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Conserved domains on  [gi|1039763615|ref|XP_017174916|]
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ankyrin-2 isoform X24 [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];
556-821 2.98e-62

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 215.97  E-value: 2.98e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  556 LLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKN 635
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  636 GYTPLHIAAKKNQMQIASTLLNYGAETNTVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKV 715
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  716 NVADILTKHGADRDAYTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPN 795
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250       260
                   ....*....|....*....|....*.
gi 1039763615  796 ATTANGNTALAIAKRLGYISVVDTLK 821
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
319-607 8.43e-62

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 214.82  E-value: 8.43e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  319 DQVVELLLERKAPLLARTKNGLSPLHMAAQGDHVECVKHLLQYKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANP 398
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  399 NARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMA 478
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  479 ARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLE 558
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1039763615  559 AGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPL 607
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 ...
 1355-1484 4.71e-58

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: 197.70  E-value: 4.71e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1355 VPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFSEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSF 1434
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1435 FAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLP 1484
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
158-442 6.59e-58

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 203.65  E-value: 6.59e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  158 IDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRL----PALHIAARKDDTKSAALLLQNDHNA 233
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADalgaLLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  234 DVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCA 313
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  314 ARSGHDQVVELLLERKAPLLARTKNGLSPLHMAAQGDHVECVKHLLQYKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLD 393
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1039763615  394 KRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPI 442
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-343 5.97e-54

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 192.09  E-value: 5.97e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   14 AELDEKEKNLDRERKKQRKIPRDRMERKRKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVG 93
Cdd:COG0666     22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLE 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   94 LVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGAnqst 173
Cdd:COG0666    102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA---- 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  174 atedgftplavalqqghnqavaillendtkgkvrlpalhiaarkddtksaalllqndhNADVQSKSGFTPLHIAAHYGNV 253
Cdd:COG0666    178 ----------------------------------------------------------DVNARDNDGETPLHLAAENGHL 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  254 NVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERKAPLL 333
Cdd:COG0666    200 EIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279

                          330
                   ....*....|
gi 1039763615  334 ARTKNGLSPL 343
Cdd:COG0666    280 AALLDLLTLL 289
Death_ank2 cd08804
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ...
 3579-3662 9.84e-49

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: 169.11  E-value: 9.84e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3579 ERMEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTILIECLTKINRMDIV 3658
Cdd:cd08804      1 ERTEERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLTQCLTKINRMDIV 80


                   ....
gi 1039763615 3659 HLLE 3662
Cdd:cd08804     81 HLME 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 997-1134 3.17e-42

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


:

Pssm-ID: 128514  Cd Length: 104  Bit Score: 150.96  E-value: 3.17e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   997 PCFLVSFMVDARGGAMRGCRhNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQflgklh 1076
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGAL------ 73

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039763615  1077 lptappplnegeslvsrilqlgppgtkFLGPVIVEIPHFAALRGKERELVVLRSENGD 1134
Cdd:smart00218   74 ---------------------------FLRPVILEVPHCASLRPRDWEIVLLRSENGG 104
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 3194-3521 1.07e-07

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 58.64  E-value: 1.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3194 EGELLPDDVSEEIEDLPASDANIDSQVIISASTETPTKEAVSTAVEEPPT---TQRSDSLSTVKQTPRPAVPGPvgqldf 3270
Cdd:PHA03307    28 PGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTeapANESRSTPTWSLSTLAPASPA------ 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3271 spvtRSVYSGQDDESPESSPEEQKSVIEIPTAPVDNVPSAESKPQIPIRTLPTLVPAPPSAEDE------SAFSDDFPSS 3344
Cdd:PHA03307   102 ----REGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAvasdaaSSRQAALPLS 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3345 LDEDSKEGGAKPKSKIPVKAPTQRTEWQPSPTDIPLQKTAVPQGQETLSRAPDGRSKSESDASSLDAK-------TKCPV 3417
Cdd:PHA03307   178 SPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSgcgwgpeNECPL 257

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3418 KARSYIETETESRERAEGFESESEDGATKPKL-FASRLPVKSRSTSSSGrPGTSPTRESREhffdlyrnsieffEEISDE 3496
Cdd:PHA03307   258 PRPAPITLPTRIWEASGWNGPSSRPGPASSSSsPRERSPSPSPSSPGSG-PAPSSPRASSS-------------SSSSRE 323

                          330       340
                   ....*....|....*....|....*
gi 1039763615 3497 ASklvdrlTQSEREQEPPSDDESSS 3521
Cdd:PHA03307   324 SS------SSSTSSSSESSRGAAVS 342
PHA03307 super family cl33723
transcriptional regulator ICP4; Provisional
 1807-2015 3.22e-05

transcriptional regulator ICP4; Provisional


The actual alignment was detected with superfamily member PHA03307:

Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.17  E-value: 3.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1807 RVEDEQKGRSKLPVRVKGKEDVPKRTTPRTHPA-VSPSSKSSTSSKAERHSSLSSSAKPerhtpvsPSSKNEKLSPVSPS 1885
Cdd:PHA03307   229 ADDAGASSSDSSSSESSGCGWGPENECPLPRPApITLPTRIWEASGWNGPSSRPGPASS-------SSSPRERSPSPSPS 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1886 AkterhspvfSGKPEKHSPGSPSTKNERHSPVSSLKTER-----HTPGSPSGKTDKRPPVPSSGRtekhPPVSPGKTEKH 1960
Cdd:PHA03307   302 S---------PGSGPAPSSPRASSSSSSSRESSSSSTSSssessRGAAVSPGPSPSRSPSPSRPP----PPADPSSPRKR 368

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039763615 1961 LPGSPSIRTPeKPAPGSATGKHEKHLPVSPGKTEKQPPISPTSKTERIEETMSVR 2015
Cdd:PHA03307   369 PRPSRAPSSP-AASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAA 422
PTZ00449 super family cl33186
104 kDa microneme/rhoptry antigen; Provisional
 2245-2652 7.30e-04

104 kDa microneme/rhoptry antigen; Provisional


The actual alignment was detected with superfamily member PTZ00449:

Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 45.84  E-value: 7.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 2245 PQISSEESYKHEGlaetPETSPESLSFSPKKSEEQIGEAKETTKvGTPTDIHSEKELPITNDITDSSQKQGagvtrgseP 2324
Cdd:PTZ00449   497 APIEEEDSDKHDE----PPEGPEASGLPPKAPGDKEGEEGEHED-SKESDEPKEGGKPGETKEGEVGKKPG--------P 563

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 2325 STEHSQKEV---TQDPHKDVCSKQDGCPESQSVSLASEVFTEKGSCGESQLPLVSSAFKTQSESEtqeslTPSEVTKPFP 2401
Cdd:PTZ00449   564 AKEHKPSKIptlSKKPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPE-----SPKSPKRPPP 638

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 2402 PS-DASVKTAEGTEpkpqgAIRSPQGLELPLPNRDSEVLSPMADESLAVSHKDSLEASPVLEDNSSH--------KTPDS 2472
Cdd:PTZ00449   639 PQrPSSPERPEGPK-----IIKSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFEsilketlpETPGT 713

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 2473 LEPSPLKESPCRDSLESSPVEP---KMKAGILPSHFPLPAA-----IAKTDLVAEVASMRSRLLRDPDGSAEDDSLEQT- 2543
Cdd:PTZ00449   714 PFTTPRPLPPKLPRDEEFPFEPigdPDAEQPDDIEFFTPPEeertfFHETPADTPLPDILAEEFKEEDIHAETGEPDEAm 793

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 2544 ----SLMESSGKSPLS-PDTP----SSEEVSYEVTPKPSDS------STPKPAVIHECAEEDDSENGEKKrftpeEEMFK 2608
Cdd:PTZ00449   794 krpdSPSEHEDKPPGDhPSLPkkrhRLDGLALSTTDLESDAgriakdASGKIVKLKRSKSFDDLTTVEEA-----EEMGA 868

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039763615 2609 MVTKIKTFDELEQ---------------EAKQKRDYKKEPRQDGSSSASDPDADYSAEV 2652
Cdd:PTZ00449   869 EARKIVVDDDGTEaddedthppeekhksEVRRRRPPKKPSKPKKPSKPKKPKKPDSAFI 927
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
556-821 2.98e-62

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 215.97  E-value: 2.98e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  556 LLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKN 635
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  636 GYTPLHIAAKKNQMQIASTLLNYGAETNTVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKV 715
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  716 NVADILTKHGADRDAYTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPN 795
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250       260
                   ....*....|....*....|....*.
gi 1039763615  796 ATTANGNTALAIAKRLGYISVVDTLK 821
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
319-607 8.43e-62

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 214.82  E-value: 8.43e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  319 DQVVELLLERKAPLLARTKNGLSPLHMAAQGDHVECVKHLLQYKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANP 398
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  399 NARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMA 478
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  479 ARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLE 558
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1039763615  559 AGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPL 607
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 ...
 1355-1484 4.71e-58

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: 197.70  E-value: 4.71e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1355 VPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFSEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSF 1434
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1435 FAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLP 1484
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
158-442 6.59e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 203.65  E-value: 6.59e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  158 IDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRL----PALHIAARKDDTKSAALLLQNDHNA 233
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADalgaLLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  234 DVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCA 313
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  314 ARSGHDQVVELLLERKAPLLARTKNGLSPLHMAAQGDHVECVKHLLQYKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLD 393
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1039763615  394 KRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPI 442
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-343 5.97e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 192.09  E-value: 5.97e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   14 AELDEKEKNLDRERKKQRKIPRDRMERKRKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVG 93
Cdd:COG0666     22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLE 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   94 LVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGAnqst 173
Cdd:COG0666    102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA---- 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  174 atedgftplavalqqghnqavaillendtkgkvrlpalhiaarkddtksaalllqndhNADVQSKSGFTPLHIAAHYGNV 253
Cdd:COG0666    178 ----------------------------------------------------------DVNARDNDGETPLHLAAENGHL 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  254 NVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERKAPLL 333
Cdd:COG0666    200 EIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279

                          330
                   ....*....|
gi 1039763615  334 ARTKNGLSPL 343
Cdd:COG0666    280 AALLDLLTLL 289
Death_ank2 cd08804
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ...
 3579-3662 9.84e-49

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: 169.11  E-value: 9.84e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3579 ERMEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTILIECLTKINRMDIV 3658
Cdd:cd08804      1 ERTEERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLTQCLTKINRMDIV 80


                   ....
gi 1039763615 3659 HLLE 3662
Cdd:cd08804     81 HLME 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 997-1134 3.17e-42

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 150.96  E-value: 3.17e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   997 PCFLVSFMVDARGGAMRGCRhNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQflgklh 1076
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGAL------ 73

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039763615  1077 lptappplnegeslvsrilqlgppgtkFLGPVIVEIPHFAALRGKERELVVLRSENGD 1134
Cdd:smart00218   74 ---------------------------FLRPVILEVPHCASLRPRDWEIVLLRSENGG 104
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 568-792 6.45e-39

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 152.51  E-value: 6.45e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  568 KKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHY-----DNQKVALLLLEKGASPHATAKNGYTPLHI 642
Cdd:PHA03100    33 KKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLY 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  643 AA--KKNQMQIASTLLNYGAETNTVTKQGVTPLHLASQEGHTD--MVTLLLDKGANIhmstksgltslhlaaqeDKVNVA 718
Cdd:PHA03100   113 AIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDI-----------------NAKNRV 175

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039763615  719 DILTKHGADRDAYTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGA 792
Cdd:PHA03100   176 NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 1001-1131 1.28e-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: 129.18  E-value: 1.28e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1001 VSFMVDARGGAMRGCrHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEvgpsgaqflgklhlpta 1080
Cdd:pfam00791    1 VSGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVE----------------- 62

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039763615 1081 ppplnegeslvsrilqLGPPGTKFLGPVIVEIPHFAALRGKERELVVLRSE 1131
Cdd:pfam00791   63 ----------------CGPPGLKFLKPVILEVPHCASLRPEEWEIVLKRSD 97
PHA03095 PHA03095
ankyrin-like protein; Provisional
 411-696 5.25e-34

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 139.39  E-value: 5.25e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  411 IACKKNRIKVMELLVKYGASIQAITESGLTPIHVaaFMGH-----LNIVLLLLQNGASPDVTNIRGETALHMAARAGQVE 485
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHL--YLHYssekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  486 -VVRCLLRNGALVDARAREEQTPLHI--ASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASV--LLEAG 560
Cdd:PHA03095    98 dVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLrlLIDAG 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  561 AahSLATKK--GFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKN--GLTPLHVAAHYDNQKVALL--LLEKGASPHATAK 634
Cdd:PHA03095   178 A--DVYAVDdrFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDmlGNTPLHSMATGSSCKRSLVlpLLIAGISINARNR 255

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039763615  635 NGYTPLHIAAKKNQMQIASTLLNYGAETNTVTKQGVTPLHLASQEGHTDMVTLLLDKGANIH 696
Cdd:PHA03095   256 YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 200-434 3.26e-33

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 135.95  E-value: 3.26e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  200 NDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYG-----NVNVATLLLNRGAAVDFTARNGI 274
Cdd:PHA03100    28 NDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYGANVNAPDNNGI 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  275 TPLHVAS--KRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHD--QVVELLLERKAPLLARTKnglsplhmaaqgd 350
Cdd:PHA03100   108 TPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNR------------- 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  351 hvecVKHLLQYKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGAS 430
Cdd:PHA03100   175 ----VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250


                   ....
gi 1039763615  431 IQAI 434
Cdd:PHA03100   251 IKTI 254
Ank_2 pfam12796
Ankyrin repeats (3 copies);
83-170 4.34e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 99.03  E-value: 4.34e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   83 LHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEgANINAQSqNGFTPLYMAAQENHIDVVK 162
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*...
gi 1039763615  163 YLLENGAN 170
Cdd:pfam12796   79 LLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
244-330 4.35e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.95  E-value: 4.35e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  244 LHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRgGQIDAKTrDGLTPLHCAARSGHDQVVE 323
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*..
gi 1039763615  324 LLLERKA 330
Cdd:pfam12796   79 LLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
376-468 8.50e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.18  E-value: 8.50e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  376 LHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGAsiQAITESGLTPIHVAAFMGHLNIVL 455
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1039763615  456 LLLQNGASPDVTN 468
Cdd:pfam12796   79 LLLEKGADINVKD 91
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 3582-3663 1.12e-22

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: 94.79  E-value: 1.12e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  3582 EERLAYIADH-LGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTILIECLTKINRMDIVHL 3660
Cdd:smart00005    5 RQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDDAVEL 84


                    ...
gi 1039763615  3661 LET 3663
Cdd:smart00005   85 LRS 87
Ank_2 pfam12796
Ankyrin repeats (3 copies);
706-797 1.51e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.72  E-value: 1.51e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  706 LHLAAQEDKVNVADILTKHGADRDAYTKLGYTPLIVACHYGNVKMVNFLLKQgANVNAKTkNGYTPLHQAAQQGHTHIIN 785
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1039763615  786 VLLQHGAKPNAT 797
Cdd:pfam12796   79 LLLEKGADINVK 90
Death pfam00531
Death domain;
3582-3662 4.95e-21

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 90.12  E-value: 4.95e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3582 EERLAYIADH---LGFSWTELARELDFTEEQIHQIRIENPNsLQDQSHALLKYWLERDGKHATDTILIECLTKINRMDIV 3658
Cdd:pfam00531    1 RKQLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAA 79


                   ....
gi 1039763615 3659 HLLE 3662
Cdd:pfam00531   80 EKIQ 83
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 562-756 1.71e-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: 1.71e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  562 AHSLATKKGF-TPLHVAAKYGSLD-VAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEkgASPH-----ATAK 634
Cdd:cd22192      8 LHLLQQKRISeSPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPElvnepMTSD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  635 --NGYTPLHIAAKKNQMQIASTLLNYGAE------TNTVTKQGVT--------PLHLASQEGHTDMVTLLLDKGANIHMS 698
Cdd:cd22192     86 lyQGETALHIAVVNQNLNLVRELIARGADvvspraTGTFFRPGPKnliyygehPLSFAACVGNEEIVRLLIEHGADIRAQ 165

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039763615  699 TKSGLTSLH-LAAQEDKVNVAD----ILTKHGADRDA--YT---KLGYTPLIVACHYGNVKMVNFLLK 756
Cdd:cd22192    166 DSLGNTVLHiLVLQPNKTFACQmydlILSYDKEDDLQplDLvpnNQGLTPFKLAAKEGNIVMFQHLVQ 233
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 407-593 8.89e-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: 81.21  E-value: 8.89e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  407 TPLHIACKKNRIKVMELLVKY-GASIQAITESGLTPIHVAAFMGHLNIVLLLLQngASPDVTNI-------RGETALHMA 478
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  479 ARAGQVEVVRCLLRNGA-LVDARA-----REEQT--------PLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHIS 544
Cdd:cd22192     97 VVNQNLNLVRELIARGAdVVSPRAtgtffRPGPKnliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039763615  545 AREGQVDVA----SVLLEA---GAAHSLAT---KKGFTPLHVAAKYGSLDVAKLLLQRR 593
Cdd:cd22192    177 VLQPNKTFAcqmyDLILSYdkeDDLQPLDLvpnNQGLTPFKLAAKEGNIVMFQHLVQKR 235
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 211-426 2.74e-14

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: 79.29  E-value: 2.74e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  211 LHIAARKDDTKSAALLLQNDHnADVQSKS--GFTPLHIAAHYGNVNVATLLL-------NRGAAVDFTArnGITPLHVAS 281
Cdd:cd22192     21 LLLAAKENDVQAIKKLLKCPS-CDLFQRGalGETALHVAALYDNLEAAVVLMeaapelvNEPMTSDLYQ--GETALHIAV 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  282 KRGNTNMVKLLLDRGGQIDA---------KTRDGLT-----PLHCAARSGHDQVVELLLERKAPLLARTKNGLSPLHMAA 347
Cdd:cd22192     98 VNQNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILV 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  348 QGDHVECVKH----LLQYKAPVDDVTLDYLtalhvaahcghyrvtkllldkranPNARalnGFTPLHIACKKNRIKVMEL 423
Cdd:cd22192    178 LQPNKTFACQmydlILSYDKEDDLQPLDLV------------------------PNNQ---GLTPFKLAAKEGNIVMFQH 230


                   ...
gi 1039763615  424 LVK 426
Cdd:cd22192    231 LVQ 233
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 298-546 3.23e-12

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: 72.81  E-value: 3.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  298 QIDAKTRDGLTPLHCAA-RSGHDQVVELLLERKAplLARTknGLSPLHMAAQGDHV---ECVKHLLQykAPVDDVTLDYL 373
Cdd:TIGR00870   44 NINCPDRLGRSALFVAAiENENLELTELLLNLSC--RGAV--GDTLLHAISLEYVDaveAILLHLLA--AFRKSGPLELA 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  374 ------------TALHVAAHCGHYRVTKLLLDKRANPNARALNGFtplhiaCKKnriKVMELLVKYGASiqaitesgltP 441
Cdd:TIGR00870  118 ndqytseftpgiTALHLAAHRQNYEIVKLLLERGASVPARACGDF------FVK---SQGVDSFYHGES----------P 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  442 IHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAA----RAGQVEVVRCLLRNGAL-VDARAREEQ----------- 505
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmeneFKAEYEELSCQMYNFALsLLDKLRDSKelevilnhqgl 258

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1039763615  506 TPLHIASRLGKTEIVQLLLQ-------HMAHPdaattngYTPLHISAR 546
Cdd:TIGR00870  259 TPLKLAAKEGRIVLFRLKLAikykqkkFVAWP-------NGQQLLSLY 299
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 40-187 7.28e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 70.76  E-value: 7.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   40 RKRKSDSnasFLR-AARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHI 118
Cdd:PHA02874   120 KDAELKT---FLHyAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039763615  119 ASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHiDVVKYLLENGANQSTATeDGFTPLAVALQ 187
Cdd:PHA02874   197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNASINDQDI-DGSTPLHHAIN 263
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 9-262 1.18e-11

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: 70.94  E-value: 1.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615    9 KKVREAELDEKEKNLDRERKKQRKiprDRMERKRKSDSNASFLRAARAGNLDKVVeYLKGGIDINTCNQNGLNALHLAAK 88
Cdd:cd22194     46 KKKRLKKVSEAAVEELGELLKELK---DLSRRRRKTDVPDFLMHKLTASDTGKTC-LMKALLNINENTKEIVRILLAFAE 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   89 EGhvGLVQELLGrgSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGF--------------TPLYMAAQ 154
Cdd:cd22194    122 EN--GILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAAC 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  155 ENHIDVVKYLLENGANQstatedgftplaVALQqghnqavaillenDTKGKVRLPALHIAArkDDTKS----------AA 224
Cdd:cd22194    198 TNQPEIVQLLMEKESTD------------ITSQ-------------DSRGNTVLHALVTVA--EDSKTqndfvkrmydMI 250

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1039763615  225 LLLQNDHNAD-VQSKSGFTPLHIAAHYGNVNVATLLLNR 262
Cdd:cd22194    251 LLKSENKNLEtIRNNEGLTPLQLAAKMGKAEILKYILSR 289
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 140-362 1.28e-08

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 61.25  E-value: 1.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  140 AQSQNGFTPlymAAQENHIDVVKYLLENGA--NQSTATEDGFTPLAVALQQGHNQAVAILLEN-DTKGKVRLPALHIAAR 216
Cdd:TIGR00870   15 SDEEKAFLP---AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENENLELTELLLNlSCRGAVGDTLLHAISL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  217 --------------KDDTKSAALLLQNDHNADVQSKsGFTPLHIAAHYGNVNVATLLLNRGAAVDFTA------------ 270
Cdd:TIGR00870   92 eyvdaveaillhllAAFRKSGPLELANDQYTSEFTP-GITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvd 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  271 --RNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCA-------------ARSGHDQVVElLLERKAPL--- 332
Cdd:TIGR00870  171 sfYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLvmenefkaeyeelSCQMYNFALS-LLDKLRDSkel 249

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1039763615  333 -LARTKNGLSPLHMAAQGDHVECVKHLLQYK 362
Cdd:TIGR00870  250 eVILNHQGLTPLKLAAKEGRIVLFRLKLAIK 280
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 6-282 6.15e-08

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 58.94  E-value: 6.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615    6 ASIKKVREAELDEKEKNLDRERKKQRKIPrDRMERkrksdsNASFLRAARAGNLD--KVVEYLKGGIDIntcnqnGLNAL 83
Cdd:TIGR00870   20 AFLPAAERGDLASVYRDLEEPKKLNINCP-DRLGR------SALFVAAIENENLEltELLLNLSCRGAV------GDTLL 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   84 HLAAKEGHVGlVQELL--------GRGSS---VDSATK---KGNTALHIASLAGQAEVVKVLVKEGANINA--------- 140
Cdd:TIGR00870   87 HAISLEYVDA-VEAILlhllaafrKSGPLelaNDQYTSeftPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvk 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  141 -QSQNGF----TPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAvaillENDTKG-KVRLPALHIA 214
Cdd:TIGR00870  166 sQGVDSFyhgeSPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKA-----EYEELScQMYNFALSLL 240

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  215 ARKDDTKSAALLLQNDhnadvqsksGFTPLHIAAHYGNVNVATLLLNRGAAV-DFTA-RNGitPLHVASK 282
Cdd:TIGR00870  241 DKLRDSKELEVILNHQ---------GLTPLKLAAKEGRIVLFRLKLAIKYKQkKFVAwPNG--QQLLSLY 299
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 3194-3521 1.07e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 58.64  E-value: 1.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3194 EGELLPDDVSEEIEDLPASDANIDSQVIISASTETPTKEAVSTAVEEPPT---TQRSDSLSTVKQTPRPAVPGPvgqldf 3270
Cdd:PHA03307    28 PGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTeapANESRSTPTWSLSTLAPASPA------ 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3271 spvtRSVYSGQDDESPESSPEEQKSVIEIPTAPVDNVPSAESKPQIPIRTLPTLVPAPPSAEDE------SAFSDDFPSS 3344
Cdd:PHA03307   102 ----REGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAvasdaaSSRQAALPLS 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3345 LDEDSKEGGAKPKSKIPVKAPTQRTEWQPSPTDIPLQKTAVPQGQETLSRAPDGRSKSESDASSLDAK-------TKCPV 3417
Cdd:PHA03307   178 SPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSgcgwgpeNECPL 257

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3418 KARSYIETETESRERAEGFESESEDGATKPKL-FASRLPVKSRSTSSSGrPGTSPTRESREhffdlyrnsieffEEISDE 3496
Cdd:PHA03307   258 PRPAPITLPTRIWEASGWNGPSSRPGPASSSSsPRERSPSPSPSSPGSG-PAPSSPRASSS-------------SSSSRE 323

                          330       340
                   ....*....|....*....|....*
gi 1039763615 3497 ASklvdrlTQSEREQEPPSDDESSS 3521
Cdd:PHA03307   324 SS------SSSTSSSSESSRGAAVS 342
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 673-809 1.36e-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: 1.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  673 LHLASQEGHTDMVTLLLDKGANIHMstksGLTSLHLAAQEDKVNVADILT---KHGADRDAYTKL----------GYTPL 739
Cdd:TIGR00870   57 FVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLEYVDAVEAILLhllAAFRKSGPLELAndqytseftpGITAL 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  740 IVACHYGNVKMVNFLLKQGANVNAKTK--------------NGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTAL 805
Cdd:TIGR00870  133 HLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLL 212


