907073017 4198 TLLE 4201
Cdd:cd08803     81 TLLE 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 1023-1160 9.11e-41

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 147.11  E-value: 9.11e-41
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  1023 SRFLVSFMVDARGGSMRGSRHhGMRIIIPPRKCTAPTRITCRLVKRHKLANPPPMVEGEGLASRLVEMGPAGAQFLgklh 1102
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPRT-GVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGALFL---- 75

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907073017  1103 lpthpppvnegeslvsrilqlgpqgtkfiGPVIVEIPHFGSMRGKERELIVLRSENGE 1160
Cdd:smart00218   76 -----------------------------RPVILEVPHCASLRPRDWEIVLLRSENGG 104
PHA03095 PHA03095
ankyrin-like protein; Provisional
 377-665 1.25e-38

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 153.26  E-value: 1.25e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  377 TALHVAAHCGHYKVAKV---LLDKKASPNAKALNGFTPLHI-ACKKNRIRVMELLLKHGASIQAVTESGLTPIHV--AAF 450
Cdd:PHA03095    49 TPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGF 128

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  451 MGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQA--EVVRYLVQDGAQVEAKAKDDQTPLHISARLGK--ADIVQQL 526
Cdd:PHA03095   129 NINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNAnvELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVREL 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  527 LQQGASPNAATTSGYTPLHLAAREGHED--VAAFLLDHGASLSITTKKGFTPLHVAAKYGKLEVASLLLQKSASPDAAGK 604
Cdd:PHA03095   209 IRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS 288

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907073017  605 SGLTPLHVAAHYDNQKVALLLLDQGASPHAAAK-------NGYTPLhIAAKKNQMdiATSLLEYGADA 665
Cdd:PHA03095   289 DGNTPLSLMVRNNNGRAVRAALAKNPSAETVAAtlntasvAGGDIP-SDATRLCV--AKVVLRGAFSL 353
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 559-796 8.84e-37

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 146.73  E-value: 8.84e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  559 LLDHGASLSITTKKGFTPLHVAAKYGKLEVASLLLQKSASPDAAGKSGLTPLHVAAHY-----DNQKVALLLLDQGASPH 633
Cdd:PHA03100    21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVN 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  634 AAAKNGYTPLHIAA--KKNQMDIATSLLEYGADANAVTRQGIASVHLAAQEGHVD--MVSLLLSRNANVNlsnksgltpl 709
Cdd:PHA03100   101 APDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDIN---------- 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  710 hlaaQEDRVNVaevLVNQGAHVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTALHQAAQQGHTHIINV 789
Cdd:PHA03100   171 ----AKNRVNY---LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243


                   ....*..
gi 1907073017  790 LLQNNAS 796
Cdd:PHA03100   244 LLNNGPS 250
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 417-764 3.17e-35

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 146.75  E-value: 3.17e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  417 KKNRIRVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQAEVVRYLVQD 496
Cdd:PHA02876   154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  497 GAQVEakaKDDqtpLHISARLGKADIVQQLL--QQGASPNAATTSGYTPLHLAAREGH-EDVAAFLLDHGASLSITTKKG 573
Cdd:PHA02876   234 RSNIN---KND---LSLLKAIRNEDLETSLLlyDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKG 307

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  574 FTPLHVAAKYG-KLEVASLLLQKSASPDAAGKSGLTPLHVAAHYD-NQKVALLLLDQGASPHAAAKNGYTPLHIAAKKNQ 651
Cdd:PHA02876   308 ETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNN 387

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  652 MDIATSLLEYGADANAVTRQGIASVHLAAQEGHVDM-VSLLLSRNANVNLSNKSGLTPLHLAAQED-RVNVAEVLVNQGA 729
Cdd:PHA02876   388 VVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGA 467

                          330       340       350
                   ....*....|....*....|....*....|....*
gi 1907073017  730 HVDAQTKMGYTPLHVGCHYGNikIVNFLLQHSAKV 764
Cdd:PHA02876   468 DVNAINIQNQYPLLIALEYHG--IVNILLHYGAEL 500
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 1027-1157 1.18e-34

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


Pssm-ID: 459941  Cd Length: 97  Bit Score: 129.57  E-value: 1.18e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1027 VSFMVDARGGSMRGSrHHGMRIIIPPRKCTAPTRITCRLVKRHKLANPPPMVEGEGLASRLVEMGPAGAQFLgklhlpth 1106
Cdd:pfam00791    1 VSGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVECGPPGLKFL-------- 71

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907073017 1107 pppvnegeslvsrilqlgpqgtkfiGPVIVEIPHFGSMRGKERELIVLRSE 1157
Cdd:pfam00791   72 -------------------------KPVILEVPHCASLRPEEWEIVLKRSD 97
PHA03095 PHA03095
ankyrin-like protein; Provisional
 414-733 5.50e-34

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 139.39  E-value: 5.50e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  414 IACKKNRIRVMELLLKHGASIQAVTESGLTPIHVaaFMGH-----VNIVSQLMHHGASPNTTNVRGETALHMAARSGQ-A 487
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHL--YLHYssekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  488 EVVRYLVQDGAQVEAKAKDDQTPLHISARlGK---ADIVQQLLQQGASPNAATTSGYTPLHLAAREGHEDVA--AFLLDH 562
Cdd:PHA03095    98 DVIKLLIKAGADVNAKDKVGRTPLHVYLS-GFninPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVEllRLLIDA 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  563 GASLSITTKKGFTPLHVAAKYGKL--EVASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALL--LLDQGASPHAAAKN 638
Cdd:PHA03095   177 GADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRY 256

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  639 GYTPLHIAAKKNQMDIATSLLEYGADANAVTRQGIASVHLAAQEGHVDMVSLLLSRNANVNL--------SNKSGLTPLH 710
Cdd:PHA03095   257 GQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETvaatlntaSVAGGDIPSD 336

                          330       340
                   ....*....|....*....|...
gi 1907073017  711 LAaqedRVNVAEVLVNQGAHVDA 733
Cdd:PHA03095   337 AT----RLCVAKVVLRGAFSLLP 355
Death_ank1 cd08805
Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and ...
 4118-4201 3.48e-33

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: 124.70  E-value: 3.48e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 4118 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 4197
Cdd:cd08805      1 ERVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSTALLNLWVDREGENAKMEPLYPALYSIDRLTIV 80


                   ....
gi 1907073017 4198 TLLE 4201
Cdd:cd08805     81 NILE 84
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
 4118-4201 4.92e-33

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: 124.30  E-value: 4.92e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 4118 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 4197
Cdd:cd08317      1 HRADLRLSDIANLLGSDWPELARELGVSEEDIDLIRSENPNSLAQQAMAMLRLWLEREGEKATGNALESALKKIGRDDIV 80


                   ....
gi 1907073017 4198 TLLE 4201
Cdd:cd08317     81 EKCE 84
PHA03095 PHA03095
ankyrin-like protein; Provisional
 487-768 4.98e-33

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 136.69  E-value: 4.98e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  487 AEVVRYLVQDGAQVEAKAKDDQTPLHISARLGK---ADIVQQLLQQGASPNAATTSGYTPLHLAAREGH-EDVAAFLLDH 562
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKA 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  563 GASLSITTKKGFTPLHV--AAKYGKLEVASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALL--LLDQGASPHAAAKN 638
Cdd:PHA03095   107 GADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLrlLIDAGADVYAVDDR 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  639 GYTPLHIAA---KKNQmDIATSLLEYGADANAVTRQGIASVHLAAQEG---HVDMVSLLLsRNANVNLSNKSGLTPLHLA 712
Cdd:PHA03095   187 FRSLLHHHLqsfKPRA-RIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLI-AGISINARNRYGQTPLHYA 264

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907073017  713 AQEDRVNVAEVLVNQGAHVDAQTKMGYTPLHVGCHYGNIKIVNFLL--QHSAKVNAKT 768
Cdd:PHA03095   265 AVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALakNPSAETVAAT 322
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 252-502 4.00e-32

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 132.87  E-value: 4.00e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  252 HYGNINVATL--LLNRAAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQ-----V 324
Cdd:PHA03100     9 KSRIIKVKNIkyIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeI 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  325 VEMLLDRSAPILSKTKNGLSPLHMA--TQGDHLNCVQLLLQHNVPVDDVTNDYLTALHVAAHCGHY--KVAKVLLDKKAS 400
Cdd:PHA03100    89 VKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVD 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  401 PNAkalngftplhiackKNRIrvmELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHM 480
Cdd:PHA03100   169 INA--------------KNRV---NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI 231

                          250       260
                   ....*....|....*....|..
gi 1907073017  481 AARSGQAEVVRYLVQDGAQVEA 502
Cdd:PHA03100   232 AILNNNKEIFKLLLNNGPSIKT 253
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 608-817 9.52e-32

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 131.71  E-value: 9.52e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  608 TPLHVAAHYDNQKVALLLLDQGASPHAAAKNGYTPLHIAA-----KKNQMDIATSLLEYGADANAVTRQGIASVHLAAQE 682
Cdd:PHA03100    37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISK 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  683 --GHVDMVSLLLSRNANVNLSNKSGLTPLHLAAQ--EDRVNVAEVLVNQGAHVDAQTKmgytplhvgchygnikiVNFLL 758
Cdd:PHA03100   117 ksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKGVDINAKNR-----------------VNYLL 179

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907073017  759 QHSAKVNAKTKNGYTALHQAAQQGHTHIINVLLQNNASPNELTVNGNTAL--AIARRLGYI 817
Cdd:PHA03100   180 SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLhiAILNNNKEI 240
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 195-437 1.44e-30

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 128.24  E-value: 1.44e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  195 NDTKGKVRLPALHIAARKDDTKAAALLLqnDTNADVESKMVVNratesgFTPLHIAAHYG-----NINVATLLLNRAAAV 269
Cdd:PHA03100    28 NDYSYKKPVLPLYLAKEARNIDVVKILL--DNGADINSSTKNN------STPLHYLSNIKynltdVKEIVKLLLEYGANV 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  270 DFTARNDITPLHVAS--KRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHE--QVVEMLLDRSAPILSKTKnglsp 345
Cdd:PHA03100   100 NAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNR----- 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  346 lhmatqgdhlncVQLLLQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKASPNAKALNGFTPLHIACKKNRIRVME 425
Cdd:PHA03100   175 ------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFK 242

                          250
                   ....*....|..
gi 1907073017  426 LLLKHGASIQAV 437
Cdd:PHA03100   243 LLLNNGPSIKTI 254
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 245-469 1.55e-30

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 127.86  E-value: 1.55e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  245 TPLHIAAHYGNINVATLLLNRAAAVDFTARNDITPLH-----VASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGA-- 317
Cdd:PHA03100    37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAIsk 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  318 RSGHEQVVEMLLDRSAPILSKTKNGLSPLHMATQGDH--LNCVQLLLQHNVPVDDVTN-DYLtalhvaahcghykvakvl 394
Cdd:PHA03100   117 KSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNRvNYL------------------ 178

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907073017  395 LDKKASPNAKALNGFTPLHIACKKNRIRVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNT 469
Cdd:PHA03100   179 LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 258-664 1.88e-30

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 131.72  E-value: 1.88e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  258 VATLLLNRAAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRSAPIls 337
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI-- 237

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  338 kTKNGLSPLHMATQGDhlncvqlllqhnvpvddvtndyltalhvaahcghYKVAKVLLDKKASPNAKALNGFTPLHIAck 417
Cdd:PHA02876   238 -NKNDLSLLKAIRNED----------------------------------LETSLLLYDAGFSVNSIDDCKNTPLHHA-- 280

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  418 knrirvmelllkhgasIQAVTESGLTPihvaafmghvnivsQLMHHGASPNTTNVRGETALHMAARSG-QAEVVRYLVQD 496
Cdd:PHA02876   281 ----------------SQAPSLSRLVP--------------KLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIML 330

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  497 GAQVEAKAKDDQTPLHISARLGK-ADIVQQLLQQGASPNAATTSGYTPLHLAAREGHEDVAAFLLDHGASLSITTKKGFT 575
Cdd:PHA02876   331 GADVNAADRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGT 410

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  576 PLHVAAkYGKLEVASL--LLQKSASPDAAGKSGLTPLHVAAHYDNQ-KVALLLLDQGASPHAAAKNGYTPLHIAAKKNqm 652
Cdd:PHA02876   411 ALHFAL-CGTNPYMSVktLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIALEYH-- 487

                          410
                   ....*....|..
gi 1907073017  653 DIATSLLEYGAD 664
Cdd:PHA02876   488 GIVNILLHYGAE 499
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 293-604 8.28e-30

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 126.23  E-value: 8.28e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  293 KLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRSAPILSKTKNGLSPLHMATQGDHLNCVQLLLQHNV-----P 367
Cdd:PHA02874    19 KIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVdtsilP 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  368 VDDVTNDYLtalhvaahcghykvaKVLLDKKASPNAKALNGFTPLHIACKKNRIRVMELLLKHGASIQAVTESGLTPIHV 447
Cdd:PHA02874    99 IPCIEKDMI---------------KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHI 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  448 AAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDDQTPLHISARLGKADIvqQLL 527
Cdd:PHA02874   164 AIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELL 241

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907073017  528 QQGASPNAATTSGYTPLHLAAR-EGHEDVAAFLLDHGASLSITTKKGFTPLHVAAKY-GKLEVASLLLQKSASPDAAGK 604
Cdd:PHA02874   242 INNASINDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKDIIANAVLIKEADK 320
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 410-671 2.23e-29

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 124.39  E-value: 2.23e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  410 TPLHIACKKNRIRVMELLLKHGASIQAVTESGLTPIHvaafmghvnIVSQLMHhgaspNTTNVRgetalhmaarsgqaEV 489
Cdd:PHA03100    37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLH---------YLSNIKY-----NLTDVK--------------EI 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  490 VRYLVQDGAQVEAKAKDDQTPLH--ISARLGKADIVQQLLQQGASPNAATTSGYTPLHLAAREGHED--VAAFLLDHGAS 565
Cdd:PHA03100    89 VKLLLEYGANVNAPDNNGITPLLyaISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVD 168

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  566 LSITTKkgftplhvaakygklevASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLLDQGASPHAAAKNGYTPLHI 645
Cdd:PHA03100   169 INAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHI 231

                          250       260
                   ....*....|....*....|....*.
gi 1907073017  646 AAKKNQMDIATSLLEYGADANAVTRQ 671
Cdd:PHA03100   232 AILNNNKEIFKLLLNNGPSIKTIIET 257
Death_ank2 cd08804
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ...
 4118-4201 2.99e-28

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: 110.56  E-value: 2.99e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 4118 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 4197
Cdd:cd08804      1 ERTEERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLTQCLTKINRMDIV 80


                   ....
gi 1907073017 4198 TLLE 4201
Cdd:cd08804     81 HLME 84
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 489-823 1.55e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 122.48  E-value: 1.55e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  489 VVRYLVQDGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLAAREGHEDVAAFLLDHGASLSi 568
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN- 238

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  569 ttkKGFTPLHVAAKYGKLEVASLLLQKSASPDAAGKSGLTPLHVAAHYDN-QKVALLLLDQGASPHAAAKNGYTPLHIAA 647
Cdd:PHA02876   239 ---KNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMA 315

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  648 KkNQMDIAT--SLLEYGADANAVTRQGIASVHLAAQ-EGHVDMVSLLLSRNANVNLSNKSGLTPLHLAAQEDRVNVAEVL 724
Cdd:PHA02876   316 K-NGYDTENirTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  725 VNQGAHVDAQTKMGYTPLHVG-CHYGNIKIVNFLLQHSAKVNAKTKNGYTALHQAAQQG-HTHIINVLLQNNASPNELTV 802
Cdd:PHA02876   395 LDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINI 474

                          330       340
                   ....*....|....*....|.
gi 1907073017  803 NGNTALAIArrLGYISVVDTL 823
Cdd:PHA02876   475 QNQYPLLIA--LEYHGIVNIL 493
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 475-700 4.77e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 117.40  E-value: 4.77e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  475 ETALHMAARSGQAEVVRYLVQDGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLAAREGHED 554
Cdd:PHA02875     3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  555 VAAFLLDHGASLS-ITTKKGFTPLHVAAKYGKLEVASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLLDQGASPH 633
Cdd:PHA02875    83 AVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907073017  634 AAAKNGYTPLHIAAKKNQMDIATSLLEYGADANAVTRQG-IASVHLAAQEGHVDMVSLLLSRNANVNL 700
Cdd:PHA02875   163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 211-566 5.59e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 120.55  E-value: 5.59e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  211 RKDDTKAAALLLQNdtNADVESKMVVNRatesgfTPLHIAAHYGNINVATLLLNRAAAVDFTARNDITPLHVASKRGNAN 290
Cdd:PHA02876   154 QQDELLIAEMLLEG--GADVNAKDIYCI------TPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNID 225

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  291 MVKLLLDRGAKIDaktRDGLTPLHCGARSGHEQVVeMLLDRSAPILSKTKNGLSPLHMATQGDHLN-CVQLLLQHNVPVD 369
Cdd:PHA02876   226 TIKAIIDNRSNIN---KNDLSLLKAIRNEDLETSL-LLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVN 301

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  370 DVTNDYLTALHVAAHCGH-YKVAKVLLDKKASPNAKALNGFTPLHIACKKNRIR-VMELLLKHGASIQAVTESGLTPIHV 447
Cdd:PHA02876   302 AKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHY 381

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  448 AAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQAEV-VRYLVQDGAQVEAKAKDDQTPLHISARLG-KADIVQQ 525
Cdd:PHA02876   382 AAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEM 461

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1907073017  526 LLQQGASPNAATTSGYTPLHLAAreGHEDVAAFLLDHGASL 566
Cdd:PHA02876   462 LLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 410-668 6.22e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 117.37  E-value: 6.22e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  410 TPLHIACKKNRIRVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASP---------------------- 467
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTsilpipciekdmiktildcgid 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  468 -NTTNVRGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHL 546
Cdd:PHA02874   117 vNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  547 AAREGHEDVAAFLLDHGASLSITTKKGFTPLHVAAKYGKLEVAslLLQKSASPDAAGKSGLTPLHVAAHYDNQK-VALLL 625
Cdd:PHA02874   197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE--LLINNASINDQDIDGSTPLHHAINPPCDIdIIDIL 274

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1907073017  626 LDQGASPHAAAKNGYTPLHIAAKK-NQMDIATSLLeygadANAV 668
Cdd:PHA02874   275 LYHKADISIKDNKGENPIDTAFKYiNKDPVIKDII-----ANAV 313
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 83-465 7.02e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 120.55  E-value: 7.02e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   83 KEGHVEVVSELLQREANVDAATKKGNTALHIASLAGQAEVVKVLVTNGANVNAQSQNGFTPLYMAAQENHLEVVRFLLDN 162
Cdd:PHA02876   154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  163 GASqslatedgftplavalqqghdqvvslLLENDTkgkvrlpALHIAARKDDTKAAALLLqndtnadvESKMVVNRATES 242
Cdd:PHA02876   234 RSN--------------------------INKNDL-------SLLKAIRNEDLETSLLLY--------DAGFSVNSIDDC 272

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  243 GFTPLHIAAHYGNIN-VATLLLNRAAAVDFTARNDITPLHVASKRG-NANMVKLLLDRGAKIDAKTRDGLTPLHCGAR-S 319
Cdd:PHA02876   273 KNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTlD 352

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  320 GHEQVVEMLLDRSAPILSKTKNGLSPLHMATQGDHLNCVQLLLQHNVPVDDVTNDYLTALHVAAhCGH--YKVAKVLLDK 397
Cdd:PHA02876   353 RNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL-CGTnpYMSVKTLIDR 431

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907073017  398 KASPNAKALNGFTPLHIACKKN-RIRVMELLLKHGASIQAVTESGLTPIHVAafMGHVNIVSQLMHHGA 465
Cdd:PHA02876   432 GANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGA 498
PHA03095 PHA03095
ankyrin-like protein; Provisional
 60-335 2.55e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 116.28  E-value: 2.55e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   60 YIKNGVDVNICNQNGLNALHLASKEGH---VEVVSELLQREANVDAATKKGNTALHI-ASLAGQAEVVKVLVTNGANVNA 135
Cdd:PHA03095    33 LLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKLLIKAGADVNA 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  136 QSQNGFTPL--YMAAQENHLEVVRFLLDNGASQSLATEDGFTPLAVALQQGH--DQVVSLLLEND----TKGKVRLPALH 207
Cdd:PHA03095   113 KDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGadvyAVDDRFRSLLH 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  208 IaarkddtkaaalLLQN-DTNADVESKMVV-----NRATESGFTPLHIAAHYG---NINVATLLLNrAAAVDFTARNDIT 278
Cdd:PHA03095   193 H------------HLQSfKPRARIVRELIRagcdpAATDMLGNTPLHSMATGSsckRSLVLPLLIA-GISINARNRYGQT 259