                   ....
gi 1039763615  806 AIAK 809
Cdd:TIGR00870  213 HLLV 216
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 144-170 2.07e-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: 46.81  E-value: 2.07e-06
                            10        20
                    ....*....|....*....|....*..
gi 1039763615   144 NGFTPLYMAAQENHIDVVKYLLENGAN 170
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 404-431 5.31e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 45.66  E-value: 5.31e-06
                            10        20
                    ....*....|....*....|....*...
gi 1039763615   404 NGFTPLHIACKKNRIKVMELLVKYGASI 431
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 767-796 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: 44.50  E-value: 1.05e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1039763615   767 NGYTPLHQAAQQGHTHIINVLLQHGAKPNA 796
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 272-301 1.53e-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: 44.12  E-value: 1.53e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1039763615   272 NGITPLHVASKRGNTNMVKLLLDRGGQIDA 301
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 1807-2015 3.22e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.17  E-value: 3.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1807 RVEDEQKGRSKLPVRVKGKEDVPKRTTPRTHPA-VSPSSKSSTSSKAERHSSLSSSAKPerhtpvsPSSKNEKLSPVSPS 1885
Cdd:PHA03307   229 ADDAGASSSDSSSSESSGCGWGPENECPLPRPApITLPTRIWEASGWNGPSSRPGPASS-------SSSPRERSPSPSPS 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1886 AkterhspvfSGKPEKHSPGSPSTKNERHSPVSSLKTER-----HTPGSPSGKTDKRPPVPSSGRtekhPPVSPGKTEKH 1960
Cdd:PHA03307   302 S---------PGSGPAPSSPRASSSSSSSRESSSSSTSSssessRGAAVSPGPSPSRSPSPSRPP----PPADPSSPRKR 368

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039763615 1961 LPGSPSIRTPeKPAPGSATGKHEKHLPVSPGKTEKQPPISPTSKTERIEETMSVR 2015
Cdd:PHA03307   369 PRPSRAPSSP-AASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAA 422
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 2245-2652 7.30e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 45.84  E-value: 7.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 2245 PQISSEESYKHEGlaetPETSPESLSFSPKKSEEQIGEAKETTKvGTPTDIHSEKELPITNDITDSSQKQGagvtrgseP 2324
Cdd:PTZ00449   497 APIEEEDSDKHDE----PPEGPEASGLPPKAPGDKEGEEGEHED-SKESDEPKEGGKPGETKEGEVGKKPG--------P 563

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 2325 STEHSQKEV---TQDPHKDVCSKQDGCPESQSVSLASEVFTEKGSCGESQLPLVSSAFKTQSESEtqeslTPSEVTKPFP 2401
Cdd:PTZ00449   564 AKEHKPSKIptlSKKPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPE-----SPKSPKRPPP 638

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 2402 PS-DASVKTAEGTEpkpqgAIRSPQGLELPLPNRDSEVLSPMADESLAVSHKDSLEASPVLEDNSSH--------KTPDS 2472
Cdd:PTZ00449   639 PQrPSSPERPEGPK-----IIKSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFEsilketlpETPGT 713

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 2473 LEPSPLKESPCRDSLESSPVEP---KMKAGILPSHFPLPAA-----IAKTDLVAEVASMRSRLLRDPDGSAEDDSLEQT- 2543
Cdd:PTZ00449   714 PFTTPRPLPPKLPRDEEFPFEPigdPDAEQPDDIEFFTPPEeertfFHETPADTPLPDILAEEFKEEDIHAETGEPDEAm 793

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 2544 ----SLMESSGKSPLS-PDTP----SSEEVSYEVTPKPSDS------STPKPAVIHECAEEDDSENGEKKrftpeEEMFK 2608
Cdd:PTZ00449   794 krpdSPSEHEDKPPGDhPSLPkkrhRLDGLALSTTDLESDAgriakdASGKIVKLKRSKSFDDLTTVEEA-----EEMGA 868

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039763615 2609 MVTKIKTFDELEQ---------------EAKQKRDYKKEPRQDGSSSASDPDADYSAEV 2652
Cdd:PTZ00449   869 EARKIVVDDDGTEaddedthppeekhksEVRRRRPPKKPSKPKKPSKPKKPKKPDSAFI 927
Treacle pfam03546
Treacher Collins syndrome protein Treacle;
3168-3425 1.00e-03

Treacher Collins syndrome protein Treacle;


Pssm-ID: 460967 [Multi-domain]  Cd Length: 531  Bit Score: 45.06  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3168 TGAEPPQTETTSESLELSEPKEAMDDEGEllpdDVSEEIEDLPASDANIDSQviisASTETPTKEAVSTAVEEPPttqrs 3247
Cdd:pfam03546    1 TPATPGKAGPAATQAKAGKPEEDSESSSE----EESDSEEETPAAKTPLQAK----PSGKTPQVRAASAPAKESP----- 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3248 dslstVKQTPrPAVPGPVGqldfsPVTRSVYSGQDDESPESSPEEQKSVIEIPTAPVDNVPSAESKP---QIPIRTLPTL 3324
Cdd:pfam03546   68 -----RKGAP-PVPPGKTG-----PAAAQAQAGKPEEDSESSSEESDSDGETPAAATLTTSPAQVKPlgkNSQVRPASTV 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3325 ---------VPAPPSAEDESAF-------SDDFPSSLDEDSKEGGAKP---KSKIPVKAPTQRTEWQPS--PTDIPLQKT 3383
Cdd:pfam03546  137 gkgpsgkgaNPAPPGKAGSAAPlvqvgkkEEDSESSSEESDSEGEAPPaatQAKPSGKILQVRPASGPAkgAAPAPPQKA 216

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1039763615 3384 --AVPQGQETLSRAPDGRSKSESDASSLDAKTKCPVKARSYIET 3425
Cdd:pfam03546  217 gpVATQVKAERSKEDSESSEESSDSEEEAPAAATPAQAKPALKT 260
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
556-821 2.98e-62

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 215.97  E-value: 2.98e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  556 LLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKN 635
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  636 GYTPLHIAAKKNQMQIASTLLNYGAETNTVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKV 715
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  716 NVADILTKHGADRDAYTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPN 795
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250       260
                   ....*....|....*....|....*.
gi 1039763615  796 ATTANGNTALAIAKRLGYISVVDTLK 821
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
319-607 8.43e-62

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 214.82  E-value: 8.43e-62
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  319 DQVVELLLERKAPLLARTKNGLSPLHMAAQGDHVECVKHLLQYKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANP 398
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  399 NARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMA 478
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  479 ARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLE 558
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1039763615  559 AGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPL 607
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
253-541 1.14e-60

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 211.35  E-value: 1.14e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  253 VNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERKAPL 332
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  333 LARTKNGLSPLHMAAQGDHVECVKHLLQYKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIA 412
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  413 CKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLR 492
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1039763615  493 NGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPL 541
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
358-640 1.53e-60

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 210.97  E-value: 1.53e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  358 LLQYKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITES 437
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  438 GLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKT 517
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  518 EIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAAD 597
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1039763615  598 SAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPL 640
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
518-805 1.58e-60

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 210.97  E-value: 1.58e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  518 EIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAAD 597
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  598 SAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNTVTKQGVTPLHLAS 677
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  678 QEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADRDAYTKLGYTPLIVACHYGNVKMVNFLLKQ 757
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1039763615  758 GANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTAL 805
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
223-508 2.95e-60

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 210.20  E-value: 2.95e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  223 AALLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAK 302
Cdd:COG0666      4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  303 TRDGLTPLHCAARSGHDQVVELLLERKAPLLARTKNGLSPLHMAAQGDHVECVKHLLQYKAPVDDVTLDYLTALHVAAHC 382
Cdd:COG0666     84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  383 GHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGA 462
Cdd:COG0666    164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1039763615  463 SPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPL 508
Cdd:COG0666    244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
191-475 3.27e-60

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 210.20  E-value: 3.27e-60
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  191 NQAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTA 270
Cdd:COG0666      5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  271 RNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERKAPLLARTKNGLSPLHMAAQGD 350
Cdd:COG0666     85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  351 HVECVKHLLQYKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGAS 430
Cdd:COG0666    165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD 244

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1039763615  431 IQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETAL 475
Cdd:COG0666    245 LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
418-704 1.44e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 208.27  E-value: 1.44e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  418 IKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALV 497
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  498 DARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVA 577
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  578 AKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLN 657
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1039763615  658 YGAETNTVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLT 704
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
490-772 7.00e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 206.34  E-value: 7.00e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  490 LLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKK 569
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  570 GFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQM 649
Cdd:COG0666     87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  650 QIASTLLNYGAETNTVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADRD 729
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|...
gi 1039763615  730 AYTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPL 772
Cdd:COG0666    247 AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
287-574 7.27e-59

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 206.34  E-value: 7.27e-59
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  287 NMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERKAPLLARTKNGLSPLHMAAQGDHVECVKHLLQYKAPVD 366
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  367 DVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAA 446
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  447 FMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQH 526
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1039763615  527 MAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPL 574
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
UPA_2 pfam17809
UPA domain; The UPA domain is conserved in UNC5, PIDD, and Ankyrins. It has a beta sandwich ...
 1355-1484 4.71e-58

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: 197.70  E-value: 4.71e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1355 VPYMAKFVVFAKSHDPIEARLRCFCMTDDKVDKTLEQQENFSEVARSRDVEVLEGKPIYVDCFGNLVPLTKSGQHHIFSF 1434
Cdd:pfam17809    1 VPYLAKFVVFAKRYDPGEARLRCACMTDDGEDKTLEFHEGFTEVARSRDVEVLEGSPVSIELSGNLVPIKKKSQSRQMDF 80

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1435 FAFKENRLPLFVKVRDTTQEPCGRLSFMKEPKSTRGLVHQAICNLNITLP 1484
Cdd:pfam17809   81 KAFRENRLDGSVRVKDPSDPPKGLLSFMRDAKVDGGTVSQPLCTLNIVLP 130
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
158-442 6.59e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 203.65  E-value: 6.59e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  158 IDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRL----PALHIAARKDDTKSAALLLQNDHNA 233
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADalgaLLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  234 DVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCA 313
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  314 ARSGHDQVVELLLERKAPLLARTKNGLSPLHMAAQGDHVECVKHLLQYKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLD 393
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1039763615  394 KRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPI 442
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
583-864 8.71e-58

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 203.26  E-value: 8.71e-58
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  583 LDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAET 662
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  663 NTVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADRDAYTKLGYTPLIVA 742
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  743 CHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTLKV 822
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1039763615  823 VTEEVTTTTTTITEKHKLNVPETMTEVLDVSDEEGDDTVTGD 864
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
390-673 1.22e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 202.88  E-value: 1.22e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  390 LLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNI 469
Cdd:COG0666      6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  470 RGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQ 549
Cdd:COG0666     86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  550 VDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASP 629
Cdd:COG0666    166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1039763615  630 HATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNTVTKQGVTPL 673
Cdd:COG0666    246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
59-376 5.80e-57

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 200.95  E-value: 5.80e-57
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   59 LDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANI 138
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  139 NAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPlavalqqghnqavaillendtkgkvrlpaLHIAARKD 218
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP-----------------------------LHLAAYNG 131

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  219 DTKSAALLLqnDHNADV--QSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRG 296
Cdd:COG0666    132 NLEIVKLLL--EAGADVnaQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  297 GQIDAKTRDGLTPLHCAARSGHDQVVELLLERKAPLLARTKNGLSPLHMAAQGDHVECVKHLLQYKAPVDDVTLDYLTAL 376
Cdd:COG0666    210 ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
451-739 6.62e-56

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 197.87  E-value: 6.62e-56
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  451 LNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHP 530
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  531 DAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVA 610
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  611 AHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNTVTKQGVTPLHLASQEGHTDMVTLLLD 690
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*....
gi 1039763615  691 KGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADRDAYTKLGYTPL 739
Cdd:COG0666    241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-343 5.97e-54

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 192.09  E-value: 5.97e-54
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   14 AELDEKEKNLDRERKKQRKIPRDRMERKRKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVG 93
Cdd:COG0666     22 ALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLE 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   94 LVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGAnqst 173
Cdd:COG0666    102 IVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA---- 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  174 atedgftplavalqqghnqavaillendtkgkvrlpalhiaarkddtksaalllqndhNADVQSKSGFTPLHIAAHYGNV 253
Cdd:COG0666    178 ----------------------------------------------------------DVNARDNDGETPLHLAAENGHL 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  254 NVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERKAPLL 333
Cdd:COG0666    200 EIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279

                          330
                   ....*....|
gi 1039763615  334 ARTKNGLSPL 343
Cdd:COG0666    280 AALLDLLTLL 289
Death_ank2 cd08804
Death domain of Ankyrin-2; Death Domain (DD) of Ankyrin-2 (ANK-2) and related proteins. ...
 3579-3662 9.84e-49

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: 169.11  E-value: 9.84e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3579 ERMEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTILIECLTKINRMDIV 3658
Cdd:cd08804      1 ERTEERLAHIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTNLTQCLTKINRMDIV 80


                   ....
gi 1039763615 3659 HLLE 3662
Cdd:cd08804     81 HLME 84
ZU5 smart00218
Domain present in ZO-1 and Unc5-like netrin receptors; Domain of unknown function.
 997-1134 3.17e-42

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


Pssm-ID: 128514  Cd Length: 104  Bit Score: 150.96  E-value: 3.17e-42
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   997 PCFLVSFMVDARGGAMRGCRhNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEVGPSGAQflgklh 1076
Cdd:smart00218    1 PSFLVSGTFDARGGRLRGPR-TGVRLIIPPGAIPQGTRYTCYLVVHKTLSTPPPLEEGETLLSPVVECGPHGAL------ 73

                            90       100       110       120       130
                    ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039763615  1077 lptappplnegeslvsrilqlgppgtkFLGPVIVEIPHFAALRGKERELVVLRSENGD 1134
Cdd:smart00218   74 ---------------------------FLRPVILEVPHCASLRPRDWEIVLLRSENGG 104
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 568-792 6.45e-39

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 152.51  E-value: 6.45e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  568 KKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHY-----DNQKVALLLLEKGASPHATAKNGYTPLHI 642
Cdd:PHA03100    33 KKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLY 112

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  643 AA--KKNQMQIASTLLNYGAETNTVTKQGVTPLHLASQEGHTD--MVTLLLDKGANIhmstksgltslhlaaqeDKVNVA 718
Cdd:PHA03100   113 AIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDI-----------------NAKNRV 175

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039763615  719 DILTKHGADRDAYTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGA 792
Cdd:PHA03100   176 NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
Death_ank cd08317
Death domain associated with Ankyrins; Death Domain (DD) associated with Ankyrins. Ankyrins ...
 3579-3662 2.54e-35

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: 130.46  E-value: 2.54e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3579 ERMEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTILIECLTKINRMDIV 3658
Cdd:cd08317      1 HRADLRLSDIANLLGSDWPELARELGVSEEDIDLIRSENPNSLAQQAMAMLRLWLEREGEKATGNALESALKKIGRDDIV 80


                   ....
gi 1039763615 3659 HLLE 3662
Cdd:cd08317     81 EKCE 84
ZU5 pfam00791
ZU5 domain; Domain present in ZO-1 and Unc5-like netrin receptors Domain of unknown function.
 1001-1131 1.28e-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: 129.18  E-value: 1.28e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1001 VSFMVDARGGAMRGCrHNGLRIIIPPRKCTAPTRVTCRLVKRHRLATMPPMVEGEGLASRLIEvgpsgaqflgklhlpta 1080
Cdd:pfam00791    1 VSGLVDSRGGRLVLP-NSGVSLLIPPGAIPEGTRIECYLAVNRDESSRPPLEEGETLLSPVVE----------------- 62

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1039763615 1081 ppplnegeslvsrilqLGPPGTKFLGPVIVEIPHFAALRGKERELVVLRSE 1131
Cdd:pfam00791   63 ----------------CGPPGLKFLKPVILEVPHCASLRPEEWEIVLKRSD 97
PHA03095 PHA03095
ankyrin-like protein; Provisional
 411-696 5.25e-34

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 139.39  E-value: 5.25e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  411 IACKKNRIKVMELLVKYGASIQAITESGLTPIHVaaFMGH-----LNIVLLLLQNGASPDVTNIRGETALHMAARAGQVE 485
Cdd:PHA03095    20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHL--YLHYssekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTL 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  486 -VVRCLLRNGALVDARAREEQTPLHI--ASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASV--LLEAG 560
Cdd:PHA03095    98 dVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELLrlLIDAG 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  561 AahSLATKK--GFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKN--GLTPLHVAAHYDNQKVALL--LLEKGASPHATAK 634
Cdd:PHA03095   178 A--DVYAVDdrFRSLLHHHLQSFKPRARIVRELIRAGCDPAATDmlGNTPLHSMATGSSCKRSLVlpLLIAGISINARNR 255

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039763615  635 NGYTPLHIAAKKNQMQIASTLLNYGAETNTVTKQGVTPLHLASQEGHTDMVTLLLDKGANIH 696
Cdd:PHA03095   256 YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 605-814 2.16e-33

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 136.33  E-value: 2.16e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  605 TPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAA-----KKNQMQIASTLLNYGAETNTVTKQGVTPLHLASQE 679
Cdd:PHA03100    37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISK 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  680 --GHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQ--EDKVNVADILTKHGADRDAYTKlgytplivachygnvkmVNFLL 755
Cdd:PHA03100   117 ksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIDKGVDINAKNR-----------------VNYLL 179

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039763615  756 KQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTAL--AIAKRLGYI 814
Cdd:PHA03100   180 SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLhiAILNNNKEI 240
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 200-434 3.26e-33

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 135.95  E-value: 3.26e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  200 NDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYG-----NVNVATLLLNRGAAVDFTARNGI 274
Cdd:PHA03100    28 NDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYGANVNAPDNNGI 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  275 TPLHVAS--KRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHD--QVVELLLERKAPLLARTKnglsplhmaaqgd 350
Cdd:PHA03100   108 TPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNR------------- 174

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  351 hvecVKHLLQYKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGAS 430
Cdd:PHA03100   175 ----VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250


                   ....
gi 1039763615  431 IQAI 434
Cdd:PHA03100   251 IKTI 254
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 369-761 4.39e-32

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 136.73  E-value: 4.39e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  369 TLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFM 448
Cdd:PHA02876   142 SIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDS 221

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  449 GHLNIVLLLLQNGASPDvtniRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGK-TEIVQLLLQHM 527
Cdd:PHA02876   222 KNIDTIKAIIDNRSNIN----KNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERG 297

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  528 AHPDAATTNGYTPLHISAREGqvdvasvlleagaahslatkkgftplhvaakYGSLDVaKLLLQRRAAADSAGKNGLTPL 607
Cdd:PHA02876   298 ADVNAKNIKGETPLYLMAKNG-------------------------------YDTENI-RTLIMLGADVNAADRLYITPL 345

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  608 HVAAHYD-NQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNTVTKQGVTPLHLASQEGHTDM-V 685
Cdd:PHA02876   346 HQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsV 425

                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039763615  686 TLLLDKGANIHMSTKSGLTSLHLAAQED-KVNVADILTKHGADRDAYTKLGYTPLIVACHYGNVkmVNFLLKQGANV 761
Cdd:PHA02876   426 KTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGI--VNILLHYGAEL 500
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 59-462 1.58e-31

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 134.81  E-value: 1.58e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   59 LDKV-VEYLKGGIDINTCNQNGLN-------ALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKV 130
Cdd:PHA02876   117 LDEAcIHILKEAISGNDIHYDKINesieymkLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNL 196

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  131 LVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANqstatedgftplavalqqghnqavaiLLENDTkgkvrlpA 210
Cdd:PHA02876   197 LLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN--------------------------INKNDL-------S 243

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  211 LHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYGNVN-VATLLLNRGAAVDFTARNGITPLHVASKRG-NTNM 288
Cdd:PHA02876   244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTEN 323

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  289 VKLLLDRGGQIDAKTRDGLTPLHCAAR-SGHDQVVELLLERKAPLLARTKNGLSPLHMAAQGDHVECVKHLLQYKAPVDD 367
Cdd:PHA02876   324 IRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA 403

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  368 VTLDYLTALHVAAhCGH--YRVTKLLLDKRANPNARALNGFTPLHIACKKN-RIKVMELLVKYGASIQAITESGLTPIHV 444
Cdd:PHA02876   404 LSQKIGTALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLI 482

                          410
                   ....*....|....*...
gi 1039763615  445 AafMGHLNIVLLLLQNGA 462
Cdd:PHA02876   483 A--LEYHGIVNILLHYGA 498
PHA03095 PHA03095
ankyrin-like protein; Provisional
 36-431 3.78e-31

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 130.53  E-value: 3.78e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   36 DRMERKRKSDSNASFLRAARAGN--LDKVVEYLKGGIDINTCNQNGLNALHLAAKEGH---VGLVQELLGRGSSVDSATK 110
Cdd:PHA03095     2 EEDESVDIIMEAALYDYLLNASNvtVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPER 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  111 KGNTALHI-ASLAGQAEVVKVLVKEGANINAQSQNGFTPL--YMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQ 187
Cdd:PHA03095    82 CGFTPLHLyLYNATTLDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLK 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  188 QgHNQAVAIllendtkgkVRLPALHIAarkddtksaalllqNDHNADVqskSGFTPLHIAAHYgnvnvatlllnrgaavd 267
Cdd:PHA03095   162 S-RNANVEL---------LRLLIDAGA--------------DVYAVDD---RFRSLLHHHLQS----------------- 197

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  268 FTARNGItplhvaskrgntnmVKLLLDRGGQIDAKTRDGLTPLHCAAR--SGHDQVVELLLERKAPLLARTKNGLSPLHM 345
Cdd:PHA03095   198 FKPRARI--------------VRELIRAGCDPAATDMLGNTPLHSMATgsSCKRSLVLPLLIAGISINARNRYGQTPLHY 263

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  346 AAQGDHVECVKHLLQYKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPN--ARALNGFTPLH--IACKKNRIKVM 421
Cdd:PHA03095   264 AAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAEtvAATLNTASVAGgdIPSDATRLCVA 343

                          410
                   ....*....|
gi 1039763615  422 ELLVKYGASI 431
Cdd:PHA03095   344 KVVLRGAFSL 353
PHA03095 PHA03095
ankyrin-like protein; Provisional
 518-821 8.11e-31

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 129.76  E-value: 8.11e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  518 EIVQLLLQHMAHPDAATTNGYTPLHI---SAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGS-LDVAKLLLQRR 593
Cdd:PHA03095    28 EEVRRLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAG 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  594 AAADSAGKNGLTPLHVAAHYDN--QKVALLLLEKGASPHATAKNGYTPLHIAAKKNQ--MQIASTLLNYGAETNTVTKQG 669
Cdd:PHA03095   108 ADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRF 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  670 VTPLH--LASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADI--LTKHGADRDAYTKLGYTPLIVACHY 745
Cdd:PHA03095   188 RSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVF 267

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039763615  746 GNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQhgAKPNATT-ANgntALAIAKRLGYISVVDTLK 821
Cdd:PHA03095   268 NNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA--KNPSAETvAA---TLNTASVAGGDIPSDATR 339
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 226-463 1.42e-30

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 127.86  E-value: 1.42e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  226 LLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLH-----VASKRGNTNMVKLLLDRGGQID 300
Cdd:PHA03100    21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVN 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  301 AKTRDGLTPLHCAA--RSGHDQVVELLLERKAPLLARTKNGLSPLHMAAQGDHV--ECVKHLLQYKAPVDDVTldyltal 376
Cdd:PHA03100   101 APDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKN------- 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  377 hvaahcghyRVtKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLL 456
Cdd:PHA03100   174 ---------RV-NYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243


                   ....*..
gi 1039763615  457 LLQNGAS 463
Cdd:PHA03100   244 LLNNGPS 250
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 407-676 2.06e-30

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 127.77  E-value: 2.06e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  407 TPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGAS------PDVTNirgetalhmaar 480
Cdd:PHA02874    37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsilpiPCIEK------------ 104

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  481 agqvEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAG 560
Cdd:PHA02874   105 ----DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  561 AAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLleKGASPHATAKNGYTPL 640
Cdd:PHA02874   181 AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLI--NNASINDQDIDGSTPL 258

                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1039763615  641 HIAAKKN-QMQIASTLLNYGAETNTVTKQGVTPLHLA 676
Cdd:PHA02874   259 HHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 259-499 7.91e-30

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 125.55  E-value: 7.91e-30
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  259 LLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQ-----VVELLLERKAPLL 333
Cdd:PHA03100    21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVN 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  334 ARTKNGLSPLHMAAQG--DHVECVKHLLQYKAPVDDVTLDYLTALHVAAHCGHY--RVTKLLLDKRANPNAralngftpl 409
Cdd:PHA03100   101 APDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINA--------- 171

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  410 hiackKNRIKvmeLLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRC 489
Cdd:PHA03100   172 -----KNRVN---YLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243

                          250
                   ....*....|
gi 1039763615  490 LLRNGALVDA 499
Cdd:PHA03100   244 LLNNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 483-820 1.01e-29

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 129.03  E-value: 1.01e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  483 QVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAgaa 562
Cdd:PHA02876   157 ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN--- 233

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  563 HSLATKKGFTPLHvAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDN-QKVALLLLEKGASPHATAKNGYTPLH 641
Cdd:PHA02876   234 RSNINKNDLSLLK-AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLY 312

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  642 IAAKKN-QMQIASTLLNYGAETNTVTKQGVTPLHLASQ-EGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVAD 719
Cdd:PHA02876   313 LMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIIN 392

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  720 ILTKHGADRDAYT-KLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQG-HTHIINVLLQHGAKPNAT 797
Cdd:PHA02876   393 TLLDYGADIEALSqKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAI 472

                          330       340
                   ....*....|....*....|...
gi 1039763615  798 TANGNTALAIAkrLGYISVVDTL 820
Cdd:PHA02876   473 NIQNQYPLLIA--LEYHGIVNIL 493
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 216-528 1.69e-29

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 128.64  E-value: 1.69e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  216 RKDDTKSAALLLQNdhNADVQSKSGF--TPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLL 293
Cdd:PHA02876   154 QQDELLIAEMLLEG--GADVNAKDIYciTPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  294 DRGGQIDAKTRDGL-----------------------------TPLHCAARSGH-DQVVELLLERKAPLLARTKNGLSPL 343
Cdd:PHA02876   232 DNRSNINKNDLSLLkairnedletslllydagfsvnsiddcknTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  344 H-MAAQGDHVECVKHLLQYKAPVDDVTLDYLTALHVAAHCGHYRVTKL-LLDKRANPNARALNGFTPLHIACKKNRIKVM 421
Cdd:PHA02876   312 YlMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVII 391

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  422 ELLVKYGASIQAITESGLTPIHVAAF-MGHLNIVLLLLQNGASPDVTNIRGETALHMAARAG-QVEVVRCLLRNGALVDA 499
Cdd:PHA02876   392 NTLLDYGADIEALSQKIGTALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNA 471