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907073017  279 PLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRSAPI 335
Cdd:PHA03095   260 PLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSA 316
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 250-480 4.04e-26

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 114.70  E-value: 4.04e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  250 AAHYGNINVATLLLNRAAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLL 329
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  330 DRSAPILSKT-KNGLSPLHMATQGDHLNCVQLLLQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKASPNAKALNG 408
Cdd:PHA02875    89 DLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907073017  409 FTPLHIACKKNRIRVMELLLKHGASIQAVTESG-LTPIHVAAFMGHVNIVSQLMHHGASPN-TTNVRGE--TALHM 480
Cdd:PHA02875   169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNiMFMIEGEecTILDM 244
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 4117-4203 5.88e-26

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: 104.42  E-value: 5.88e-26
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  4117 CERTDIRMAIVADH-LGLSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDALTSVLTKINRID 4195
Cdd:smart00005    1 PELTRQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDD 80


                    ....*...
gi 1907073017  4196 IVTLLEGP 4203
Cdd:smart00005   81 AVELLRSE 88
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 478-778 9.45e-26

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 113.91  E-value: 9.45e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  478 LHMAARSGQAEVVRYLVQD-GAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLAAREGHEDVA 556
Cdd:PHA02874     5 LRMCIYSGDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDII 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  557 AFLLDHGASLSITtkkgftPLHVAAKygklEVASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLLDQGASPHAAA 636
Cdd:PHA02874    85 KLLIDNGVDTSIL------PIPCIEK----DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIED 154

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  637 KNGYTPLHIAAKKNQMDIATSLLEYGADANAVTRQGIASVHLAAQEGHVDMVSLLLSRNANVNLSNKSGLTPLHLAAQED 716
Cdd:PHA02874   155 DNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN 234

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907073017  717 RvNVAEVLVNQgAHVDAQTKMGYTPLHVGCHYG-NIKIVNFLLQHSAKVNAKTKNGYTALHQA 778
Cdd:PHA02874   235 R-SAIELLINN-ASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 543-816 7.13e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 111.90  E-value: 7.13e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  543 PLHLAAREGHEDVAAFLLDHGASLSITTKKGFTPLHVAA----KYGKLEVASLLLQKSASpdaagkSGLTPLHVAAHYDN 618
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnKLGMKEMIRSINKCSVF------YTLVAIKDAFNNRN 113

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  619 QKVA-LLLLDQgasphaaAKNGYTPLHIAAKKNQMD------IATSLLEYGADANAVTR-QGIASVHLAAQEGHVDMVSL 690
Cdd:PHA02878   114 VEIFkIILTNR-------YKNIQTIDLVYIDKKSKDdiieaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTEL 186

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  691 LLSRNANVNLSNKSGLTPLHLAAQEDRVNVAEVLVNQGAHVDAQTKMGYTPLHVGCHY-GNIKIVNFLLQHSAKVNAK-T 768
Cdd:PHA02878   187 LLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKsY 266

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907073017  769 KNGYTALHQAAQQghTHIINVLLQNNASPNELTVNGNTALAIA--RRLGY 816
Cdd:PHA02878   267 ILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAvkQYLCI 314
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 59-304 8.20e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 110.91  E-value: 8.20e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   59 DYIKNGVDVNICNQNGLNA-----------------LHLASKEGHVEVVSELLQREANVDAATKKGNTALHIASLAGQA- 120
Cdd:PHA03100     3 SYIVLTKSRIIKVKNIKYIimeddlndysykkpvlpLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNl 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  121 ----EVVKVLVTNGANVNAQSQNGFTPLYMAAQE--NHLEVVRFLLDNGASQSLATEDGFTPLAVALQQGHD--QVVSLL 192
Cdd:PHA03100    83 tdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLL 162

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  193 LEN----DTKGKVRlpalhiaarkddtkaaaLLLQNDTNADVESKMvvnratesGFTPLHIAAHYGNINVATLLLNRAAA 268
Cdd:PHA03100   163 IDKgvdiNAKNRVN-----------------YLLSYGVPINIKDVY--------GFTPLHYAVYNNNPEFVKYLLDLGAN 217

                          250       260       270
                   ....*....|....*....|....*....|....*.
gi 1907073017  269 VDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDA 304
Cdd:PHA03100   218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 214-483 1.03e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 110.82  E-value: 1.03e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  214 DTKAAALLLQNDTNadveskmVVNRATESGFTPLHIAAHYGNINVATLLLNRAAAVDFTARNDITPLHVASKRGNANMVK 293
Cdd:PHA02874    13 DIEAIEKIIKNKGN-------CINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIK 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  294 LLLDRGA-----------------------KIDAKTRDGLTPLHCGARSGHEQVVEMLLDRSAPILSKTKNGLSPLHMAT 350
Cdd:PHA02874    86 LLIDNGVdtsilpipciekdmiktildcgiDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAI 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  351 QGDHLNCVQLLLQhNVPVDDVTNDYL-TALHVAAHCGHYKVAKVLLDKKASPNAKALNGFTPLHIACKKNRiRVMELLLK 429
Cdd:PHA02874   166 KHNFFDIIKLLLE-KGAYANVKDNNGeSPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLIN 243

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907073017  430 HgASIQAVTESGLTPIHVA-AFMGHVNIVSQLMHHGASPNTTNVRGETALHMAAR 483
Cdd:PHA02874   244 N-ASINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 563-823 1.25e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 110.44  E-value: 1.25e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  563 GASLSITTKKGFTPLHVAAKYGKLEVASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLLDQGASPhaaakngyTP 642
Cdd:PHA02874    25 GNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDT--------SI 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  643 LHIAAKKNQMdiATSLLEYGADANAVTRQGIASVHLAAQEGHVDMVSLLLSRNANVNLSNKSGLTPLHLAAQEDRVNVAE 722
Cdd:PHA02874    97 LPIPCIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIK 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  723 VLVNQGAHVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTALHQAAQQGHTHIinVLLQNNASPNELTV 802
Cdd:PHA02874   175 LLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDI 252

                          250       260
                   ....*....|....*....|....
gi 1907073017  803 NGNTALAIArrLGY---ISVVDTL 823
Cdd:PHA02874   253 DGSTPLHHA--INPpcdIDIIDIL 274
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 419-669 2.49e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 109.31  E-value: 2.49e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  419 NRIRVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQAEVVRYLVQDGA 498
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  499 QV-EAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLAAREGHEDVAAFLLDHGASLSITTKKGFTPL 577
Cdd:PHA02875    93 FAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  578 HVAAKYGKLEVASLLLQKSASPDAAGKSGltplhvaahydnqKVALLLLdqgasphaaakngytplhiAAKKNQMDIATS 657
Cdd:PHA02875   173 IIAMAKGDIAICKMLLDSGANIDYFGKNG-------------CVAALCY-------------------AIENNKIDIVRL 220

                          250
                   ....*....|..
gi 1907073017  658 LLEYGADANAVT 669
Cdd:PHA02875   221 FIKRGADCNIMF 232
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 279-600 2.82e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 109.97  E-value: 2.82e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  279 PLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLldrsapILSKTKnglsplhmatqgdhlncv 358
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEM------IRSINK------------------ 95

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  359 qlllqhnvpvDDVTNDYlTALHVAAHCGHYKVAKVLL----DKKASPNAKALngftplhiaCKKNRIRVME-----LLLK 429
Cdd:PHA02878    96 ----------CSVFYTL-VAIKDAFNNRNVEIFKIILtnryKNIQTIDLVYI---------DKKSKDDIIEaeitkLLLS 155

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  430 HGASIQAVTE-SGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDDQ 508
Cdd:PHA02878   156 YGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGN 235

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  509 TPLHIS-ARLGKADIVQQLLQQGASPNAATT-SGYTPLHLAAREghEDVAAFLLDHGASLSITTKKGFTPLHVAAKY--- 583
Cdd:PHA02878   236 TPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKQylc 313

                          330       340
                   ....*....|....*....|
gi 1907073017  584 ---GKLEVASLLLQKSASPD 600
Cdd:PHA02878   314 iniGRILISNICLLKRIKPD 333
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 580-802 8.44e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 107.77  E-value: 8.44e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  580 AAKYGKLEVASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLLDQGASPHAAAKNGYTPLHIAAKKNQMDIATSLL 659
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  660 EYGADANAVT-RQGIASVHLAAQEGHVDMVSLLLSRNANVNLSNKSGLTPLHLAAQEDRVNVAEVLVNQGAHVDAQTKMG 738
Cdd:PHA02875    89 DLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907073017  739 YTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNG-YTALHQAAQQGHTHIINVLLQNNASPNELTV 802
Cdd:PHA02875   169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMFM 233
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 423-712 2.04e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 106.97  E-value: 2.04e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  423 VMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQAEVVRYLVQDGAqvea 502
Cdd:PHA02874    17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGV---- 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  503 kakdDQTPLHISARlgKADIVQQLLQQGASPNAATTSGYTPLHLAAREGHEDVAAFLLDHGASLSITTKKGFTPLHVAAK 582
Cdd:PHA02874    93 ----DTSILPIPCI--EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIK 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  583 YGKLEVASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLLDQGASPHAAAKNGYTPLHIAAKKNQMdiATSLLEYG 662
Cdd:PHA02874   167 HNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS--AIELLINN 244

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1907073017  663 ADANAVTRQGIASVHLAAQ-EGHVDMVSLLLSRNANVNLSNKSGLTPLHLA 712
Cdd:PHA02874   245 ASINDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 345-613 4.09e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 106.50  E-value: 4.09e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  345 PLHMATQGDHLNCVQLLLQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKAspNAKALNGFTPLHIACKKNRIRVM 424
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSIN--KCSVFYTLVAIKDAFNNRNVEIF 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  425 E-LLLKHGASIQAVTESGLTPIHVAAFMgHVNIVSQLMHHGASPN-TTNVRGETALHMAARSGQAEVVRYLVQDGAQVEA 502
Cdd:PHA02878   118 KiILTNRYKNIQTIDLVYIDKKSKDDII-EAEITKLLLSYGADINmKDRHKGNTALHYATENKDQRLTELLLSYGANVNI 196

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  503 KAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLA-AREGHEDVAAFLLDHGASLSI-TTKKGFTPLHVA 580
Cdd:PHA02878   197 PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAkSYILGLTALHSS 276

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1907073017  581 AKygKLEVASLLLQKSASPDAAGKSGLTPLHVA 613
Cdd:PHA02878   277 IK--SERKLKLLLEYGADINSLNSYKLTPLSSA 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
78-165 8.35e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.57  E-value: 8.35e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   78 LHLASKEGHVEVVSELLQREANVDAATKKGNTALHIASLAGQAEVVKVLVTNgANVNAQSqNGFTPLYMAAQENHLEVVR 157
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*...
gi 1907073017  158 FLLDNGAS 165
Cdd:pfam12796   79 LLLEKGAD 86
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 613-808 2.77e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 103.15  E-value: 2.77e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  613 AAHYDNQKVALLLLDQGASPHAAAKNGYTPLHIAAKKNQMDIATSLLEYGADANaVTRQGIAS-VHLAAQEGHVDMVSLL 691
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPD-VKYPDIESeLHDAVEEGDVKAVEEL 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  692 LSRNANVN-LSNKSGLTPLHLAAQEDRVNVAEVLVNQGAHVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKN 770
Cdd:PHA02875    88 LDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1907073017  771 GYTALHQAAQQGHTHIINVLLQNNASPNELTVNGNTAL 808
Cdd:PHA02875   168 GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
Ank_2 pfam12796
Ankyrin repeats (3 copies);
478-569 4.49e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.26  E-value: 4.49e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  478 LHMAARSGQAEVVRYLVQDGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASpnAATTSGYTPLHLAAREGHEDVAA 557
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1907073017  558 FLLDHGASLSIT 569
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 151-381 6.49e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 101.99  E-value: 6.49e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  151 NHLEVVRFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLLENDTKGKVRLPA----LHIAARKDDTKAAALLLQNDT 226
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDieseLHDAVEEGDVKAVEELLDLGK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  227 NADveskmvvNRATESGFTPLHIAAHYGNINVATLLLNRAAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKT 306
Cdd:PHA02875    93 FAD-------DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIED 165

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907073017  307 RDGLTPLHCGARSGHEQVVEMLLDRSAPILSKTKNG-LSPLHMATQGDHLNCVQLLLQHNVPVDDVT---NDYLTALHV 381
Cdd:PHA02875   166 CCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMFmieGEECTILDM 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
511-601 8.13e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 8.13e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  511 LHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLAAREGHEDVAAFLLDHGASLSITtkKGFTPLHVAAKYGKLEVAS 590
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 1907073017  591 LLLQKSASPDA 601
Cdd:pfam12796   79 LLLEKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 85-455 8.22e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 101.96  E-value: 8.22e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   85 GHVEVVSELLQREAN-VDAATKKGNTALHIASLAGQAEVVKVLVTNGANVNAQSQNGFTPLYMAAQENHLEVVRFLLDNG 163
Cdd:PHA02874    12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  164 ASQSLatedgfTPLAValqqghdqvvsllLENDTkgkvrlpalhiaarkddtkaaalllqndTNADVESKMVVNRATESG 243
Cdd:PHA02874    92 VDTSI------LPIPC-------------IEKDM----------------------------IKTILDCGIDVNIKDAEL 124

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  244 FTPLHIAAHYGNINVATLLLNRAAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQ 323
Cdd:PHA02874   125 KTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYA 204

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  324 VVEMLLDRSAPILSKTKNGLSPLHMAtqgdhlncvqllLQHNvpvddvtndyltalhvaahcghyKVAKVLLDKKASPNA 403
Cdd:PHA02874   205 CIKLLIDHGNHIMNKCKNGFTPLHNA------------IIHN-----------------------RSAIELLINNASIND 249

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907073017  404 KALNGFTPLHIA----CKKNrirVMELLLKHGASIQAVTESGLTPIHVAafMGHVN 455
Cdd:PHA02874   250 QDIDGSTPLHHAinppCDID---IIDILLYHKADISIKDNKGENPIDTA--FKYIN 300
Ank_2 pfam12796
Ankyrin repeats (3 copies);
379-471 1.46e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.72  E-value: 1.46e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  379 LHVAAHCGHYKVAKVLLDKKASPNAKALNGFTPLHIACKKNRIRVMELLLKHGAsiQAVTESGLTPIHVAAFMGHVNIVS 458
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1907073017  459 QLMHHGASPNTTN 471
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
677-767 1.91e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.72  E-value: 1.91e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  677 HLAAQEGHVDMVSLLLSRNANVNLSNKSGLTPLHLAAQEDRVNVAEVLVNQgAHVDAQTKmGYTPLHVGCHYGNIKIVNF 756
Cdd:pfam12796    2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKL 79

                           90
                   ....*....|.
gi 1907073017  757 LLQHSAKVNAK 767
Cdd:pfam12796   80 LLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
111-198 1.97e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 1.97e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  111 LHIASLAGQAEVVKVLVTNGANVNAQSQNGFTPLYMAAQENHLEVVRFLLDNGASQSlaTEDGFTPLAVALQQGHDQVVS 190
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78


                   ....*...
gi 1907073017  191 LLLENDTK 198
Cdd:pfam12796   79 LLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
47-136 4.55e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.56  E-value: 4.55e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   47 RAARAGHLEKALDYIKNGVDVNICNQNGLNALHLASKEGHVEVVSELLQrEANVDAATkKGNTALHIASLAGQAEVVKVL 126
Cdd:pfam12796    3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVKLL 80

                           90
                   ....*....|
gi 1907073017  127 VTNGANVNAQ 136
Cdd:pfam12796   81 LEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 409-668 4.55e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 100.34  E-value: 4.55e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  409 FTPLHIACKKNRIRVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMhhgASPNTTNV-RGETALHMAARSGQA 487
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVfYTLVAIKDAFNNRNV 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  488 EVVRYLV---------QDGAQVEAKAKDDQTplhisarlgKADIVQQLLQQGASPNAAT-TSGYTPLHLAAREGHEDVAA 557
Cdd:PHA02878   115 EIFKIILtnrykniqtIDLVYIDKKSKDDII---------EAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTE 185

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  558 FLLDHGASLSITTKKGFTPLHVAAKYGKLEVASLLLQKSASPDAAGKSGLTPLHVAAHY-DNQKVALLLLDQGASPHAAA 636
Cdd:PHA02878   186 LLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKS 265

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1907073017  637 K-NGYTPLHIAAKKNQmdIATSLLEYGADANAV 668
Cdd:PHA02878   266 YiLGLTALHSSIKSER--KLKLLLEYGADINSL 296
Ank_2 pfam12796
Ankyrin repeats (3 copies);
412-503 5.42e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.18  E-value: 5.42e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  412 LHIACKKNRIRVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNvrGETALHMAARSGQAEVVR 491
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1907073017  492 YLVQDGAQVEAK 503
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
346-436 7.47e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.79  E-value: 7.47e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  346 LHMATQGDHLNCVQLLLQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDkKASPNAKaLNGFTPLHIACKKNRIRVME 425
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLK-DNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 1907073017  426 LLLKHGASIQA 436
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
313-404 1.23e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.40  E-value: 1.23e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  313 LHCGARSGHEQVVEMLLDRSAPILSKTKNGLSPLHMATQGDHLNCVQLLLQHNVPvdDVTNDYLTALHVAAHCGHYKVAK 392
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1907073017  393 VLLDKKASPNAK 404
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
445-535 1.35e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 1.35e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  445 IHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQAEVVRYLVqDGAQVEAKAkDDQTPLHISARLGKADIVQ 524
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 1907073017  525 QLLQQGASPNA 535
Cdd:pfam12796   79 LLLEKGADINV 89
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 111-429 1.74e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 98.41  E-value: 1.74e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  111 LHIASLAGQAEVVKVLVTNGANVNAQSQNGFTPLYMAAQENHLEVVRFLLDNGASQSLATEdgFTPLAVALQQGHDQVVS 190
Cdd:PHA02878    41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYT--LVAIKDAFNNRNVEIFK 118

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  191 LLLENDTKGKVRLPALHIAAR-KDD---TKAAALLLQNdtNADVESKmvvnrATESGFTPLHIAAHYGNINVATLLLNRA 266
Cdd:PHA02878   119 IILTNRYKNIQTIDLVYIDKKsKDDiieAEITKLLLSY--GADINMK-----DRHKGNTALHYATENKDQRLTELLLSYG 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  267 AAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCG-ARSGHEQVVEMLLDRSAPILSK-TKNGLS 344
Cdd:PHA02878   192 ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKsYILGLT 271

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  345 PLHMATQGDHLncVQLLLQHNVPVDDVTNDYLTALHVAA------HCGHYKVAKVLLDKKASPNAKALNGFTpLHIACKK 418
Cdd:PHA02878   272 ALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAVkqylciNIGRILISNICLLKRIKPDIKNSEGFI-DNMDCIT 348

                          330
                   ....*....|.
gi 1907073017  419 NRIRVMELLLK 429
Cdd:PHA02878   349 SNKRLNQIKDK 359
Ank_2 pfam12796
Ankyrin repeats (3 copies);
643-734 1.77e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 1.77e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  643 LHIAAKKNQMDIATSLLEYGADANAVTRQGIASVHLAAQEGHVDMVSLLLSrNANVNLSNKsGLTPLHLAAQEDRVNVAE 722
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1907073017  723 VLVNQGAHVDAQ 734
Cdd:pfam12796   79 LLLEKGADINVK 90
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 4127-4201 2.07e-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: 88.11  E-value: 2.07e-20
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907073017 4127 VADHLGLSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTLLE 4201
Cdd:cd01670      5 VAEELGRDWKKLARKLGLSEGDIDQIEEDNRDDLKEQAYQMLERWREREGDEATLGRLIQALREIGRRDLAEKLE 79
Ank_2 pfam12796
Ankyrin repeats (3 copies);
280-366 1.13e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 1.13e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  280 LHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRsaPILSKTKNGLSPLHMATQGDHLNCVQ 359
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDNGRTALHYAARSGHLEIVK 78


                   ....*..
gi 1907073017  360 LLLQHNV 366
Cdd:pfam12796   79 LLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
577-667 1.52e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 1.52e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  577 LHVAAKYGKLEVASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLLDQGASphAAAKNGYTPLHIAAKKNQMDIAT 656
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 1907073017  657 SLLEYGADANA 667
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
247-338 2.25e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 2.25e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  247 LHIAAHYGNINVATLLLNRAAAVDFTARNDITPLHVASKRGNANMVKLLLDRgAKIDAKTrDGLTPLHCGARSGHEQVVE 326
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1907073017  327 MLLDRSAPILSK 338
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 61-285 2.33e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 94.65  E-value: 2.33e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   61 IKNGVDVNICNQNGLNALHLASKEGHVEVVSELLQREANVDAATKKGNTALHIASLAGQAEVVKVLVTNGANVNAQSQNG 140
Cdd:PHA02874   111 LDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG 190

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  141 FTPLYMAAQENHLEVVRFLLDNGASQSLATEDGFTPLAVALQQGHdQVVSLLLENDTKgkvrlpalhiaarkddtkaaal 220
Cdd:PHA02874   191 ESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNASI---------------------- 247

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907073017  221 llqNDTNADveskmvvnratesGFTPLHIAAHYG-NINVATLLLNRAAAVDFTARNDITPLHVASK 285
Cdd:PHA02874   248 ---NDQDID-------------GSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
709-798 2.48e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 2.48e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  709 LHLAAQEDRVNVAEVLVNQGAHVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHsAKVNAKTkNGYTALHQAAQQGHTHIIN 788
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|
gi 1907073017  789 VLLQNNASPN 798
Cdd:pfam12796   79 LLLEKGADIN 88
Death pfam00531
Death domain;
4123-4201 8.74e-18

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 80.87  E-value: 8.74e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 4123 RMAIVADH---LGLSWTELARELNFSVDEINQIRVENPNsLISQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTL 4199
Cdd:pfam00531    3 QLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAAEK 81


                   ..
gi 1907073017 4200 LE 4201
Cdd:pfam00531   82 IQ 83
Ank_2 pfam12796
Ankyrin repeats (3 copies);
610-702 9.35e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 9.35e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  610 LHVAAHYDNQKVALLLLDQGASPHAAAKNGYTPLHIAAKKNQMDIATSLLEYgADANAVTRQGIAsVHLAAQEGHVDMVS 689
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTA-LHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1907073017  690 LLLSRNANVNLSN 702
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 48-313 2.19e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 88.48  E-value: 2.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   48 AARAGHLEKALDYIKNGVDVNICNQNGLNALHLASKEGHVEVVSELLqrEANVDAATkkgntaLHIASLagQAEVVKVLV 127
Cdd:PHA02874    42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI--DNGVDTSI------LPIPCI--EKDMIKTIL 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  128 TNGANVNAQSQNGFTPLYMAAQENHLEVVRFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLLENDTKGKVR----L 203
Cdd:PHA02874   112 DCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKdnngE 191

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  204 PALHIAARKDDTKAAALLLQNDTNADVESKmvvnrateSGFTPLHIAAHYgNINVATLLLNRaAAVDFTARNDITPLHVA 283
Cdd:PHA02874   192 SPLHNAAEYGDYACIKLLIDHGNHIMNKCK--------NGFTPLHNAIIH-NRSAIELLINN-ASINDQDIDGSTPLHHA 261

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1907073017  284 -SKRGNANMVKLLLDRGAKIDAKTRDGLTPL 313
Cdd:PHA02874   262 iNPPCDIDIIDILLYHKADISIKDNKGENPI 292
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 53-364 1.81e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 86.09  E-value: 1.81e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   53 HLEKALDYIKNGVDVNicnqNGLNA-----LHLASKEGHVEVVSELLQREANVDAATKKGNTALHIASLAGQAEVVKVLV 127
Cdd:PHA02878    15 TILKYIEYIDHTENYS----TSASLipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  128 tngANVNAQS-QNGFTPLYMAAQENHLEVVRFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLLEN--DTKGKVRLP 204
Cdd:PHA02878    91 ---RSINKCSvFYTLVAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYgaDINMKDRHK 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  205 ---ALHIAARKDDTKAAALLLQNDTNADveskmVVNRATESgftPLHIAAHYGNINVATLLLNRAAAVDFTARNDITPLH 281
Cdd:PHA02878   168 gntALHYATENKDQRLTELLLSYGANVN-----IPDKTNNS---PLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  282 VASKR-GNANMVKLLLDRGAKIDAK-TRDGLTPLHCGARSghEQVVEMLLDRSAPILSKTKNGLSPLHMAT-QGDHLNCV 358
Cdd:PHA02878   240 ISVGYcKDYDILKLLLEHGVDVNAKsYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIG 317


                   ....*.
gi 1907073017  359 QLLLQH 364
Cdd:PHA02878   318 RILISN 323
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 52-300 2.55e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 85.04  E-value: 2.55e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   52 GHLEKALDYIKNGVDVNICNQNGLNALHLASKEGHVEVVSELLQREANVDAATKKGNTALHIASLAGQAEVVKVLVTNGA 131
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  132 NVN-AQSQNGFTPLYMAAQENHLEVVRFLLDNGASQSLATEDGFTPlavalqqghdqvvslllendtkgkvrlpaLHIAA 210
Cdd:PHA02875    93 FADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP-----------------------------LHLAV 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  211 RKDDTKAAALLLQNDTNADVESKMvvnratesGFTPLHIAAHYGNINVATLLLNRAAAVDFTARN-DITPLHVASKRGNA 289
Cdd:PHA02875   144 MMGDIKGIELLIDHKACLDIEDCC--------GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKI 215

                          250
                   ....*....|.
gi 1907073017  290 NMVKLLLDRGA 300
Cdd:PHA02875   216 DIVRLFIKRGA 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
742-823 8.08e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 8.08e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  742 LHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTALHQAAQQGHTHIINVLLQNNASpnELTVNGNTALAIARRLGYISVVD 821
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78


                   ..
gi 1907073017  822 TL 823
Cdd:pfam12796   79 LL 80
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 575-759 1.85e-15

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 83.52  E-value: 1.85e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  575 TPLHVAAKYGKLE-VASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLLDqgASPH-------AAAKNGYTPLHIA 646
Cdd:cd22192     19 SPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPElvnepmtSDLYQGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  647 AKKNQMDIATSLLEYGADANA--VT----RQGIAS--------VHLAAQEGHVDMVSLLLSRNANVNLSNKSGLTPLH-L 711
Cdd:cd22192     97 VVNQNLNLVRELIARGADVVSprATgtffRPGPKNliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHiL 176

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907073017  712 AAQEDRVNVAEV---LVNQGAHVDAQT------KMGYTPLHVGCHYGNIKIVNFLLQ 759
Cdd:cd22192    177 VLQPNKTFACQMydlILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQHLVQ 233
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 515-702 6.76e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 82.22  E-value: 6.76e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  515 ARLGKADIVQQLLQQGASPNAATTSGYTPLHLAAREGHEDVAAFLLDHGASLSITTKKGFTPLHVAAKYGKLEVASLLLQ 594
Cdd:PLN03192   533 ASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYH 612

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  595 KSASPDaagksgltplhvaahydnqkvalllldqgasPHAAAKngytPLHIAAKKNQMDIATSLLEYGADANAVTRQGIA 674
Cdd:PLN03192   613 FASISD-------------------------------PHAAGD----LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGAT 657

                          170       180
                   ....*....|....*....|....*...
gi 1907073017  675 SVHLAAQEGHVDMVSLLLSRNANVNLSN 702
Cdd:PLN03192   658 ALQVAMAEDHVDMVRLLIMNGADVDKAN 685
Ank_2 pfam12796
Ankyrin repeats (3 copies);
144-275 1.36e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 1.36e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  144 LYMAAQENHLEVVRFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLLEndtkgkvrlpalHIAARKDDtkaaalllq 223
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE------------HADVNLKD--------- 59

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907073017  224 ndtnadveskmvvnrateSGFTPLHIAAHYGNINVATLLLNRAAavDFTARN 275
Cdd:pfam12796   60 ------------------NGRTALHYAARSGHLEIVKLLLEKGA--DINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 509-731 1.69e-13

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: 76.98  E-value: 1.69e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  509 TPLHISARLGKADIVQQLL-QQGASPNAATTSGYTPLHLAAREGHEDVAAFLLDHGASL---SITTK--KGFTPLHVAAK 582
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnePMTSDlyQGETALHIAVV 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  583 YGKLEVASLLLQKSA---SPDAAG------KSGLT-----PLHVAAHYDNQKVALLLLDQGASPHAAAKNGYTPLHIAAK 648
Cdd:cd22192     99 NQNLNLVRELIARGAdvvSPRATGtffrpgPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  649 KNQMDIATSLLEYgadanavtrqgiasvhLAAQEGHVDMVSLLLsrnanvnLSNKSGLTPLHLAAQEDRVNVAEVLVNQG 728
Cdd:cd22192    179 QPNKTFACQMYDL----------------ILSYDKEDDLQPLDL-------VPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235


                   ...
gi 1907073017  729 AHV 731
Cdd:cd22192    236 RHI 238
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 650-823 1.83e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 75.80  E-value: 1.83e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  650 NQMDIATSLLEYGADANAVTRQGIASVHLAAQEGHVDMVSLLLSRNANVNLSNKSGLTPLHLAAQEDRVNVAEVLVNQGA 729
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  730 HV-DAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTALHQAAQQGHTHIINVLLQNNASPNELTVNGNTAL 808
Cdd:PHA02875    93 FAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                          170
                   ....*....|....*
gi 1907073017  809 AIARRLGYISVVDTL 823
Cdd:PHA02875   173 IIAMAKGDIAICKML 187
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 617-823 2.14e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.03  E-value: 2.14e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  617 DNQKVALLLLDQGASPHAAAKNGYTPLHIAAKKNQMDIATSLLEYGADANAVTRQGIASVHLAAQEGHVDMVSLLLSRNA 696
Cdd:PHA02876   156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  697 NVnlsNKSGLTPLHLAAQEDrVNVAEVLVNQGAHVDAQTKMGYTPLHVGCHYGNI-KIVNFLLQHSAKVNAKTKNGYTAL 775
Cdd:PHA02876   236 NI---NKNDLSLLKAIRNED-LETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPL 311

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907073017  776 HQAAQQGH-THIINVLLQNNASPNELTVNGNTALAIARRLG-YISVVDTL 823
Cdd:PHA02876   312 YLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITL 361
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 471-596 4.29e-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: 75.95  E-value: 4.29e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  471 NVRGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDD--------------QTPLHISARLGKADIVQQLLQQGASPNAA 536
Cdd:cd22194    138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIVQLLMEKESTDITS 217

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907073017  537 TTS-GYTPLH--LAAREGHEDVAAF--------LLDH-GASL-SITTKKGFTPLHVAAKYGKLEVASLLLQKS 596
Cdd:cd22194    218 QDSrGNTVLHalVTVAEDSKTQNDFvkrmydmiLLKSeNKNLeTIRNNEGLTPLQLAAKMGKAEILKYILSRE 290
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 385-594 6.18e-13

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: 75.50  E-value: 6.18e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  385 CGHYKVAKVLLDKKASPNAKALN-------GFTPLHIACKKNRIR-VMELLLKHGASIqavtESGLTPIHVAAfMGHVNI 456
Cdd:TIGR00870   22 LPAAERGDLASVYRDLEEPKKLNincpdrlGRSALFVAAIENENLeLTELLLNLSCRG----AVGDTLLHAIS-LEYVDA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  457 VSQLM-----HHGASPNTTNV---------RGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDD--------------Q 508
Cdd:TIGR00870   97 VEAILlhllaAFRKSGPLELAndqytseftPGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgE 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  509 TPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLAAREGHEDVA---------AFLLDHGASLS-------ITTKK 572
Cdd:TIGR00870  177 SPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKAEyeelscqmyNFALSLLDKLRdskelevILNHQ 256

                          250       260
                   ....*....|....*....|..
gi 1907073017  573 GFTPLHVAAKYGKLEVASLLLQ 594
Cdd:TIGR00870  257 GLTPLKLAAKEGRIVLFRLKLA 278
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 424-577 2.69e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 73.75  E-value: 2.69e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  424 MELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQAEVVRYLVQDGAQVEAK 503
Cdd:PLN03192   541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH 620

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907073017  504 AKDDQtpLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLAAREGHEDVAAFLLDHGASL-SITTKKGFTPL 577
Cdd:PLN03192   621 AAGDL--LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVdKANTDDDFSPT 693
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 106-265 3.29e-12

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: 73.25  E-value: 3.29e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  106 KGNTALHIASLAGQAEVVKVLVTNGANVNAQSQNGF--------------TPLYMAAQENHLEVVRFLLDNGasqslate 171
Cdd:cd22194    140 EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKE-------- 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  172 dgftPLAVALQqghdqvvslllenDTKGKVRLPALHIAArkDDTKAaalllQNDTNADVESKMVVNRATES--------G 243
Cdd:cd22194    212 ----STDITSQ-------------DSRGNTVLHALVTVA--EDSKT-----QNDFVKRMYDMILLKSENKNletirnneG 267

                          170       180
                   ....*....|....*....|..
gi 1907073017  244 FTPLHIAAHYGNINVATLLLNR 265
Cdd:cd22194    268 LTPLQLAAKMGKAEILKYILSR 289
PHA02798 PHA02798
ankyrin-like protein; Provisional
 87-313 4.07e-12

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 72.17  E-value: 4.07e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   87 VEVVSELLQREANVDAATKKGNTAL-----HIASLAGQAEVVKVLVTNGANVNAQSQNGFTPLYMAAQE---NHLEVVRF 158
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLF 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  159 LLDNGASQSLATEDGFTPLAVALQQGHD---QVVSLLLE-----NDTKGKVRLPALHIAARKD----DTKAAALLLQNDT 226
Cdd:PHA02798   131 MIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEkgvdiNTHNNKEKYDTLHCYFKYNidriDADILKLFVDNGF 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  227 NADVEskmvvNRATESGFTPLHIAAHYGNINVATLLLNRA-AAVDFTARN--DITPLHVASKRGNANMVKLLLDRGAKID 303
Cdd:PHA02798   211 IINKE-----NKSHKKKFMEYLNSLLYDNKRFKKNILDFIfSYIDINQVDelGFNPLYYSVSHNNRKIFEYLLQLGGDIN 285

                          250
                   ....*....|
gi 1907073017  304 AKTRDGLTPL 313
Cdd:PHA02798   286 IITELGNTCL 295
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 142-363 1.00e-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: 71.20  E-value: 1.00e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  142 TPLYMAAQENHLEVVRFLLDNgasqslATEDGFTplavalqqghdqvvslllendtKGKVRLPALHIAARKDDTKAAALL 221
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKC------PSCDLFQ----------------------RGALGETALHVAALYDNLEAAVVL 70

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  222 LQNDTNadveskmVVNRATES----GFTPLHIAAHYGNINVATLLLNRAAAVdFTARNDIT---------------PLHV 282
Cdd:cd22192     71 MEAAPE-------LVNEPMTSdlyqGETALHIAVVNQNLNLVRELIARGADV-VSPRATGTffrpgpknliyygehPLSF 142

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  283 ASKRGNANMVKLLLDRGAKIDAKTRDGLTPLH-----------CgarsgheQVVEMLL-----DRSAPiLSKTKN--GLS 344
Cdd:cd22192    143 AACVGNEEIVRLLIEHGADIRAQDSLGNTVLHilvlqpnktfaC-------QMYDLILsydkeDDLQP-LDLVPNnqGLT 214

                          250
                   ....*....|....*....
gi 1907073017  345 PLHMATQGDHLNCVQLLLQ 363
Cdd:cd22192    215 PFKLAAKEGNIVMFQHLVQ 233
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 377-595 1.26e-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: 71.20  E-value: 1.26e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  377 TALHVAAHCGHYKVAKVLLDkkASP-------NAKALNGFTPLHIACKKNRIRVMELLLKHGASIQAVTESGLtpihvaA 449
Cdd:cd22192     53 TALHVAALYDNLEAAVVLME--AAPelvnepmTSDLYQGETALHIAVVNQNLNLVRELIARGADVVSPRATGT------F 124

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  450 FmghvnivsqlmhhgaSPNTTNV--RGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDDQTPLHISARLGKADIVQQLL 527
Cdd:cd22192    125 F---------------RPGPKNLiyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMY 189

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907073017  528 QQgaspnaattsgytplhLAAREGHEDVAAflLDHgaslsITTKKGFTPLHVAAKYGKLEVASLLLQK 595
Cdd:cd22192    190 DL----------------ILSYDKEDDLQP--LDL-----VPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Herpes_BLLF1 pfam05109
Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 ...
 1547-1954 3.53e-11

Herpes virus major outer envelope glycoprotein (BLLF1); This family consists of the BLLF1 viral late glycoprotein, also termed gp350/220. It is the most abundantly expressed glycoprotein in the viral envelope of the Herpesviruses and is the major antigen responsible for stimulating the production of neutralising antibodies in vivo.


Pssm-ID: 282904 [Multi-domain]  Cd Length: 886  Bit Score: 69.95  E-value: 3.53e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1547 TEPSMKTVERSSGTArslpTTYSHKPFFSTRPYQSWTT---------APITVPGPAKSGSLSSSPSNTPSASPLKSIWSV 1617
Cdd:pfam05109  398 TAPKTLIITRTATNA----TTTTHKVIFSKAPESTTTSptlnttgfaAPNTTTGLPSSTHVPTNLTAPASTGPTVSTADV 473

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1618 STPSPIKSTLGASTTSSVKS---------ISDVASPIRSfrtVSSPIKTVVSPSPY----NPQVASGTLGR--------- 1675
Cdd:pfam05109  474 TSPTPAGTTSGASPVTPSPSprdngteskAPDMTSPTSA---VTTPTPNATSPTPAvttpTPNATSPTLGKtsptsavtt 550

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1676 -VPTITEATP-IKGLAPNSTFSS--RTSPVTTAGSLLERSSITMTPPASPKSNITMYSSSLpfksiiTSATPLISSPLKS 1751
Cdd:pfam05109  551 pTPNATSPTPaVTTPTPNATIPTlgKTSPTSAVTTPTPNATSPTVGETSPQANTTNHTLGG------TSSTPVVTSPPKN 624

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1752 VVSP-TKSAADVISTAKATMA---SSLS---SPLKQMSGHAEVALVNGSvsplkYPSSSALINGCKATATLQDKISTA-- 1822
Cdd:pfam05109  625 ATSAvTTGQHNITSSSTSSMSlrpSSISetlSPSTSDNSTSHMPLLTSA-----HPTGGENITQVTPASTSTHHVSTSsp 699

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1823 ------TNAVSSVVSAASDTVEKALSTTTAMPfsPLRSYVSAAPS----AFQSLRTPSASALYTSLG---------SSIA 1883
Cdd:pfam05109  700 aprpgtTSQASGPGNSSTSTKPGEVNVTKGTP--PKNATSPQAPSgqktAVPTVTSTGGKANSTTGGkhttghgarTSTE 777

                          410       420       430       440       450       460       470
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907073017 1884 ATTSSVTSSIITVPVYSVVNVLPEPALKKLPDSNSFTksaaallSPIKTLTTETRPQPhfnRTSSPVKSSL 1954
Cdd:pfam05109  778 PTTDYGGDSTTPRTRYNATTYLPPSTSSKLRPRWTFT-------SPPVTTAQATVPVP---PTSQPRFSNL 838
Ank_4 pfam13637
Ankyrin repeats (many copies);
540-593 4.17e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.75  E-value: 4.17e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907073017  540 GYTPLHLAAREGHEDVAAFLLDHGASLSITTKKGFTPLHVAAKYGKLEVASLLL 593
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
278-329 7.71e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 7.71e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907073017  278 TPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLL 329
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
441-494 9.02e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 9.02e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907073017  441 GLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQAEVVRYLV 494
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 78-265 9.82e-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: 68.12  E-value: 9.82e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   78 LHLASKEGHVEVVSELL-QREANVDAATKKGNTALHIASLAGQAEVVKVLVTNG---ANVNAQSQ--NGFTPLYMAAQEN 151
Cdd:cd22192     21 LLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelVNEPMTSDlyQGETALHIAVVNQ 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  152 HLEVVRFLLDNGASQSLATEDG--FT------------PLAVALQQGHDQVVSLLLEN--DTKGKVRL--PALHIAARKD 213
Cdd:cd22192    101 NLNLVRELIARGADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEIVRLLIEHgaDIRAQDSLgnTVLHILVLQP 180

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907073017  214 DTKAAA----LLLQNDTNADVES-KMVVNRAtesGFTPLHIAAHYGNINVATLLLNR 265
Cdd:cd22192    181 NKTFACqmydLILSYDKEDDLQPlDLVPNNQ---GLTPFKLAAKEGNIVMFQHLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
375-428 1.14e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.60  E-value: 1.14e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907073017  375 YLTALHVAAHCGHYKVAKVLLDKKASPNAKALNGFTPLHIACKKNRIRVMELLL 428
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 592-803 1.20e-10

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 67.39  E-value: 1.20e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  592 LLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLLDQGASPHAAAKNGYTPLHIAAKKNQ--MDIATSLLEYGADA-NAV 668
Cdd:PHA02946    58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKInNSV 137

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  669 TRQGIASVhLAAQEGHVDMVSLLLSRNANVNLSNKSGLTPL--HLAAQEDRVNVAEVLVNQGAHVDAQTKMGYTPLHVGC 746
Cdd:PHA02946   138 DEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVC 216

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  747 H--YGNIKIVNFLLQhSAKVNAKTKNGYTALHQAAQQ-GHTHIINVLLQNNASPNELTVN 803
Cdd:PHA02946   217 SktVKNVDIINLLLP-STDVNKQNKFGDSPLTLLIKTlSPAHLINKLLSTSNVITDQTVN 275
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 51-177 1.22e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.97  E-value: 1.22e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   51 AGHLEkalDYIKNGVDVNICNQNGLNALHLASKEGHVEVVSELLQREANVDAATKKGNTAL----------------HIA 114
Cdd:PLN03192   538 AALLE---ELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrilyHFA 614

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907073017  115 SLA---------------GQAEVVKVLVTNGANVNAQSQNGFTPLYMAAQENHLEVVRFLLDNGASQSLA-TEDGFTPL 177
Cdd:PLN03192   615 SISdphaagdllctaakrNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAnTDDDFSPT 693
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 342-471 1.35e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.97  E-value: 1.35e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  342 GLSPLHMATQGDHLNCVQLLLQH--NVPVDDVTNDylTALHVAAHCGHYKVAKVLLDKKASPNAKAlnGFTPLHIACKKN 419
Cdd:PLN03192   558 GRTPLHIAASKGYEDCVLVLLKHacNVHIRDANGN--TALWNAISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKRN 633

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907073017  420 RIRVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTN 471
Cdd:PLN03192   634 DLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 377-598 1.74e-10

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: 67.21  E-value: 1.74e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  377 TALHVAA---HCGHYKVAKVLLD-KKASPNAKAL----------NGFTPLHIACKKNRIRVMELLLKHGASIQAVTESgl 442
Cdd:cd21882     28 TCLHKAAlnlNDGVNEAIMLLLEaAPDSGNPKELvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSARATG-- 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  443 tpihvAAFMGHvnivsqlmhhgasPNTTNVRGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDD---QTPLHIsarlgk 519
Cdd:cd21882    106 -----RFFRKS-------------PGNLFYFGELPLSLAACTNQEEIVRLLLENGAQPAALEAQDslgNTVLHA------ 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  520 adIVQQLLQQGASPNAATTSGYTPLHLAAReghedvaaflLDHGASLS-ITTKKGFTPLHVAAKYGKLEVASLLLQKSAS 598
Cdd:cd21882    162 --LVLQADNTPENSAFVCQMYNLLLSYGAH----------LDPTQQLEeIPNHQGLTPLKLAAVEGKIVMFQHILQREFS 229
Ank_4 pfam13637
Ankyrin repeats (many copies);
410-458 2.78e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 2.78e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1907073017  410 TPLHIACKKNRIRVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVS 458
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLK 51
PHA02798 PHA02798
ankyrin-like protein; Provisional
 488-789 2.83e-10

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 66.40  E-value: 2.83e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  488 EVVRYLVQDGAQVEAKAKDDQTPL-----HISARLGKADIVQQLLQQGASPNAATTSGYTPLHLAAREGH---EDVAAFL 559
Cdd:PHA02798    52 DIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLFM 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  560 LDHGASLSITTKKGFTPLHVAAKYG---KLEVASLLLQKSASPDA-AGKSGLTPLHVAAHYD----NQKVALLLLDQGAS 631
Cdd:PHA02798   132 IENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNidriDADILKLFVDNGFI 211

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  632 PHAAAKngytplhiAAKKNQMDIATSLLEYGADANAvtrqgiasvhlaaqeghvDMVSLLLSRnANVNLSNKSGLTPLHL 711
Cdd:PHA02798   212 INKENK--------SHKKKFMEYLNSLLYDNKRFKK------------------NILDFIFSY-IDINQVDELGFNPLYY 264

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907073017  712 AAQEDRVNVAEVLVNQGAHVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHsaKVNAKT-KNGYTALHQaaqqghtHIINV 789
Cdd:PHA02798   265 SVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNK--KPNKNTiSYTYYKLRK-------HILNV 334
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 355-546 3.09e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.82  E-value: 3.09e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  355 LNCVQLLLQHNVPVDDVTNDylTALHVAAHCGHYKVAKVLLDKKASPNAKALNGFTPLHIACKKNRIRVMELLLKHGASI 434
Cdd:PLN03192   507 LNVGDLLGDNGGEHDDPNMA--SNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNV 584

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  435 QAVTESGLTPIHVAAFMGHVNIVsQLMHHGASPNTTNVRGETaLHMAARSGQAEVVRYLVQDGAQVEAKAKDDQTPLHIS 514
Cdd:PLN03192   585 HIRDANGNTALWNAISAKHHKIF-RILYHFASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVA 662

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1907073017  515 ARLGKADIVQQLLQQGASPNAATT-SGYTPLHL 546
Cdd:PLN03192   663 MAEDHVDMVRLLIMNGADVDKANTdDDFSPTEL 695
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 573-744 3.27e-10

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: 66.44  E-value: 3.27e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  573 GFTPLHVAAKY---GKLEVASLLLQ---KSASPDAAGKS--------GLTPLHVAAHYDNQKVALLLLDQGASPHAAAKN 638
Cdd:cd21882     26 GKTCLHKAALNlndGVNEAIMLLLEaapDSGNPKELVNApctdefyqGQTALHIAIENRNLNLVRLLVENGADVSARATG 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  639 -------------GYTPLHIAAKKNQMDIATSLLEYGADANAVTRQ---GIASVHLAAQEGH---------VDMVSLLLS 693
Cdd:cd21882    106 rffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHALVLQADntpensafvCQMYNLLLS 185

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907073017  694 RNANVN-------LSNKSGLTPLHLAAQEDRVNVAEVLVNQGAHVDAQ------TKMGYTPLHV 744
Cdd:cd21882    186 YGAHLDptqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQREFSGPYQplsrkfTEWTYGPVTS 249
Ank_4 pfam13637
Ankyrin repeats (many copies);
738-791 3.87e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 3.87e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907073017  738 GYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTALHQAAQQGHTHIINVLL 791
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
107-160 3.99e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 3.99e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907073017  107 GNTALHIASLAGQAEVVKVLVTNGANVNAQSQNGFTPLYMAAQENHLEVVRFLL 160
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 473-595 5.03e-10

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: 65.98  E-value: 5.03e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  473 RGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDD--------------QTPLHISARLGKADIVQQLLQQGASPN--AA 536
Cdd:cd22196     93 KGQTALHIAIERRNMHLVELLVQNGADVHARASGEffkkkkggpgfyfgELPLSLAACTNQLDIVKFLLENPHSPAdiSA 172

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907073017  537 TTS-GYTPLH--LAAREGHEDVAAF-------LLDHGASL-------SITTKKGFTPLHVAAKYGKLEVASLLLQK 595
Cdd:cd22196    173 RDSmGNTVLHalVEVADNTPENTKFvtkmyneILILGAKIrpllkleEITNKKGLTPLKLAAKTGKIGIFAYILGR 248
PHA02946 PHA02946
ankyin-like protein; Provisional
 523-814 7.55e-10

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 64.69  E-value: 7.55e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  523 VQQLLQQGASPNAATTSGYTPLHLAAREGHEDVAAFLLDHGASLSITTKKGFTPLHVAAKYGK--LEVASLLLQKSAS-P 599
Cdd:PHA02946    55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKiN 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  600 DAAGKSGLTPLhVAAHYDNQKVALLLLDQGASPHAAAKNGYTPL--HIAAKKNQMDIATSLLEYGADANAVTRQGIASVH 677
Cdd:PHA02946   135 NSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLH 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  678 LAAQE--GHVDMVSLLLSrNANVNLSNKSGLTPLHLAAQE----------------------------DRVNVAEVLVNQ 727
Cdd:PHA02946   214 IVCSKtvKNVDIINLLLP-STDVNKQNKFGDSPLTLLIKTlspahlinkllstsnvitdqtvnicifyDRDDVLEIINDK 292

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  728 GAHVDAqtkmgyTPLHVGCHYGNIKIVNFLLQHSAKVNaktkngyTALHQAAQQGHTHIINVLLQNNASPnELTVNGNTA 807
Cdd:PHA02946   293 GKQYDS------TDFKMAVEVGSIRCVKYLLDNDIICE-------DAMYYAVLSEYETMVDYLLFNHFSV-DSVVNGHTC 358


                   ....*..
gi 1907073017  808 LAIARRL 814
Cdd:PHA02946   359 MSECVRL 365
Ank_4 pfam13637
Ankyrin repeats (many copies);
74-127 1.26e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 1.26e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907073017   74 GLNALHLASKEGHVEVVSELLQREANVDAATKKGNTALHIASLAGQAEVVKVLV 127
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
639-692 1.76e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 1.76e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907073017  639 GYTPLHIAAKKNQMDIATSLLEYGADANAVTRQGIASVHLAAQEGHVDMVSLLL 692
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
394-448 1.99e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 56.20  E-value: 1.99e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907073017  394 LLDKK-ASPNAKALNGFTPLHIACKKNRIRVMELLLKHGASIQAVTESGLTPIHVA 448
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 410-614 3.45e-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: 63.11  E-value: 3.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  410 TPLHIACKKNRIRVMELLLK-HGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHhgASPNTTNV-------RGETALHMA 481
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  482 ARSGQAEVVRYLVQDGAQVeakakddqtplhISARLGKADIVQqllqqgaSPNAATTSGYTPLHLAAREGHEDVAAFLLD 561
Cdd:cd22192     97 VVNQNLNLVRELIARGADV------------VSPRATGTFFRP-------GPKNLIYYGEHPLSFAACVGNEEIVRLLIE 157

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907073017  562 HGASLSITTKKGFTPLHV----AAKYGKLEVASLLL-----QKSASPD-AAGKSGLTPLHVAA 614
Cdd:cd22192    158 HGADIRAQDSLGNTVLHIlvlqPNKTFACQMYDLILsydkeDDLQPLDlVPNNQGLTPFKLAA 220
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 473-595 3.45e-09

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: 63.28  E-value: 3.45e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  473 RGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDD--------------QTPLHISARLGKADIVQQLLQ---QGASPNA 535
Cdd:cd22193     75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRffqpkyqgegfyfgELPLSLAACTNQPDIVQYLLEnehQPADIEA 154

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907073017  536 ATTSGYTPLH--LAAREGHEDVAAF-------LLDHGASL-------SITTKKGFTPLHVAAKYGKLEVASLLLQK 595
Cdd:cd22193    155 QDSRGNTVLHalVTVADNTKENTKFvtrmydmILIRGAKLcptveleEIRNNDGLTPLQLAAKMGKIEILKYILQR 230
Ank_4 pfam13637
Ankyrin repeats (many copies);
309-362 3.90e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 3.90e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907073017  309 GLTPLHCGARSGHEQVVEMLLDRSAPILSKTKNGLSPLHMATQGDHLNCVQLLL 362
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 115-193 4.46e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 4.46e-09
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907073017  115 SLAGQAEVVKVLVTNGANVNAQSQNGFTPLYMAAQENHLEVVRFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLL 193
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
342-395 4.60e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 4.60e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907073017  342 GLSPLHMATQGDHLNCVQLLLQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLL 395
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 479-562 7.62e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.22  E-value: 7.62e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  479 HMAArSGQAEVVRYLVQDGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLAAREGHEDVAAF 558
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                   ....
gi 1907073017  559 LLDH 562
Cdd:PTZ00322   167 LSRH 170
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 61-170 1.10e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.78  E-value: 1.10e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   61 IKNGVDVNICNQNGLNALHLASKEGHVEVVSELLQREANVDAATKKGNTALHIASLAGQAEVVKVLVTNGANVNAQSQNG 140
Cdd:PHA02875   122 IARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG 201

                           90       100       110
                   ....*....|....*....|....*....|.
gi 1907073017  141 -FTPLYMAAQENHLEVVRFLLDNGASQSLAT 170
Cdd:PHA02875   202 cVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 512-606 1.22e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.45  E-value: 1.22e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  512 HISARlGKADIVQQLLQQGASPNAATTSGYTPLHLAAREGHEDVAAFLLDHGASLSITTKKGFTPLHVAAKYGKLEVASL 591
Cdd:PTZ00322    88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                           90
                   ....*....|....*
gi 1907073017  592 LLQKSASPDAAGKSG 606
Cdd:PTZ00322   167 LSRHSQCHFELGANA 181
Death_RAIDD cd08319
Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) ...
 4120-4192 1.27e-08

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: 54.64  E-value: 1.27e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907073017 4120 TDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDALTSVLTKIN 4192
Cdd:cd08319      1 TDRQLNKLAQRLGPEWEQVLLDLGLSKADIYRCKADHPYNVQSQIVEALVKWKQRQGKKATVQSLIQSLKAVE 73
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 76-195 1.51e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.42  E-value: 1.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   76 NALHLASKeGHVEVVSELLQREANVDAATKKGNTALHIASLAGQAEVVKVLVTNGANVNAQSQNGFTPLY---------- 145
Cdd:PLN03192   528 NLLTVAST-GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWnaisakhhki 606

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907073017  146 ---------------------MAAQENHLEVVRFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLLEN 195
Cdd:PLN03192   607 frilyhfasisdphaagdllcTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMN 677
Death_FADD cd08306
Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in ...
 4126-4202 1.77e-08

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: 54.22  E-value: 1.77e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907073017 4126 IVADHLGLSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIVTLLEG 4202
Cdd:cd08306      7 VICENLGRDWRQLARKLGLSETKIESISEAHPRNLREQVRQSLREWKKIKKAEATVADLIKALRDCQLNLVADLVEK 83
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 714-802 2.43e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.46  E-value: 2.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  714 QEDRVNVAEVLVNQGAHVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTALHQAAQQGHTHIINVLLQN 793
Cdd:PHA02876   154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233

                           90
                   ....*....|.
gi 1907073017  794 --NASPNELTV 802
Cdd:PHA02876   234 rsNINKNDLSL 244
Ank_4 pfam13637
Ankyrin repeats (many copies);
575-626 2.65e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 2.65e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907073017  575 TPLHVAAKYGKLEVASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLL 626
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 561-693 3.52e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.91  E-value: 3.52e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  561 DHGASLSITTKKGFTPLHVAAKYGKLEVASL------LLQKSASPDAAGksgltplhvaahydnqkvALLLLDQGASPHA 634
Cdd:PTZ00322    49 THLEALEATENKDATPDHNLTTEEVIDPVVAhmltveLCQLAASGDAVG------------------ARILLTGGADPNC 110

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907073017  635 AAKNGYTPLHIAAKKNQMDIATSLLEYGADANAVTRQGIASVHLAAQEGHVDMVSLLLS 693
Cdd:PTZ00322   111 RDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PHA02798 PHA02798
ankyrin-like protein; Provisional
 621-811 3.68e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 59.46  E-value: 3.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  621 VALLLLDQGASPHAAAKNGYTPLHIAAKK---NQMDIATSLLEYGADANAVTRQGIASVHLAAQEGH---VDMVSLLLSR 694
Cdd:PHA02798    91 IVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEK 170

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  695 NANVNL-SNKSGLTPLH--LAAQEDR--VNVAEVLVNQG---AHVDAQTKMGYTPLHVGCHYGNIK----IVNFLLQHsA 762
Cdd:PHA02798   171 GVDINThNNKEKYDTLHcyFKYNIDRidADILKLFVDNGfiiNKENKSHKKKFMEYLNSLLYDNKRfkknILDFIFSY-I 249

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1907073017  763 KVNAKTKNGYTALHQAAQQGHTHIINVLLQNNASPNELTVNGNTALAIA 811
Cdd:PHA02798   250 DINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTA 298
Ank_5 pfam13857
Ankyrin repeats (many copies);
261-314 4.26e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.35  E-value: 4.26e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907073017  261 LLLNRAAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLH 314
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 58-135 6.34e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.52  E-value: 6.34e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907073017   58 LDY-IKNGVDVNICNQNGLNALHLASKEGHVEVVSELLQREANVDAATKKGNTALHIASLAGQAEVVKVLVTNGANVNA 135
Cdd:PHA03100   175 VNYlLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 473-598 6.89e-08

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: 59.10  E-value: 6.89e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  473 RGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDD-------------QTPLHISARLGKADIVQQLLQ---QGASPNAA 536
Cdd:cd22197     93 RGHSALHIAIEKRSLQCVKLLVENGADVHARACGRffqkkqgtcfyfgELPLSLAACTKQWDVVNYLLEnphQPASLQAQ 172

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907073017  537 TTSGYTPLH---LAAREGHEDVAAF------LLDHGASL-------SITTKKGFTPLHVAAKYGKLEVASLLLQKSAS 598
Cdd:cd22197    173 DSLGNTVLHalvMIADNSPENSALVikmydgLLQAGARLcptvqleEISNHEGLTPLKLAAKEGKIEIFRHILQREFS 250
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 105-445 6.97e-08

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 59.16  E-value: 6.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  105 KKGNTALH--IASLAGQAEVVKVLVTNGANVNAQSQNGFTPL--YMAAQENHLEVVRFLLDNGASQSLATEDGFTPLAVA 180
Cdd:PHA02716   175 KTGYGILHayLGNMYVDIDILEWLCNNGVNVNLQNNHLITPLhtYLITGNVCASVIKKIIELGGDMDMKCVNGMSPIMTY 254

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  181 LQQG---HDQVVSLLLENDTKGKVR-LPA-LHI---AARKDDTKAAALLLQNDTNADVESkmvvnratESGFTPLH--IA 250
Cdd:PHA02716   255 IINIdniNPEITNIYIESLDGNKVKnIPMiLHSyitLARNIDISVVYSFLQPGVKLHYKD--------SAGRTCLHqyIL 326

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  251 AHYGNINVATLLLNRAAAVDFTARNDITPLHVASKRG--------------NANMVKLLLDRGAKIDAKTRDGLTPLH-- 314
Cdd:PHA02716   327 RHNISTDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMLsvvnildpetdndiRLDVIQCLISLGADITAVNCLGYTPLTsy 406

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  315 -CGARS-GHEQVVEMLLdrSAPILSKTKNGLSPlHMATQGDHLNCV--QLLLQHNVPVDDVTNDY----LTALHVAAHCG 386
Cdd:PHA02716   407 iCTAQNyMYYDIIDCLI--SDKVLNMVKHRILQ-DLLIRVDDTPCIihHIIAKYNIPTDLYTDEYepydSTKIHDVYHCA 483

                          330       340       350       360       370       380
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907073017  387 hykvakvlLDKKASPNAKALNGFTPLHIA--CKKNRIRVME---LLLKHGASIQAVTESGLTPI 445
Cdd:PHA02716   484 --------IIERYNNAVCETSGMTPLHVSiiSHTNANIVMDsfvYLLSIQYNINIPTKNGVTPL 539
PHA02798 PHA02798
ankyrin-like protein; Provisional
 256-481 8.19e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 58.31  E-value: 8.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  256 INVATLLLNRAAAVDFTARNDITPL-----HVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLL- 329
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLf 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  330 --DRSAPILSKTKNGLSPLHMATQGDH---LNCVQLLLQHNVPVDDVTNDY-LTALHV----AAHCGHYKVAKVLLD--- 396
Cdd:PHA02798   131 miENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNNKEkYDTLHCyfkyNIDRIDADILKLFVDngf 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  397 ----KKASPNAKALNGFTPLHIACKKNRIRVMELLLKHgASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNV 472
Cdd:PHA02798   211 iinkENKSHKKKFMEYLNSLLYDNKRFKKNILDFIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITE 289