                          330       340
                   ....*....|....*....|....*....
gi 1039763615  500 RAREEQTPLHIAsrLGKTEIVQLLLQHMA 528
Cdd:PHA02876   472 INIQNQYPLLIA--LEYHGIVNILLHYGA 498
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 255-661 1.98e-29

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 128.26  E-value: 1.98e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  255 VATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAarsghdqvvelllerkaplla 334
Cdd:PHA02876   160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECA--------------------- 218

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  335 rtknglsplhmaaqgdhvecvkhllqykapVDDVTLDYLTAlhvaahcghyrvtklLLDKRANPNARALNgftpLHIACK 414
Cdd:PHA02876   219 ------------------------------VDSKNIDTIKA---------------IIDNRSNINKNDLS----LLKAIR 249

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  415 KNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLN-IVLLLLQNGASPDVTNIRGETALHMAARAG-QVEVVRCLLR 492
Cdd:PHA02876   250 NEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIM 329

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  493 NGALVDARAREEQTPLHIASRLGK-TEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGF 571
Cdd:PHA02876   330 LGADVNAADRLYITPLHQASTLDRnKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG 409

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  572 TPLHVAAkYGS--LDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQ-KVALLLLEKGASPHATAKNGYTPLHIAAKKNq 648
Cdd:PHA02876   410 TALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIALEYH- 487

                          410
                   ....*....|...
gi 1039763615  649 mQIASTLLNYGAE 661
Cdd:PHA02876   488 -GIVNILLHYGAE 499
PHA03095 PHA03095
ankyrin-like protein; Provisional
 150-448 4.30e-29

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 124.37  E-value: 4.30e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  150 YMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHnqavaillendtkgkvrlpalhiaarKDDTKSAALLLQN 229
Cdd:PHA03095    19 LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSS--------------------------EKVKDIVRLLLEA 72

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  230 DHNADVQSKSGFTPLHIAAHYGNV-NVATLLLNRGAAVDFTARNGITPLHV--ASKRGNTNMVKLLLDRGGQIDAKTRDG 306
Cdd:PHA03095    73 GADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYG 152

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  307 LTPLHCAARSGH--DQVVELLLERKAPLLARTKNGLSPLHMAAQG--DHVECVKHLLQYKAPVDDVTLDYLTALHVAAHC 382
Cdd:PHA03095   153 MTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATG 232

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039763615  383 GHYRVTKL--LLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIhvaAFM 448
Cdd:PHA03095   233 SSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL---SLM 297
Death_ank3 cd08803
Death domain of Ankyrin-3; Death Domain (DD) of the human protein ankyrin-3 (ANK-3) and ...
 3579-3662 1.18e-27

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: 108.99  E-value: 1.18e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3579 ERMEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTILIECLTKINRMDIV 3658
Cdd:cd08803      1 ERTDIRMAIVADHLGLSWTELARELNFSVDEINQIRVENPNSLIAQSFMLLKKWVTRDGKNATTDALTSVLTKINRIDIV 80


                   ....
gi 1039763615 3659 HLLE 3662
Cdd:cd08803     81 TLLE 84
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 484-695 1.77e-27

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 118.61  E-value: 1.77e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  484 VEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQV-----DVASVLLE 558
Cdd:PHA03100    15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLE 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  559 AGAAHSLATKKGFTPLHVAA--KYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHY--DNQKVALLLLEKGAspHATAK 634
Cdd:PHA03100    95 YGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESnkIDLKILKLLIDKGV--DINAK 172

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039763615  635 N------------------GYTPLHIAAKKNQMQIASTLLNYGAETNTVTKQGVTPLHLASQEGHTDMVTLLLDKGANI 695
Cdd:PHA03100   173 NrvnyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 241-538 2.96e-27

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 119.21  E-value: 2.96e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  241 FTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLldrggqIDAKTRDGLTPLHCAARSG-HD 319
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEM------IRSINKCSVFYTLVAIKDAfNN 111

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  320 QVVELLlerKAPLLARTKN----GLSPLHMAAQGDHVEC--VKHLLQYKAPVDDVTLDYL-TALHVAAHCGHYRVTKLLL 392
Cdd:PHA02878   112 RNVEIF---KIILTNRYKNiqtiDLVYIDKKSKDDIIEAeiTKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLL 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  393 DKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVA-AFMGHLNIVLLLLQNGASPDV-TNIR 470
Cdd:PHA02878   189 SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAkSYIL 268

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039763615  471 GETALHMAARAGQveVVRCLLRNGALVDARAREEQTPLHIASR------LGKTEIVQLLLQHMAHPDAATTNGY 538
Cdd:PHA02878   269 GLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKqylcinIGRILISNICLLKRIKPDIKNSEGF 340
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 247-477 4.56e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 117.40  E-value: 4.56e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  247 AAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLL 326
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  327 E-RKAPLLARTKNGLSPLHMAAQGDHVECVKHLLQYKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNG 405
Cdd:PHA02875    89 DlGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  406 FTPLHIACKKNRIKVMELLVKYGASIQAITESG-LTPIHVAAFMGHLNIVLLLLQNGASPD-VTNIRGE--TALHM 477
Cdd:PHA02875   169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNiMFMIEGEecTILDM 244
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 577-798 6.73e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 116.63  E-value: 6.73e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  577 AAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLL 656
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  657 NYGAETNTVT-KQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADRDAYTKLG 735
Cdd:PHA02875    89 DLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039763615  736 YTPLIVACHYGNVKMVNFLLKQGANVNAKTKNG-YTPLHQAAQQGHTHIINVLLQHGAKPNATT 798
Cdd:PHA02875   169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 472-699 1.16e-26

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 116.24  E-value: 1.16e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  472 ETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVD 551
Cdd:PHA02875     3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  552 VASVLLEAGA-AHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPH 630
Cdd:PHA02875    83 AVEELLDLGKfADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  631 ATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNTVTKQG-VTPLHLASQEGHTDMVTLLLDKGANIHMST 699
Cdd:PHA02875   163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 116-456 2.58e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 116.13  E-value: 2.58e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  116 LHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLenganqSTATEDGFTPLAVALQQG-HNQAV 194
Cdd:PHA02878    41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI------RSINKCSVFYTLVAIKDAfNNRNV 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  195 AI---LLENDTKGKVRLPALHIAAR-KDD---TKSAALLLQndHNADVQSK---SGFTPLHIAAHYGNVNVATLLLNRGA 264
Cdd:PHA02878   115 EIfkiILTNRYKNIQTIDLVYIDKKsKDDiieAEITKLLLS--YGADINMKdrhKGNTALHYATENKDQRLTELLLSYGA 192

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  265 AVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHD-QVVELLLERKAPLLAR-TKNGLSP 342
Cdd:PHA02878   193 NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNAKsYILGLTA 272

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  343 LHMAAQGDHVecVKHLLQYKAPVDDVTLDYLTALHVAA------HCGHYRVTKLLLDKRANPNARALNGFTpLHIACKKN 416
Cdd:PHA02878   273 LHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAVkqylciNIGRILISNICLLKRIKPDIKNSEGFI-DNMDCITS 349

                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1039763615  417 RIKVMELLVKYGASIQAITESGLTPIHVAA-FMGHLNIVLL 456
Cdd:PHA02878   350 NKRLNQIKDKCEDELNRLASIKITNTYSFDdFLKCDNSTLL 390
Death_ank1 cd08805
Death domain of Ankyrin-1; Death Domain (DD) of the human protein ankyrin-1 (ANK-1) and ...
 3579-3662 4.20e-26

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: 104.28  E-value: 4.20e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3579 ERMEERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTILIECLTKINRMDIV 3658
Cdd:cd08805      1 ERVEMKMAVIREHLGLSWAELARELQFSVEDINRIRVENPNSLLEQSTALLNLWVDREGENAKMEPLYPALYSIDRLTIV 80


                   ....
gi 1039763615 3659 HLLE 3662
Cdd:cd08805     81 NILE 84
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 19-301 4.96e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 114.38  E-value: 4.96e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   19 KEKNLDRERKKQRKIP-RDRMERKRKSDSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVglvqe 97
Cdd:PHA03100     7 LTKSRIIKVKNIKYIImEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYN----- 81

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   98 lLGRGssvdsatkkgntalhiaslagqAEVVKVLVKEGANINAQSQNGFTPLYMAAQE--NHIDVVKYLLENGANQSTAT 175
Cdd:PHA03100    82 -LTDV----------------------KEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKN 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  176 EDGFTPLAVALQQGHN--QAVAILLEN----DTKGKVRlpalhiaarkddtksaaLLLQNDHNADVQSKSGFTPLHIAAH 249
Cdd:PHA03100   139 SDGENLLHLYLESNKIdlKILKLLIDKgvdiNAKNRVN-----------------YLLSYGVPINIKDVYGFTPLHYAVY 201

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039763615  250 YGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDA 301
Cdd:PHA03100   202 NNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 255-601 6.73e-26

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 114.29  E-value: 6.73e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  255 VATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLErkaplla 334
Cdd:PHA02874    17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID------- 89

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  335 rtkNGLSPLHMaaqgdhvecvkhllqykaPVDDVTLDyltalhvaahcghyrVTKLLLDKRANPNARALNGFTPLHIACK 414
Cdd:PHA02874    90 ---NGVDTSIL------------------PIPCIEKD---------------MIKTILDCGIDVNIKDAELKTFLHYAIK 133

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  415 KNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNG 494
Cdd:PHA02874   134 KGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG 213

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  495 ALVDARAREEQTPLHIASrLGKTEIVQLLLQHmAHPDAATTNGYTPLHISAR-EGQVDVASVLLEAGAAHSLATKKGFTP 573
Cdd:PHA02874   214 NHIMNKCKNGFTPLHNAI-IHNRSAIELLINN-ASINDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENP 291

                          330       340
                   ....*....|....*....|....*....
gi 1039763615  574 LHVAAKYGSLD-VAKLLLQRRAAADSAGK 601
Cdd:PHA02874   292 IDTAFKYINKDpVIKDIIANAVLIKEADK 320
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 90-348 3.28e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 109.28  E-value: 3.28e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   90 GHVGLVQELL-GRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENG 168
Cdd:PHA02874    12 GDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  169 ANQSTatedgftplaVALQQGHNQAVAILLEN----DTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKSGFTPL 244
Cdd:PHA02874    92 VDTSI----------LPIPCIEKDMIKTILDCgidvNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPI 161

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  245 HIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARsgHDQVVEL 324
Cdd:PHA02874   162 HIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIE 239

                          250       260
                   ....*....|....*....|....
gi 1039763615  325 LLERKAPLLARTKNGLSPLHMAAQ 348
Cdd:PHA02874   240 LLINNASINDQDIDGSTPLHHAIN 263
Ank_2 pfam12796
Ankyrin repeats (3 copies);
83-170 4.34e-24

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 99.03  E-value: 4.34e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   83 LHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEgANINAQSqNGFTPLYMAAQENHIDVVK 162
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*...
gi 1039763615  163 YLLENGAN 170
Cdd:pfam12796   79 LLLEKGAD 86
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 610-805 5.96e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 107.77  E-value: 5.96e-24
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  610 AAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNTVTKQGVTPLHLASQEGHTDMVTLLL 689
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  690 DKGANIH-MSTKSGLTSLHLAAQEDKVNVADILTKHGADRDAYTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNG 768
Cdd:PHA02875    89 DLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                          170       180       190
                   ....*....|....*....|....*....|....*..
gi 1039763615  769 YTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTAL 805
Cdd:PHA02875   169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 524-813 1.93e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 107.27  E-value: 1.93e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  524 LQHMAH-PDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLqRRAAADSAGkN 602
Cdd:PHA02878    23 IDHTENySTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI-RSINKCSVF-Y 100

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  603 GLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNTVTK-QGVTPLHLASQEGH 681
Cdd:PHA02878   101 TLVAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKD 180

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  682 TDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADRDAYTKLGYTPLIVACHY-GNVKMVNFLLKQGAN 760
Cdd:PHA02878   181 QRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVD 260

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  761 VNAK-TKNGYTPLHQAAQQghTHIINVLLQHGAKPNATTANGNTALAIA--KRLGY 813
Cdd:PHA02878   261 VNAKsYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAvkQYLCI 314
Ank_2 pfam12796
Ankyrin repeats (3 copies);
244-330 4.35e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.95  E-value: 4.35e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  244 LHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRgGQIDAKTrDGLTPLHCAARSGHDQVVE 323
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ....*..
gi 1039763615  324 LLLERKA 330
Cdd:pfam12796   79 LLLEKGA 85
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 383-627 6.24e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 104.69  E-value: 6.24e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  383 GHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGAsiqaitesgltpihvaafmghlnivlllLQNGA 462
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA----------------------------IPDVK 64

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  463 SPDVtnirgETALHMAARAGQVEVVRCLLRNGALV-DARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPL 541
Cdd:PHA02875    65 YPDI-----ESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL 139

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  542 HISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQ-KVAL 620
Cdd:PHA02875   140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVR 219


                   ....*..
gi 1039763615  621 LLLEKGA 627
Cdd:PHA02875   220 LFIKRGA 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
376-468 8.50e-23

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 95.18  E-value: 8.50e-23
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  376 LHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGAsiQAITESGLTPIHVAAFMGHLNIVL 455
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|...
gi 1039763615  456 LLLQNGASPDVTN 468
Cdd:pfam12796   79 LLLEKGADINVKD 91
DEATH smart00005
DEATH domain, found in proteins involved in cell death (apoptosis); Alpha-helical domain ...
 3582-3663 1.12e-22

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: 94.79  E-value: 1.12e-22
                            10        20        30        40        50        60        70        80
                    ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  3582 EERLAYIADH-LGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTILIECLTKINRMDIVHL 3660
Cdd:smart00005    5 RQKLAKLLDHpLGLDWRELARKLGLSEADIDQIRTEAPRDLAEQSVQLLRLWEQREGKNATLGTLLEALRKMGRDDAVEL 84


                    ...
gi 1039763615  3661 LET 3663
Cdd:smart00005   85 LRS 87
Ank_2 pfam12796
Ankyrin repeats (3 copies);
442-532 2.81e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 93.64  E-value: 2.81e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  442 IHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNgalVDARAREE-QTPLHIASRLGKTEIV 520
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNgRTALHYAARSGHLEIV 77

                           90
                   ....*....|..
gi 1039763615  521 QLLLQHMAHPDA 532
Cdd:pfam12796   78 KLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
343-433 5.14e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.87  E-value: 5.14e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  343 LHMAAQGDHVECVKHLLQYKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKrANPNARaLNGFTPLHIACKKNRIKVME 422
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 1039763615  423 LLVKYGASIQA 433
Cdd:pfam12796   79 LLLEKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 53-315 7.63e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 101.96  E-value: 7.63e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   53 AARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRG---------------------SSVDSATK- 110
Cdd:PHA02874    42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGvdtsilpipciekdmiktildCGIDVNIKd 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  111 -KGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPlavalqqg 189
Cdd:PHA02874   122 aELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESP-------- 193

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  190 hnqavaillendtkgkvrlpaLHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYgNVNVATLLLNrGAAVDFT 269
Cdd:PHA02874   194 ---------------------LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLIN-NASINDQ 250

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1039763615  270 ARNGITPLHVA-SKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAAR 315
Cdd:PHA02874   251 DIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTAFK 297
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 156-378 7.65e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 101.61  E-value: 7.65e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  156 NHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLENDTKGKVRLPA----LHIAARKDDTKSAALLLQ-ND 230
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDieseLHDAVEEGDVKAVEELLDlGK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  231 HNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPL 310
Cdd:PHA02875    93 FADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039763615  311 HCAARSGHDQVVELLLERKAPLLARTKNG-LSPLHMAAQGDHVECVKHLLQYKAPVDDVTL---DYLTALHV 378
Cdd:PHA02875   173 IIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMFMiegEECTILDM 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
277-363 7.74e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 92.49  E-value: 7.74e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  277 LHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERKAplLARTKNGLSPLHMAAQGDHVECVK 356
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78


                   ....*..
gi 1039763615  357 HLLQYKA 363
Cdd:pfam12796   79 LLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
706-797 1.51e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.72  E-value: 1.51e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  706 LHLAAQEDKVNVADILTKHGADRDAYTKLGYTPLIVACHYGNVKMVNFLLKQgANVNAKTkNGYTPLHQAAQQGHTHIIN 785
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1039763615  786 VLLQHGAKPNAT 797
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 355-646 2.08e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 101.11  E-value: 2.08e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  355 VKHLLQYKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKK-NRIKVMELLVKYgasIQA 433
Cdd:PHA02878    20 IEYIDHTENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEpNKLGMKEMIRSI---NKC 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  434 ITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREE-QTPLHIAS 512
Cdd:PHA02878    97 SVFYTLVAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHKgNTALHYAT 176

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  513 RLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKY-GSLDVAKLLLQ 591
Cdd:PHA02878   177 ENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLE 256

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  592 RRAAADSAGK-NGLTPLHVAAHydNQKVALLLLEKGASPHATAKNGYTPLHIAAKK 646
Cdd:PHA02878   257 HGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
Ank_2 pfam12796
Ankyrin repeats (3 copies);
310-401 2.34e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 2.34e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  310 LHCAARSGHDQVVELLLERKAPLLARTKNGLSPLHMAAQGDHVECVKHLLQYKAPvdDVTLDYLTALHVAAHCGHYRVTK 389
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1039763615  390 LLLDKRANPNAR 401
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
211-302 3.78e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.56  E-value: 3.78e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  211 LHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTarNGITPLHVASKRGNTNMVK 290
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1039763615  291 LLLDRGGQIDAK 302
Cdd:pfam12796   79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
116-203 4.50e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.18  E-value: 4.50e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  116 LHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENgaNQSTATEDGFTPLAVALQQGHNQAVA 195
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH--ADVNLKDNGRTALHYAARSGHLEIVK 78


                   ....*...
gi 1039763615  196 ILLENDTK 203
Cdd:pfam12796   79 LLLEKGAD 86
Death pfam00531
Death domain;
3582-3662 4.95e-21

Death domain;


Pssm-ID: 459845 [Multi-domain]  Cd Length: 86  Bit Score: 90.12  E-value: 4.95e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3582 EERLAYIADH---LGFSWTELARELDFTEEQIHQIRIENPNsLQDQSHALLKYWLERDGKHATDTILIECLTKINRMDIV 3658
Cdd:pfam00531    1 RKQLDRLLDPpppLGKDWRELARKLGLSENEIDEIESENPR-LRSQTYELLRLWEQREGKNATVGTLLEALRKLGRRDAA 79


                   ....
gi 1039763615 3659 HLLE 3662
Cdd:pfam00531   80 EKIQ 83
Ank_2 pfam12796
Ankyrin repeats (3 copies);
607-696 6.26e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.79  E-value: 6.26e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  607 LHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYgAETNtVTKQGVTPLHLASQEGHTDMVT 686
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|
gi 1039763615  687 LLLDKGANIH 696
Cdd:pfam12796   79 LLLEKGADIN 88
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 510-808 6.29e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 101.29  E-value: 6.29e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  510 IASRLGKTE--IVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAK 587
Cdd:PHA02876   149 IKERIQQDEllIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  588 LLLQRRAaadSAGKNGLTPLHVAAHYDnQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQM-QIASTLLNYGAETNTVT 666
Cdd:PHA02876   229 AIIDNRS---NINKNDLSLLKAIRNED-LETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKN 304

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  667 KQGVTPLHLASQEGH-TDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKvnvadiltkhgadrdaytklgytplivachy 745
Cdd:PHA02876   305 IKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDR------------------------------- 353

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039763615  746 gNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIA 808
Cdd:PHA02876   354 -NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA 415
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 119-330 6.83e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 98.52  E-value: 6.83e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  119 ASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILL 198
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  199 E-----NDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNG 273
Cdd:PHA02875    89 DlgkfaDDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039763615  274 ITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAA-RSGHDQVVELLLERKA 330
Cdd:PHA02875   169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAiENNKIDIVRLFIKRGA 226
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 342-610 7.82e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 99.18  E-value: 7.82e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  342 PLHMAAQGDHVECVKHLLQYKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLdkrANPNARAL-NGFTPLHIACKKNRIKV 420
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVfYTLVAIKDAFNNRNVEI 116

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  421 ME-LLVKYGASIQAITESGLTPIHVAAFMgHLNIVLLLLQNGASPD-VTNIRGETALHMAARAGQVEVVRCLLRNGALVD 498
Cdd:PHA02878   117 FKiILTNRYKNIQTIDLVYIDKKSKDDII-EAEITKLLLSYGADINmKDRHKGNTALHYATENKDQRLTELLLSYGANVN 195

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  499 ARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHIS-AREGQVDVASVLLEAGAA-HSLATKKGFTPLHV 576
Cdd:PHA02878   196 IPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDvNAKSYILGLTALHS 275

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1039763615  577 AAKygSLDVAKLLLQRRAAADSAGKNGLTPLHVA 610
Cdd:PHA02878   276 SIK--SERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 475-820 1.10e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 98.50  E-value: 1.10e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  475 LHMAARAGQVEVVRCLLRN-GALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNgyTPlhisaregqvdva 553
Cdd:PHA02874     5 LRMCIYSGDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTK--IP------------- 69

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  554 svlleagaahslatkkgfTPLHVAAKYGSLDVAKLLLQrraaadsagkNGLTPLHVAAHYDNQKVALLLLEKGASPHATA 633
Cdd:PHA02874    70 ------------------HPLLTAIKIGAHDIIKLLID----------NGVDTSILPIPCIEKDMIKTILDCGIDVNIKD 121

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  634 KNGYTPLHIAAKKNQMQIASTLLNYGAETNTVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQed 713
Cdd:PHA02874   122 AELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAE-- 199

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  714 kvnvadiltkhgadrdaytklgytplivachYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIinVLLQHGAK 793
Cdd:PHA02874   200 -------------------------------YGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNAS 246

                          330       340       350
                   ....*....|....*....|....*....|
gi 1039763615  794 PNATTANGNTALAIAkrLGY---ISVVDTL 820
Cdd:PHA02874   247 INDQDIDGSTPLHHA--INPpcdIDIIDIL 274
Ank_2 pfam12796
Ankyrin repeats (3 copies);
508-594 2.33e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 2.33e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  508 LHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEagAAHSLATKKGFTPLHVAAKYGSLDVAK 587
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVK 78


                   ....*..
gi 1039763615  588 LLLQRRA 594
Cdd:pfam12796   79 LLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
574-664 4.56e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.48  E-value: 4.56e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  574 LHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATakNGYTPLHIAAKKNQMQIAS 653
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|.
gi 1039763615  654 TLLNYGAETNT 664
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
50-141 5.22e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 5.22e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   50 FLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSvdSATKKGNTALHIASLAGQAEVVK 129
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1039763615  130 VLVKEGANINAQ 141
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 406-676 1.08e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 95.72  E-value: 1.08e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  406 FTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNirGETALHMAARAGQVE 485
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFY--TLVAIKDAFNNRNVE 115

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  486 VVRCLLRNG-----ALVDARAREEQTPLHIasrlgKTEIVQLLLQHMAHPDAATTN-GYTPLHISAREGQVDVASVLLEA 559
Cdd:PHA02878   116 IFKIILTNRykniqTIDLVYIDKKSKDDII-----EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSY 190

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  560 GAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHY-DNQKVALLLLEKGASPHATAK-NGY 637
Cdd:PHA02878   191 GANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGL 270

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1039763615  638 TPLHIAAKKNqmQIASTLLNYGAETNTVTKQGVTPLHLA 676
Cdd:PHA02878   271 TALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSA 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
541-632 1.12e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 1.12e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  541 LHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRrAAADSAGkNGLTPLHVAAHYDNQKVAL 620
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1039763615  621 LLLEKGASPHAT 632
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 475-769 1.69e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 95.33  E-value: 1.69e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  475 LHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIA----SRLGKTEIVQLLLQhmahpdAATTNGYTPLHISAREGQV 550
Cdd:PHA02878    41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckepNKLGMKEMIRSINK------CSVFYTLVAIKDAFNNRNV 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  551 DVASVLLEAgaahslATKKGFTPLHVAAKYGSLD------VAKLLLQRRAAADSAGKNGL-TPLHVAAHYDNQKVALLLL 623
Cdd:PHA02878   115 EIFKIILTN------RYKNIQTIDLVYIDKKSKDdiieaeITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLL 188

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  624 EKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNTVTKQGVTPLHLASQE-GHTDMVTLLLDKGANIHM-STKS 701
Cdd:PHA02878   189 SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAkSYIL 268

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039763615  702 GLTSLHLAAQ-EDKVNvadILTKHGADRDAYTKLGYTPLIVAC------HYGNVKMVNFLLKQGANVNAKTKNGY 769
Cdd:PHA02878   269 GLTALHSSIKsERKLK---LLLEYGADINSLNSYKLTPLSSAVkqylciNIGRILISNICLLKRIKPDIKNSEGF 340
Ank_2 pfam12796
Ankyrin repeats (3 copies);
409-500 1.80e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 1.80e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  409 LHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNirGETALHMAARAGQVEVVR 488
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLEIVK 78

                           90
                   ....*....|..
gi 1039763615  489 CLLRNGALVDAR 500
Cdd:pfam12796   79 LLLEKGADINVK 90
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 57-296 5.02e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 93.13  E-value: 5.02e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   57 GNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGA 136
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  137 NIN-AQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPlavalqqghnqavaillendtkgkvrlpaLHIAA 215
Cdd:PHA02875    93 FADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP-----------------------------LHLAV 143

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  216 RKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNG-ITPLHVASKRGNTNMVKLLLD 294
Cdd:PHA02875   144 MMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIK 223


                   ..
gi 1039763615  295 RG 296
Cdd:PHA02875   224 RG 225
Death cd01670
Death Domain: a protein-protein interaction domain; Death Domains (DDs) are protein-protein ...
 3585-3662 1.02e-18

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: 83.10  E-value: 1.02e-18
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039763615 3585 LAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTILIECLTKINRMDIVHLLE 3662
Cdd:cd01670      2 FDLVAEELGRDWKKLARKLGLSEGDIDQIEEDNRDDLKEQAYQMLERWREREGDEATLGRLIQALREIGRRDLAEKLE 79
Ank_2 pfam12796
Ankyrin repeats (3 copies);
640-727 1.97e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 1.97e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  640 LHIAAKKNQMQIASTLLNYGAETNTVTKQGVTPLHLASQEGHTDMVTLLLDKgANIHMSTKsGLTSLHLAAQEDKVNVAD 719
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78