                   ....*....
gi 1907073017  473 RGETALHMA 481
Cdd:PHA02798   290 LGNTCLFTA 298
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 611-826 9.26e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.73  E-value: 9.26e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  611 HVAAHydNQKVALLLLDQGASpHAAAKNGYTPLHIAAKKNQmDIATSLLEYGADANAVTRQGIASVHLAAQEGHVDMVSL 690
Cdd:PLN03192   501 HKELH--DLNVGDLLGDNGGE-HDDPNMASNLLTVASTGNA-ALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLV 576

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  691 LLSRNANVNLSNKSGLTPLHLAAQEDRVNVAEVLVNQGAHVDAQTkmGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKN 770
Cdd:PLN03192   577 LLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQ 654

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907073017  771 GYTALHQAAQQGHTHIINVLLQNNAS------PNELTVNGNTALAIARRLGY-ISVVDTLKVV 826
Cdd:PLN03192   655 GATALQVAMAEDHVDMVRLLIMNGADvdkantDDDFSPTELRELLQKRELGHsITIVDSVPAD 717
Ank_4 pfam13637
Ankyrin repeats (many copies);
676-725 9.39e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 9.39e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907073017  676 VHLAAQEGHVDMVSLLLSRNANVNLSNKSGLTPLHLAAQEDRVNVAEVLV 725
Cdd:pfam13637    5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 135-450 1.25e-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: 58.17  E-value: 1.25e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  135 AQSQNGFTPlymAAQENHLEVVRFLLDNGASQSLATED--GFTPLAVALQQG-HDQVVSLLLENDTKGKVRLPALHIAAR 211
Cdd:TIGR00870   15 SDEEKAFLP---AAERGDLASVYRDLEEPKKLNINCPDrlGRSALFVAAIENeNLELTELLLNLSCRGAVGDTLLHAISL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  212 --KDDTKAAALLLQNDTNADVESKMVVNRATeSGFTPlhiaahygninvatlllnraaavdftarnDITPLHVASKRGNA 289
Cdd:TIGR00870   92 eyVDAVEAILLHLLAAFRKSGPLELANDQYT-SEFTP-----------------------------GITALHLAAHRQNY 141

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  290 NMVKLLLDRGAKIDAKT--------------RDGLTPLHCGARSGHEQVVEMLLDRSAPILSKTKNGLSPLHMAtqgdhl 355
Cdd:TIGR00870  142 EIVKLLLERGASVPARAcgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLL------ 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  356 ncvqlllqhnVPVDDVTNDYLTalhVAAHCghYKVAKVLLDKKASPNAKAL----NGFTPLHIACKKNRIRVMELLLKHG 431
Cdd:TIGR00870  216 ----------VMENEFKAEYEE---LSCQM--YNFALSLLDKLRDSKELEVilnhQGLTPLKLAAKEGRIVLFRLKLAIK 280

                          330
                   ....*....|....*....
gi 1907073017  432 ASIQAVTESGLTPIHVAAF 450
Cdd:TIGR00870  281 YKQKKFVAWPNGQQLLSLY 299
Ank_4 pfam13637
Ankyrin repeats (many copies);
705-758 1.28e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 1.28e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907073017  705 GLTPLHLAAQEDRVNVAEVLVNQGAHVDAQTKMGYTPLHVGCHYGNIKIVNFLL 758
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 106-265 1.31e-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: 57.97  E-value: 1.31e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  106 KGNTALHIASLAGQAEVVKVLVTNGANVNAQS---------QNGF----TPLYMAAQENHLEVVRFLLDNGASqslated 172
Cdd:cd21882     72 QGQTALHIAIENRNLNLVRLLVENGADVSARAtgrffrkspGNLFyfgeLPLSLAACTNQEEIVRLLLENGAQ------- 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  173 gftPLAVALQqghdqvvslllenDTKGKVRLPALHIAARK--DDTKAAA----LLLQNDTNAD--VESKMVVNRateSGF 244
Cdd:cd21882    145 ---PAALEAQ-------------DSLGNTVLHALVLQADNtpENSAFVCqmynLLLSYGAHLDptQQLEEIPNH---QGL 205

                          170       180
                   ....*....|....*....|.
gi 1907073017  245 TPLHIAAHYGNINVATLLLNR 265
Cdd:cd21882    206 TPLKLAAVEGKIVMFQHILQR 226
PHA02946 PHA02946
ankyin-like protein; Provisional
 383-582 1.48e-07

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 57.37  E-value: 1.48e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  383 AHCG----HYKVAKVLLDKKASPNAKALNGFTPLHIACKKNRIRVMELLLKHGASIQAVTESGLTPIHVAAFMGH--VNI 456
Cdd:PHA02946    43 AYCGikglDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIER 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  457 VSQLMHHGASPNTTNVRGETALHMAARSGQAEVVRYLVQDG--AQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPN 534
Cdd:PHA02946   123 INLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGfeARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPS 202

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*....
gi 1907073017  535 AATTSGYTPLHLAAREGHEDVAAF-LLDHGASLSITTKKGFTPLHVAAK 582
Cdd:PHA02946   203 KPDHDGNTPLHIVCSKTVKNVDIInLLLPSTDVNKQNKFGDSPLTLLIK 251
Ank_4 pfam13637
Ankyrin repeats (many copies);
142-193 1.56e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 1.56e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907073017  142 TPLYMAAQENHLEVVRFLLDNGASQSLATEDGFTPLAVALQQGHDQVVSLLL 193
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
559-613 2.19e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 2.19e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907073017  559 LLDHG-ASLSITTKKGFTPLHVAAKYGKLEVASLLLQKSASPDAAGKSGLTPLHVA 613
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 364-463 2.19e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 2.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  364 HNVPVDDVTNDYLTAL------HVAAHcGHYKVAKVLLDKKASPNAKALNGFTPLHIACKKNRIRVMELLLKHGASIQAV 437
Cdd:PTZ00322    66 HNLTTEEVIDPVVAHMltvelcQLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLL 144

                           90       100
                   ....*....|....*....|....*.
gi 1907073017  438 TESGLTPIHVAAFMGHVNIVSQLMHH 463
Cdd:PTZ00322   145 DKDGKTPLELAEENGFREVVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
509-560 2.25e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 2.25e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907073017  509 TPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLAAREGHEDVAAFLL 560
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 540-725 2.35e-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: 57.40  E-value: 2.35e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  540 GYTPLHLAAREG-HEDVAAFLLDHGASLSIttkkGFTPLHVAAK--YGKLEVASLLLQKSAS--------PDAAGKS--- 605
Cdd:TIGR00870   52 GRSALFVAAIENeNLELTELLLNLSCRGAV----GDTLLHAISLeyVDAVEAILLHLLAAFRksgplelaNDQYTSEftp 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  606 GLTPLHVAAHYDNQKVALLLLDQGASPHAAAK--------------NGYTPLHIAAKKNQMDIATSLLEYGADANAVTRQ 671
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  672 GIASVHLAAQEGHVD---------MVSLLLSRNANVNLS-------NKSGLTPLHLAAQEDRVNVAEVLV 725
Cdd:TIGR00870  208 GNTLLHLLVMENEFKaeyeelscqMYNFALSLLDKLRDSkelevilNHQGLTPLKLAAKEGRIVLFRLKL 277
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 256-528 2.47e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 57.06  E-value: 2.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  256 INVATLLLNRAAAVDFTAR-NDITPLHVASKRGNANMVKLLLDRGAKIDAKtrdGL--TPLHCGAR------SGHEQVVE 326
Cdd:PHA02989    16 KNALEFLLRTGFDVNEEYRgNSILLLYLKRKDVKIKIVKLLIDNGADVNYK---GYieTPLCAVLRnreitsNKIKKIVK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  327 MLLDRSAPILSKTKNGLSPLHMATQGDHLNCV---QLLLQHNVPVDDVTND--------YLTALHVAAHcghykVAKVLL 395
Cdd:PHA02989    93 LLLKFGADINLKTFNGVSPIVCFIYNSNINNCdmlRFLLSKGINVNDVKNSrgynllhmYLESFSVKKD-----VIKILL 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  396 DKKASPNAKA-LNGFTPLHIACKKN----RIRVMELLLKHGASI-------QAVTESGLTPiHVAAFMGHVNIVSQLMHH 463
Cdd:PHA02989   168 SFGVNLFEKTsLYGLTPMNIYLRNDidviSIKVIKYLIKKGVNIetnnngsESVLESFLDN-NKILSKKEFKVLNFILKY 246

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907073017  464 gASPNTTNVRGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDDQTPLHISARLGKADIVQQLLQ 528
Cdd:PHA02989   247 -IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
606-659 2.84e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 2.84e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907073017  606 GLTPLHVAAHYDNQKVALLLLDQGASPHAAAKNGYTPLHIAAKKNQMDIATSLL 659
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 48-144 3.43e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.80  E-value: 3.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   48 AARAGHLEKALDYIKNGVDVNICNQNGLNAL-------H------------------------LASKEGHVEVVSELLQR 96
Cdd:PLN03192   565 AASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHhkifrilyhfasisdphaagdllcTAAKRNDLTAMKELLKQ 644

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*....
gi 1907073017   97 EANVDAATKKGNTALHIASLAGQAEVVKVLVTNGANVN-AQSQNGFTPL 144
Cdd:PLN03192   645 GLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDkANTDDDFSPT 693
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 106-265 3.62e-07

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: 56.73  E-value: 3.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  106 KGNTALHIASLAGQAEVVKVLVTNGANVNAQSQNGF--------------TPLYMAAQENHLEVVRFLLDNgaSQSLATe 171
Cdd:cd22193     75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLEN--EHQPAD- 151

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  172 dgftplavalqqghdqvvslLLENDTKGKVRLPALHIAArkDDTKAAA--------LLLQNDTN--ADVESKMVVNRate 241
Cdd:cd22193    152 --------------------IEAQDSRGNTVLHALVTVA--DNTKENTkfvtrmydMILIRGAKlcPTVELEEIRNN--- 206

                          170       180
                   ....*....|....*....|....
gi 1907073017  242 SGFTPLHIAAHYGNINVATLLLNR 265
Cdd:cd22193    207 DGLTPLQLAAKMGKIEILKYILQR 230
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 619-821 4.43e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 55.90  E-value: 4.43e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  619 QKVALLLLDQGASPHAAAKNGYTPL-------HIaakkNQMDIATSLLEYGADANAV-TRQGIASVHLAAQEGHV--DMV 688
Cdd:PHA02989    88 KKIVKLLLKFGADINLKTFNGVSPIvcfiynsNI----NNCDMLRFLLSKGINVNDVkNSRGYNLLHMYLESFSVkkDVI 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  689 SLLLsrNANVNLSNKS---GLTPLHLAAQED----RVNVAEVLVNQGAHVDAQTKMGYTPL------HVGCHYGNIKIVN 755
Cdd:PHA02989   164 KILL--SFGVNLFEKTslyGLTPMNIYLRNDidviSIKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLN 241

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907073017  756 FLLQHsAKVNAKTKNGYTALHQAAQQGHTHIINVLLQNNASPNELTVNGNTALAIARRLGYISVVD 821
Cdd:PHA02989   242 FILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLN 306
Ank_4 pfam13637
Ankyrin repeats (many copies);
245-296 4.64e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 4.64e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907073017  245 TPLHIAAHYGNINVATLLLNRAAAVDFTARNDITPLHVASKRGNANMVKLLL 296
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 460-527 4.70e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 4.70e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907073017  460 LMHHGASPNTTNVRGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDDQTPLHISARLGKADIVQQLL 527
Cdd:PTZ00322   101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
126-180 5.77e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 5.77e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907073017  126 LVTNG-ANVNAQSQNGFTPLYMAAQENHLEVVRFLLDNGASQSLATEDGFTPLAVA 180
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 74-184 6.03e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 55.79  E-value: 6.03e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   74 GLNALHLASKEGHVEVVSELLQREANVDA--AT----KKGNTAL-----HIASLA---GQAEVVKVLVTNGANVNAQSQN 139
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVSprATgtffRPGPKNLiyygeHPLSFAacvGNEEIVRLLIEHGADIRAQDSL 168

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907073017  140 GFTPLYM-AAQENHL---EVVRFLLD---NGASQSLAT---EDGFTPLAVALQQG 184
Cdd:cd22192    169 GNTVLHIlVLQPNKTfacQMYDLILSydkEDDLQPLDLvpnNQGLTPFKLAAKEG 223
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 106-265 6.33e-07

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: 55.97  E-value: 6.33e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  106 KGNTALHIASLAGQAEVVKVLVTNGANVNA----------QSQNGF----TPLYMAAQENHLEVVRFLLDNgasqslate 171
Cdd:cd22196     93 KGQTALHIAIERRNMHLVELLVQNGADVHArasgeffkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLEN--------- 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  172 dGFTPLAVALQqghdqvvslllenDTKGKVRLPALHIAA--RKDDTKAAA------LLLQNDTNADVESKMVVNRateSG 243
Cdd:cd22196    164 -PHSPADISAR-------------DSMGNTVLHALVEVAdnTPENTKFVTkmyneiLILGAKIRPLLKLEEITNK---KG 226

                          170       180
                   ....*....|....*....|..
gi 1907073017  244 FTPLHIAAHYGNINVATLLLNR 265
Cdd:cd22196    227 LTPLKLAAKTGKIGIFAYILGR 248
Ank_4 pfam13637
Ankyrin repeats (many copies);
202-263 8.35e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 8.35e-07
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907073017  202 RLPALHIAARKDDTKAAALLLQNDTNadveskmvVNRATESGFTPLHIAAHYGNINVATLLL 263
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGAD--------INAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 278-495 8.54e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 55.40  E-value: 8.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  278 TPLHVASKRGNANMVKLLLdRGAKIDAKTRDGL--TPLHCGARSGHEQVVEMLLDRSA-----PILSKTKNGLSPLHMAT 350
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLL-KCPSCDLFQRGALgeTALHVAALYDNLEAAVVLMEAAPelvnePMTSDLYQGETALHIAV 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  351 QGDHLNCVQLLLQHNVpvdDVTNdyltalhvAAHCGHYkvakvlldkkASPNAKALNGFTPlHI----ACKKNRIRVmEL 426
Cdd:cd22192     98 VNQNLNLVRELIARGA---DVVS--------PRATGTF----------FRPGPKNLIYYGE-HPlsfaACVGNEEIV-RL 154

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907073017  427 LLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMH---------HGASPNT-TNVRGETALHMAARSGQAEVVRYLVQ 495
Cdd:cd22192    155 LIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYDlilsydkedDLQPLDLvPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 196-348 9.40e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.26  E-value: 9.40e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  196 DTKGKVrlpALHIAARKDDTKAAALLLQNDTNADVESKmvvnrateSGFTPLHIAAHYGNINVATLLLNRAAAVDFTARN 275
Cdd:PLN03192   555 DSKGRT---PLHIAASKGYEDCVLVLLKHACNVHIRDA--------NGNTALWNAISAKHHKIFRILYHFASISDPHAAG 623

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907073017  276 DItpLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRSAPIL-SKTKNGLSPLHM 348
Cdd:PLN03192   624 DL--LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDkANTDDDFSPTEL 695
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 106-265 9.77e-07

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: 55.25  E-value: 9.77e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  106 KGNTALHIASLAGQAEVVKVLVTNGANVNAQSQNGF-------------TPLYMAAQENHLEVVRFLLDNGASQSlated 172
Cdd:cd22197     93 RGHSALHIAIEKRSLQCVKLLVENGADVHARACGRFfqkkqgtcfyfgeLPLSLAACTKQWDVVNYLLENPHQPA----- 167

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  173 gftplavALQqghdqvvslllENDTKGKVRLPALHIAArkDDTKA-AAL-------LLQNDTNADVESKM--VVNRAtes 242
Cdd:cd22197    168 -------SLQ-----------AQDSLGNTVLHALVMIA--DNSPEnSALvikmydgLLQAGARLCPTVQLeeISNHE--- 224

                          170       180
                   ....*....|....*....|...
gi 1907073017  243 GFTPLHIAAHYGNINVATLLLNR 265
Cdd:cd22197    225 GLTPLKLAAKEGKIEIFRHILQR 247
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 426-508 1.00e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 1.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  426 LLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARSGQAEVVRYLV---QDGAQVEA 502
Cdd:PTZ00322   100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSrhsQCHFELGA 179


                   ....*.
gi 1907073017  503 KAKDDQ 508
Cdd:PTZ00322   180 NAKPDS 185
Ank_4 pfam13637
Ankyrin repeats (many copies);
47-94 1.02e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.02e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1907073017   47 RAARAGHLEKALDYIKNGVDVNICNQNGLNALHLASKEGHVEVVSELL 94
Cdd:pfam13637    7 AAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 356-704 1.05e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 54.75  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  356 NCVQLLLQHNVPVDDV-TNDYLTALHVAAHCGHYKVAKVLLDKKASPNAKALNGfTPL-------HIACKKNRiRVMELL 427
Cdd:PHA02989    17 NALEFLLRTGFDVNEEyRGNSILLLYLKRKDVKIKIVKLLIDNGADVNYKGYIE-TPLcavlrnrEITSNKIK-KIVKLL 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  428 LKHGASIQAVTESGLTPIHVAAFMGHVN---IVSQLMHHGASPNTT-NVRGETALHMAAR--SGQAEVVRYLVQDGAQV- 500
Cdd:PHA02989    95 LKFGADINLKTFNGVSPIVCFIYNSNINncdMLRFLLSKGINVNDVkNSRGYNLLHMYLEsfSVKKDVIKILLSFGVNLf 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  501 EAKAKDDQTPLHISAR----LGKADIVQQLLQQGASPNAATtsgytplhlaarEGHEDVAAFLLDHGASLSittKKGFTP 576
Cdd:PHA02989   175 EKTSLYGLTPMNIYLRndidVISIKVIKYLIKKGVNIETNN------------NGSESVLESFLDNNKILS---KKEFKV 239

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  577 LHVAAKYGKLevaslllqksaspdaagksgltplhvaahydnqkvalllldqgaspHAAAKNGYTPLHIAAKKNQMDIAT 656
Cdd:PHA02989   240 LNFILKYIKI----------------------------------------------NKKDKKGFNPLLISAKVDNYEAFN 273

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*...
gi 1907073017  657 SLLEYGADANAVTRQGIASVHLAAQEGHVDMVSLLLSRNANVNLSNKS 704
Cdd:PHA02989   274 YLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQLKPGKYLIKKT 321
Ank_5 pfam13857
Ankyrin repeats (many copies);
757-811 1.26e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 1.26e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907073017  757 LLQH-SAKVNAKTKNGYTALHQAAQQGHTHIINVLLQNNASPNELTVNGNTALAIA 811
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
476-527 1.29e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 1.29e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907073017  476 TALHMAARSGQAEVVRYLVQDGAQVEAKAKDDQTPLHISARLGKADIVQQLL 527
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
526-580 1.35e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 1.35e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907073017  526 LLQQG-ASPNAATTSGYTPLHLAAREGHEDVAAFLLDHGASLSITTKKGFTPLHVA 580
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 191-303 1.36e-06

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 51.03  E-value: 1.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  191 LLLENDTKGKvrlPALHIAARKD--DTKAAALLLQnDTNADVESKMVVNratesGFTPLHIAAHYGNINVATLLLNRAAa 268
Cdd:PHA02736    47 LVLEYNRHGK---QCVHIVSNPDkaDPQEKLKLLM-EWGADINGKERVF-----GNTPLHIAVYTQNYELATWLCNQPG- 116

                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1907073017  269 VDFTARNDI--TPLHVASKRGNANMVKLLLDRGAKID 303
Cdd:PHA02736   117 VNMEILNYAfkTPYYVACERHDAKMMNILRAKGAQCK 153
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 540-571 1.46e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 47.28  E-value: 1.46e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1907073017  540 GYTPLHLAA-REGHEDVAAFLLDHGASLSITTK 571
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 658-724 1.48e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 1.48e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907073017  658 LLEYGADANAVTRQGIASVHLAAQEGHVDMVSLLLSRNANVNLSNKSGLTPLHLAAQEDRVNVAEVL 724
Cdd:PTZ00322   101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 54-265 1.53e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 54.70  E-value: 1.53e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   54 LEKALDYIKNGVDVnicnqnGLNALHLASKEgHVEVVSELLQREANVDAATK--------------KGNTALHIASLAGQ 119
Cdd:TIGR00870   68 LTELLLNLSCRGAV------GDTLLHAISLE-YVDAVEAILLHLLAAFRKSGplelandqytseftPGITALHLAAHRQN 140

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  120 AEVVKVLVTNGANVNA----------QSQNGF----TPLYMAAQENHLEVVRFLLDNGASQSLATEDGFTPLavalqqgH 185
Cdd:TIGR00870  141 YEIVKLLLERGASVPAracgdffvksQGVDSFyhgeSPLNAAACLGSPSIVALLSEDPADILTADSLGNTLL-------H 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  186 DQVVslllENDTKGKVRLPALHIaarKDdtkaaaLLLQNDTNAD--VESKMVVNRAtesGFTPLHIAAHYGNINVATLLL 263
Cdd:TIGR00870  214 LLVM----ENEFKAEYEELSCQM---YN------FALSLLDKLRdsKELEVILNHQ---GLTPLKLAAKEGRIVLFRLKL 277


                   ..
gi 1907073017  264 NR 265
Cdd:TIGR00870  278 AI 279
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 606-720 1.75e-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: 54.43  E-value: 1.75e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  606 GLTPLHVAAHYDNQKVALLLLDQGASPHAAA----------KNGY----TPLHIAAKKNQMDIATSLLE---YGADANAV 668
Cdd:cd22196     94 GQTALHIAIERRNMHLVELLVQNGADVHARAsgeffkkkkgGPGFyfgeLPLSLAACTNQLDIVKFLLEnphSPADISAR 173

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907073017  669 TRQGIASVH--LAAQEGHVD-------MVSLLLSRNANVN-------LSNKSGLTPLHLAAQEDRVNV 720
Cdd:cd22196    174 DSMGNTVLHalVEVADNTPEntkfvtkMYNEILILGAKIRpllkleeITNKKGLTPLKLAAKTGKIGI 241
Ank_5 pfam13857
Ankyrin repeats (many copies);
690-744 1.78e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 1.78e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1907073017  690 LLLSRNANVNLSNKSGLTPLHLAAQEDRVNVAEVLVNQGAHVDAQTKMGYTPLHV 744
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 284-364 1.92e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 1.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  284 SKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRSAPILSKTKNGLSPLHMATQGDHLNCVQLLLQ 363
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169


                   .
gi 1907073017  364 H 364
Cdd:PTZ00322   170 H 170
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 407-434 3.19e-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: 46.43  E-value: 3.19e-06
                            10        20
                    ....*....|....*....|....*...
gi 1907073017   407 NGFTPLHIACKKNRIRVMELLLKHGASI 434
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_5 pfam13857
Ankyrin repeats (many copies);
591-646 3.37e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 3.37e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907073017  591 LLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLLDQGASPHAAAKNGYTPLHIA 646
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 185-412 3.40e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 3.40e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  185 HDQVVslLLENDTKGKVRLPALHIaarkDDtkaaalLLQNDTNADVESKMVVNRATesgftplhiAAHYGNINVATLLLN 264
Cdd:PLN03192   488 EDNVV--ILKNFLQHHKELHDLNV----GD------LLGDNGGEHDDPNMASNLLT---------VASTGNAALLEELLK 546

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  265 RAAAVDFTARNDITPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLLDRSApiLSKTKNGLS 344
Cdd:PLN03192   547 AKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS--ISDPHAAGD 624

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907073017  345 PLHMATQGDHLNCVQLLLQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKASPNAKAL-NGFTPL 412
Cdd:PLN03192   625 LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTdDDFSPT 693
Ank_5 pfam13857
Ankyrin repeats (many copies);
60-114 3.83e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 3.83e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907073017   60 YIKNG-VDVNICNQNGLNALHLASKEGHVEVVSELLQREANVDAATKKGNTALHIA 114
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 685-798 3.93e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 52.91  E-value: 3.93e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  685 VDMVSLLLSRNANVNLSNKSGLTPL-----HLAAQEDRVNVAEVLVNQGAHVDAQTKMGYTPLHVGCHYG---NIKIVNF 756
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLF 130

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*
gi 1907073017  757 LLQHSAKVNAKTKNGYTALHQAAQQGHT---HIINVLLQNNASPN 798
Cdd:PHA02798   131 MIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDIN 175
Ank_5 pfam13857
Ankyrin repeats (many copies);
462-513 3.94e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 3.94e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907073017  462 HHGASPNTTNVRGETALHMAARSGQAEVVRYLVQDGAQVEAKAKDDQTPLHI 513
Cdd:pfam13857    4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
 4134-4201 4.34e-06

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: 47.28  E-value: 4.34e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907073017 4134 SWTELARELNFSVDEINQI-RVENPnslisqSFMLLKKWVTRDGknATTDALTSVLTKINRIDIVTLLE 4201
Cdd:cd08311     20 DWRALAGELGYSAEEIDSFaREADP------CRALLTDWSAQDG--ATLGVLLTALRKIGRDDIVEILQ 80
Death_DRs cd08784
Death Domain of Death Receptors; Death domain (DD) found in death receptor proteins. Death ...
 4133-4192 4.40e-06

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: 47.57  E-value: 4.40e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 4133 LSWTELARELNFSVDEINQIRVENPNSLISQSFMLLKKWVTRDGKNATTDALTSVLTKIN 4192
Cdd:cd08784     12 SQWKGFVRKLGLNEAEIDEIKNDNVQDTAEAKYQMLRNWHQLTGRKAAYDTLIKDLKKMN 71
Ank_5 pfam13857
Ankyrin repeats (many copies);
625-679 4.61e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 4.61e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907073017  625 LLDQG-ASPHAAAKNGYTPLHIAAKKNQMDIATSLLEYGADANAVTRQGIASVHLA 679
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
93-147 7.84e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 7.84e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907073017   93 LLQRE-ANVDAATKKGNTALHIASLAGQAEVVKVLVTNGANVNAQSQNGFTPLYMA 147
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 670-763 8.02e-06

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 48.72  E-value: 8.02e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  670 RQGIASVHLAAQEGHVD---MVSLLLSRNANVNLSN-KSGLTPLHLAAQEDRVNVAEVLVNQ-GAHVDAQTKMGYTPLHV 744
Cdd:PHA02736    53 RHGKQCVHIVSNPDKADpqeKLKLLMEWGADINGKErVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYV 132

                           90
                   ....*....|....*....
gi 1907073017  745 GCHYGNIKIVNFLLQHSAK 763
Cdd:PHA02736   133 ACERHDAKMMNILRAKGAQ 151
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 275-304 9.36e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.89  E-value: 9.36e-06
                            10        20        30
                    ....*....|....*....|....*....|
gi 1907073017   275 NDITPLHVASKRGNANMVKLLLDRGAKIDA 304
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 540-568 1.05e-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: 44.89  E-value: 1.05e-05
                            10        20
                    ....*....|....*....|....*....
gi 1907073017   540 GYTPLHLAAREGHEDVAAFLLDHGASLSI 568
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 589-668 1.07e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 1.07e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  589 ASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALLLLDQGASPHAAAKNGYTPLHIAAKKNQMDIATSLLEYG-----A 663
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSqchfeL 177


                   ....*
gi 1907073017  664 DANAV 668
Cdd:PTZ00322   178 GANAK 182
Ank_5 pfam13857
Ankyrin repeats (many copies);
362-415 1.07e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 1.07e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907073017  362 LQHNVPVDDVTNDY--LTALHVAAHCGHYKVAKVLLDKKASPNAKALNGFTPLHIA 415
Cdd:pfam13857    1 LLEHGPIDLNRLDGegYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
771-823 1.13e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 1.13e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907073017  771 GYTALHQAAQQGHTHIINVLLQNNASPNELTVNGNTALAIARRLGYISVVDTL 823
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02946 PHA02946
ankyin-like protein; Provisional
 90-370 1.24e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 51.21  E-value: 1.24e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   90 VSELLQREANVDAATKKGNTALHIASLAGQAEVVKVLVTNGANVNAQSQNGFTPLYM--AAQENHLEVVRFLLDNGAS-Q 166
Cdd:PHA02946    55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKiN 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  167 SLATEDGFTPLAVAL---QQGHDQVVSLLLENDTKGKVRLPALHIAARKDDTKAAALLLQndtnadVESKMVVNRATESG 243
Cdd:PHA02946   135 NSVDEEGCGPLLACTdpsERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKASTISWM------MKLGISPSKPDHDG 208

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  244 FTPLHI--AAHYGNINVATLLLnraAAVDFTARNDI--TPLHVASKR-GNANMVKLLLDRGAKIDAKTrdgltpLHCGAR 318
Cdd:PHA02946   209 NTPLHIvcSKTVKNVDIINLLL---PSTDVNKQNKFgdSPLTLLIKTlSPAHLINKLLSTSNVITDQT------VNICIF 279

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907073017  319 SGHEQVVEMLLDRSAPILSktknglSPLHMATQGDHLNCVQLLLQHNVPVDD 370
Cdd:PHA02946   280 YDRDDVLEIINDKGKQYDS------TDFKMAVEVGSIRCVKYLLDNDIICED 325
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 61-298 1.32e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 51.28  E-value: 1.32e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   61 IKNGVDVN-ICNQNGLNALHLASKEGHVEVVSELLQREANVDaatKKGNTALHIASLAGQAEV--------VKVLVTNGA 131
Cdd:PHA02989    23 LRTGFDVNeEYRGNSILLLYLKRKDVKIKIVKLLIDNGADVN---YKGYIETPLCAVLRNREItsnkikkiVKLLLKFGA 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  132 NVNAQSQNGFTPL--YMAAQE-NHLEVVRFLLDNGAS-QSLATEDGFTPLAVALQQG--HDQVVSLLLEN-----DTKGK 200
Cdd:PHA02989   100 DINLKTFNGVSPIvcFIYNSNiNNCDMLRFLLSKGINvNDVKNSRGYNLLHMYLESFsvKKDVIKILLSFgvnlfEKTSL 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  201 VRLPALHIAARKD----DTKAAALLLQN-------------------DTNADVESKMV-----------VNRATESGFTP 246
Cdd:PHA02989   180 YGLTPMNIYLRNDidviSIKVIKYLIKKgvnietnnngsesvlesflDNNKILSKKEFkvlnfilkyikINKKDKKGFNP 259

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1907073017  247 LHIAAHYGNINVATLLLNRAAAVDFTARNDITPLHVASKRGNANMVKLLLDR 298
Cdd:PHA02989   260 LLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQL 311
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 545-639 1.44e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 1.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  545 HLAArEGHEDVAAFLLDHGASLSITTKKGFTPLHVAAKYGKLEVASLLLQKSASPDAAGKSGLTPLHVAAHYDNQKVALL 624
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                           90
                   ....*....|....*
gi 1907073017  625 LLDQGASPHAAAKNG 639
Cdd:PTZ00322   167 LSRHSQCHFELGANA 181
Ank_5 pfam13857
Ankyrin repeats (many copies);
658-712 1.75e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 1.75e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907073017  658 LLEYG-ADANAVTRQGIASVHLAAQEGHVDMVSLLLSRNANVNLSNKSGLTPLHLA 712
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 241-577 1.82e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 51.07  E-value: 1.82e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  241 ESGFTPLHiaAHYGNINVAT----LLLNRAAAVDFTARNDITPLHVASKRGN--ANMVKLLLDRGAKIDAKTRDGLTPLH 314
Cdd:PHA02716   175 KTGYGILH--AYLGNMYVDIdileWLCNNGVNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMSPIM 252

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  315 ---CGARSGHEQVVEMLLDRSAPilSKTKNGLSPLH----MATQGDhLNCVQLLLQHNVPVDDVTNDYLTALH--VAAHC 385
Cdd:PHA02716   253 tyiINIDNINPEITNIYIESLDG--NKVKNIPMILHsyitLARNID-ISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHN 329

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  386 GHYKVAKVLLDKKASPNAKALNGFTPLH----IACKKN----------RIRVMELLLKHGASIQAVTESGLTP----IHV 447
Cdd:PHA02716   330 ISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsMLSVVNildpetdndiRLDVIQCLISLGADITAVNCLGYTPltsyICT 409

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  448 AAFMGHVNIVSQLMhhgaspnttnvrGETALHMaarsgqaeVVRYLVQDgaqveAKAKDDQTPLHISARLGKADIVQQLL 527
Cdd:PHA02716   410 AQNYMYYDIIDCLI------------SDKVLNM--------VKHRILQD-----LLIRVDDTPCIIHHIIAKYNIPTDLY 464

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907073017  528 QQGASP--------------------NAATTSGYTPLHLAAREGHE-----DVAAFLLDHGASLSITTKKGFTPL 577
Cdd:PHA02716   465 TDEYEPydstkihdvyhcaiierynnAVCETSGMTPLHVSIISHTNanivmDSFVYLLSIQYNINIPTKNGVTPL 539
Ank_5 pfam13857
Ankyrin repeats (many copies);
427-481 1.97e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 1.97e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907073017  427 LLKHG-ASIQAVTESGLTPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMA 481
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02791 PHA02791
ankyrin-like protein; Provisional
 406-576 1.98e-05

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 49.66  E-value: 1.98e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  406 LNGFTPLHIACKKNRIRVMELLLKHGAsIQAVTESGLtPIHVAAFMGHVNIVSQLMHHGASPNTTNVRGETALHMAARSG 485
Cdd:PHA02791    28 VHGHSALYYAIADNNVRLVCTLLNAGA-LKNLLENEF-PLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSG 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  486 QAEVVRYLVQDGAQVEAKAKDD-QTPLHISARLGKADIVQQLLQQGASPNAATTSgYTPLHLAAREGHEDVAAFLLDHGA 564
Cdd:PHA02791   106 NMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPSTFDLAIL-LSCIHITIKNGHVDMMILLLDYMT 184

                          170
                   ....*....|..
gi 1907073017  565 SLSITTKKGFTP 576
Cdd:PHA02791   185 STNTNNSLLFIP 196
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 106-136 2.08e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.20  E-value: 2.08e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1907073017  106 KGNTALHIASL-AGQAEVVKVLVTNGANVNAQ 136
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 638-670 2.23e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 44.20  E-value: 2.23e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1907073017  638 NGYTPLHIAAKK-NQMDIATSLLEYGADANAVTR 670
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 738-769 2.39e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.82  E-value: 2.39e-05
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1907073017  738 GYTPLHVGC-HYGNIKIVNFLLQHSAKVNAKTK 769
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 407-439 2.43e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.82  E-value: 2.43e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1907073017  407 NGFTPLHIACKK-NRIRVMELLLKHGASIQAVTE 439
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 603-759 2.47e-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: 50.65  E-value: 2.47e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  603 GKSGLTPLHVAAHYDNQKV---ALLLLD---QGASPHAAAK--------NGYTPLHIAAKKNQMDIATSLLEYGADANAV 668
Cdd:cd21882     23 GATGKTCLHKAALNLNDGVneaIMLLLEaapDSGNPKELVNapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSAR 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  669 TRQ-------------GIASVHLAAQEGHVDMVSLLLSRN---ANVNLSNKSGLTPLH-LAAQEDRVNVAEVLVNQ---- 727
Cdd:cd21882    103 ATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLHaLVLQADNTPENSAFVCQmynl 182

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|...
gi 1907073017  728 ----GAHVDAQTKM-------GYTPLHVGCHYGNIKIVNFLLQ 759
Cdd:cd21882    183 llsyGAHLDPTQQLeeipnhqGLTPLKLAAVEGKIVMFQHILQ 225
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 710-804 2.48e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 2.48e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  710 HLAAQEDRVNvAEVLVNQGAHVDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTALHQAAQQGHTHIINV 789
Cdd:PTZ00322    88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                           90
                   ....*....|....*
gi 1907073017  790 LLQNNASPNELTVNG 804
Cdd:PTZ00322   167 LSRHSQCHFELGANA 181
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 139-165 2.65e-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: 43.73  E-value: 2.65e-05
                            10        20
                    ....*....|....*....|....*..
gi 1907073017   139 NGFTPLYMAAQENHLEVVRFLLDNGAS 165
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 347-430 2.81e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 2.81e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  347 HMATQGDHLNcVQLLLQHNVPVDDVTNDYLTALHVAAHCGHYKVAKVLLDKKASPNAKALNGFTPLHIACKKNRIRVMEL 426
Cdd:PTZ00322    88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                   ....
gi 1907073017  427 LLKH 430
Cdd:PTZ00322   167 LSRH 170
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 606-720 2.85e-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: 50.56  E-value: 2.85e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  606 GLTPLHVAAHYDNQKVALLLLDQGASPHAAAKN--------------GYTPLHIAAKKNQMDIATSLLEYG---ADANAV 668
Cdd:cd22193     76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEhqpADIEAQ 155

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907073017  669 TRQGIASVH--LAAQEGHVD-------MVSLLLSRNANV-------NLSNKSGLTPLHLAAQEDRVNV 720
Cdd:cd22193    156 DSRGNTVLHalVTVADNTKEntkfvtrMYDMILIRGAKLcptveleEIRNNDGLTPLQLAAKMGKIEI 223
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 677-761 3.22e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 3.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  677 HLAAQEGHVDmVSLLLSRNANVNLSNKSGLTPLHLAAQEDRVNVAEVLVNQGAHVDAQTKMGYTPLHVGCHYGNIKIVNF 756
Cdd:PTZ00322    88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                   ....*
gi 1907073017  757 LLQHS 761
Cdd:PTZ00322   167 LSRHS 171
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 275-307 3.71e-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: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.43  E-value: 3.71e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1907073017  275 NDITPLHVASKR-GNANMVKLLLDRGAKIDAKTR 307
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 407-436 4.00e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 43.40  E-value: 4.00e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1907073017  407 NGFTPLHIACKKNRIRVMELLLKHGASIQA 436
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 202-329 4.56e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 4.56e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  202 RLPALHIAARKDDTKAAALLLQNDTNADVESKMVVNRAtesgftplHIAAHyGNINVATLLLNRAAAVDFTARNDITPLH 281
Cdd:PTZ00322    50 HLEALEATENKDATPDHNLTTEEVIDPVVAHMLTVELC--------QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLH 120

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*...
gi 1907073017  282 VASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGARSGHEQVVEMLL 329
Cdd:PTZ00322   121 IACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 73-105 5.18e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.05  E-value: 5.18e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1907073017   73 NGLNALHLAS-KEGHVEVVSELLQREANVDAATK 105
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 106-135 5.91e-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: 5.91e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1907073017   106 KGNTALHIASLAGQAEVVKVLVTNGANVNA 135
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 93-160 6.03e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 6.03e-05
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907073017   93 LLQREANVDAATKKGNTALHIASLAGQAEVVKVLVTNGANVNAQSQNGFTPLYMAAQENHLEVVRFLL 160
Cdd:PTZ00322   101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 606-714 6.54e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 49.37  E-value: 6.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  606 GLTPLHVAAHYDNQKVALLLLDQGASPHAAAKN--------------GYTPLHIAAKKNQMDIATSLLEYGAD------- 664
Cdd:cd22194    141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTditsqds 220

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907073017  665 -ANAVTRqgiASVHLAAQ-EGHVD----MVSLLLSRNANVNL---SNKSGLTPLHLAAQ 714
Cdd:cd22194    221 rGNTVLH---ALVTVAEDsKTQNDfvkrMYDMILLKSENKNLetiRNNEGLTPLQLAAK 276
Ank_5 pfam13857
Ankyrin repeats (many copies);
492-547 7.35e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 7.35e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907073017  492 YLVQDGAQVEAKAKDDQTPLHISARLGKADIVQQLLQQGASPNAATTSGYTPLHLA 547
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 392-527 7.62e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 48.99  E-value: 7.62e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  392 KVLLDkkASPNAKALNGFTPLHIACKKNRIRVMELLLKHGASIQAVTES--------------GLTPIHVAAFMGHVNIV 457
Cdd:cd22194    127 DRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIV 204

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  458 SQLMHHGASPNTT-NVRGETALH---MAARSGQAE---VVR-----YLVQDGAQVEA-KAKDDQTPLHISARLGKADIVQ 524
Cdd:cd22194    205 QLLMEKESTDITSqDSRGNTVLHalvTVAEDSKTQndfVKRmydmiLLKSENKNLETiRNNEGLTPLQLAAKMGKAEILK 284