                   ....*...
gi 1039763615  720 ILTKHGAD 727
Cdd:pfam12796   79 LLLEKGAD 86
Ank_2 pfam12796
Ankyrin repeats (3 copies);
739-820 1.58e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 1.58e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  739 LIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHgAKPNATTaNGNTALAIAKRLGYISVVD 818
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                   ..
gi 1039763615  819 TL 820
Cdd:pfam12796   79 LL 80
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 614-820 3.57e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 88.97  E-value: 3.57e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  614 DNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNTVTKQGVTPLHLASQEGHTDMVTLLLDKGA 693
Cdd:PHA02876   156 DELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  694 NIHmstKSGLTSLHLAAQEDkVNVADILTKHGADRDAYTKLGYTPLIVACHYGNV-KMVNFLLKQGANVNAKTKNGYTPL 772
Cdd:PHA02876   236 NIN---KNDLSLLKAIRNED-LETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPL 311

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|
gi 1039763615  773 HQAAQQGH-THIINVLLQHGAKPNATTANGNTALAIAKRLG-YISVVDTL 820
Cdd:PHA02876   312 YLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITL 361
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 562-756 1.71e-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: 1.71e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  562 AHSLATKKGF-TPLHVAAKYGSLD-VAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEkgASPH-----ATAK 634
Cdd:cd22192      8 LHLLQQKRISeSPLLLAAKENDVQaIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPElvnepMTSD 85

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  635 --NGYTPLHIAAKKNQMQIASTLLNYGAE------TNTVTKQGVT--------PLHLASQEGHTDMVTLLLDKGANIHMS 698
Cdd:cd22192     86 lyQGETALHIAVVNQNLNLVRELIARGADvvspraTGTFFRPGPKnliyygehPLSFAACVGNEEIVRLLIEHGADIRAQ 165

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039763615  699 TKSGLTSLH-LAAQEDKVNVAD----ILTKHGADRDA--YT---KLGYTPLIVACHYGNVKMVNFLLK 756
Cdd:cd22192    166 DSLGNTVLHiLVLQPNKTFACQmydlILSYDKEDDLQplDLvpnNQGLTPFKLAAKEGNIVMFQHLVQ 233
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 502-691 2.93e-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: 82.75  E-value: 2.93e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  502 REEQTPLHIASRLGKTEIVQ-LLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAgaAHSLATK-------KGFTP 573
Cdd:cd22192     15 RISESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEA--APELVNEpmtsdlyQGETA 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  574 LHVAAKYGSLDVAKLLLQRRAAADSA---------GKNGLT-----PLHVAAHYDNQKVALLLLEKGASPHATAKNGYTP 639
Cdd:cd22192     93 LHIAVVNQNLNLVRELIARGADVVSPratgtffrpGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039763615  640 LHI----AAKKNQMQIASTLLNYGAETNTVT------KQGVTPLHLASQEGHTDMVTLLLDK 691
Cdd:cd22192    173 LHIlvlqPNKTFACQMYDLILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQHLVQK 234
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 407-593 8.89e-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: 81.21  E-value: 8.89e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  407 TPLHIACKKNRIKVMELLVKY-GASIQAITESGLTPIHVAAFMGHLNIVLLLLQngASPDVTNI-------RGETALHMA 478
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEpmtsdlyQGETALHIA 96

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  479 ARAGQVEVVRCLLRNGA-LVDARA-----REEQT--------PLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHIS 544
Cdd:cd22192     97 VVNQNLNLVRELIARGAdVVSPRAtgtffRPGPKnliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039763615  545 AREGQVDVA----SVLLEA---GAAHSLAT---KKGFTPLHVAAKYGSLDVAKLLLQRR 593
Cdd:cd22192    177 VLQPNKTFAcqmyDLILSYdkeDDLQPLDLvpnNQGLTPFKLAAKEGNIVMFQHLVQKR 235
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 211-426 2.74e-14

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: 79.29  E-value: 2.74e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  211 LHIAARKDDTKSAALLLQNDHnADVQSKS--GFTPLHIAAHYGNVNVATLLL-------NRGAAVDFTArnGITPLHVAS 281
Cdd:cd22192     21 LLLAAKENDVQAIKKLLKCPS-CDLFQRGalGETALHVAALYDNLEAAVVLMeaapelvNEPMTSDLYQ--GETALHIAV 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  282 KRGNTNMVKLLLDRGGQIDA---------KTRDGLT-----PLHCAARSGHDQVVELLLERKAPLLARTKNGLSPLHMAA 347
Cdd:cd22192     98 VNQNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILV 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  348 QGDHVECVKH----LLQYKAPVDDVTLDYLtalhvaahcghyrvtkllldkranPNARalnGFTPLHIACKKNRIKVMEL 423
Cdd:cd22192    178 LQPNKTFACQmydlILSYDKEDDLQPLDLV------------------------PNNQ---GLTPFKLAAKEGNIVMFQH 230


                   ...
gi 1039763615  424 LVK 426
Cdd:cd22192    231 LVQ 233
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 647-820 3.01e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 78.11  E-value: 3.01e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  647 NQMQIASTLLNYGAETNTVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHG- 725
Cdd:PHA02875    13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGk 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  726 -ADrDAYTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTA 804
Cdd:PHA02875    93 fAD-DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTP 171

                          170
                   ....*....|....*.
gi 1039763615  805 LAIAKRLGYISVVDTL 820
Cdd:PHA02875   172 LIIAMAKGDIAICKML 187
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 180-360 3.79e-14

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: 78.90  E-value: 3.79e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  180 TPLAVALQQGHNQAVAILLENDT-----KGKVRLPALHIAARKDDTKSAALLLQNDH---NADVQSK--SGFTPLHIAAH 249
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCPScdlfqRGALGETALHVAALYDNLEAAVVLMEAAPelvNEPMTSDlyQGETALHIAVV 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  250 YGNVNVATLLLNRGAAVdFTARN---------------GITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHC-- 312
Cdd:cd22192     99 NQNLNLVRELIARGADV-VSPRAtgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIlv 177

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  313 --AARSGHDQVVELLLERKAPL----LARTKN--GLSPLHMAAQGDHVECVKHLLQ 360
Cdd:cd22192    178 lqPNKTFACQMYDLILSYDKEDdlqpLDLVPNnqGLTPFKLAAKEGNIVMFQHLVQ 233
Ank_4 pfam13637
Ankyrin repeats (many copies);
438-491 1.97e-13

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 67.30  E-value: 1.97e-13
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039763615  438 GLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLL 491
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 15-469 5.51e-13

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 75.72  E-value: 5.51e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   15 ELDEKEKNL-DRERKKQRKIPRD--------RMERKRKSDSN--ASFLRAARAGNLD-KVVEYL--KGGIDIN-TCNQNG 79
Cdd:PHA02716    98 KLDRKNKSLvDQYKQFYKQIIKDnksktanhVFDIPNNGDMDilYTYFNSPNTRGIDlDLIKYMvdVGIVNLNyVCKKTG 177

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   80 LNALHlaakeghvglvqellgrgssvdsaTKKGNTALHIaslagqaEVVKVLVKEGANINAQSQNGFTPL--YMAAQENH 157
Cdd:PHA02716   178 YGILH------------------------AYLGNMYVDI-------DILEWLCNNGVNVNLQNNHLITPLhtYLITGNVC 226

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  158 IDVVKYLLENGANQSTATEDGFTPLAVALQQGHN---QAVAILLENDTKGKVR-LPA-LHI---AARKDDTKSAALLLQN 229
Cdd:PHA02716   227 ASVIKKIIELGGDMDMKCVNGMSPIMTYIINIDNinpEITNIYIESLDGNKVKnIPMiLHSyitLARNIDISVVYSFLQP 306

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  230 DHNADVQSKSGFTPLH--IAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRG--------------NTNMVKLLL 293
Cdd:PHA02716   307 GVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMLsvvnildpetdndiRLDVIQCLI 386

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  294 DRGGQIDAKTRDGLTPLH---CAARS--GHDqVVELLLERKapLLARTKNGLSPLHMAAQGDHVECVKHLL-QYKAPVDD 367
Cdd:PHA02716   387 SLGADITAVNCLGYTPLTsyiCTAQNymYYD-IIDCLISDK--VLNMVKHRILQDLLIRVDDTPCIIHHIIaKYNIPTDL 463

                          410       420       430       440       450       460       470       480
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  368 VTLDY----LTALHVAAHCGhyrvtkllLDKRANPNARALNGFTPLHIA-CKKNRIKVMELLVKY----GASIQAITESG 438
Cdd:PHA02716   464 YTDEYepydSTKIHDVYHCA--------IIERYNNAVCETSGMTPLHVSiISHTNANIVMDSFVYllsiQYNINIPTKNG 535

                          490       500       510
                   ....*....|....*....|....*....|....*.
gi 1039763615  439 LTPIHVA----AFMGH-LNIVLLLLQNgaSPDVTNI 469
Cdd:PHA02716   536 VTPLMLTmrnnRLSGHqWYIVKNILDK--RPNVDIV 569
PHA02798 PHA02798
ankyrin-like protein; Provisional
 579-798 6.35e-13

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 74.49  E-value: 6.35e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  579 KYGS-LDVAKLLLQRRAAADSAGKNGLTPLHVAAH---YDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKN---QMQI 651
Cdd:PHA02798    84 DYKHmLDIVKILIENGADINKKNSDGETPLYCLLSngyINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEI 163

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  652 ASTLLNYGAETNTVT-KQGVTPLHLASQEGHT----DMVTLLLDKGANIHMSTKSG-------LTSLHLAAQEDKVNVAD 719
Cdd:PHA02798   164 IKLLLEKGVDINTHNnKEKYDTLHCYFKYNIDridaDILKLFVDNGFIINKENKSHkkkfmeyLNSLLYDNKRFKKNILD 243

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039763615  720 ILTKHgADRDAYTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHgaKPNATT 798
Cdd:PHA02798   244 FIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNK--KPNKNT 319
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 571-821 9.24e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 74.15  E-value: 9.24e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  571 FTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDN-QKVALLLLEKGaspHATAKNGYTPLHIAAKKNQM 649
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNkLGMKEMIRSIN---KCSVFYTLVAIKDAFNNRNV 114

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  650 QIA-STLLNYGAETNTV-TKQGVTPLHLASQEghTDMVTLLLDKGANIHMSTK-SGLTSLHLAAqEDKvnvadiltkhga 726
Cdd:PHA02878   115 EIFkIILTNRYKNIQTIdLVYIDKKSKDDIIE--AEITKLLLSYGADINMKDRhKGNTALHYAT-ENK------------ 179

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  727 drdaytklgytplivachygNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALA 806
Cdd:PHA02878   180 --------------------DQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLH 239

                          250
                   ....*....|....*
gi 1039763615  807 IAkrLGYISVVDTLK 821
Cdd:PHA02878   240 IS--VGYCKDYDILK 252
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 298-546 3.23e-12

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: 72.81  E-value: 3.23e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  298 QIDAKTRDGLTPLHCAA-RSGHDQVVELLLERKAplLARTknGLSPLHMAAQGDHV---ECVKHLLQykAPVDDVTLDYL 373
Cdd:TIGR00870   44 NINCPDRLGRSALFVAAiENENLELTELLLNLSC--RGAV--GDTLLHAISLEYVDaveAILLHLLA--AFRKSGPLELA 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  374 ------------TALHVAAHCGHYRVTKLLLDKRANPNARALNGFtplhiaCKKnriKVMELLVKYGASiqaitesgltP 441
Cdd:TIGR00870  118 ndqytseftpgiTALHLAAHRQNYEIVKLLLERGASVPARACGDF------FVK---SQGVDSFYHGES----------P 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  442 IHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAA----RAGQVEVVRCLLRNGAL-VDARAREEQ----------- 505
Cdd:TIGR00870  179 LNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmeneFKAEYEELSCQMYNFALsLLDKLRDSKelevilnhqgl 258

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*...
gi 1039763615  506 TPLHIASRLGKTEIVQLLLQ-------HMAHPdaattngYTPLHISAR 546
Cdd:TIGR00870  259 TPLKLAAKEGRIVLFRLKLAikykqkkFVAWP-------NGQQLLSLY 299
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 332-525 3.32e-12

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 72.74  E-value: 3.32e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  332 LLARTKNGLSPLHMAAQGDHVECVKHLLQYKApVDDVTLDYL--TALHVAAHCGHYRVTKLLLDkranpNARAL------ 403
Cdd:cd22192     10 LLQQKRISESPLLLAAKENDVQAIKKLLKCPS-CDLFQRGALgeTALHVAALYDNLEAAVVLME-----AAPELvnepmt 83

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  404 ----NGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLT--------------PIHVAAFMGHLNIVLLLLQNGASPD 465
Cdd:cd22192     84 sdlyQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIR 163

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039763615  466 VTNIRGETALHMAARAGQVEVVrCLLRNGAL-VDARAREEQ----------TPLHIASRLGKTEIVQLLLQ 525
Cdd:cd22192    164 AQDSLGNTVLHILVLQPNKTFA-CQMYDLILsYDKEDDLQPldlvpnnqglTPFKLAAKEGNIVMFQHLVQ 233
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 655-792 4.98e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 72.59  E-value: 4.98e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  655 LLNYGAETNTVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADRDAYTkl 734
Cdd:PLN03192   544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA-- 621

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039763615  735 GYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGA 792
Cdd:PLN03192   622 AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 40-187 7.28e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 70.76  E-value: 7.28e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   40 RKRKSDSnasFLR-AARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHI 118
Cdd:PHA02874   120 KDAELKT---FLHyAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHN 196

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039763615  119 ASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHiDVVKYLLENGANQSTATeDGFTPLAVALQ 187
Cdd:PHA02874   197 AAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNASINDQDI-DGSTPLHHAIN 263
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 48-182 8.64e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.82  E-value: 8.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   48 ASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTAL----------- 116
Cdd:PLN03192   527 SNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhki 606

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  117 -----HIASLA---------------GQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTA-T 175
Cdd:PLN03192   607 frilyHFASISdphaagdllctaakrNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAnT 686


                   ....*..
gi 1039763615  176 EDGFTPL 182
Cdd:PLN03192   687 DDDFSPT 693
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 9-262 1.18e-11

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: 70.94  E-value: 1.18e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615    9 KKVREAELDEKEKNLDRERKKQRKiprDRMERKRKSDSNASFLRAARAGNLDKVVeYLKGGIDINTCNQNGLNALHLAAK 88
Cdd:cd22194     46 KKKRLKKVSEAAVEELGELLKELK---DLSRRRRKTDVPDFLMHKLTASDTGKTC-LMKALLNINENTKEIVRILLAFAE 121

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   89 EGhvGLVQELLGrgSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGF--------------TPLYMAAQ 154
Cdd:cd22194    122 EN--GILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFfnpkykhegfyfgeTPLALAAC 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  155 ENHIDVVKYLLENGANQstatedgftplaVALQqghnqavaillenDTKGKVRLPALHIAArkDDTKS----------AA 224
Cdd:cd22194    198 TNQPEIVQLLMEKESTD------------ITSQ-------------DSRGNTVLHALVTVA--EDSKTqndfvkrmydMI 250

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1039763615  225 LLLQNDHNAD-VQSKSGFTPLHIAAHYGNVNVATLLLNR 262
Cdd:cd22194    251 LLKSENKNLEtIRNNEGLTPLQLAAKMGKAEILKYILSR 289
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 94-293 1.21e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 70.29  E-value: 1.21e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   94 LVQELLGRGSSVDSATK-KGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQS 172
Cdd:PHA02878   149 ITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  173 TATEDGFTPLAVALQQGHNQAV-AILLEndtkgkvrlpalhiaarkddtksaalllqndHNADVQSKS---GFTPLHIAA 248
Cdd:PHA02878   229 ARDKCGNTPLHISVGYCKDYDIlKLLLE-------------------------------HGVDVNAKSyilGLTALHSSI 277

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1039763615  249 HygNVNVATLLLNRGAAVDFTARNGITPLHVASK-RGNTNMVKLLL 293
Cdd:PHA02878   278 K--SERKLKLLLEYGADINSLNSYKLTPLSSAVKqYLCINIGRILI 321
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 86-200 1.62e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 70.67  E-value: 1.62e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   86 AAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLY--------------- 150
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWnaisakhhkifrily 611

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  151 ----------------MAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILLEN 200
Cdd:PLN03192   612 hfasisdphaagdllcTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMN 677
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 83-329 1.70e-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: 70.43  E-value: 1.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   83 LHLAAKEGHVGLVQELLgRGSSVDSATKK--GNTALHIASLAGQAEVVKVL---VKEGANINAQSQ--NGFTPLYMAAQE 155
Cdd:cd22192     21 LLLAAKENDVQAIKKLL-KCPSCDLFQRGalGETALHVAALYDNLEAAVVLmeaAPELVNEPMTSDlyQGETALHIAVVN 99

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  156 NHIDVVKYLLENGANQSTATEDG--FTPlavalqqghnqavaillendtkgkvrlpalhiaaRKDdtksaALLLQNDHna 233
Cdd:cd22192    100 QNLNLVRELIARGADVVSPRATGtfFRP----------------------------------GPK-----NLIYYGEH-- 138

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  234 dvqsksgftPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHV----ASKRGNTNMVKLLLDRGGQIDAKT------ 303
Cdd:cd22192    139 ---------PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIlvlqPNKTFACQMYDLILSYDKEDDLQPldlvpn 209

                          250       260
                   ....*....|....*....|....*.
gi 1039763615  304 RDGLTPLHCAARSGHDQVVELLLERK 329
Cdd:cd22192    210 NQGLTPFKLAAKEGNIVMFQHLVQKR 235
PHA02798 PHA02798
ankyrin-like protein; Provisional
 582-808 1.70e-11

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 69.86  E-value: 1.70e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  582 SLDVAKLLLQRRAAADSAGKNGLTPL-----HVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKK---NQMQIAS 653
Cdd:PHA02798    50 STDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILL 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  654 TLLNYGAETNTVTKQGVTPLHLASQEGHT---DMVTLLLDKGANIHM-STKSGLTSLHLAAQED----KVNVADILTKHG 725
Cdd:PHA02798   130 FMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNidriDADILKLFVDNG 209

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  726 ---ADRDAYTKLGYTPLIVACHYGNVK----MVNFLLKQgANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATT 798
Cdd:PHA02798   210 fiiNKENKSHKKKFMEYLNSLLYDNKRfkknILDFIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIIT 288

                          250
                   ....*....|
gi 1039763615  799 ANGNTALAIA 808
Cdd:PHA02798   289 ELGNTCLFTA 298
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 58-198 1.79e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.48  E-value: 1.79e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   58 NLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIAsLAGQAEV--VKVLVKEG 135
Cdd:PHA02876   354 NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-LCGTNPYmsVKTLIDRG 432

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039763615  136 ANINAQSQNGFTPLYMAAQEN-HIDVVKYLLENGANQSTATEDGFTPLAVALqqGHNQAVAILL 198
Cdd:PHA02876   433 ANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILL 494
Ank_4 pfam13637
Ankyrin repeats (many copies);
275-326 4.64e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 4.64e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039763615  275 TPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLL 326
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 723-820 4.97e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.15  E-value: 4.97e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  723 KHGADRDAYTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGH--TH---IINVLLQHGAKPNAT 797
Cdd:PHA03100    23 MEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnlTDvkeIVKLLLEYGANVNAP 102

                           90       100
                   ....*....|....*....|....*
gi 1039763615  798 TANGNTALAIA--KRLGYISVVDTL 820
Cdd:PHA03100   103 DNNGITPLLYAisKKSNSYSIVEYL 127
Ank_4 pfam13637
Ankyrin repeats (many copies);
306-359 6.67e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 6.67e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039763615  306 GLTPLHCAARSGHDQVVELLLERKAPLLARTKNGLSPLHMAAQGDHVECVKHLL 359
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
407-458 9.76e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.60  E-value: 9.76e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039763615  407 TPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLL 458
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
112-165 1.12e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.60  E-value: 1.12e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039763615  112 GNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLL 165
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
735-788 1.16e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.21  E-value: 1.16e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039763615  735 GYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLL 788
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
 61-329 1.21e-10

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 67.17  E-value: 1.21e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   61 KVVEYLKGGIDIN-TCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTAL-----HIASLAGQAEVVKVLVKE 134
Cdd:PHA02798    19 STVKLLIKSCNPNeIVNEYSIFQKYLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIEN 98

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  135 GANINAQSQNGFTPLYMAAQE---NHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHN---QAVAILLE-----NDTK 203
Cdd:PHA02798    99 GADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEkgvdiNTHN 178

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  204 GKVRLPALHIAARKD----DTKSAALLLQND---HNADVQSKSGFTPLHIAAHYGNVNVATLLLNR-GAAVDFTARN--G 273
Cdd:PHA02798   179 NKEKYDTLHCYFKYNidriDADILKLFVDNGfiiNKENKSHKKKFMEYLNSLLYDNKRFKKNILDFiFSYIDINQVDelG 258

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  274 ITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERK 329
Cdd:PHA02798   259 FNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKK 314
Ank_4 pfam13637
Ankyrin repeats (many copies);
372-425 1.25e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.21  E-value: 1.25e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039763615  372 YLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLV 425
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 556-708 1.70e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.59  E-value: 1.70e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  556 LLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLL--LEKGASPHAta 633
Cdd:PLN03192   544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHA-- 621

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  634 knGYTPLHIAAKKNQMQIASTLLNYGAETNTVTKQGVTPLHLASQEGHTDMVTLLLDKGANI-HMSTKSGLTSLHL 708
Cdd:PLN03192   622 --AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVdKANTDDDFSPTEL 695
Ank_4 pfam13637
Ankyrin repeats (many copies);
339-392 2.11e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.83  E-value: 2.11e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039763615  339 GLSPLHMAAQGDHVECVKHLLQYKAPVDDVTLDYLTALHVAAHCGHYRVTKLLL 392
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 53-199 2.30e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.17  E-value: 2.30e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   53 AARAGNLDKVVEYLKGGIDIN-TCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVL 131
Cdd:PHA02875    75 AVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039763615  132 VKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDG-FTPLAVALQQGHNQAVAILLE 199
Cdd:PHA02875   155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIK 223
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 285-469 2.37e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.82  E-value: 2.37e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  285 NTNMVKLLLDRGGQIDAKTRDglTPLHCAARSGHDQVVELLLE-RKAPLLARTKnGLSPLHMAAQGDHVECVKHLLQYKA 363
Cdd:PLN03192   506 DLNVGDLLGDNGGEHDDPNMA--SNLLTVASTGNAALLEELLKaKLDPDIGDSK-GRTPLHIAASKGYEDCVLVLLKHAC 582

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  364 PVDDVTLDYLTALHVAAHCGHYRVTKLL--LDKRANPNAralnGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTP 441
Cdd:PLN03192   583 NVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658

                          170       180
                   ....*....|....*....|....*...
gi 1039763615  442 IHVAAFMGHLNIVLLLLQNGASPDVTNI 469
Cdd:PLN03192   659 LQVAMAEDHVDMVRLLIMNGADVDKANT 686
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 69-199 2.52e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.06  E-value: 2.52e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   69 GIDINTCNQNGLN-ALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFT 147
Cdd:PHA02878   157 GADINMKDRHKGNtALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039763615  148 PLYMAAQE-NHIDVVKYLLENGAN-QSTATEDGFTPLAVALQQghNQAVAILLE 199
Cdd:PHA02878   237 PLHISVGYcKDYDILKLLLEHGVDvNAKSYILGLTALHSSIKS--ERKLKLLLE 288
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 468-592 3.76e-10

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: 66.32  E-value: 3.76e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  468 NIRGETALHMAARAGQVEVVRCLLRNGALVDARA---------REE-----QTPLHIASRLGKTEIVQLLLQHMAHPDAA 533
Cdd:cd22194    138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkyKHEgfyfgETPLALAACTNQPEIVQLLMEKESTDITS 217

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039763615  534 T-TNGYTPLH---ISAREGQVDVASV------LLEAGAAHSLAT---KKGFTPLHVAAKYGSLDVAKLLLQR 592
Cdd:cd22194    218 QdSRGNTVLHalvTVAEDSKTQNDFVkrmydmILLKSENKNLETirnNEGLTPLQLAAKMGKAEILKYILSR 289
Ank_4 pfam13637
Ankyrin repeats (many copies);
603-656 7.84e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.90  E-value: 7.84e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039763615  603 GLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLL 656
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 421-574 1.00e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.89  E-value: 1.00e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  421 MELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDAR 500
Cdd:PLN03192   541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH 620

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039763615  501 AREEQtpLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLA-TKKGFTPL 574
Cdd:PLN03192   621 AAGDL--LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAnTDDDFSPT 693
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 394-593 2.05e-09

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 63.95  E-value: 2.05e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  394 KRANPNARALN-------GFTPLHIACKKNRIK-VMELLVKYGASIqaitESGLTPIHVAAFMGHLN---IVLLLLQNGA 462
Cdd:TIGR00870   34 YRDLEEPKKLNincpdrlGRSALFVAAIENENLeLTELLLNLSCRG----AVGDTLLHAISLEYVDAveaILLHLLAAFR 109

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  463 SPDVTNI----------RGETALHMAARAGQVEVVRCLLRNGALVDARA--------------REEQTPLHIASRLGKTE 518
Cdd:TIGR00870  110 KSGPLELandqytseftPGITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvdsfYHGESPLNAAACLGSPS 189

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  519 IVQLLLQHMAHPDAATTNGYTPLHISAREG-----------QVDVASVLLEAGAAHSLATK-----KGFTPLHVAAKYGS 582
Cdd:TIGR00870  190 IVALLSEDPADILTADSLGNTLLHLLVMENefkaeyeelscQMYNFALSLLDKLRDSKELEvilnhQGLTPLKLAAKEGR 269

                          250
                   ....*....|.
gi 1039763615  583 LDVAKLLLQRR 593
Cdd:TIGR00870  270 IVLFRLKLAIK 280
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 445-599 2.12e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 63.73  E-value: 2.12e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  445 AAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQlLL 524
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR-IL 610

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039763615  525 QHMAHPDAATTNGyTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSA 599
Cdd:PLN03192   611 YHFASISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKA 684
Ank_4 pfam13637
Ankyrin repeats (many copies);
636-689 2.30e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 2.30e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039763615  636 GYTPLHIAAKKNQMQIASTLLNYGAETNTVTKQGVTPLHLASQEGHTDMVTLLL 689
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 671-807 2.43e-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: 63.49  E-value: 2.43e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  671 TPLHLASQEGHTDMV-TLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKhgADR---------DAYtkLGYTPLI 740
Cdd:cd22192     19 SPLLLAAKENDVQAIkKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPelvnepmtsDLY--QGETALH 94

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  741 VACHYGNVKMVNFLLKQGANVNAKTKNGYT--------------PLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALA 806
Cdd:cd22192     95 IAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174


                   .
gi 1039763615  807 I 807
Cdd:cd22192    175 I 175
PHA02946 PHA02946
ankyin-like protein; Provisional
 574-788 2.49e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 62.76  E-value: 2.49e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  574 LHVAAKYGS--LDVAKLLLQrraAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQI 651
Cdd:PHA02946    11 LSLYAKYNSknLDVFRNMLQ---AIEPSGNYHILHAYCGIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRI 87

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  652 ASTLLNYGAETNTVTKQGVTPLHLAS--QEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADRD 729
Cdd:PHA02946    88 VAMLLTHGADPNACDKQHKTPLYYLSgtDDEVIERINLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEAR 167

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039763615  730 AYTKLGYTPLIVACHYGNVK--MVNFLLKQGANVNAKTKNGYTPLHQAAQQ--GHTHIINVLL 788
Cdd:PHA02946   168 IVDKFGKNHIHRHLMSDNPKasTISWMMKLGISPSKPDHDGNTPLHIVCSKtvKNVDIINLLL 230
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 456-537 3.09e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.99  E-value: 3.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  456 LLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATT 535
Cdd:PTZ00322   100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGA 179


                   ..
gi 1039763615  536 NG 537
Cdd:PTZ00322   180 NA 181
Ank_4 pfam13637
Ankyrin repeats (many copies);
207-260 3.18e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 3.18e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039763615  207 RLPALHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHYGNVNVATLLL 260
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
242-293 4.34e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 4.34e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039763615  242 TPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLL 293
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 45-175 4.86e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.93  E-value: 4.86e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   45 DSNASFLRAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQ 124
Cdd:PHA02875   101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039763615  125 AEVVKVLVKEGANINAQSQNG-FTPLYMAAQENHIDVVKYLLENGANQSTAT 175
Cdd:PHA02875   181 IAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 515-603 4.94e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.61  E-value: 4.94e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  515 GKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRA 594
Cdd:PTZ00322    93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172


                   ....*....
gi 1039763615  595 AADSAGKNG 603
Cdd:PTZ00322   173 CHFELGANA 181
PHA02946 PHA02946
ankyin-like protein; Provisional
 507-755 5.73e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 61.61  E-value: 5.73e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  507 PLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPL-HISAREGQV-DVASVLLEAGAA-HSLATKKGFTPLhVAAKYGSL 583
Cdd:PHA02946    75 PLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLyYLSGTDDEViERINLLVQYGAKiNNSVDEEGCGPL-LACTDPSE 153

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  584 DVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALL--LLEKGASPHATAKNGYTPLHIAAKKNQMQI-ASTLLNYGA 660
Cdd:PHA02946   154 RVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKASTIswMMKLGISPSKPDHDGNTPLHIVCSKTVKNVdIINLLLPST 233

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  661 ETNTVTKQGVTPLHLASQeghtdmvTLLLDKGANIHMSTKSGLT--SLHLAAQEDKVNVADILTKHGADRDAytklgyTP 738
Cdd:PHA02946   234 DVNKQNKFGDSPLTLLIK-------TLSPAHLINKLLSTSNVITdqTVNICIFYDRDDVLEIINDKGKQYDS------TD 300

                          250
                   ....*....|....*..
gi 1039763615  739 LIVACHYGNVKMVNFLL 755
Cdd:PHA02946   301 FKMAVEVGSIRCVKYLL 317
Ank_4 pfam13637
Ankyrin repeats (many copies);
79-132 6.88e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 6.88e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039763615   79 GLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLV 132
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
258-313 9.07e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 54.27  E-value: 9.07e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  258 LLLNRGAAVDFTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCA 313
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 436-592 9.30e-09

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 61.43  E-value: 9.30e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  436 ESGLTPIHVAAF---MGHLNIVLLLLQngASPDVTNIR-------------GETALHMAARAGQVEVVRCLLRNGALVDA 499
Cdd:cd21882     24 ATGKTCLHKAALnlnDGVNEAIMLLLE--AAPDSGNPKelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSA 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  500 RA-----REEQT--------PLHIASRLGKTEIVQLLLQHMAHPDAATTN---GYTPLHI------SAREGQVDVASV-- 555
Cdd:cd21882    102 RAtgrffRKSPGnlfyfgelPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHAlvlqadNTPENSAFVCQMyn 181

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1039763615  556 -LLEAGAA-------HSLATKKGFTPLHVAAKYGSLDVAKLLLQR 592
Cdd:cd21882    182 lLLSYGAHldptqqlEEIPNHQGLTPLKLAAVEGKIVMFQHILQR 226
Ank_4 pfam13637
Ankyrin repeats (many copies);
506-557 1.13e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 1.13e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039763615  506 TPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASVLL 557
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 140-362 1.28e-08

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 61.25  E-value: 1.28e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  140 AQSQNGFTPlymAAQENHIDVVKYLLENGA--NQSTATEDGFTPLAVALQQGHNQAVAILLEN-DTKGKVRLPALHIAAR 216
Cdd:TIGR00870   15 SDEEKAFLP---AAERGDLASVYRDLEEPKklNINCPDRLGRSALFVAAIENENLELTELLLNlSCRGAVGDTLLHAISL 91

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  217 --------------KDDTKSAALLLQNDHNADVQSKsGFTPLHIAAHYGNVNVATLLLNRGAAVDFTA------------ 270
Cdd:TIGR00870   92 eyvdaveaillhllAAFRKSGPLELANDQYTSEFTP-GITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvd 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  271 --RNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCA-------------ARSGHDQVVElLLERKAPL--- 332
Cdd:TIGR00870  171 sfYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLvmenefkaeyeelSCQMYNFALS-LLDKLRDSkel 249

                          250       260       270
                   ....*....|....*....|....*....|.
gi 1039763615  333 -LARTKNGLSPLHMAAQGDHVECVKHLLQYK 362
Cdd:TIGR00870  250 eVILNHQGLTPLKLAAKEGRIVLFRLKLAIK 280
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 79-189 1.66e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 60.80  E-value: 1.66e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   79 GLNALHLAAKEGHVGLVQELLGRGSSVDS--AT----KKGNTAL-----HIASLA---GQAEVVKVLVKEGANINAQSQN 144
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVVSprATgtffRPGPKNLiyygeHPLSFAacvGNEEIVRLLIEHGADIRAQDSL 168

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039763615  145 GFTPLYM-AAQENH------IDVVKYLLENGANQSTAT---EDGFTPLAVALQQG 189
Cdd:cd22192    169 GNTVLHIlVLQPNKtfacqmYDLILSYDKEDDLQPLDLvpnNQGLTPFKLAAKEG 223
Ank_5 pfam13857
Ankyrin repeats (many copies);
390-445 1.97e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.12  E-value: 1.97e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  390 LLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVA 445
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 470-592 2.15e-08

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: 60.59  E-value: 2.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  470 RGETALHMAARAGQVEVVRCLLRNGALVDARAREE--------------QTPLHIASRLGKTEIVQLLLQHMAHP---DA 532
Cdd:cd22196     93 KGQTALHIAIERRNMHLVELLVQNGADVHARASGEffkkkkggpgfyfgELPLSLAACTNQLDIVKFLLENPHSPadiSA 172

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  533 ATTNGYTPLHI---SAREGQVDVASV------LLEAGAA-------HSLATKKGFTPLHVAAKYGSLDVAKLLLQR 592
Cdd:cd22196    173 RDSMGNTVLHAlveVADNTPENTKFVtkmyneILILGAKirpllklEEITNKKGLTPLKLAAKTGKIGIFAYILGR 248
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 514-700 2.68e-08

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 59.89  E-value: 2.68e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  514 LGKTEIVQLLLQHMAHPDAATtnGYTPLHISA---REGQVDVASVLLEA----GAAHSLATK-------KGFTPLHVAAK 579
Cdd:cd21882      5 LGLLECLRWYLTDSAYQRGAT--GKTCLHKAAlnlNDGVNEAIMLLLEAapdsGNPKELVNApctdefyQGQTALHIAIE 82

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  580 YGSLDVAKLLLQRRAAADSAGKN-------------GLTPLHVAAHYDNQKVALLLLEKGASPHATAKN---GYTPLHI- 642
Cdd:cd21882     83 NRNLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHAl 162

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  643 --------AAKKNQMQIASTLLNYGAETNTVTK-------QGVTPLHLASQEGHTDMVTLLLDK---GANIHMSTK 700
Cdd:cd21882    163 vlqadntpENSAFVCQMYNLLLSYGAHLDPTQQleeipnhQGLTPLKLAAVEGKIVMFQHILQRefsGPYQPLSRK 238
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 374-544 2.84e-08

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 59.89  E-value: 2.84e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  374 TALHVAA---HCGHYRVTKLLLD---KRANP----NARALN----GFTPLHIACKKNRIKVMELLVKYGASIQAITES-- 437
Cdd:cd21882     28 TCLHKAAlnlNDGVNEAIMLLLEaapDSGNPkelvNAPCTDefyqGQTALHIAIENRNLNLVRLLVENGADVSARATGrf 107

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  438 -----------GLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIR---GETALH----MAARAGQVEVVRCLLRNGALV-D 498
Cdd:cd21882    108 frkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHalvlQADNTPENSAFVCQMYNLLLSyG 187

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039763615  499 ARAREEQ-----------TPLHIASRLGKTEIVQLLLQHMAHPDAA------TTNGYTPLHIS 544
Cdd:cd21882    188 AHLDPTQqleeipnhqglTPLKLAAVEGKIVMFQHILQREFSGPYQplsrkfTEWTYGPVTSS 250
Ank_5 pfam13857
Ankyrin repeats (many copies);
556-610 3.06e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.73  E-value: 3.06e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  556 LLEAG-AAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVA 610
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
720-775 5.34e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.96  E-value: 5.34e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  720 ILTKHGADRDAYTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQA 775
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 476-564 5.97e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.14  E-value: 5.97e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  476 HMAArAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHISAREGQVDVASV 555
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                   ....*....
gi 1039763615  556 LLEAGAAHS 564
Cdd:PTZ00322   167 LSRHSQCHF 175
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 6-282 6.15e-08

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 58.94  E-value: 6.15e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615    6 ASIKKVREAELDEKEKNLDRERKKQRKIPrDRMERkrksdsNASFLRAARAGNLD--KVVEYLKGGIDIntcnqnGLNAL 83
Cdd:TIGR00870   20 AFLPAAERGDLASVYRDLEEPKKLNINCP-DRLGR------SALFVAAIENENLEltELLLNLSCRGAV------GDTLL 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   84 HLAAKEGHVGlVQELL--------GRGSS---VDSATK---KGNTALHIASLAGQAEVVKVLVKEGANINA--------- 140
Cdd:TIGR00870   87 HAISLEYVDA-VEAILlhllaafrKSGPLelaNDQYTSeftPGITALHLAAHRQNYEIVKLLLERGASVPAracgdffvk 165

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  141 -QSQNGF----TPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAvaillENDTKG-KVRLPALHIA 214
Cdd:TIGR00870  166 sQGVDSFyhgeSPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEFKA-----EYEELScQMYNFALSLL 240

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  215 ARKDDTKSAALLLQNDhnadvqsksGFTPLHIAAHYGNVNVATLLLNRGAAV-DFTA-RNGitPLHVASK 282
Cdd:TIGR00870  241 DKLRDSKELEVILNHQ---------GLTPLKLAAKEGRIVLFRLKLAIKYKQkKFVAwPNG--QQLLSLY 299
PHA02791 PHA02791
ankyrin-like protein; Provisional
 233-431 7.21e-08

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 56.97  E-value: 7.21e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  233 ADVQsksGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNgiTPLHVASKRGNTNMVKLLLDRG---GQIDAKtrdGLTP 309
Cdd:PHA02791    26 ADVH---GHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGmddSQFDDK---GNTA 97

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  310 LHCAARSGHDQVVELLLERKAPLLARTKNGL-SPLHMAAQGDHVECVKHLLQYKAPVDDVTLdYLTALHVAAHCGHYRVT 388
Cdd:PHA02791    98 LYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLSEIPSTFDLAI-LLSCIHITIKNGHVDMM 176

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1039763615  389 KLLLDKRANPNARALNGFTP-LHIACKKNRIKVMELLVKYGASI 431
Cdd:PHA02791   177 ILLLDYMTSTNTNNSLLFIPdIKLAIDNKDLEMLQALFKYDINI 220
Ank_5 pfam13857
Ankyrin repeats (many copies);
423-478 7.38e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.58  E-value: 7.38e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  423 LLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMA 478
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
754-808 7.82e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.58  E-value: 7.82e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  754 LLKQG-ANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIA 808
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
473-524 8.44e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 8.44e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039763615  473 TALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLL 524
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Death_FADD cd08306
Fas-associated Death Domain protein-protein interaction domain; Death domain (DD) found in ...
 3588-3664 8.62e-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: 52.30  E-value: 8.62e-08
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039763615 3588 IADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTILIECLTKINRMDIVHLLETN 3664
Cdd:cd08306      8 ICENLGRDWRQLARKLGLSETKIESISEAHPRNLREQVRQSLREWKKIKKAEATVADLIKALRDCQLNLVADLVEKK 84
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 3194-3521 1.07e-07

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 58.64  E-value: 1.07e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3194 EGELLPDDVSEEIEDLPASDANIDSQVIISASTETPTKEAVSTAVEEPPT---TQRSDSLSTVKQTPRPAVPGPvgqldf 3270
Cdd:PHA03307    28 PGDAADDLLSGSQGQLVSDSAELAAVTVVAGAAACDRFEPPTGPPPGPGTeapANESRSTPTWSLSTLAPASPA------ 101

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3271 spvtRSVYSGQDDESPESSPEEQKSVIEIPTAPVDNVPSAESKPQIPIRTLPTLVPAPPSAEDE------SAFSDDFPSS 3344
Cdd:PHA03307   102 ----REGSPTPPGPSSPDPPPPTPPPASPPPSPAPDLSEMLRPVGSPGPPPAASPPAAGASPAAvasdaaSSRQAALPLS 177

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3345 LDEDSKEGGAKPKSKIPVKAPTQRTEWQPSPTDIPLQKTAVPQGQETLSRAPDGRSKSESDASSLDAK-------TKCPV 3417
Cdd:PHA03307   178 SPEETARAPSSPPAEPPPSTPPAAASPRPPRRSSPISASASSPAPAPGRSAADDAGASSSDSSSSESSgcgwgpeNECPL 257

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3418 KARSYIETETESRERAEGFESESEDGATKPKL-FASRLPVKSRSTSSSGrPGTSPTRESREhffdlyrnsieffEEISDE 3496
Cdd:PHA03307   258 PRPAPITLPTRIWEASGWNGPSSRPGPASSSSsPRERSPSPSPSSPGSG-PAPSSPRASSS-------------SSSSRE 323

                          330       340
                   ....*....|....*....|....*
gi 1039763615 3497 ASklvdrlTQSEREQEPPSDDESSS 3521
Cdd:PHA03307   324 SS------SSSTSSSSESSRGAAVS 342
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 448-640 1.27e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.96  E-value: 1.27e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  448 MGHLNIVLLLLQNGASPDVTNIrgETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHM 527
Cdd:PLN03192   504 LHDLNVGDLLGDNGGEHDDPNM--ASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  528 AHPDAATTNGYTPLHISAREGQVDVASVLLEAGAAHSLATkkGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPL 607
Cdd:PLN03192   582 CNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATAL 659

                          170       180       190
                   ....*....|....*....|....*....|....
gi 1039763615  608 HVAAHYDNQKVALLLLEKGAS-PHATAKNGYTPL 640
Cdd:PLN03192   660 QVAMAEDHVDMVRLLIMNGADvDKANTDDDFSPT 693
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 192-326 1.42e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 1.42e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  192 QAVAILLENDTKGKVRLPALHIAARKDDTKSAALLLQNDHNADVQSKSGFTPLHIAAHyGNVNVATLLLNRGAAVDFTAR 271
Cdd:PTZ00322    35 ERMAAIQEEIARIDTHLEALEATENKDATPDHNLTTEEVIDPVVAHMLTVELCQLAAS-GDAVGARILLTGGADPNCRDY 113

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039763615  272 NGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLL 326
Cdd:PTZ00322   114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
655-709 1.49e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.81  E-value: 1.49e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  655 LLNYG-AETNTVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLA 709
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 572-689 1.55e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.60  E-value: 1.55e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  572 TPLHVAAKYGSLD--VAKLL----LQRRAAADSAGkngltplhvaahydnqkvALLLLEKGASPHATAKNGYTPLHIAAK 645
Cdd:PTZ00322    63 TPDHNLTTEEVIDpvVAHMLtvelCQLAASGDAVG------------------ARILLTGGADPNCRDYDGRTPLHIACA 124

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1039763615  646 KNQMQIASTLLNYGAETNTVTKQGVTPLHLASQEGHTDMVTLLL 689
Cdd:PTZ00322   125 NGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 570-739 1.63e-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: 57.58  E-value: 1.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  570 GFTPLHVAAKY---GSLDVAKLLLQRRAAADSAGK-----------NGLTPLHVAAHYDNQKVALLLLEKGASPHATAKN 635
Cdd:cd21882     26 GKTCLHKAALNlndGVNEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSARATG 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  636 -------------GYTPLHIAAKKNQMQIASTLLNYGAETNTVTKQ---GVTPLH-LASQEGHT--------DMVTLLLD 690
Cdd:cd21882    106 rffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHaLVLQADNTpensafvcQMYNLLLS 185

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039763615  691 KGANIH-------MSTKSGLTSLHLAAQEDKVNV-ADILTK--HGADRDA---YTKLGYTPL 739
Cdd:cd21882    186 YGAHLDptqqleeIPNHQGLTPLKLAAVEGKIVMfQHILQRefSGPYQPLsrkFTEWTYGPV 247
Ank_5 pfam13857
Ankyrin repeats (many copies);
457-511 1.83e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 1.83e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  457 LLQNG-ASPDVTNIRGETALHMAARAGQVEVVRCLLRNGALVDARAREEQTPLHIA 511
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 632-788 2.17e-07

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: 57.08  E-value: 2.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  632 TAKN--GYTPLHIAAKKNQMQIASTLLNYGAETNTVTKQ--------------GVTPLHLASQEGHTDMVTLLLDKGANI 695
Cdd:cd22194    135 TEEAyeGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTD 214

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  696 HMSTKS-GLTSLHLAaqedkVNVADILTKHgadrDAYTKLGYTPLIVACHYGNVKMVnfllkqganvnaKTKNGYTPLHQ 774
Cdd:cd22194    215 ITSQDSrGNTVLHAL-----VTVAEDSKTQ----NDFVKRMYDMILLKSENKNLETI------------RNNEGLTPLQL 273

                          170
                   ....*....|....
gi 1039763615  775 AAQQGHTHIINVLL 788
Cdd:cd22194    274 AAKMGKAEILKYIL 287
Ank_4 pfam13637
Ankyrin repeats (many copies);
147-198 2.71e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 2.71e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039763615  147 TPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILL 198
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 670-801 2.83e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 2.83e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  670 VTPLHLASQEGHTDMVTLlldkganiHMSTksgLTSLHLAAQEDKVNvADILTKHGADRDAYTKLGYTPLIVACHYGNVK 749
Cdd:PTZ00322    62 ATPDHNLTTEEVIDPVVA--------HMLT---VELCQLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQ 129

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039763615  750 MVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANG 801
Cdd:PTZ00322   130 VVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANA 181
Death_p75NR cd08311
Death domain of p75 Neurotrophin Receptor; Death Domain (DD) found in p75 neurotrophin ...
 3574-3662 2.86e-07

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: 50.75  E-value: 2.86e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3574 PQDEQERMEERLAyiADHLGFSWTELARELDFTEEQIHQIrienpNSLQDQSHALLKYWLERDGkhATDTILIECLTKIN 3653
Cdd:cd08311      1 PPHKQEEVEKLLN--AGREGSDWRALAGELGYSAEEIDSF-----AREADPCRALLTDWSAQDG--ATLGVLLTALRKIG 71


                   ....*....
gi 1039763615 3654 RMDIVHLLE 3662
Cdd:cd08311     72 RDDIVEILQ 80
Ank_4 pfam13637
Ankyrin repeats (many copies);
768-820 2.93e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 2.93e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039763615  768 GYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTL 820
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 40-262 3.30e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.56  E-value: 3.30e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   40 RKRKSDSnaSFLRAARAGNLDKVVEYLK-GGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSS-----VDSATKKGN 113
Cdd:cd22192     13 QKRISES--PLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGE 90

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  114 TALHIASLAGQAEVVKVLVKEGANINAQSQNG--FT------------PLYMAAQENHIDVVKYLLENGANQSTATEDGF 179
Cdd:cd22192     91 TALHIAVVNQNLNLVRELIARGADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  180 TPLAV-ALQQGHN---QAVAILLENDTKGkvRLPALhiaarkddtksaalllqnDHnadVQSKSGFTPLHIAAHYGNVNV 255
Cdd:cd22192    171 TVLHIlVLQPNKTfacQMYDLILSYDKED--DLQPL------------------DL---VPNNQGLTPFKLAAKEGNIVM 227


                   ....*..
gi 1039763615  256 ATLLLNR 262
Cdd:cd22192    228 FQHLVQK 234
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 652-724 3.38e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 3.38e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039763615  652 ASTLLNYGAETNTVTKQGVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADILTKH 724
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
572-623 4.78e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 4.78e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039763615  572 TPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLL 623
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 111-295 4.87e-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: 56.02  E-value: 4.87e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  111 KGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGF-------------TPLYMAAQENHIDVVKYLLENGANQstated 177
Cdd:cd22197     93 RGHSALHIAIEKRSLQCVKLLVENGADVHARACGRFfqkkqgtcfyfgeLPLSLAACTKQWDVVNYLLENPHQP------ 166

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  178 gftplavalqqghnqavAILLENDTKGKVRLPALHIAArkDDTKSAALLLQNDHNADVQSKSGFTPlhiaahygnvnvaT 257
Cdd:cd22197    167 -----------------ASLQAQDSLGNTVLHALVMIA--DNSPENSALVIKMYDGLLQAGARLCP-------------T 214

                          170       180       190
                   ....*....|....*....|....*....|....*...
gi 1039763615  258 LLLNrgaavDFTARNGITPLHVASKRGNTNMVKLLLDR 295
Cdd:cd22197    215 VQLE-----EISNHEGLTPLKLAAKEGKIEIFRHILQR 247
Ank_4 pfam13637
Ankyrin repeats (many copies);
669-721 4.97e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 4.97e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039763615  669 GVTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDKVNVADIL 721
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 188-409 5.16e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 5.16e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  188 QGHNQAVAILLENDTKGKVRLPALHIAARKDDtksaalllQNDHNADVQSKSGftpLHIAAHYGNVNVATLLLNRGAAVD 267
Cdd:PLN03192   484 QTRQEDNVVILKNFLQHHKELHDLNVGDLLGD--------NGGEHDDPNMASN---LLTVASTGNAALLEELLKAKLDPD 552

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  268 FTARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLErkaplLARTKN---GLSPLH 344
Cdd:PLN03192   553 IGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYH-----FASISDphaAGDLLC 627

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  345 MAAQGDHVECVKHLLQYKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARAL-NGFTPL 409
Cdd:PLN03192   628 TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTdDDFSPT 693
Ank_5 pfam13857
Ankyrin repeats (many copies);
68-119 5.66e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 5.66e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039763615   68 GGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIA 119
Cdd:pfam13857    5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 389-458 5.82e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 5.82e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  389 KLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLL 458
Cdd:PTZ00322    99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
226-280 6.18e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 6.18e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  226 LLQNDH-NADVQSKSGFTPLHIAAHYGNVNVATLLLNRGAAVDFTARNGITPLHVA 280
Cdd:pfam13857    1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02946 PHA02946
ankyin-like protein; Provisional
 94-359 8.54e-07

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 54.67  E-value: 8.54e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   94 LVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYM--AAQENHIDVVKYLLENGAN- 170
Cdd:PHA02946    54 FVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKi 133

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  171 QSTATEDGFTPLAVAL---QQGHNQAVAILLENDTKGKVRLPALHIAARKDDTKSAAL--LLQNDHNADVQSKSGFTPLH 245
Cdd:PHA02946   134 NNSVDEEGCGPLLACTdpsERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKASTIswMMKLGISPSKPDHDGNTPLH 213

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  246 I--AAHYGNVNVATLLLnrgAAVDFTARN--GITPLHVASKR-GNTNMVKLLLDRGGQIDAKTrdgltpLHCAARSGHDQ 320
Cdd:PHA02946   214 IvcSKTVKNVDIINLLL---PSTDVNKQNkfGDSPLTLLIKTlSPAHLINKLLSTSNVITDQT------VNICIFYDRDD 284