                   ...
gi 1907073017  525 QLL 527
Cdd:cd22194    285 YIL 287
Ank_5 pfam13857
Ankyrin repeats (many copies);
731-778 7.87e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 7.87e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1907073017  731 VDAQTKMGYTPLHVGCHYGNIKIVNFLLQHSAKVNAKTKNGYTALHQA 778
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 572-604 8.38e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.28  E-value: 8.38e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1907073017  572 KGFTPLHVAA-KYGKLEVASLLLQKSASPDAAGK 604
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 737-766 1.14e-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: 41.80  E-value: 1.14e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1907073017   737 MGYTPLHVGCHYGNIKIVNFLLQHSAKVNA 766
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 60-306 1.32e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.91  E-value: 1.32e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   60 YIKNGVDVNICNQNGLNALHLASKEGHV---EVVSELLQREANVDAATKKGNTALHIASLAG---QAEVVKVLVTNGANV 133
Cdd:PHA02798    95 LIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDI 174

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  134 NAQS-QNGFTPLYMAAQEN----HLEVVRFLLDNGAsqSLATEDGFTPlavalQQGHDQVVSLLLENdtkgkvrlpalhi 208
Cdd:PHA02798   175 NTHNnKEKYDTLHCYFKYNidriDADILKLFVDNGF--IINKENKSHK-----KKFMEYLNSLLYDN------------- 234

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  209 aaRKDDTKAAALLLqndtnadveSKMVVNRATESGFTPLHIAAHYGNINVATLLLNRAAAVDFTARNDITPLHVASKRGN 288
Cdd:PHA02798   235 --KRFKKNILDFIF---------SYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENES 303

                          250
                   ....*....|....*...
gi 1907073017  289 ANMVKLLLDRgaKIDAKT 306
Cdd:PHA02798   304 KFIFNSILNK--KPNKNT 319
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 683-823 1.34e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.04  E-value: 1.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  683 GHVDMVSLLLSRNAN-VNLSNKSGLTPLHLAAQEDRVNVAEVLVNQGAHVD-AQTKMGY---TPLHVGCH--------YG 749
Cdd:PHA02874    12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINhINTKIPHpllTAIKIGAHdiikllidNG 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  750 -----------NIKIVNFLLQHSAKVNAKTKNGYTALHQAAQQGHTHIINVLLQNNASPNELTVNGNTALAIARRLGYIS 818
Cdd:PHA02874    92 vdtsilpipciEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFD 171


                   ....*
gi 1907073017  819 VVDTL 823
Cdd:PHA02874   172 IIKLL 176
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 738-766 1.55e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.47  E-value: 1.55e-04
                           10        20
                   ....*....|....*....|....*....
gi 1907073017  738 GYTPLHVGCHYGNIKIVNFLLQHSAKVNA 766
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 572-601 1.58e-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: 41.42  E-value: 1.58e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1907073017   572 KGFTPLHVAAKYGKLEVASLLLQKSASPDA 601
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 540-568 1.60e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.47  E-value: 1.60e-04
                           10        20
                   ....*....|....*....|....*....
gi 1907073017  540 GYTPLHLAAREGHEDVAAFLLDHGASLSI 568
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 139-165 1.67e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.51  E-value: 1.67e-04
                           10        20
                   ....*....|....*....|....*...
gi 1907073017  139 NGFTPLYMAA-QENHLEVVRFLLDNGAS 165
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGAD 28
Ank_5 pfam13857
Ankyrin repeats (many copies);
327-382 2.10e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 2.10e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907073017  327 MLLDRSAPILSKTKNGLSPLHMATQGDHLNCVQLLLQHNVPVDDVTNDYLTALHVA 382
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 1590-1949 2.11e-04

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 47.26  E-value: 2.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1590 PGPAKSGSLSSSPSNTPSASPLKSIWSVST--PSPIKSTLGAS---------TTSSVKSISDVASPIRSFRT----VSSP 1654
Cdd:pfam17823   35 NGAGKQNASGDAVPRADNKSSEQ*NFCAATaaPAPVTLTKGTSaahlnstevTAEHTPHGTDLSEPATREGAadgaASRA 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1655 IKTVVSPSPYN-PQVASGTLGRVPTITEATPIKGLAPNSTFSSRTSPVTTAGSLLERSSITMTPPASPksniTMYSSSLP 1733
Cdd:pfam17823  115 LAAAASSSPSSaAQSLPAAIAALPSEAFSAPRAAACRANASAAPRAAIAAASAPHAASPAPRTAASST----TAASSTTA 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1734 FKSIITSATplISSPlkSVVSPtksAADVISTAKATMASSLSSPLKQMsghaevalvnGSVSPLKYPSSSALINGCKAT- 1812
Cdd:pfam17823  191 ASSAPTTAA--SSAP--ATLTP---ARGISTAATATGHPAAGTALAAV----------GNSSPAAGTVTAAVGTVTPAAl 253

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1813 ATLQDKISTATNavSSVVSAASDTVEKALSTTTAMPfSPLRSYVSAAPSAFQSLRT----------------PSASALYT 1876
Cdd:pfam17823  254 ATLAAAAGTVAS--AAGTINMGDPHARRLSPAKHMP-SDTMARNPAAPMGAQAQGPiiqvstdqpvhntagePTPSPSNT 330

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1877 SLGSSIAATTSSVTSSIITV-------PVYSVVNVLPEpalKKLPDSNSftksaaalLSPiktlTTETRPQPHFNRTSSP 1949
Cdd:pfam17823  331 TLEPNTPKSVASTNLAVVTTtkaqakePSASPVPVLHT---SMIPEVEA--------TSP----TTQPSPLLPTQGAAGP 395
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 641-773 2.25e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.58  E-value: 2.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  641 TPLH--IAAKKNQMDIATSLLEYGADANAVTR-QGIASVH--LAAQEG-HVDMVSLLLSRNANVNLSNKSGLTPLH--LA 712
Cdd:PHA02859    53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRdNNLSALHhyLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHmyMC 132

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907073017  713 AQEDRVNVAEVLVnqgahvdaqtKMGYTPLHVGCHYGNI-----------KIVNFLLQHSAKVNAKTKNGYT 773
Cdd:PHA02859   133 NFNVRINVIKLLI----------DSGVSFLNKDFDNNNIlysyilfhsdkKIFDFLTSLGIDINETNKSGYN 194
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 241-429 2.39e-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: 47.18  E-value: 2.39e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  241 ESGFTPLHIAA---HYGNINVATLLLNRAAAVDFTAR-----------NDITPLHVASKRGNANMVKLLLDRGAKIDAKT 306
Cdd:cd21882     24 ATGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSARA 103

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  307 RD-------------GLTPLHCGARSGHEQVVEMLLDRSAPILSKTKN---GLSPLHMatqgdhlncvqLLLQHNVPVDD 370
Cdd:cd21882    104 TGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHA-----------LVLQADNTPEN 172

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907073017  371 ---VTNDYLTALHVAAHCGHykvakvLLDKKASPNAKalnGFTPLHIACKKNRIRVMELLLK 429
Cdd:cd21882    173 safVCQMYNLLLSYGAHLDP------TQQLEEIPNHQ---GLTPLKLAAVEGKIVMFQHILQ 225
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 473-505 2.64e-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. Repeats 13-24 are especially active, with known sites of interaction for the Na/K ATPase, Cl/HCO(3) anion exchanger, voltage-gated sodium channel, clathrin heavy chain and L1 family cell adhesion molecules. The ANK repeats are found to form a contiguous spiral stack such that ion transporters like the anion exchanger associate in a large central cavity formed by the ANK repeat spiral, while clathrin and cell adhesion molecules associate with specific regions outside this cavity.


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.12  E-value: 2.64e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1907073017  473 RGETALHMAA-RSGQAEVVRYLVQDGAQVEAKAK 505
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
221-283 2.94e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 2.94e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907073017  221 LLQNDTNAdveskmvVNRATESGFTPLHIAAHYGNINVATLLLNRAAAVDFTARNDITPLHVA 283
Cdd:pfam13857    1 LLEHGPID-------LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 64-144 3.00e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 3.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   64 GVDVNICNQNGLNALHLASKEGHVEVVSELLQREANVDAATKKGNTALHIASLAGQAEVVKVLVTN-------GANVNAQ 136
Cdd:PTZ00322   105 GADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfelGANAKPD 184


                   ....*...
gi 1907073017  137 SQNGFTPL 144
Cdd:PTZ00322   185 SFTGKPPS 192
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 369-529 3.02e-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: 47.16  E-value: 3.02e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  369 DDVTNDYLTALHVAAHCGHYKVakvLLDkkASPNAKALNGFTPLHIACKKNRIRVMELLLKHGASIQAVTES-------- 440
Cdd:cd22197     60 DGVNACIMPLLEIDKDSGNPKP---LVN--AQCTDEYYRGHSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqg 134

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  441 -----GLTPIHVAAFMGHVNIVSQLM---HHGASPNTTNVRGETALH----MAARSGQ--AEVVRY---LVQDGAQVEAK 503
Cdd:cd22197    135 tcfyfGELPLSLAACTKQWDVVNYLLenpHQPASLQAQDSLGNTVLHalvmIADNSPEnsALVIKMydgLLQAGARLCPT 214

                          170       180       190
                   ....*....|....*....|....*....|...
gi 1907073017  504 AKDDQ-------TPLHISARLGKADIVQQLLQQ 529
Cdd:cd22197    215 VQLEEisnheglTPLKLAAKEGKIEIFRHILQR 247
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 441-471 3.18e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 3.18e-04
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1907073017  441 GLTPIHVAAFM-GHVNIVSQLMHHGASPNTTN 471
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 638-667 3.29e-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: 3.29e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1907073017   638 NGYTPLHIAAKKNQMDIATSLLEYGADANA 667
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 770-799 3.36e-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: 40.65  E-value: 3.36e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1907073017   770 NGYTALHQAAQQGHTHIINVLLQNNASPNE 799
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 377-404 3.41e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 3.41e-04
                           10        20
                   ....*....|....*....|....*....
gi 1907073017  377 TALHVAA-HCGHYKVAKVLLDKKASPNAK 404
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 638-667 3.46e-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: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.70  E-value: 3.46e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1907073017  638 NGYTPLHIAAKKNQMDIATSLLEYGADANA 667
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 705-736 3.58e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 3.58e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1907073017  705 GLTPLHLAA-QEDRVNVAEVLVNQGAHVDAQTK 736
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 770-798 3.62e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 3.62e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1907073017  770 NGYTALHQAAQQ-GHTHIINVLLQNNASPN 798
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
PHA02791 PHA02791
ankyrin-like protein; Provisional
 238-434 3.77e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 45.80  E-value: 3.77e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  238 RATESGFTPLHIAAHYGNINVATLLLNrAAAVDFTARNDItPLHVASKRGNANMVKLLLDRGAKIDAKTRDGLTPLHCGA 317
Cdd:PHA02791    25 KADVHGHSALYYAIADNNVRLVCTLLN-AGALKNLLENEF-PLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAV 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  318 RSGHEQVVEMLLDRSAPILSKTKNGL-SPLHMATQGDHLNCVQLLLQHnVPVDDVTNDYLTALHVAAHCGHYKVAKVLLD 396
Cdd:PHA02791   103 DSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLSE-IPSTFDLAILLSCIHITIKNGHVDMMILLLD 181

                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1907073017  397 KKASPNAKALNGFTP-LHIACKKNRIRVMELLLKHGASI 434
Cdd:PHA02791   182 YMTSTNTNNSLLFIPdIKLAIDNKDLEMLQALFKYDINI 220
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 308-340 3.99e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 3.99e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1907073017  308 DGLTPLHCGA-RSGHEQVVEMLLDRSAPILSKTK 340
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 506-537 4.07e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 4.07e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1907073017  506 DDQTPLHISA-RLGKADIVQQLLQQGASPNAAT 537
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 630-791 4.72e-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: 46.29  E-value: 4.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  630 ASPHAAAKNGYTPLHIAAKKNQMDIATSLLEYGADANAVTRQ--------------GIASVHLAAQEGHVDMVSLLLSRN 695
Cdd:cd22194    132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKE 211

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  696 ANVNLSNKS-GLTPLHLAaqedrVNVAEVLVNQGAHVdaqtkmgytplhvgchygnIKIVNFLLQHSAKVNAKT---KNG 771
Cdd:cd22194    212 STDITSQDSrGNTVLHAL-----VTVAEDSKTQNDFV-------------------KRMYDMILLKSENKNLETirnNEG 267

                          170       180
                   ....*....|....*....|
gi 1907073017  772 YTALHQAAQQGHTHIINVLL 791
Cdd:cd22194    268 LTPLQLAAKMGKAEILKYIL 287
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 374-403 4.78e-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: 4.78e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1907073017   374 DYLTALHVAAHCGHYKVAKVLLDKKASPNA 403
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 473-502 5.07e-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: 5.07e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1907073017   473 RGETALHMAARSGQAEVVRYLVQDGAQVEA 502
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 73-102 5.33e-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: 5.33e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1907073017    73 NGLNALHLASKEGHVEVVSELLQREANVDA 102
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 473-502 5.83e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.93  E-value: 5.83e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1907073017  473 RGETALHMAARSGQAEVVRYLVQDGAQVEA 502
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 278-452 5.86e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.42  E-value: 5.86e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  278 TPLH--VASKRGNANMVKLLLDRGAKIDAKTRD-GLTPLH---CGARSGHEQVVEMLLDRSAPILSKTKNGLSPLHMatq 351
Cdd:PHA02859    53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRDnNLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLLHM--- 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  352 gdhlncvqlllqhnvpvddvtndYLTALHVaahcgHYKVAKVLLDKKASPNAKALNGFTPLH-IACKKNRIRVMELLLKH 430
Cdd:PHA02859   130 -----------------------YMCNFNV-----RINVIKLLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSL 181

                          170       180
                   ....*....|....*....|..
gi 1907073017  431 GASIQAVTESGLTPIHVAAFMG 452
Cdd:PHA02859   182 GIDINETNKSGYNCYDLIKFRN 203
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 684-803 6.00e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 45.36  E-value: 6.00e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  684 HVDMVSLLLSRNANVN----LSNKSGLTPLHLAAQEDRVNVAEVLVNQGAHVDAQTK-MGYTPLHVGCHYGNIKIVNFLL 758
Cdd:PHA02884    45 YTDIIDAILKLGADPEapfpLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEeAKITPLYISVLHGCLKCLEILL 124

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1907073017  759 QHSAKVNAKTKNGYTALHQAAQQGHTHIINVLLQNNAS-----PNELTVN 803
Cdd:PHA02884   125 SYGADINIQTNDMVTPIELALMICNNFLAFMICDNEISnfykhPKKILIN 174
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 606-720 6.10e-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: 46.00  E-value: 6.10e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  606 GLTPLHVAAHYDNQKVALLLLDQGASPHAAA------KN-------GYTPLHIAAKKNQMDIATSLLEYGADANAVTRQG 672
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqKKqgtcfyfGELPLSLAACTKQWDVVNYLLENPHQPASLQAQD 173

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907073017  673 ------------IASVHLAAQEGHVDMVSLLLSRNANVN-------LSNKSGLTPLHLAAQEDRVNV 720
Cdd:cd22197    174 slgntvlhalvmIADNSPENSALVIKMYDGLLQAGARLCptvqleeISNHEGLTPLKLAAKEGKIEI 240
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 1657-1952 6.34e-04

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 45.72  E-value: 6.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1657 TVVSPSP--YNPQVASGTLGRVPTITEATPikglapnsTFSSRTSPVTTAGSLLERSSITMTPPASpkSNITMYSSSLPf 1734
Cdd:pfam17823   63 ATAAPAPvtLTKGTSAAHLNSTEVTAEHTP--------HGTDLSEPATREGAADGAASRALAAAAS--SSPSSAAQSLP- 131

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1735 KSIITSATPLISSPLKSVVSPTKSAAD--VISTAKATMASSLSSPLKQMSGHAEVALVNGSVSPLKYPSSSAlingckAT 1812
Cdd:pfam17823  132 AAIAALPSEAFSAPRAAACRANASAAPraAIAAASAPHAASPAPRTAASSTTAASSTTAASSAPTTAASSAP------AT 205

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1813 ATLQDKISTATNAvssvvsaasdTVEKALSTTTAMpfSPLRSYVSAAPSAFQSLRTPSASAlytslgsSIAATTSSVTSS 1892
Cdd:pfam17823  206 LTPARGISTAATA----------TGHPAAGTALAA--VGNSSPAAGTVTAAVGTVTPAALA-------TLAAAAGTVASA 266

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1907073017 1893 IITVPVYSVVNVLPEPAlKKLPdSNSFTKSAAALLSPIKTLTTE--TRPQPHFNRTSSPVKS 1952
Cdd:pfam17823  267 AGTINMGDPHARRLSPA-KHMP-SDTMARNPAAPMGAQAQGPIIqvSTDQPVHNTAGEPTPS 326
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 67-165 6.60e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.42  E-value: 6.60e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   67 VNICNQNGLNALH--LASKEGHVEVVSELLQREANVDAATKKGNTALHIASLA----GQAEVVKVLVTNGANVNAQSQNG 140
Cdd:PHA02859    44 VNDCNDLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRDNNLSALHHYLSfnknVEPEILKILIDSGSSITEEDEDG 123

                           90       100
                   ....*....|....*....|....*..
gi 1907073017  141 FTPL--YMAAQENHLEVVRFLLDNGAS 165
Cdd:PHA02859   124 KNLLhmYMCNFNVRINVIKLLIDSGVS 150
Adeno_L433K_22K pfam11081
Adenovirus L4-33K/L4-22K; Adenoviruses express up to 20 distinct mRNAs from five major late ...
 3301-3417 7.03e-04

Adenovirus L4-33K/L4-22K; Adenoviruses express up to 20 distinct mRNAs from five major late transcription unit (MLTU) regions, L1 to L5. The L4 region expresses L4-33K and a related protein, L4-22K. L4-22K and L4-33K have complementary but not redundant functions that provide the normal pattern of mRNA production during the late phase of infection. L4-33K is an alternative RNA splicing factor that up-regulates several MLTU splice acceptor sites as the late phase progresses. L4-22K plays a role in genome packaging via its binding, in association with IVa2, to the A2 sequence within the packaging signal. Additionally, L4-22K plays an important role in the temporal switch from the early to late phase of infection by regulating both early and late gene expression.