                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1039763615  321 VVELLLERKapllarTKNGLSPLHMAAQGDHVECVKHLL 359
Cdd:PHA02946   285 VLEIINDKG------KQYDSTDFKMAVEVGSIRCVKYLL 317
Ank_5 pfam13857
Ankyrin repeats (many copies);
622-676 8.80e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 8.80e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  622 LLEKG-ASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAETNTVTKQGVTPLHLA 676
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 617-818 9.14e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 54.75  E-value: 9.14e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  617 KVALLLLEKGASphaTAKNGY--TPL-------HIAAKKNQmQIASTLLNYGAETNTVTKQGVTPLH---LASQEGHTDM 684
Cdd:PHA02989    51 KIVKLLIDNGAD---VNYKGYieTPLcavlrnrEITSNKIK-KIVKLLLKFGADINLKTFNGVSPIVcfiYNSNINNCDM 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  685 VTLLLDKGANIH-MSTKSGLTSLHLAAQEDKVN--VADILTKHGADRDAYTKL-GYTPLIVACHYG----NVKMVNFLLK 756
Cdd:PHA02989   127 LRFLLSKGINVNdVKNSRGYNLLHMYLESFSVKkdVIKILLSFGVNLFEKTSLyGLTPMNIYLRNDidviSIKVIKYLIK 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  757 QGAN--------------------------------------VNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATT 798
Cdd:PHA02989   207 KGVNietnnngsesvlesfldnnkilskkefkvlnfilkyikINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVS 286

                          250       260
                   ....*....|....*....|
gi 1039763615  799 ANGNTALAIAKRLGYISVVD 818
Cdd:PHA02989   287 KDGDTVLTYAIKHGNIDMLN 306
Ank_4 pfam13637
Ankyrin repeats (many copies);
537-590 1.26e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 1.26e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039763615  537 GYTPLHISAREGQVDVASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLL 590
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 423-531 1.30e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 1.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  423 LLVKYGASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNGAL---VDA 499
Cdd:PTZ00322   100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQChfeLGA 179

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1039763615  500 RAREEqtplhiaSRLGKTEIVQLLLQHMAHPD 531
Cdd:PTZ00322   180 NAKPD-------SFTGKPPSLEDSPISSHHPD 204
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 111-262 1.30e-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: 1.30e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  111 KGNTALHIASLAGQAEVVKVLVKEGANINA----------QSQNGF----TPLYMAAQENHIDVVKYLLEN---GANQST 173
Cdd:cd22196     93 KGQTALHIAIERRNMHLVELLVQNGADVHArasgeffkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLENphsPADISA 172

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  174 ATEDGFTPL----AVALQQGHNQAVAILLEND--TKGKVRLPALHIAArkddtksaalllqndhnadVQSKSGFTPLHIA 247
Cdd:cd22196    173 RDSMGNTVLhalvEVADNTPENTKFVTKMYNEilILGAKIRPLLKLEE-------------------ITNKKGLTPLKLA 233

                          170
                   ....*....|....*
gi 1039763615  248 AHYGNVNVATLLLNR 262
Cdd:cd22196    234 AKTGKIGIFAYILGR 248
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 673-809 1.36e-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: 1.36e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  673 LHLASQEGHTDMVTLLLDKGANIHMstksGLTSLHLAAQEDKVNVADILT---KHGADRDAYTKL----------GYTPL 739
Cdd:TIGR00870   57 FVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLEYVDAVEAILLhllAAFRKSGPLELAndqytseftpGITAL 132

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  740 IVACHYGNVKMVNFLLKQGANVNAKTK--------------NGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTAL 805
Cdd:TIGR00870  133 HLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLL 212


                   ....
gi 1039763615  806 AIAK 809
Cdd:TIGR00870  213 HLLV 216
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 751-820 1.36e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 1.36e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  751 VNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATTANGNTALAIAKRLGYISVVDTL 820
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Death_RAIDD cd08319
Death domain of RIP-associated ICH-1 homologous protein with a death domain; Death domain (DD) ...
 3582-3653 1.43e-06

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


Pssm-ID: 260031  Cd Length: 83  Bit Score: 48.86  E-value: 1.43e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039763615 3582 EERLAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTILIECLTKIN 3653
Cdd:cd08319      2 DRQLNKLAQRLGPEWEQVLLDLGLSKADIYRCKADHPYNVQSQIVEALVKWKQRQGKKATVQSLIQSLKAVE 73
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 84-165 1.56e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 1.56e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   84 HLAAKEGHVGlVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKY 163
Cdd:PTZ00322    88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                   ..
gi 1039763615  164 LL 165
Cdd:PTZ00322   167 LS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
292-346 1.87e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.73  E-value: 1.87e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  292 LLDRGGQ-IDAKTRDGLTPLHCAARSGHDQVVELLLERKAPLLARTKNGLSPLHMA 346
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Death_DRs cd08784
Death Domain of Death Receptors; Death domain (DD) found in death receptor proteins. Death ...
 3595-3662 1.90e-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: 48.34  E-value: 1.90e-06
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039763615 3595 SWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLERDGKHATDTILIECLtkiNRMDIVHLLE 3662
Cdd:cd08784     13 QWKGFVRKLGLNEAEIDEIKNDNVQDTAEAKYQMLRNWHQLTGRKAAYDTLIKDL---KKMNLCTLAE 77
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 735-766 1.94e-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: 46.90  E-value: 1.94e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1039763615  735 GYTPLIVAC-HYGNVKMVNFLLKQGANVNAKTK 766
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 120-198 1.96e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 1.96e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039763615  120 SLAGQAEVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQGHNQAVAILL 198
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 537-714 2.00e-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: 53.93  E-value: 2.00e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  537 GYTPLHISAREGQV-DVASVLLEagaaHSLATKKGFTPLHVAAKyGSLDVAKLLLQRRAAADSAGKN------------- 602
Cdd:TIGR00870   52 GRSALFVAAIENENlELTELLLN----LSCRGAVGDTLLHAISL-EYVDAVEAILLHLLAAFRKSGPlelandqytseft 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  603 -GLTPLHVAAHYDNQKVALLLLEKGASPHATAK--------------NGYTPLHIAAKKNQMQIASTLLNYGAETNTVTK 667
Cdd:TIGR00870  127 pGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039763615  668 QGVTPLHLASQEGH---------TDMVTLLLDKGANIHMSTK-------SGLTSLHLAAQEDK 714
Cdd:TIGR00870  207 LGNTLLHLLVMENEfkaeyeelsCQMYNFALSLLDKLRDSKElevilnhQGLTPLKLAAKEGR 269
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 111-262 2.01e-06

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 54.03  E-value: 2.01e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  111 KGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGF--------------TPLYMAAQENHIDVVKYLLENganqstate 176
Cdd:cd22193     75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLEN--------- 145

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  177 dgftplavalqqghNQAVAILLENDTKGKVRLPALHIAArkDDTKSAALLLQNDHNADVQ---------------SKSGF 241
Cdd:cd22193    146 --------------EHQPADIEAQDSRGNTVLHALVTVA--DNTKENTKFVTRMYDMILIrgaklcptveleeirNNDGL 209

                          170       180
                   ....*....|....*....|.
gi 1039763615  242 TPLHIAAHYGNVNVATLLLNR 262
Cdd:cd22193    210 TPLQLAAKMGKIEILKYILQR 230
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 144-170 2.07e-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: 46.81  E-value: 2.07e-06
                            10        20
                    ....*....|....*....|....*..
gi 1039763615   144 NGFTPLYMAAQENHIDVVKYLLENGAN 170
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 111-262 2.25e-06

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 53.73  E-value: 2.25e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  111 KGNTALHIASLAGQAEVVKVLVKEGANINAQS---------QNGF----TPLYMAAQENHIDVVKYLLENGANqstated 177
Cdd:cd21882     72 QGQTALHIAIENRNLNLVRLLVENGADVSARAtgrffrkspGNLFyfgeLPLSLAACTNQEEIVRLLLENGAQ------- 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  178 gftplavalqqghnqaVAILLENDTKGKVRLPALHIAARKDDTKSA------ALLLQNDHNAD-------VQSKSGFTPL 244
Cdd:cd21882    145 ----------------PAALEAQDSLGNTVLHALVLQADNTPENSAfvcqmyNLLLSYGAHLDptqqleeIPNHQGLTPL 208

                          170
                   ....*....|....*...
gi 1039763615  245 HIAAHYGNVNVATLLLNR 262
Cdd:cd21882    209 KLAAVEGKIVMFQHILQR 226
Ank_5 pfam13857
Ankyrin repeats (many copies);
588-643 2.32e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 2.32e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  588 LLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIA 643
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 547-739 2.47e-06

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 53.66  E-value: 2.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  547 EGQVDVASVLLEagaahsLATKKGFTPLHVAAKYgsldvaklllqrraaADSAGKnGLTPLHVAAHYDNQKVALLLLEKG 626
Cdd:cd22196     60 NGQNDTISLLLD------IAEKTGNLKEFVNAAY---------------TDSYYK-GQTALHIAIERRNMHLVELLVQNG 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  627 ASPHATA----------KNGY----TPLHIAAKKNQMQIASTLLN---YGAETNTVTKQGVTPLH---------LASQEG 680
Cdd:cd22196    118 ADVHARAsgeffkkkkgGPGFyfgeLPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLHalvevadntPENTKF 197

                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039763615  681 HTDMVTLLLDKGANIH-------MSTKSGLTSLHLAAQEDKVNV-ADILTKHGADRDA------YTKLGYTPL 739
Cdd:cd22196    198 VTKMYNEILILGAKIRpllkleeITNKKGLTPLKLAAKTGKIGIfAYILGREIKEPECrhlsrkFTEWAYGPV 270
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 603-717 2.50e-06

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 53.61  E-value: 2.50e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  603 GLTPLHVAAHYDNQKVALLLLEKGASPHATAKN--------------GYTPLHIAAKKNQMQIASTLLNygAETNTVTKQ 668
Cdd:cd22194    141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLME--KESTDITSQ 218

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039763615  669 ---GVTPLHL-----ASQEGHTDMVTLLLD------KGANIH-MSTKSGLTSLHLAAQEDKVNV 717
Cdd:cd22194    219 dsrGNTVLHAlvtvaEDSKTQNDFVKRMYDmillksENKNLEtIRNNEGLTPLQLAAKMGKAEI 282
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 767-798 2.60e-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: 46.51  E-value: 2.60e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1039763615  767 NGYTPLHQAAQQ-GHTHIINVLLQHGAKPNATT 798
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 600-757 3.16e-06

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 53.35  E-value: 3.16e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  600 GKNGLTPLHVAAHYDNQKV---ALLLLE---KGASPHATAK--------NGYTPLHIAAKKNQMQIASTLLNYGAE---- 661
Cdd:cd21882     23 GATGKTCLHKAALNLNDGVneaIMLLLEaapDSGNPKELVNapctdefyQGQTALHIAIENRNLNLVRLLVENGADvsar 102

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  662 -TNTVTKQ--------GVTPLHLASQEGHTDMVTLLLDKGANIHMSTKS---GLTSLH-LAAQEDK--------VNVADI 720
Cdd:cd21882    103 aTGRFFRKspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHaLVLQADNtpensafvCQMYNL 182

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....
gi 1039763615  721 LTKHGADRDAYTKL-------GYTPLIVACHYGNVKMVNFLLKQ 757
Cdd:cd21882    183 LLSYGAHLDPTQQLeeipnhqGLTPLKLAAVEGKIVMFQHILQR 226
Death_NMPP84 cd08318
Death domain of Nuclear Matrix Protein P84; Death domain (DD) found in the Nuclear Matrix ...
 3573-3657 3.29e-06

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: 47.90  E-value: 3.29e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3573 DPQDEQERMEErlayIADHLGFSWTELARELDFTEEQIHQIRiENPNSLQDQSHALLKYWLERDGKHATDTILIECLTKI 3652
Cdd:cd08318      2 DKPVTSEQIDV----LANKLGEQWKTLAPYLEMKDKDIRQIE-SDSEDMKMRAKQLLVTWQDREGAQATPEILMTALNAA 76


                   ....*
gi 1039763615 3653 NRMDI 3657
Cdd:cd08318     77 GLNEI 81
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 196-300 3.65e-06

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 49.87  E-value: 3.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  196 ILLENDTKGKvrlPALHIAARKD--DTKSAALLLQnDHNADVQSKS---GFTPLHIAAHYGNVNVATLLLNRgAAVDFTA 270
Cdd:PHA02736    47 LVLEYNRHGK---QCVHIVSNPDkaDPQEKLKLLM-EWGADINGKErvfGNTPLHIAVYTQNYELATWLCNQ-PGVNMEI 121

                           90       100       110
                   ....*....|....*....|....*....|..
gi 1039763615  271 RNGI--TPLHVASKRGNTNMVKLLLDRGGQID 300
Cdd:PHA02736   122 LNYAfkTPYYVACERHDAKMMNILRAKGAQCK 153
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 61-329 4.06e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 52.82  E-value: 4.06e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   61 KVVEYL-KGGIDIN-TCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSatkKGNTALHIASLAGQAEV--------VKV 130
Cdd:PHA02989    17 NALEFLlRTGFDVNeEYRGNSILLLYLKRKDVKIKIVKLLIDNGADVNY---KGYIETPLCAVLRNREItsnkikkiVKL 93

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  131 LVKEGANINAQSQNGFTPLYMAAQENHI---DVVKYLLENGAN-QSTATEDGFTPLAVALQQG--HNQAVAILLEN---- 200
Cdd:PHA02989    94 LLKFGADINLKTFNGVSPIVCFIYNSNInncDMLRFLLSKGINvNDVKNSRGYNLLHMYLESFsvKKDVIKILLSFgvnl 173

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  201 -DTKGKVRLPALHIAARKD----DTKSAALLLQND---HNADVQSKS---GFTPLHIAAHYGNVNVATLLLNRgAAVDFT 269
Cdd:PHA02989   174 fEKTSLYGLTPMNIYLRNDidviSIKVIKYLIKKGvniETNNNGSESvleSFLDNNKILSKKEFKVLNFILKY-IKINKK 252

                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  270 ARNGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERK 329
Cdd:PHA02989   253 DKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQLK 312
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 525-661 4.32e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 4.32e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  525 QHMAHPDAATTNGYTPLHISAREGQVDVAsvlleagAAHSLATKKgftpLHVAAKyGSLDVAKLLLQRRAAADSAGKNGL 604
Cdd:PTZ00322    49 THLEALEATENKDATPDHNLTTEEVIDPV-------VAHMLTVEL----CQLAAS-GDAVGARILLTGGADPNCRDYDGR 116

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039763615  605 TPLHVAAHYDNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQMQIASTLLNYGAE 661
Cdd:PTZ00322   117 TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 305-337 4.34e-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: 45.74  E-value: 4.34e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1039763615  305 DGLTPLHCAA-RSGHDQVVELLLERKAPLLARTK 337
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
358-412 4.76e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 4.76e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1039763615  358 LLQYKaPVDDVTLDY--LTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIA 412
Cdd:pfam13857    1 LLEHG-PIDLNRLDGegYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 470-592 4.99e-06

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 52.49  E-value: 4.99e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  470 RGETALHMAARAGQVEVVRCLLRNGALVDARAREE--------------QTPLHIASRLGKTEIVQLLLQHMAHP---DA 532
Cdd:cd22193     75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRffqpkyqgegfyfgELPLSLAACTNQPDIVQYLLENEHQPadiEA 154

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  533 ATTNGYTPLHI------SAREGQVDVASV---LLEAGAA-------HSLATKKGFTPLHVAAKYGSLDVAKLLLQR 592
Cdd:cd22193    155 QDSRGNTVLHAlvtvadNTKENTKFVTRMydmILIRGAKlcptvelEEIRNNDGLTPLQLAAKMGKIEILKYILQR 230
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 386-593 5.08e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 52.44  E-value: 5.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  386 RVTKLLLDKRANPNARALNGfTPL-------HIACKKNRiKVMELLVKYGASIQAITESGLTPIhvAAFM-----GHLNI 453
Cdd:PHA02989    51 KIVKLLIDNGADVNYKGYIE-TPLcavlrnrEITSNKIK-KIVKLLLKFGADINLKTFNGVSPI--VCFIynsniNNCDM 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  454 VLLLLQNGAS-PDVTNIRGETALHMAARAGQV--EVVRCLLRNGA-LVDARAREEQTPLHIASR---------------- 513
Cdd:PHA02989   127 LRFLLSKGINvNDVKNSRGYNLLHMYLESFSVkkDVIKILLSFGVnLFEKTSLYGLTPMNIYLRndidvisikvikylik 206

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  514 -------------------------LGKTE--IVQLLLQHMA--HPDAAttnGYTPLHISAREGQVDVASVLLEAGAAHS 564
Cdd:PHA02989   207 kgvnietnnngsesvlesfldnnkiLSKKEfkVLNFILKYIKinKKDKK---GFNPLLISAKVDNYEAFNYLLKLGDDIY 283

                          250       260
                   ....*....|....*....|....*....
gi 1039763615  565 LATKKGFTPLHVAAKYGSLDVAKLLLQRR 593
Cdd:PHA02989   284 NVSKDGDTVLTYAIKHGNIDMLNRILQLK 312
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 404-431 5.31e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 45.66  E-value: 5.31e-06
                            10        20
                    ....*....|....*....|....*...
gi 1039763615   404 NGFTPLHIACKKNRIKVMELLVKYGASI 431
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 235-607 5.47e-06

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 52.61  E-value: 5.47e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  235 VQSKSGFTPLHiaAHYGNVNVAT----LLLNRGAAVDFTARNGITPLHVASKRGN--TNMVKLLLDRGGQIDAKTRDGLT 308
Cdd:PHA02716   172 VCKKTGYGILH--AYLGNMYVDIdileWLCNNGVNVNLQNNHLITPLHTYLITGNvcASVIKKIIELGGDMDMKCVNGMS 249

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  309 PLH---CAARSGHDQVVELLLERKAPllARTKNGLSPLHM---AAQGDHVECVKHLLQykapvDDVTLDY-----LTALH 377
Cdd:PHA02716   250 PIMtyiINIDNINPEITNIYIESLDG--NKVKNIPMILHSyitLARNIDISVVYSFLQ-----PGVKLHYkdsagRTCLH 322

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  378 --VAAHCGHYRVTKLLLDKRANPNARALNGFTPLH----IACKKN----------RIKVMELLVKYGASIQAITESGLTP 441
Cdd:PHA02716   323 qyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsMLSVVNildpetdndiRLDVIQCLISLGADITAVNCLGYTP 402

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  442 ihvaafmghLNIVLLLLQNGASPDVTN-IRGETALHMaaragqvevvrclLRNGALVDARAREEQTPLHIASRLGKTEIv 520
Cdd:PHA02716   403 ---------LTSYICTAQNYMYYDIIDcLISDKVLNM-------------VKHRILQDLLIRVDDTPCIIHHIIAKYNI- 459

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  521 qlllqhmahPDAATTNGYTPLHISAREgqvDVASVLLEAGAAHSLATKKGFTPLHVAAKYGS-----LDVAKLLLQRRAA 595
Cdd:PHA02716   460 ---------PTDLYTDEYEPYDSTKIH---DVYHCAIIERYNNAVCETSGMTPLHVSIISHTnanivMDSFVYLLSIQYN 527

                          410
                   ....*....|..
gi 1039763615  596 ADSAGKNGLTPL 607
Cdd:PHA02716   528 INIPTKNGVTPL 539
Ank_4 pfam13637
Ankyrin repeats (many copies);
52-99 5.72e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 5.72e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 1039763615   52 RAARAGNLDKVVEYLKGGIDINTCNQNGLNALHLAAKEGHVGLVQELL 99
Cdd:pfam13637    7 AAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
131-185 5.73e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 5.73e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  131 LVKEG-ANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVA 185
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Death_TRAILR_DR4_DR5 cd08315
Death domain of Tumor necrosis factor-Related Apoptosis-Inducing Ligand Receptors; Death ...
 3587-3661 5.86e-06

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


Pssm-ID: 260027  Cd Length: 88  Bit Score: 47.27  E-value: 5.86e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3587 YIADHLGF-SWTELARELDFTEEQIHQIRIENPNSlQDQSHALLKYWLERDGKHATDTILIECLTKIN----RMDIVHLL 3661
Cdd:cd08315      4 YFEDIVPFkSWKRLMRALGLSDNEIKLAEANDPGS-QEPLYQMLNKWLNKTGRKASVNTLLDALEDLGlrgaAETIADKL 82
Ank_5 pfam13857
Ankyrin repeats (many copies);
490-543 6.14e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 6.14e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039763615  490 LLRNG-ALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPDAATTNGYTPLHI 543
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank_4 pfam13637
Ankyrin repeats (many copies);
702-755 6.37e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 6.37e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039763615  702 GLTSLHLAAQEDKVNVADILTKHGADRDAYTKLGYTPLIVACHYGNVKMVNFLL 755
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 281-361 6.65e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 6.65e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  281 SKRGNTNMVKLLLDRGGQIDAKTRDGLTPLHCAARSGHDQVVELLLERKAPLLARTKNGLSPLHMAAQGDHVECVKHLLQ 360
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169


                   .
gi 1039763615  361 Y 361
Cdd:PTZ00322   170 H 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 715-808 6.92e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.18  E-value: 6.92e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  715 VNVADILTKHGADRDayTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKP 794
Cdd:PLN03192   507 LNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNV 584

                           90
                   ....*....|....*.
gi 1039763615  795 NATTANGNTAL--AIA 808
Cdd:PLN03192   585 HIRDANGNTALwnAIS 600
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 668-700 7.01e-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: 45.36  E-value: 7.01e-06
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1039763615  668 QGVTPLHLAS-QEGHTDMVTLLLDKGANIHMSTK 700
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 767-796 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: 44.50  E-value: 1.05e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1039763615   767 NGYTPLHQAAQQGHTHIINVLLQHGAKPNA 796
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 574-691 1.16e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 50.37  E-value: 1.16e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  574 LHVAAKYGSLDVAKLLLQRRAAADSAGKNGL----TPLHVAAHYDNQKVALLLLEKGASPHATAKNG-YTPLHIAAKKNQ 648
Cdd:PHA02884    37 LYSSIKFHYTDIIDAILKLGADPEAPFPLSEnsktNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkITPLYISVLHGC 116

                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1039763615  649 MQIASTLLNYGAETNTVTKQGVTPLHLASQEGHTDMVTLLLDK 691
Cdd:PHA02884   117 LKCLEILLSYGADINIQTNDMVTPIELALMICNNFLAFMICDN 159
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 668-697 1.27e-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: 44.50  E-value: 1.27e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1039763615   668 QGVTPLHLASQEGHTDMVTLLLDKGANIHM 697
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 438-468 1.45e-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: 1.45e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1039763615  438 GLTPIHVAAFM-GHLNIVLLLLQNGASPDVTN 468
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 272-301 1.53e-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: 44.12  E-value: 1.53e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1039763615   272 NGITPLHVASKRGNTNMVKLLLDRGGQIDA 301
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02741 PHA02741
hypothetical protein; Provisional
 76-199 1.54e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 48.12  E-value: 1.54e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   76 NQNGLNALHLAAKEGHVGLVQELLG--RGSSVDSATK----KGNTALHIASLAGQA----EVVKVLVKEGANINAQ-SQN 144
Cdd:PHA02741    18 NSEGENFFHEAARCGCFDIIARFTPfiRGDCHAAALNatddAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQeMLE 97

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  145 GFTPLYMAAQENHIDVVKYLL-ENGANQSTATEDGFTPLAVALQQGHNQAVAILLE 199
Cdd:PHA02741    98 GDTALHLAAHRRDHDLAEWLCcQPGIDLHFCNADNKSPFELAIDNEDVAMMQILRE 153
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 452-797 1.55e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 50.90  E-value: 1.55e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  452 NIVLLLLQNGAspDVTNI-RGETALHMAARAGQV--EVVRCLLRNGALVDARAREEqTPL-------HIASRLGKtEIVQ 521
Cdd:PHA02989    17 NALEFLLRTGF--DVNEEyRGNSILLLYLKRKDVkiKIVKLLIDNGADVNYKGYIE-TPLcavlrnrEITSNKIK-KIVK 92

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  522 LLLQHMAHPDAATTNGYTPL-------HISaregQVDVASVLLEAGA-AHSLATKKGFTPLHVAAKYGSL--DVAKLLLq 591
Cdd:PHA02989    93 LLLKFGADINLKTFNGVSPIvcfiynsNIN----NCDMLRFLLSKGInVNDVKNSRGYNLLHMYLESFSVkkDVIKILL- 167

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  592 rRAAADSAGKN---GLTPLHVAAHYD----NQKVALLLLEKGASphatakngytplhiaakknqmqiastllnygAETNT 664
Cdd:PHA02989   168 -SFGVNLFEKTslyGLTPMNIYLRNDidviSIKVIKYLIKKGVN-------------------------------IETNN 215

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  665 vtkqgvtplhlasqEGHTDMVTLLLDKgaNIHMSTKSgLTSLHLAAQEDKVNVADiltkhgadrdaytKLGYTPLIVACH 744
Cdd:PHA02989   216 --------------NGSESVLESFLDN--NKILSKKE-FKVLNFILKYIKINKKD-------------KKGFNPLLISAK 265

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039763615  745 YGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQhgAKPNAT 797
Cdd:PHA02989   266 VDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ--LKPGKY 316
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 111-140 1.90e-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: 44.12  E-value: 1.90e-05
                            10        20        30
                    ....*....|....*....|....*....|
gi 1039763615   111 KGNTALHIASLAGQAEVVKVLVKEGANINA 140
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 405-544 1.93e-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: 1.93e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  405 GFTPLHIACKKNRIKVMELLVKYGASIQAITES--------------GLTPIHVAAFMGHLNIVLLLLQNG---ASPDVT 467
Cdd:cd22193     76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEhqpADIEAQ 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  468 NIRGETALH--------------MAARAGQVEVVRC--LLRNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPD 531
Cdd:cd22193    156 DSRGNTVLHalvtvadntkentkFVTRMYDMILIRGakLCPTVELEEIRNNDGLTPLQLAAKMGKIEILKYILQREIKEP 235

                          170       180
                   ....*....|....*....|
gi 1039763615  532 AA-------TTNGYTPLHIS 544
Cdd:cd22193    236 ELrhlsrkfTDWAYGPVSSS 255
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 111-141 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: 43.82  E-value: 2.08e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1039763615  111 KGNTALHIASL-AGQAEVVKVLVKEGANINAQ 141
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 470-592 2.09e-05

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: 50.62  E-value: 2.09e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  470 RGETALHMAARAGQVEVVRCLLRNGALVDARAREE-------------QTPLHIASRLGKTEIVQLLLQHMAHP---DAA 533
Cdd:cd22197     93 RGHSALHIAIEKRSLQCVKLLVENGADVHARACGRffqkkqgtcfyfgELPLSLAACTKQWDVVNYLLENPHQPaslQAQ 172