Pssm-ID: 314108  Cd Length: 168  Bit Score: 43.46  E-value: 7.03e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 3301 IEFPPPPPLDADQMESDKKHQYLPErEVDMMEV--SLQDESDKYQLAE--PVIRVQPPSPVPPGAEASDSSDDESLYQPV 3376
Cdd:pfam11081    7 LQLPPPPPTDEEEYWDSQAEEVLDE-EEEMMEDwdSLDEASEAEEVSDetPSPSVAFPSPAPQKLATVPSIATTSAPQAP 85

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|.
gi 1907073017 3377 PVKKYTFKLKEVDEGQKDTAKSKTAATKASNQKEADGNGRE 3417
Cdd:pfam11081   86 PALPVRRPNRRWDTTGTRAGKSKQPPPLAQEQQQRQGYRSW 126
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 258-473 7.11e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 45.50  E-value: 7.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  258 VATLLLNRAAAVDFTARNDITPLHV---ASKRGNANMVKLLLDRGAKI-DAKTRDGLTPLH-----CGARsghEQVVEML 328
Cdd:PHA02989    90 IVKLLLKFGADINLKTFNGVSPIVCfiyNSNINNCDMLRFLLSKGINVnDVKNSRGYNLLHmylesFSVK---KDVIKIL 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  329 LDRSAPILSKTK-NGLSPLHMATQGD----HLNCVQLLLQHNVPVDDVTNDYLTAL------HVAAHCGHYKVAKVLLdK 397
Cdd:PHA02989   167 LSFGVNLFEKTSlYGLTPMNIYLRNDidviSIKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLNFIL-K 245

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907073017  398 KASPNAKALNGFTPLHIACKKNRIRVMELLLKHGASIQAVTESGLTPIHVAAFMGHVNIVSQLMhhGASPNTTNVR 473
Cdd:PHA02989   246 YIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRIL--QLKPGKYLIK 319
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 121-181 7.31e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.04  E-value: 7.31e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907073017  121 EVVKVLVTNGANVNAQSQ-NGFTPL--YMAAQEN-HLEVVRFLLDNGASQSLATEDGFTPLAVAL 181
Cdd:PHA02859    67 EILKFLIENGADVNFKTRdNNLSALhhYLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMYM 131
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 1547-1953 8.33e-04

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 45.34  E-value: 8.33e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1547 TEPSMKTVERSSGTARSLPTTYSHKPFFSTrpyqswTTAPITVPGPAKSgslssspsntpSASPLKSIWSVSTPSPIKST 1626
Cdd:pfam17823   67 PAPVTLTKGTSAAHLNSTEVTAEHTPHGTD------LSEPATREGAADG-----------AASRALAAAASSSPSSAAQS 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1627 LgaSTTSSVKSISDVASPirsfRTVSSPIKTVVSPspynpqvasgtlgRVPTITEATPIKGlapnstfssRTSPVTTAGS 1706
Cdd:pfam17823  130 L--PAAIAALPSEAFSAP----RAAACRANASAAP-------------RAAIAAASAPHAA---------SPAPRTAASS 181

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1707 LLERSSITMTPPASPKSNITMYSSSLPFKSIITSATPLISSPLKSVVSPTKSAADVISTAKATMASSLSSPLKQMSGHAE 1786
Cdd:pfam17823  182 TTAASSTTAASSAPTTAASSAPATLTPARGISTAATATGHPAAGTALAAVGNSSPAAGTVTAAVGTVTPAALATLAAAAG 261

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1787 VALVNGSVSPLKYPSSSALINGCKATATLQDKISTATNAVSSVVSAASDTVEKALSTTTAMPfSPLRSYVSAAPSAFQSL 1866
Cdd:pfam17823  262 TVASAAGTINMGDPHARRLSPAKHMPSDTMARNPAAPMGAQAQGPIIQVSTDQPVHNTAGEP-TPSPSNTTLEPNTPKSV 340

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1867 RTPSASALYTSlgssiAATTSSVTSSIITVPVYSVVNVLPEPALKKLPDSNSFTKSAAALLSPIKTLTTETRPQPHFNRT 1946
Cdd:pfam17823  341 ASTNLAVVTTT-----KAQAKEPSASPVPVLHTSMIPEVEATSPTTQPSPLLPTQGAAGPGILLAPEQVATEATAGTASA 415


                   ....*..
gi 1907073017 1947 SSPVKSS 1953
Cdd:pfam17823  416 GPTPRSS 422
PHA02741 PHA02741
hypothetical protein; Provisional
 471-580 9.01e-04

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 43.11  E-value: 9.01e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  471 NVRGETALHMAARSGQAEVVR----YLVQDGAQVEAKAKDD--QTPLHISARLGKA----DIVQQLLQQGASPNAATT-S 539
Cdd:PHA02741    18 NSEGENFFHEAARCGCFDIIArftpFIRGDCHAAALNATDDagQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQEMlE 97

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|..
gi 1907073017  540 GYTPLHLAAREGHEDVAAFLLDH-GASLSITTKKGFTPLHVA 580
Cdd:PHA02741    98 GDTALHLAAHRRDHDLAEWLCCQpGIDLHFCNADNKSPFELA 139
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 341-373 1.01e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 1.01e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1907073017  341 NGLSPLHMA-TQGDHLNCVQLLLQHNVPVDDVTN 373
Cdd:pfam00023    1 DGNTPLHLAaGRRGNLEIVKLLLSKGADVNARDK 34
PHA03095 PHA03095
ankyrin-like protein; Provisional
 58-111 1.02e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.02  E-value: 1.02e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1907073017   58 LDYIKNGVDVNICNQNGLNALHLASKEGHVEVVSELLQREANVDAATKKGNTAL 111
Cdd:PHA03095   241 LPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 441-468 1.06e-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: 39.11  E-value: 1.06e-03
                            10        20
                    ....*....|....*....|....*...
gi 1907073017   441 GLTPIHVAAFMGHVNIVSQLMHHGASPN 468
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02741 PHA02741
hypothetical protein; Provisional
 71-194 1.17e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 42.72  E-value: 1.17e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017   71 NQNGLNALHLASKEGHVEVVSELL------QREANVDAATKKGNTALHIASLAGQA----EVVKVLVTNGANVNAQ-SQN 139
Cdd:PHA02741    18 NSEGENFFHEAARCGCFDIIARFTpfirgdCHAAALNATDDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQeMLE 97

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907073017  140 GFTPLYMAAQENHLEVVRFLL-DNGASQSLATEDGFTPLAVALQQGHDQVVSLLLE 194
Cdd:PHA02741    98 GDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPFELAIDNEDVAMMQILRE 153
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 377-432 1.23e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 42.56  E-value: 1.23e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1907073017  377 TALHVAAHCGHYKVAKVLLdKKASPNAKALNGF--TPLHIACKKNRIRVMELLLKHGA 432
Cdd:PHA02736    94 TPLHIAVYTQNYELATWLC-NQPGVNMEILNYAfkTPYYVACERHDAKMMNILRAKGA 150
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 606-634 1.43e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 1.43e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1907073017  606 GLTPLHVAA-HYDNQKVALLLLDQGASPHA 634
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 106-135 1.44e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 1.44e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1907073017  106 KGNTALHIASLAGQAEVVKVLVTNGANVNA 135
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
COG5099 COG5099
RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal ...
 1682-1960 1.57e-03

RNA-binding protein of the Puf family, translational repressor [Translation, ribosomal structure and biogenesis];


Pssm-ID: 227430 [Multi-domain]  Cd Length: 777  Bit Score: 44.74  E-value: 1.57e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1682 ATPIKGLAPNSTFSSRTSPVTTAGSLleRSSITMTPPASPKSN--ITMYSSSLPFKSIITSATPLISSPLKSVVSPTKSA 1759
Cdd:COG5099     27 STTSQELMNGNSTPNSFSPIPSKASS--SATFTLNLPINNSVNhkITSSSSSRRKPSGSWSVAISSSTSGSQSLLMELPS 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1760 AdviSTAKATMASSLSSPLkqmsgHAEVALVNGSVSPLKYPSSSAlinGCKATATLQDKISTATNavSSVVSAASDTVEK 1839
Cdd:COG5099    105 S---SFNPSTSSRNKSNSA-----LSSTQQGNANSSVTLSSSTAS---SMFNSNKLPLPNPNHSN--SATTNQSGSSFIN 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1840 ALSTTTampFSPLRSYVSAAPSAFQSLRTPSASALYTSLGSSIAATTSSVTSSIIT-VPVYSVVNVLPEPALKKLPDSNS 1918
Cdd:COG5099    172 TPASSS---SQPLTNLVVSSIKRFPYLTSLSPFFNYLIDPSSDSATASADTSPSFNpPPNLSPNNLFSTSDLSPLPDTQS 248

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1907073017 1919 FTKSAAALLS-PIKTLTTETRPQPHF-NRTSSPVKSSLFLASSA 1960
Cdd:COG5099    249 VENNIILNSSsSINELTSIYGSVPSIrNLRGLNSALVSFLNVSS 292
DUF5585 pfam17823
Family of unknown function (DUF5585); This is a family of unknown function found in chordata.
 1516-1804 1.72e-03

Family of unknown function (DUF5585); This is a family of unknown function found in chordata.


Pssm-ID: 465521 [Multi-domain]  Cd Length: 506  Bit Score: 44.57  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1516 ETESDQDDEAEKADRRQSFASLALRKrysyltePSMKTVERSSGTARSLPTTYSHKP--FFST-------RPYQSWTTAP 1586
Cdd:pfam17823   89 EHTPHGTDLSEPATREGAADGAASRA-------LAAAASSSPSSAAQSLPAAIAALPseAFSApraaacrANASAAPRAA 161

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1587 ITV--------PGPAKSGSLSSSPSNTPSASPLKSIWSVSTPSPIKSTLGASTTSsvksisdVASPIRSFRTVSSPIKTv 1658
Cdd:pfam17823  162 IAAasaphaasPAPRTAASSTTAASSTTAASSAPTTAASSAPATLTPARGISTAA-------TATGHPAAGTALAAVGN- 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1659 VSPSPYNPQVASGTLGRVPTITEATPIKGLAPNSTFSSRTSPVTTAGSLLER-----SSITMTPPASPKSN--ITMYSSS 1731
Cdd:pfam17823  234 SSPAAGTVTAAVGTVTPAALATLAAAAGTVASAAGTINMGDPHARRLSPAKHmpsdtMARNPAAPMGAQAQgpIIQVSTD 313

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 1732 LPFKSIITSATPLISSPLKSVVSPTKSAAD---VIST----AKATMASSLSSPLKQMSGHAEVALVNGSVSPLKYPSSSA 1804
Cdd:pfam17823  314 QPVHNTAGEPTPSPSNTTLEPNTPKSVASTnlaVVTTtkaqAKEPSASPVPVLHTSMIPEVEATSPTTQPSPLLPTQGAA 393
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 243-270 1.82e-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: 38.34  E-value: 1.82e-03
                            10        20
                    ....*....|....*....|....*...
gi 1907073017   243 GFTPLHIAAHYGNINVATLLLNRAAAVD 270
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
Death_NMPP84 cd08318
Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix ...
 4120-4196 1.88e-03

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: 40.20  E-value: 1.88e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907073017 4120 TDIRMAIVADHLGLSWTELARELNFSVDEINQIRvENPNSLISQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDI 4196
Cdd:cd08318      6 TSEQIDVLANKLGEQWKTLAPYLEMKDKDIRQIE-SDSEDMKMRAKQLLVTWQDREGAQATPEILMTALNAAGLNEI 81
PHA02741 PHA02741
hypothetical protein; Provisional
 633-724 1.91e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 42.34  E-value: 1.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  633 HAAAKN-----GYTPLHIAAKKNQMDIATS----LLEYGADANAVTR-QGIASVHLAAQEGHVDMVSLLLSR-NANVNLS 701
Cdd:PHA02741    49 HAAALNatddaGQMCIHIAAEKHEAQLAAEiidhLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCCQpGIDLHFC 128

                           90       100
                   ....*....|....*....|...
gi 1907073017  702 NKSGLTPLHLAAQEDRVNVAEVL 724
Cdd:PHA02741   129 NADNKSPFELAIDNEDVAMMQIL 151
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 577-679 2.02e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 43.82  E-value: 2.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  577 LHVAAKYGKLEVASLLLQKSASPDA----AGKSGLTPLHVAAHYDNQKVALLLLDQGASPHAAAKNG-YTPLHIAAKKNQ 651
Cdd:PHA02884    37 LYSSIKFHYTDIIDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkITPLYISVLHGC 116

                           90       100
                   ....*....|....*....|....*...
gi 1907073017  652 MDIATSLLEYGADANAVTRQGIASVHLA 679
Cdd:PHA02884   117 LKCLEILLSYGADINIQTNDMVTPIELA 144
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 236-347 2.08e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.88  E-value: 2.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  236 VNRATESGFTPLH--IAAHYGNINVATLLLNRAAAVDFTAR-NDITPLH---VASKRGNANMVKLLLDRGAKIDAKTRDG 309
Cdd:PHA02859    44 VNDCNDLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRdNNLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDG 123

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1907073017  310 LTPLH-----CGARSgheQVVEMLLDRSAPILSKTKNGLSPLH 347
Cdd:PHA02859   124 KNLLHmymcnFNVRI---NVIKLLIDSGVSFLNKDFDNNNILY 163
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 191-303 2.58e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 41.73  E-value: 2.58e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  191 LLLENDTKGKVrlpALHIAARKDDTKAA---ALLLQndTNADVESkmvvnRATESGFTPLHIAAHYGNINVATLLLnRAA 267
Cdd:PHA02743    49 LLHRYDHHGRQ---CTHMVAWYDRANAVmkiELLVN--MGADINA-----RELGTGNTLLHIAASTKNYELAEWLC-RQL 117

                           90       100       110
                   ....*....|....*....|....*....|....*...
gi 1907073017  268 AVDFTARNDI--TPLHVASKRGNANMVKLLLDRGAKID 303
Cdd:PHA02743   118 GVNLGAINYQheTAYHIAYKMRDRRMMEILRANGAVCD 155
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 770-799 2.81e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.01  E-value: 2.81e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1907073017  770 NGYTALHQAAQQGHTHIINVLLQNNASPNE 799
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 572-601 3.22e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.01  E-value: 3.22e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1907073017  572 KGFTPLHVAAKYGKLEVASLLLQKSASPDA 601
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 139-165 3.32e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 3.32e-03
                           10        20
                   ....*....|....*....|....*..
gi 1907073017  139 NGFTPLYMAAQENHLEVVRFLLDNGAS 165
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 374-403 3.59e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 3.59e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1907073017  374 DYLTALHVAAHCGHYKVAKVLLDKKASPNA 403
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 669-823 3.65e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 43.75  E-value: 3.65e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  669 TRQGIASVHLAAQEGHVDMVSLLLSRNANVNLSNKSGLTPLHLAAQEDRV--NVAEVLVNQGAHVDAQTKMGYTP----- 741
Cdd:PHA02716   176 TGYGILHAYLGNMYVDIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNVcaSVIKKIIELGGDMDMKCVNGMSPimtyi 255

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  742 ------------LHVGCHYGN--------------------IKIVNFLLQHSAKVNAKTKNGYTALHQAAQQGH--THII 787
Cdd:PHA02716   256 inidninpeitnIYIESLDGNkvknipmilhsyitlarnidISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTDII 335

                          170       180       190
                   ....*....|....*....|....*....|....*.
gi 1907073017  788 NVLLQNNASPNELTVNGNTALAIarRLGYISVVDTL 823
Cdd:PHA02716   336 KLLHEYGNDLNEPDNIGNTVLHT--YLSMLSVVNIL 369
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 506-535 3.84e-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: 37.57  E-value: 3.84e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1907073017   506 DDQTPLHISARLGKADIVQQLLQQGASPNA 535
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 639-819 4.25e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.53  E-value: 4.25e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  639 GYTPLHIAAKKNQMDIATSLLEYGADANAVtrqGIASVHLAAqEGHVDMVSLLLS-------RNANVNLSNKS------- 704
Cdd:TIGR00870   52 GRSALFVAAIENENLELTELLLNLSCRGAV---GDTLLHAIS-LEYVDAVEAILLhllaafrKSGPLELANDQytseftp 127

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  705 GLTPLHLAAQEDRVNVAEVLVNQGAHVDAQTKMG---YTPlHVGCHY------------GNIKIVNFLLQHSAKVNAKTK 769
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARACGDffvKSQ-GVDSFYhgesplnaaaclGSPSIVALLSEDPADILTADS 206

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907073017  770 NGYTALHQAAQQGH---------THIINVLLQNNA---SPNELTV----NGNTALAIARRLGYISV 819
Cdd:TIGR00870  207 LGNTLLHLLVMENEfkaeyeelsCQMYNFALSLLDklrDSKELEVilnhQGLTPLKLAAKEGRIVL 272
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 243-276 4.44e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.65  E-value: 4.44e-03
                           10        20        30
                   ....*....|....*....|....*....|....*
gi 1907073017  243 GFTPLHIAA-HYGNINVATLLLNRAAAVDftARND 276
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN--ARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 308-335 4.54e-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: 37.57  E-value: 4.54e-03
                            10        20
                    ....*....|....*....|....*...
gi 1907073017   308 DGLTPLHCGARSGHEQVVEMLLDRSAPI 335
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 275-304 4.82e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 4.82e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1907073017  275 NDITPLHVASKRGNANMVKLLLDRGAKIDA 304
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 341-370 5.31e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 5.31e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1907073017   341 NGLSPLHMATQGDHLNCVQLLLQHNVPVDD 370
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 506-535 6.22e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.85  E-value: 6.22e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1907073017  506 DDQTPLHISARLGKADIVQQLLQQGASPNA 535
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 754-823 6.23e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 6.23e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  754 VNFLLQHSAKVNAKTKNGYTALHQAAQQGHTHIINVLLQNNASPNELTVNGNTALAIARRLGYISVVDTL 823
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 639-792 6.68e-03

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 42.53  E-value: 6.68e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  639 GYTPLHIAAKKNQMDIATSLLEYGADanavtrqgiasVHLAAqEGHvdmvslLLSRNANVnlSNKSGLTPLHLAAQEDRV 718
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGAD-----------VHARA-CGR------FFQKKQGT--CFYFGELPLSLAACTKQW 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  719 NVAEVLVN---QGAHVDAQTKMGYTPLHVGCHYGN---------IKIVNFLLQHSAKVNAKTK-------NGYTALHQAA 779
Cdd:cd22197    154 DVVNYLLEnphQPASLQAQDSLGNTVLHALVMIADnspensalvIKMYDGLLQAGARLCPTVQleeisnhEGLTPLKLAA 233

                          170
                   ....*....|...
gi 1907073017  780 QQGHTHIINVLLQ 792
Cdd:cd22197    234 KEGKIEIFRHILQ 246
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 390-514 6.78e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 41.34  E-value: 6.78e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  390 VAKVLLDKKASPNAKAL-NGFTPLH--IACKKN-RIRVMELLLKHGASIQAVTESGLTPIHV--AAFMGHVNIVSQLMHH 463
Cdd:PHA02859    68 ILKFLIENGADVNFKTRdNNLSALHhyLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLIDS 147

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1907073017  464 GASPNTTNVRGETALH--MAARSGQaEVVRYLVQDGAQVEAKAKDDQTPLHIS 514
Cdd:PHA02859   148 GVSFLNKDFDNNNILYsyILFHSDK-KIFDFLTSLGIDINETNKSGYNCYDLI 199
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 278-410 7.16e-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: 42.44  E-value: 7.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  278 TPLHVASKRGNANMVKLLLDRGAKIDAKTRD--------------GLTPLHCGARSGHEQVVEMLLDR-SAPILSKTKNG 342
Cdd:cd22194    143 TALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKeSTDITSQDSRG 222

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  343 LSPLH-MATQGD----HLNCV-----QLLLQH-NVPVDDVTN-DYLTALHVAAHCGHYKVAKVLLDK--KASPNAKALNG 408
Cdd:cd22194    223 NTVLHaLVTVAEdsktQNDFVkrmydMILLKSeNKNLETIRNnEGLTPLQLAAKMGKAEILKYILSReiKEKPNRSLSRK 302


                   ..
gi 1907073017  409 FT 410
Cdd:cd22194    303 FT 304
Death_MyD88 cd08312
Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of ...
 4117-4200 7.82e-03

Death domain of Myeloid Differentation primary response protein MyD88; Death Domain (DD) of Myeloid Differentiation primary response protein 88 (MyD88). MyD88 is an adaptor protein involved in interleukin-1 receptor (IL-1R)- and Toll-like receptor (TLR)-induced activation of nuclear factor-kappaB (NF-kB) and mitogen activated protein kinase pathways that lead to the induction of proinflammatory cytokines. It is a key component in the signaling pathway of pathogen recognition in the innate immune system. MyD88 contains an N-terminal DD and a C-terminal Toll/IL-1 Receptor (TIR) homology domain that mediates interaction with TLRs and IL-1R. 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: 260026  Cd Length: 79  Bit Score: 38.35  E-value: 7.82e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017 4117 CERTDIRMAIVADhlglsWTELARELNFSVDEINQI-RVENPnslisqSFMLLKKWVTRDgKNATTDALTSVLTKINRID 4195
Cdd:cd08312      6 SLYLNPEKVVAND-----WRGLAELMGFDYLEIRNFeRQSSP------TERLLEDWETRP-PGATVGNLLEILEELERKD 73


                   ....*
gi 1907073017 4196 IVTLL 4200
Cdd:cd08312     74 VLEDL 78
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 677-700 7.87e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 7.87e-03
                            10        20
                    ....*....|....*....|....
gi 1907073017   677 HLAAQEGHVDMVSLLLSRNANVNL 700
Cdd:smart00248    7 HLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 153-331 9.16e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.17  E-value: 9.16e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  153 LEVVRFLLDNGASQSLATedGFTPLAVA---LQQGHDQVVSLLLENDTKGKVRLP---------------ALHIAARKDD 214
Cdd:cd21882      8 LECLRWYLTDSAYQRGAT--GKTCLHKAalnLNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyqgqtALHIAIENRN 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907073017  215 TKAAALLLQNdtNADVESkmvvnRATESGFT------------PLHIAAHYGNINVATLLL-NRAAAVDFTARNDI--TP 279
Cdd:cd21882     86 LNLVRLLVEN--GADVSA-----RATGRFFRkspgnlfyfgelPLSLAACTNQEEIVRLLLeNGAQPAALEAQDSLgnTV 158

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907073017  280 LHVASKRGN---------ANMVKLLLDRGAKID-------AKTRDGLTPLHCGARSGHEQVVEMLLDR 331
Cdd:cd21882    159 LHALVLQADntpensafvCQMYNLLLSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQR 226
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 606-634 9.48e-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: 9.48e-03
                            10        20
                    ....*....|....*....|....*....
gi 1907073017   606 GLTPLHVAAHYDNQKVALLLLDQGASPHA 634
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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