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039763615  534 TTNGYTPLH---ISAREGQVDVASV------LLEAGAA-------HSLATKKGFTPLHVAAKYGSLDVAKLLLQR 592
Cdd:cd22197    173 DSLGNTVLHalvMIADNSPENSALVikmydgLLQAGARlcptvqlEEISNHEGLTPLKLAAKEGKIEIFRHILQR 247
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 654-798 2.33e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 50.12  E-value: 2.33e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  654 TLLNYGAETNTVTK-QGVTPLHLASQEGHTDMVTLLLDKGANI----HMSTK--SGLTSLHLAAQEDKvNVADILTKHGA 726
Cdd:PHA02989    21 FLLRTGFDVNEEYRgNSILLLYLKRKDVKIKIVKLLIDNGADVnykgYIETPlcAVLRNREITSNKIK-KIVKLLLKFGA 99

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039763615  727 DRDAYTKLGYTPL---IVACHYGNVKMVNFLLKQGANVNA-KTKNGYTPLHQAAQQG--HTHIINVLLQHGAKPNATT 798
Cdd:PHA02989   100 DINLKTFNGVSPIvcfIYNSNINNCDMLRFLLSKGINVNDvKNSRGYNLLHMYLESFsvKKDVIKILLSFGVNLFEKT 177
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 272-304 2.37e-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: 2.37e-05
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1039763615  272 NGITPLHVASKR-GNTNMVKLLLDRGGQIDAKTR 304
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PRK14949 PRK14949
DNA polymerase III subunits gamma and tau; Provisional
 3156-3417 2.49e-05

DNA polymerase III subunits gamma and tau; Provisional


Pssm-ID: 237863 [Multi-domain]  Cd Length: 944  Bit Score: 50.49  E-value: 2.49e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3156 EEAISEDLKEGATGAEPPQTETtSESLELSEPKEAMDDE---------------GELLPDDVSEEIEDLPASDAnidSQV 3220
Cdd:PRK14949   422 QAANAEAVAEADASAEPADTVE-QALDDESELLAALNAEqavilsqaqsqgfeaSSSLDADNSAVPEQIDSTAE---QSV 497

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3221 IISASTETPTKEAVSTAVEEPPTTQRSDSLSTVKQTPRPAVPGpvgqlDFSPVTRSVYSGQDDESPESSpEEQKSVIEIP 3300
Cdd:PRK14949   498 VNPSVTDTQVDDTSASNNSAADNTVDDNYSAEDTLESNGLDEG-----DYAQDSAPLDAYQDDYVAFSS-ESYNALSDDE 571

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3301 TAPVDNVPSAESKPQIPIRTLPTLVPAPPSAEDESAfSDDFPSS-----------LDEDS-KEGGAKP-----KSKIPVK 3363
Cdd:PRK14949   572 QHSANVQSAQSAAEAQPSSQSLSPISAVTTAAASLA-DDDILDAvlaardsllsdLDALSpKEGDGKKssadrKPKTPPS 650

                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1039763615 3364 APTQRTEWQPsPTDIPLQKTAVPQGQETLSRAPDGRSKSESDASSLDAKTKCPV 3417
Cdd:PRK14949   651 RAPPASLSKP-ASSPDASQTSASFDLDPDFELATHQSVPEAALASGSAPAPPPV 703
Ank_5 pfam13857
Ankyrin repeats (many copies);
104-152 3.01e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 3.01e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1039763615  104 SVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGFTPLYMA 152
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 478-700 3.11e-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: 50.14  E-value: 3.11e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  478 AARAGQVEVVRCLLRNGALVDARAREEQTPLHI-----ASRLGKTEIVQLLLQHmahpdAATTNGYTPLHISAREGQvDV 552
Cdd:cd22194     52 KVSEAAVEELGELLKELKDLSRRRRKTDVPDFLmhkltASDTGKTCLMKALLNI-----NENTKEIVRILLAFAEEN-GI 125

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  553 ASVLLEAgaAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKN--------------GLTPLHVAAHYDNQKV 618
Cdd:cd22194    126 LDRFINA--EYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEI 203

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  619 ALLLLEKGASPHATAKN-GYTPLH---IAAKKNQMQIASTLLNY--------GAETNTVT-KQGVTPLHLASQEGHTDMV 685
Cdd:cd22194    204 VQLLMEKESTDITSQDSrGNTVLHalvTVAEDSKTQNDFVKRMYdmillkseNKNLETIRnNEGLTPLQLAAKMGKAEIL 283

                          250       260
                   ....*....|....*....|
gi 1039763615  686 TLLL-----DKGaNIHMSTK 700
Cdd:cd22194    284 KYILsreikEKP-NRSLSRK 302
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 603-717 3.19e-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: 50.18  E-value: 3.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  603 GLTPLHVAAHYDNQKVALLLLEKGASPHATAKN--------------GYTPLHIAAKKNQMQIASTLLNYGAETNTVTKQ 668
Cdd:cd22193     76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEHQPADIEAQ 155

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039763615  669 ---GVTPLHLA-----SQEGHTDMVT----LLLDKGANIH-------MSTKSGLTSLHLAAQEDKVNV 717
Cdd:cd22193    156 dsrGNTVLHALvtvadNTKENTKFVTrmydMILIRGAKLCptveleeIRNNDGLTPLQLAAKMGKIEI 223
PHA03307 PHA03307
transcriptional regulator ICP4; Provisional
 1807-2015 3.22e-05

transcriptional regulator ICP4; Provisional


Pssm-ID: 223039 [Multi-domain]  Cd Length: 1352  Bit Score: 50.17  E-value: 3.22e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1807 RVEDEQKGRSKLPVRVKGKEDVPKRTTPRTHPA-VSPSSKSSTSSKAERHSSLSSSAKPerhtpvsPSSKNEKLSPVSPS 1885
Cdd:PHA03307   229 ADDAGASSSDSSSSESSGCGWGPENECPLPRPApITLPTRIWEASGWNGPSSRPGPASS-------SSSPRERSPSPSPS 301

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1886 AkterhspvfSGKPEKHSPGSPSTKNERHSPVSSLKTER-----HTPGSPSGKTDKRPPVPSSGRtekhPPVSPGKTEKH 1960
Cdd:PHA03307   302 S---------PGSGPAPSSPRASSSSSSSRESSSSSTSSssessRGAAVSPGPSPSRSPSPSRPP----PPADPSSPRKR 368

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1039763615 1961 LPGSPSIRTPeKPAPGSATGKHEKHLPVSPGKTEKQPPISPTSKTERIEETMSVR 2015
Cdd:PHA03307   369 PRPSRAPSSP-AASAGRPTRRRARAAVAGRARRRDATGRFPAGRPRPSPLDAGAA 422
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 735-763 3.39e-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: 43.35  E-value: 3.39e-05
                            10        20
                    ....*....|....*....|....*....
gi 1039763615   735 GYTPLIVACHYGNVKMVNFLLKQGANVNA 763
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 438-677 3.51e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.08  E-value: 3.51e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  438 GLTPIHVAAFMG-HLNIVLLLLQNGASPDVtnirGETALHmAARAGQVEVVRCLLR----------NGALVDARAREE-- 504
Cdd:TIGR00870   52 GRSALFVAAIENeNLELTELLLNLSCRGAV----GDTLLH-AISLEYVDAVEAILLhllaafrksgPLELANDQYTSEft 126

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  505 --QTPLHIASRLGKTEIVQLLLQhmahpdaattNGYTplhISAREGQVDVASVLLEAGAAHSLAtkkgftPLHVAAKYGS 582
Cdd:TIGR00870  127 pgITALHLAAHRQNYEIVKLLLE----------RGAS---VPARACGDFFVKSQGVDSFYHGES------PLNAAACLGS 187

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  583 LDVAKLLLQRRA---AADSAGKnglTPLHVAA-----HYDNQKV-------ALLLLEKGASP----HATAKNGYTPLHIA 643
Cdd:TIGR00870  188 PSIVALLSEDPAdilTADSLGN---TLLHLLVmenefKAEYEELscqmynfALSLLDKLRDSkeleVILNHQGLTPLKLA 264

                          250       260       270
                   ....*....|....*....|....*....|....
gi 1039763615  644 AKKNQMQIASTLLNYGAETNTVTKQGVTPLHLAS 677
Cdd:TIGR00870  265 AKEGRIVLFRLKLAIKYKQKKFVAWPNGQQLLSL 298
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 144-170 3.64e-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: 3.64e-05
                           10        20
                   ....*....|....*....|....*...
gi 1039763615  144 NGFTPLYMAA-QENHIDVVKYLLENGAN 170
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGAD 28
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 400-524 4.25e-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: 49.76  E-value: 4.25e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  400 ARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITES--------------GLTPIHVAAFMGHLNIVLLLLQNGASP- 464
Cdd:cd22194    136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDi 215

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1039763615  465 DVTNIRGETALH---MAARAGQ------VEVVRCLLR---NGALVDARAREEQTPLHIASRLGKTEIVQLLL 524
Cdd:cd22194    216 TSQDSRGNTVLHalvTVAEDSKtqndfvKRMYDMILLkseNKNLETIRNNEGLTPLQLAAKMGKAEILKYIL 287
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 159-329 4.50e-05

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 49.49  E-value: 4.50e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  159 DVVKYLLENGANQSTATedGFTPLAVA---LQQGHNQAVAILLENDTKGKVRLP---------------ALHIAARKDDT 220
Cdd:cd21882      9 ECLRWYLTDSAYQRGAT--GKTCLHKAalnLNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyqgqtALHIAIENRNL 86

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  221 KSAALLLQNdhNADVQSKS---------------GFTPLHIAAHYGNVNVATLLLNRGAAV-DFTARN--GITPLHVASK 282
Cdd:cd21882     87 NLVRLLVEN--GADVSARAtgrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPaALEAQDslGNTVLHALVL 164

                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1039763615  283 RGN---------TNMVKLLLDRGGQID-------AKTRDGLTPLHCAARSGHDQVVELLLERK 329
Cdd:cd21882    165 QADntpensafvCQMYNLLLSYGAHLDptqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQRE 227
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 344-427 4.57e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.51  E-value: 4.57e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  344 HMAAQGDHVEcVKHLLQYKAPVDDVTLDYLTALHVAAHCGHYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMEL 423
Cdd:PTZ00322    88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                   ....
gi 1039763615  424 LVKY 427
Cdd:PTZ00322   167 LSRH 170
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 405-564 4.71e-05

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: 49.47  E-value: 4.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  405 GFTPLHIACKKNRIKVMELLVKYGASIQAITES-------------GLTPIHVAAFMGHLNIVLLLLQNGASP---DVTN 468
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELPLSLAACTKQWDVVNYLLENPHQPaslQAQD 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  469 IRGETALH----MAARAGQVEVVRC-----LLRNGALVDARAREEQ-------TPLHIASRLGKTEIVQLLLQ-HMAHPD 531
Cdd:cd22197    174 SLGNTVLHalvmIADNSPENSALVIkmydgLLQAGARLCPTVQLEEisnheglTPLKLAAKEGKIEIFRHILQrEFSGPY 253

                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*
gi 1039763615  532 AATTNGYT-----PLHISAregqVDVASV-------LLEAGAAHS 564
Cdd:cd22197    254 QHLSRKFTewcygPVRVSL----YDLSSVdsweknsVLEIIAFHS 294
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 470-500 5.50e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 5.50e-05
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1039763615  470 RGETALHMAA-RAGQVEVVRCLLRNGALVDAR 500
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1829-2005 5.63e-05

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 49.55  E-value: 5.63e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1829 PKRTTPRthPAVSPSSKSSTSSKAERHSSLSSSAKPERHTPVSPSSKNEKLSPVSPSAKTERHSPVFSGKPEKHSPG--- 1905
Cdd:PHA03247  2779 PPRRLTR--PAVASLSESRESLPSPWDPADPPAAVLAPAAALPPAASPAGPLPPPTSAQPTAPPPPPGPPPPSLPLGgsv 2856

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1906 SPSTKNERHSPVSSLKTERHTPGSPSGKTDKRPPVPSSGRTEKHPPVSPGKTEKHLPGSPSIRTPEKPAPGSATgkhekh 1985
Cdd:PHA03247  2857 APGGDVRRRPPSRSPAAKPAAPARPPVRRLARPAVSRSTESFALPPDQPERPPQPQAPPPPQPQPQPPPPPQPQ------ 2930

                          170       180
                   ....*....|....*....|
gi 1039763615 1986 lPVSPGKTEKQPPISPTSKT 2005
Cdd:PHA03247  2931 -PPPPPPPRPQPPLAPTTDP 2949
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 374-401 6.19e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 6.19e-05
                           10        20
                   ....*....|....*....|....*....
gi 1039763615  374 TALHVAA-HCGHYRVTKLLLDKRANPNAR 401
Cdd:pfam00023    4 TPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 681-775 6.71e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 48.06  E-value: 6.71e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  681 HTDMVTLLLDKGANIH----MSTKSGLTSLHLAAQEDKVNVADILTKHGADRDAYTK-LGYTPLIVACHYGNVKMVNFLL 755
Cdd:PHA02884    45 YTDIIDAILKLGADPEapfpLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEeAKITPLYISVLHGCLKCLEILL 124

                           90       100
                   ....*....|....*....|
gi 1039763615  756 KQGANVNAKTKNGYTPLHQA 775
Cdd:PHA02884   125 SYGADINIQTNDMVTPIELA 144
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 404-433 7.51e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 42.24  E-value: 7.51e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1039763615  404 NGFTPLHIACKKNRIKVMELLVKYGASIQA 433
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 735-763 9.50e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.86  E-value: 9.50e-05
                           10        20
                   ....*....|....*....|....*....
gi 1039763615  735 GYTPLIVACHYGNVKMVNFLLKQGANVNA 763
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 767-796 9.69e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.86  E-value: 9.69e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1039763615  767 NGYTPLHQAAQQGHTHIINVLLQHGAKPNA 796
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 614-693 9.88e-05

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 45.64  E-value: 9.88e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  614 DNQKVALLLLEKGASPHAT-AKNGYTPLHIAAKKNQMQIASTLLNY-GAETNTVTKQGVTPLHLASQEGHTDMVTLLLDK 691
Cdd:PHA02736    69 DPQEKLKLLMEWGADINGKeRVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAK 148


                   ..
gi 1039763615  692 GA 693
Cdd:PHA02736   149 GA 150
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 602-634 1.05e-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: 41.89  E-value: 1.05e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1039763615  602 NGLTPLHVAA-HYDNQKVALLLLEKGASPHATAK 634
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
324-379 1.12e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 1.12e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  324 LLLERKAPLLARTKNGLSPLHMAAQGDHVECVKHLLQYKAPVDDVTLDYLTALHVA 379
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02795 PHA02795
ankyrin-like protein; Provisional
 126-189 1.14e-04

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 48.07  E-value: 1.14e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1039763615  126 EVVKVLVKEGANINAQSQNGFTPLYMAAQENHIDVVKYLLENGANQSTATEDGFTPLAVALQQG 189
Cdd:PHA02795   202 EIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRG 265
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 458-627 1.22e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 45.25  E-value: 1.22e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  458 LQNGASPDVTNIRGETALHMaaragqvevvrcLLRNGALVDARAReeQTPLHIASRlgkteivQLLLQHMAHpdaattnG 537
Cdd:PHA02736     4 PEEIIFASEPDIEGENILHY------------LCRNGGVTDLLAF--KNAISDENR-------YLVLEYNRH-------G 55

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  538 YTPLHISAREGQVDVAS---VLLEAGA-AHSLATKKGFTPLHVAAKYGSLDVAKLLLQrRAAADSAGKNGL--TPLHVAA 611
Cdd:PHA02736    56 KQCVHIVSNPDKADPQEklkLLMEWGAdINGKERVFGNTPLHIAVYTQNYELATWLCN-QPGVNMEILNYAfkTPYYVAC 134

                          170
                   ....*....|....*.
gi 1039763615  612 HYDNQKVALLLLEKGA 627
Cdd:PHA02736   135 ERHDAKMMNILRAKGA 150
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 126-186 1.31e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 46.35  E-value: 1.31e-04
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1039763615  126 EVVKVLVKEGANINAQSQ-NGFTPL--YMAAQEN-HIDVVKYLLENGANQSTATEDGFTPLAVAL 186
Cdd:PHA02859    67 EILKFLIENGADVNFKTRdNNLSALhhYLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMYM 131
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 667-759 1.34e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 45.25  E-value: 1.34e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  667 KQGVTPLHLASQEGHTD---MVTLLLDKGANIH-MSTKSGLTSLHLAAQEDKVNVADILTKH-GADRDAYTKLGYTPLIV 741
Cdd:PHA02736    53 RHGKQCVHIVSNPDKADpqeKLKLLMEWGADINgKERVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYV 132

                           90
                   ....*....|....*...
gi 1039763615  742 ACHYGNVKMVNFLLKQGA 759
Cdd:PHA02736   133 ACERHDAKMMNILRAKGA 150
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 404-436 1.62e-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: 41.51  E-value: 1.62e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1039763615  404 NGFTPLHIACKK-NRIKVMELLVKYGASIQAITE 436
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 338-367 1.73e-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: 1.73e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1039763615   338 NGLSPLHMAAQGDHVECVKHLLQYKAPVDD 367
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 470-499 2.04e-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: 41.03  E-value: 2.04e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1039763615   470 RGETALHMAARAGQVEVVRCLLRNGALVDA 499
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 240-267 2.09e-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: 2.09e-04
                           10        20
                   ....*....|....*....|....*....
gi 1039763615  240 GFTPLHIAA-HYGNVNVATLLLNRGAAVD 267
Cdd:pfam00023    2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 72-170 2.12e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.58  E-value: 2.12e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   72 INTCNQNGLNALH--LAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLA----GQAEVVKVLVKEGANINAQSQNG 145
Cdd:PHA02859    44 VNDCNDLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRDNNLSALHHYLSfnknVEPEILKILIDSGSSITEEDEDG 123

                           90       100
                   ....*....|....*....|....*..
gi 1039763615  146 FTPL--YMAAQENHIDVVKYLLENGAN 170
Cdd:PHA02859   124 KNLLhmYMCNFNVRINVIKLLIDSGVS 150
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 305-330 2.29e-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: 41.03  E-value: 2.29e-04
                            10        20
                    ....*....|....*....|....*.
gi 1039763615   305 DGLTPLHCAARSGHDQVVELLLERKA 330
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 338-369 2.33e-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: 2.33e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1039763615  338 NGLSPLHMAA-QGDHVECVKHLLQYKAPVDDVT 369
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 719-810 2.35e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 2.35e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  719 DILTKHGADRDAYTKLGYTPLIVACHYGNVKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAKPNATT 798
Cdd:PLN03192   542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA 621

                           90
                   ....*....|..
gi 1039763615  799 AnGNTALAIAKR 810
Cdd:PLN03192   622 A-GDLLCTAAKR 632
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 66-149 2.37e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 2.37e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   66 LKGGIDINTCNQNGLNALHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKE-------GANI 138
Cdd:PTZ00322   102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfelGANA 181

                           90
                   ....*....|.
gi 1039763615  139 NAQSQNGFTPL 149
Cdd:PTZ00322   182 KPDSFTGKPPS 192
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 569-594 2.74e-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: 2.74e-04
                            10        20
                    ....*....|....*....|....*.
gi 1039763615   569 KGFTPLHVAAKYGSLDVAKLLLQRRA 594
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 553-636 2.76e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 2.76e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  553 ASVLLEAGAAHSLATKKGFTPLHVAAKYGSLDVAKLLLQRRAAADSAGKNGLTPLHVAAHYDNQKVALLLLEKGASPHAT 632
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177


                   ....
gi 1039763615  633 AKNG 636
Cdd:PTZ00322   178 GANA 181
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 240-267 2.90e-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: 2.90e-04
                            10        20
                    ....*....|....*....|....*...
gi 1039763615   240 GFTPLHIAAHYGNVNVATLLLNRGAAVD 267
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
PLN03209 PLN03209
translocon at the inner envelope of chloroplast subunit 62; Provisional
 1782-2043 3.18e-04

translocon at the inner envelope of chloroplast subunit 62; Provisional


Pssm-ID: 178748 [Multi-domain]  Cd Length: 576  Bit Score: 46.84  E-value: 3.18e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1782 AKATSPLieeTPIGSIKDKVKAlqKRVEDEQKGRSKLPVRVKGKEDVPKRTTPRTH--PAVSPSSKSSTSSKAERHSSLS 1859
Cdd:PLN03209   307 AETTAPL---TPMEELLAKIPS--QRVPPKESDAADGPKPVPTKPVTPEAPSPPIEeePPQPKAVVPRPLSPYTAYEDLK 381

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1860 SSAKPerhTPVSPSSKNEKLSPVSPSAKTERHSPVfsgkpekHSPGSPSTKNERHSPVSSLKTERhtPGSPSGKTDKRPP 1939
Cdd:PLN03209   382 PPTSP---IPTPPSSSPASSKSVDAVAKPAEPDVV-------PSPGSASNVPEVEPAQVEAKKTR--PLSPYARYEDLKP 449

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1940 VPSSGRTEKHPPVSPGKTEKHLPGSPSiRTPEKPAPGSATGKHEKHLPVSPGKT--EKQPPISPT-SKTERIEETMSVRE 2016
Cdd:PLN03209   450 PTSPSPTAPTGVSPSVSSTSSVPAVPD-TAPATAATDAAAPPPANMRPLSPYAVydDLKPPTSPSpAAPVGKVAPSSTNE 528

                          250       260
                   ....*....|....*....|....*..
gi 1039763615 2017 LMKAFQSGQDPSKHKTGlfEHKSAKQK 2043
Cdd:PLN03209   529 VVKVGNSAPPTALADEQ--HHAQPKPR 553
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 635-663 3.47e-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: 3.47e-04
                            10        20
                    ....*....|....*....|....*....
gi 1039763615   635 NGYTPLHIAAKKNQMQIASTLLNYGAETN 663
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 438-466 3.71e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 3.71e-04
                            10        20
                    ....*....|....*....|....*....
gi 1039763615   438 GLTPIHVAAFMGHLNIVLLLLQNGASPDV 466
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 305-334 3.94e-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: 40.32  E-value: 3.94e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1039763615  305 DGLTPLHCAARSGHDQVVELLLERKAPLLA 334
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
 111-262 4.11e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 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: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 46.38  E-value: 4.11e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  111 KGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGF--------------TPLYMAAQENHIDVVKYLLENganqstate 176
Cdd:cd22195    136 RGQTALHIAIERRCKHYVELLVEKGADVHAQARGRFfqpkdeggyfyfgeLPLSLAACTNQPDIVHYLTEN--------- 206

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  177 dgftplavalqqGHNQavAILLENDTKGKVRLPAL-HIAARKDD-----TKSAALLLQN------DHNAD-VQSKSGFTP 243
Cdd:cd22195    207 ------------AHKK--ADLRRQDSRGNTVLHALvAIADNTREntkfvTKMYDLLLIKcaklypDCNLEaILNNDGMSP 272

                          170
                   ....*....|....*....
gi 1039763615  244 LHIAAHYGNVNVATLLLNR 262
Cdd:cd22195    273 LMMAAKLGKIGIFQHIIRR 291
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 387-695 4.93e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 46.44  E-value: 4.93e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  387 VTKLLLDKRANPNARALNGFTPLHIACKKNRI--KVMELLVKYGASIQAITESGLTPI--HVAAFMG-HLNIVLLLLQNG 461
Cdd:PHA02716   194 ILEWLCNNGVNVNLQNNHLITPLHTYLITGNVcaSVIKKIIELGGDMDMKCVNGMSPImtYIINIDNiNPEITNIYIESL 273

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  462 ASPDVTNIRGETALHMA-ARAGQVEVVRCLLRNGALVDARAREEQTPLH--IASRLGKTEIVQLLLQHMAHPDAATTNGY 538
Cdd:PHA02716   274 DGNKVKNIPMILHSYITlARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGN 353

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  539 TPLHI--------------SAREGQVDVASVLLEAGAAHSLATKKGFTPLH----VAAKYGSLDVAKLLL--------QR 592
Cdd:PHA02716   354 TVLHTylsmlsvvnildpeTDNDIRLDVIQCLISLGADITAVNCLGYTPLTsyicTAQNYMYYDIIDCLIsdkvlnmvKH 433

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  593 RAAADSAGKNGLTPL---HVAAHY-----------------DNQKVALLLLEKGASPHATAKNGYTPLHIAAKKNQ---- 648
Cdd:PHA02716   434 RILQDLLIRVDDTPCiihHIIAKYniptdlytdeyepydstKIHDVYHCAIIERYNNAVCETSGMTPLHVSIISHTnani 513

                          330       340       350       360       370
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1039763615  649 -MQIASTLLNYGAETNTVTKQGVTPLHLASQE----GHTD-MVTLLLDKGANI 695
Cdd:PHA02716   514 vMDSFVYLLSIQYNINIPTKNGVTPLMLTMRNnrlsGHQWyIVKNILDKRPNV 566
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 144-170 5.14e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.93  E-value: 5.14e-04
                           10        20
                   ....*....|....*....|....*..
gi 1039763615  144 NGFTPLYMAAQENHIDVVKYLLENGAN 170
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 635-667 5.26e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 5.26e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1039763615  635 NGYTPLHIAAKK-NQMQIASTLLNYGAETNTVTK 667
Cdd:pfam00023    1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 244-491 5.52e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 45.89  E-value: 5.52e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  244 LHIAAHYGNVNVATLLLNRGAAVDFtaRNGI-TPL-------HVASKRGNtNMVKLLLDRGGQIDAKTRDGLTPLHCAAR 315
Cdd:PHA02989    41 LYLKRKDVKIKIVKLLIDNGADVNY--KGYIeTPLcavlrnrEITSNKIK-KIVKLLLKFGADINLKTFNGVSPIVCFIY 117

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  316 SGHDQVVELL--LERKAPLLARTKN--GLSPLHMAAQGDHV--ECVKHLLQYKA-PVDDVTLDYLTALHV----AAHCGH 384
Cdd:PHA02989   118 NSNINNCDMLrfLLSKGINVNDVKNsrGYNLLHMYLESFSVkkDVIKILLSFGVnLFEKTSLYGLTPMNIylrnDIDVIS 197

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  385 YRVTKLLLDKRA---NPNAR---ALNGFTPLHIACKKNRIKVMELLVKYgASIQAITESGLTPIHVAAFMGHLNIVLLLL 458
Cdd:PHA02989   198 IKVIKYLIKKGVnieTNNNGsesVLESFLDNNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLL 276

                          250       260       270
                   ....*....|....*....|....*....|...
gi 1039763615  459 QNGASPDVTNIRGETALHMAARAGQVEVVRCLL 491
Cdd:PHA02989   277 KLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRIL 309
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 505-534 5.70e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 5.70e-04
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1039763615  505 QTPLHIAS-RLGKTEIVQLLLQHMAHPDAAT 534
Cdd:pfam00023    3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 569-594 6.35e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.58  E-value: 6.35e-04
                           10        20
                   ....*....|....*....|....*..
gi 1039763615  569 KGFTPLHVAA-KYGSLDVAKLLLQRRA 594
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGA 27
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 371-400 6.37e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 6.37e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1039763615   371 DYLTALHVAAHCGHYRVTKLLLDKRANPNA 400
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03377 PHA03377
EBNA-3C; Provisional
 1816-2105 6.40e-04

EBNA-3C; Provisional


Pssm-ID: 177614 [Multi-domain]  Cd Length: 1000  Bit Score: 45.81  E-value: 6.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1816 SKLPVRVKGKEDVPkrtTPRTHPAVSPSSKSstsskaerhSSLSSSAKPERHTPVSPSSKNEKLSPVSPSAKTER----- 1890
Cdd:PHA03377   409 SRVPWRKPRTLPWP---TPKTHPVKRTLVKT---------SGRSDEAEQAQSTPERPGPSDQPSVPVEPAHLTPVehttv 476

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1891 --HSPVFSGKPEKHSPGSPSTKNERHSPVSSL----------KTERHTPGSPSGKTDKRPP--VPSSGRTEKH---PPVS 1953
Cdd:PHA03377   477 ilHQPPQSPPTVAIKPAPPPSRRRRGACVVYDddiievidveTTEEEESVTQPAKPHRKVQdgFQRSGRRQKRatpPKVS 556

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1954 PGKTEKHLPGSPSIRTPEKPAPGSATGKHEKHLPVSPGKTEKQ-------PPIS------PTSKTERIEETMSVRELMKA 2020
Cdd:PHA03377   557 PSDRGPPKASPPVMAPPSTGPRVMATPSTGPRDMAPPSTGPRQqakckdgPPASgphekqPPSSAPRDMAPSVVRMFLRE 636

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 2021 FQSGQDPSKHKTGLFEHKSAKQ-KQPQDKSKSRVEkekghTVTQRETQR---------IESQTAKRGQRFQVSAATESRR 2090
Cdd:PHA03377   637 RLLEQSTGPKPKSFWEMRAGRDgSGIQQEPSSRRQ-----PATQSTPPRpswlpsvfvLPSVDAGRAQPSEESHLSSMSP 711

                          330
                   ....*....|....*
gi 1039763615 2091 FRSTTITVGLRMEDP 2105
Cdd:PHA03377   712 TQPISHEEQPRYEDP 726
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 470-499 6.51e-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: 39.55  E-value: 6.51e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1039763615  470 RGETALHMAARAGQVEVVRCLLRNGALVDA 499
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 621-709 6.61e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 44.97  E-value: 6.61e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  621 LLLEKGASP---HATAKNGYT-PLHIAAKKNQMQIASTLLNYGAETNTVTKQGV-TPLHLASQEGHTDMVTLLLDKGANI 695
Cdd:PHA02884    51 AILKLGADPeapFPLSENSKTnPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSYGADI 130

                           90
                   ....*....|....
gi 1039763615  696 HMSTKSGLTSLHLA 709
Cdd:PHA02884   131 NIQTNDMVTPIELA 144
PHA03247 PHA03247
large tegument protein UL36; Provisional
 1829-2005 7.25e-04

large tegument protein UL36; Provisional


Pssm-ID: 223021 [Multi-domain]  Cd Length: 3151  Bit Score: 46.08  E-value: 7.25e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1829 PKRTTPRTHPAVSPSSKSSTSSKAerhsslSSSAKPERHTPVSPSSKNEKLSPVSPSAKTERHSPvfSGKPEKHSPGSPS 1908
Cdd:PHA03247  2705 PPTPEPAPHALVSATPLPPGPAAA------RQASPALPAAPAPPAVPAGPATPGGPARPARPPTT--AGPPAPAPPAAPA 2776

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1909 TKNERHSP---VSSLKTERHTPGSPSGKTDkrPPVPSSGRTEKHPPvspgkTEKHLPGSPSIRTPEKPAPGSATGKHEKH 1985
Cdd:PHA03247  2777 AGPPRRLTrpaVASLSESRESLPSPWDPAD--PPAAVLAPAAALPP-----AASPAGPLPPPTSAQPTAPPPPPGPPPPS 2849

                          170       180       190
                   ....*....|....*....|....*....|
gi 1039763615 1986 LP----VSPG------KTEKQPPISPTSKT 2005
Cdd:PHA03247  2850 LPlggsVAPGgdvrrrPPSRSPAAKPAAPA 2879
PTZ00449 PTZ00449
104 kDa microneme/rhoptry antigen; Provisional
 2245-2652 7.30e-04

104 kDa microneme/rhoptry antigen; Provisional


Pssm-ID: 185628 [Multi-domain]  Cd Length: 943  Bit Score: 45.84  E-value: 7.30e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 2245 PQISSEESYKHEGlaetPETSPESLSFSPKKSEEQIGEAKETTKvGTPTDIHSEKELPITNDITDSSQKQGagvtrgseP 2324
Cdd:PTZ00449   497 APIEEEDSDKHDE----PPEGPEASGLPPKAPGDKEGEEGEHED-SKESDEPKEGGKPGETKEGEVGKKPG--------P 563

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 2325 STEHSQKEV---TQDPHKDVCSKQDGCPESQSVSLASEVFTEKGSCGESQLPLVSSAFKTQSESEtqeslTPSEVTKPFP 2401
Cdd:PTZ00449   564 AKEHKPSKIptlSKKPEFPKDPKHPKDPEEPKKPKRPRSAQRPTRPKSPKLPELLDIPKSPKRPE-----SPKSPKRPPP 638

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 2402 PS-DASVKTAEGTEpkpqgAIRSPQGLELPLPNRDSEVLSPMADESLAVSHKDSLEASPVLEDNSSH--------KTPDS 2472
Cdd:PTZ00449   639 PQrPSSPERPEGPK-----IIKSPKPPKSPKPPFDPKFKEKFYDDYLDAAAKSKETKTTVVLDESFEsilketlpETPGT 713

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 2473 LEPSPLKESPCRDSLESSPVEP---KMKAGILPSHFPLPAA-----IAKTDLVAEVASMRSRLLRDPDGSAEDDSLEQT- 2543
Cdd:PTZ00449   714 PFTTPRPLPPKLPRDEEFPFEPigdPDAEQPDDIEFFTPPEeertfFHETPADTPLPDILAEEFKEEDIHAETGEPDEAm 793

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 2544 ----SLMESSGKSPLS-PDTP----SSEEVSYEVTPKPSDS------STPKPAVIHECAEEDDSENGEKKrftpeEEMFK 2608
Cdd:PTZ00449   794 krpdSPSEHEDKPPGDhPSLPkkrhRLDGLALSTTDLESDAgriakdASGKIVKLKRSKSFDDLTTVEEA-----EEMGA 868

                          410       420       430       440       450
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039763615 2609 MVTKIKTFDELEQ---------------EAKQKRDYKKEPRQDGSSSASDPDADYSAEV 2652
Cdd:PTZ00449   869 EARKIVVDDDGTEaddedthppeekhksEVRRRRPPKKPSKPKKPSKPKKPKKPDSAFI 927
PLN03237 PLN03237
DNA topoisomerase 2; Provisional
 3177-3469 9.96e-04

DNA topoisomerase 2; Provisional


Pssm-ID: 215641 [Multi-domain]  Cd Length: 1465  Bit Score: 45.62  E-value: 9.96e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3177 TTSESLELSEpKEAMDDEGELLPDD---VSEEIEDLPASDANIDSQVIISASTETPTKEA---VSTAVEEPPTTQRSDSL 3250
Cdd:PLN03237  1148 TTPKSLWLKD-LDALEKELDKLDKEdakAEEAREKLQRAAARGESGAAKKVSRQAPKKPApkkTTKKASESETTEETYGS 1226

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3251 STVKQTPRPAVPGPVGQldfSPVTRSVYSGQDDESPESSPEEQKSVI---EIPTAPVDNVPSAESKPQIPIR---TLPTL 3324
Cdd:PLN03237  1227 SAMETENVAEVVKPKGR---AGAKKKAPAAAKEKEEEDEILDLKDRLaayNLDSAPAQSAKMEETVKAVPARraaARKKP 1303

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3325 VPAPPSAEDESAFSDDFP---SSLDEDSKEGGAKPKSKIPVKAPTQRTEWQPSPTDIP---LQKTAVPQGQETLSRAPDg 3398
Cdd:PLN03237  1304 LASVSVISDSDDDDDDFAvevSLAERLKKKGGRKPAAANKKAAKPPAAAKKRGPATVQsgqKLLTEMLKPAEAIGISPE- 1382

                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039763615 3399 rSKSESDASSLDAKTKCPVKARSYIETETESRERAEGFESESEDGATkpklfasrLPVKSRSTSSSGRPGT 3469
Cdd:PLN03237  1383 -KKVRKMRASPFNKKSGSVLGRAATNKETESSENVSGSSSSEKDEID--------VSAKPRPQRANRKQTT 1444
Treacle pfam03546
Treacher Collins syndrome protein Treacle;
3168-3425 1.00e-03

Treacher Collins syndrome protein Treacle;


Pssm-ID: 460967 [Multi-domain]  Cd Length: 531  Bit Score: 45.06  E-value: 1.00e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3168 TGAEPPQTETTSESLELSEPKEAMDDEGEllpdDVSEEIEDLPASDANIDSQviisASTETPTKEAVSTAVEEPPttqrs 3247
Cdd:pfam03546    1 TPATPGKAGPAATQAKAGKPEEDSESSSE----EESDSEEETPAAKTPLQAK----PSGKTPQVRAASAPAKESP----- 67

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3248 dslstVKQTPrPAVPGPVGqldfsPVTRSVYSGQDDESPESSPEEQKSVIEIPTAPVDNVPSAESKP---QIPIRTLPTL 3324
Cdd:pfam03546   68 -----RKGAP-PVPPGKTG-----PAAAQAQAGKPEEDSESSSEESDSDGETPAAATLTTSPAQVKPlgkNSQVRPASTV 136

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3325 ---------VPAPPSAEDESAF-------SDDFPSSLDEDSKEGGAKP---KSKIPVKAPTQRTEWQPS--PTDIPLQKT 3383
Cdd:pfam03546  137 gkgpsgkgaNPAPPGKAGSAAPlvqvgkkEEDSESSSEESDSEGEAPPaatQAKPSGKILQVRPASGPAkgAAPAPPQKA 216

                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....
gi 1039763615 3384 --AVPQGQETLSRAPDGRSKSESDASSLDAKTKCPVKARSYIET 3425
Cdd:pfam03546  217 gpVATQVKAERSKEDSESSEESSDSEEEAPAAATPAQAKPALKT 260
PHA02798 PHA02798
ankyrin-like protein; Provisional
 286-460 1.27e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.83  E-value: 1.27e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  286 TNMVKLLLDRGGQIDAKTRDGLTPLhCAARSGHDQ------VVELLLERKAPLLARTKNGLSPLH-MAAQG--DHVECVK 356
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPL-CTILSNIKDykhmldIVKILIENGADINKKNSDGETPLYcLLSNGyiNNLEILL 129

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  357 HLLQYKAPVDDVTLDYLTALHVAAHCGHY---RVTKLLLDKRANPNARA-LNGFTPLHIACKKN--RIKV--MELLVKYG 428
Cdd:PHA02798   130 FMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNnKEKYDTLHCYFKYNidRIDAdiLKLFVDNG 209

                          170       180       190
                   ....*....|....*....|....*....|..
gi 1039763615  429 ASIQAITESgltpiHVAAFMGHLNIVLLLLQN 460
Cdd:PHA02798   210 FIINKENKS-----HKKKFMEYLNSLLYDNKR 236
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 111-140 1.47e-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: 1.47e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1039763615  111 KGNTALHIASLAGQAEVVKVLVKEGANINA 140
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 176-331 1.49e-03

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 44.80  E-value: 1.49e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  176 EDGFTPLAVA---LQQGHNQAVAILLE------------------NDTKGKVrlpALHIAARKDDTKSAALLLQNdhNAD 234
Cdd:cd22196     45 ETGKTCLLKAmlnLHNGQNDTISLLLDiaektgnlkefvnaaytdSYYKGQT---ALHIAIERRNMHLVELLVQN--GAD 119

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  235 VQ------------SKSGF----TPLHIAAHYGNVNVATLLL-NRGAAVDFTARN--GITPLH---------VASKRGNT 286
Cdd:cd22196    120 VHarasgeffkkkkGGPGFyfgeLPLSLAACTNQLDIVKFLLeNPHSPADISARDsmGNTVLHalvevadntPENTKFVT 199

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1039763615  287 NMVKLLLDRGGQIDAK-------TRDGLTPLHCAARSGHDQVVELLLERKAP 331
Cdd:cd22196    200 KMYNEILILGAKIRPLlkleeitNKKGLTPLKLAAKTGKIGIFAYILGREIK 251
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 602-631 1.56e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 1.56e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1039763615   602 NGLTPLHVAAHYDNQKVALLLLEKGASPHA 631
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 242-311 1.83e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.88  E-value: 1.83e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  242 TPLH--IAAHYGNVNVATLLLNRGAAVDFTAR-NGITPLH---VASKRGNTNMVKLLLDRGGQIDAKTRDGLTPLH 311
Cdd:PHA02859    53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRdNNLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLLH 128
Death_PIDD cd08779
Death Domain of p53-induced protein with a death domain; Death domain (DD) found in PIDD ...
 3585-3663 1.83e-03

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


Pssm-ID: 260049  Cd Length: 86  Bit Score: 39.99  E-value: 1.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3585 LAYIADHLGFSWTELARELDFTEEQIHQIRIENPNSLQDQSHALLKYWLErdgKHATDT----ILIECLTKINRMDIVHL 3660
Cdd:cd08779      5 LLSLAKELGEDWQKLALHLGVSYSRIQRIKRKNRDDLDEQILDMLFSWAK---TLPTSPdkvgLLVTALSKSGRSDLAEE 81


                   ...
gi 1039763615 3661 LET 3663
Cdd:cd08779     82 LRD 84
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 668-793 2.14e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 41.79  E-value: 2.14e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  668 QGVTPLHLASQEGhtDMVTLLLDKGA----NIHMST---KSGLTSLHLAAQEDKV---NVADILTKHGADRDAY-TKLGY 736
Cdd:PHA02736    16 EGENILHYLCRNG--GVTDLLAFKNAisdeNRYLVLeynRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKeRVFGN 93

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1039763615  737 TPLIVACHYGNVKMVNFLLKQ-GANVNAKTKNGYTPLHQAAQQGHTHIINVLLQHGAK 793
Cdd:PHA02736    94 TPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQ 151
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 78-110 2.51e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 2.51e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1039763615   78 NGLNALHLAA-KEGHVGLVQELLGRGSSVDSATK 110
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02791 PHA02791
ankyrin-like protein; Provisional
 635-805 2.87e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 42.72  E-value: 2.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  635 NGYTPLHIAAKKNQMQIASTLLNYGAETNTVTKQgvTPLHLASQEGHTDMVTLLLDKGANIHMSTKSGLTSLHLAAQEDK 714
Cdd:PHA02791    29 HGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGN 106

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  715 VNVADILTKHGADRDAYTKLGY-TPLIVACHYGNVKMVNFLLKQGANvNAKTKNGYTPLHQAAQQGHTHIINVLLQHgak 793
Cdd:PHA02791   107 MQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLSEIPS-TFDLAILLSCIHITIKNGHVDMMILLLDY--- 182

                          170
                   ....*....|..
gi 1039763615  794 pnATTANGNTAL 805
Cdd:PHA02791   183 --MTSTNTNNSL 192
Death_RIP1 cd08777
Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in ...
 3582-3661 2.87e-03

Death Domain of Receptor-Interacting Protein 1; Death domain (DD) found in Receptor-Interacting Protein 1 (RIP1) and related proteins. RIP kinases serve as essential sensors of cellular stress. Vertebrates contain several types containing a homologous N-terminal kinase domain and varying C-terminal domains. RIP1 harbors a C-terminal DD, which binds death receptors (DRs) including TNF receptor 1, Fas, TNF-related apoptosis-inducing ligand receptor 1 (TRAILR1), and TRAILR2. It also interacts with other DD-containing adaptor proteins such as TRADD and FADD. RIP1 plays a crucial role in determining a cell's fate, between survival or death, following exposure to stress signals. It is important in the signaling of NF-kappaB and MAPKs, and it links DR-associated signaling to reactive oxygen species (ROS) production. Abnormal RIP1 function may result in ROS accumulation affecting inflammatory responses, innate immunity, stress responses, and cell survival. 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: 260048  Cd Length: 86  Bit Score: 39.34  E-value: 2.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 3582 EERLAYIADHLGFSWTELARELDFTEEQIHQIRIE-NPNSLQDQSHALLKYWLERDG-KHATDTILIECLTKINRMDIVH 3659
Cdd:cd08777      2 EKHLDLLRENLGKKWKRCARRLGLTEVEIEEIDHDyERDGLKEKVHQMLEKWKMKEGsKGATVGKLAKALEGCIKSDLLV 81


                   ..
gi 1039763615 3660 LL 3661
Cdd:cd08777     82 SL 83
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 272-301 2.95e-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: 2.95e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1039763615  272 NGITPLHVASKRGNTNMVKLLLDRGGQIDA 301
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 438-466 3.07e-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: 3.07e-03
                           10        20
                   ....*....|....*....|....*....
gi 1039763615  438 GLTPIHVAAFMGHLNIVLLLLQNGASPDV 466
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02791 PHA02791
ankyrin-like protein; Provisional
 403-558 3.13e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 42.72  E-value: 3.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  403 LNGFTPLHIACKKNRIKVMELLVKYGAsIQAITESGLtPIHVAAFMGHLNIVLLLLQNGASPDVTNIRGETALHMAARAG 482
Cdd:PHA02791    28 VHGHSALYYAIADNNVRLVCTLLNAGA-LKNLLENEF-PLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSG 105

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1039763615  483 QVEVVRCLL-RNGALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHP-DAATTngYTPLHISAREGQVDVASVLLE 558
Cdd:PHA02791   106 NMQTVKLFVkKNWRLMFYGKTGWKTSFYHAVMLNDVSIVSYFLSEIPSTfDLAIL--LSCIHITIKNGHVDMMILLLD 181
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 240-267 3.23e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 3.23e-03
                           10        20
                   ....*....|....*....|....*...
gi 1039763615  240 GFTPLHIAAHYGNVNVATLLLNRGAAVD 267
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02946 PHA02946
ankyin-like protein; Provisional
 380-632 3.41e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 43.12  E-value: 3.41e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  380 AHCG----HYRVTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELLVKYGASIQAITESGLTPIHVAAFMGHLNI-- 453
Cdd:PHA02946    43 AYCGikglDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIer 122

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  454 VLLLLQNGASPDVTNIRGETALHMAARAGQVEVVRCLLRNG--ALVDARAREEQTPLHIASRLGKTEIVQLLLQHMAHPD 531
Cdd:PHA02946   123 INLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGfeARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPS 202

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  532 AATTNGYTPLHI--SAREGQVDVASVLLEAGAAHSlATKKGFTPLHVAAKYGSLD--VAKLLLQRRAAADSAgkngltpL 607
Cdd:PHA02946   203 KPDHDGNTPLHIvcSKTVKNVDIINLLLPSTDVNK-QNKFGDSPLTLLIKTLSPAhlINKLLSTSNVITDQT-------V 274

                          250       260
                   ....*....|....*....|....*
gi 1039763615  608 HVAAHYDNQKVALLLLEKGASPHAT 632
Cdd:PHA02946   275 NICIFYDRDDVLEIINDKGKQYDST 299
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 569-597 3.42e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 3.42e-03
                           10        20
                   ....*....|....*....|....*....
gi 1039763615  569 KGFTPLHVAAKYGSLDVAKLLLQRRAAAD 597
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 636-789 3.73e-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: 43.30  E-value: 3.73e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  636 GYTPLHIAAKKNQMQIASTLLNYGAETNTVT-------KQGVT------PLHLASQEGHTDMVTLLLDKG---ANIHMST 699
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqkKQGTCfyfgelPLSLAACTKQWDVVNYLLENPhqpASLQAQD 173

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  700 KSGLTSLHLAaqedkVNVADiltkhgaDRDAYTKLgytplivachygNVKMVNFLLKQGANVNAKTK-------NGYTPL 772
Cdd:cd22197    174 SLGNTVLHAL-----VMIAD-------NSPENSAL------------VIKMYDGLLQAGARLCPTVQleeisnhEGLTPL 229

                          170
                   ....*....|....*..
gi 1039763615  773 HQAAQQGHTHIINVLLQ 789
Cdd:cd22197    230 KLAAKEGKIEIFRHILQ 246
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 389-466 3.86e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 41.02  E-value: 3.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  389 KLLLDKRANPNAR-ALNGFTPLHIACKKNRIKVMELLVKY-GASIQAITESGLTPIHVAAFMGHLNIVLLLLQNGASPDV 466
Cdd:PHA02736    75 KLLMEWGADINGKeRVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCKV 154
PHA02791 PHA02791
ankyrin-like protein; Provisional
 83-232 3.91e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 42.34  E-value: 3.91e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   83 LHLAAKEGHVGLVQELLGRGSSVDSATKKGNTALHIASLAGQAEVVKVLVKEGANINAQSQNGF-TPLYMAAQENHIDVV 161
Cdd:PHA02791    65 LHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIV 144

                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039763615  162 KYLLengaNQSTATEDGFTPLA---VALQQGHNQAVAILLE-----NDTKGKVRLPALHIAARKDDTKSAALLLQNDHN 232
Cdd:PHA02791   145 SYFL----SEIPSTFDLAILLScihITIKNGHVDMMILLLDymtstNTNNSLLFIPDIKLAIDNKDLEMLQALFKYDIN 219
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 536-561 3.92e-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: 3.92e-03
                            10        20
                    ....*....|....*....|....*.
gi 1039763615   536 NGYTPLHISAREGQVDVASVLLEAGA 561
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGA 26
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 603-717 4.06e-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: 43.30  E-value: 4.06e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  603 GLTPLHVAAHYDNQKVALLLLEKGASPHATA------KN-------GYTPLHIAAKKNQMQIASTLLNYGAETNTVTKQ- 668
Cdd:cd22197     94 GHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqKKqgtcfyfGELPLSLAACTKQWDVVNYLLENPHQPASLQAQd 173

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039763615  669 --GVTPLHLA-----SQEGHTDMVTL----LLDKGANI-------HMSTKSGLTSLHLAAQEDKVNV 717
Cdd:cd22197    174 slGNTVLHALvmiadNSPENSALVIKmydgLLQAGARLcptvqleEISNHEGLTPLKLAAKEGKIEI 240
PHA03378 PHA03378
EBNA-3B; Provisional
 1867-2057 4.32e-03

EBNA-3B; Provisional


Pssm-ID: 223065 [Multi-domain]  Cd Length: 991  Bit Score: 43.13  E-value: 4.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1867 HTPVSPSSKNEKLSPVSPSAKTERHSPVFSGKPEKhSPGSPSTKNERhsPVSSLKTERHTPGSPsgkTDKRPPVPSSGRT 1946
Cdd:PHA03378   671 HIPYQPSPTGANTMLPIQWAPGTMQPPPRAPTPMR-PPAAPPGRAQR--PAAATGRARPPAAAP---GRARPPAAAPGRA 744

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 1947 EkhPPVSPGKTEKHLPGSPSIRTPEKPAPGSATGKHEKHLPVSPgktEKQPPISPTSKTERIEETMSVRELMKAFQSGQD 2026
Cdd:PHA03378   745 R--PPAAAPGRARPPAAAPGRARPPAAAPGAPTPQPPPQAPPAP---QQRPRGAPTPQPPPQAGPTSMQLMPRAAPGQQG 819

                          170       180       190
                   ....*....|....*....|....*....|.
gi 1039763615 2027 PSKHKTGLFEHKSAKQKQPQDKSKSRVEKEK 2057
Cdd:PHA03378   820 PTKQILRQLLTGGVKRGRPSLKKPAALERQA 850
Ank_5 pfam13857
Ankyrin repeats (many copies);
688-742 4.40e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 4.40e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1039763615  688 LLDKG-ANIHMSTKSGLTSLHLAAQEDKVNVADILTKHGADRDAYTKLGYTPLIVA 742
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 363-492 4.64e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 42.86  E-value: 4.64e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  363 APVDDVTLDYLTALHVAAH--CGHYrvTKLLLDKRANPNARALNGF--------------TPLHIACKKNRIKVMELLVK 426
Cdd:cd22193     67 AEYTDEYYEGQTALHIAIErrQGDI--VALLVENGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLE 144

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  427 YG---ASIQAITESGLTPIH----VA-------AFMGHLNIVLLLLQNGASPDV-----TNIRGETALHMAARAGQVEVV 487
Cdd:cd22193    145 NEhqpADIEAQDSRGNTVLHalvtVAdntkentKFVTRMYDMILIRGAKLCPTVeleeiRNNDGLTPLQLAAKMGKIEIL 224


                   ....*
gi 1039763615  488 RCLLR 492
Cdd:cd22193    225 KYILQ 229
PHA02798 PHA02798
ankyrin-like protein; Provisional
 352-577 4.83e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.90  E-value: 4.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  352 VECVKHLLQYKAPVDDVTLDYLTAL-HVAAHCGHYR----VTKLLLDKRANPNARALNGFTPLHIACKKNRIKVMELL-- 424
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLcTILSNIKDYKhmldIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILlf 130

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  425 -VKYGASIQAITESGLTPIHVAAFMGH---LNIVLLLLQNGASPDV-TNIRGETALHMAARAG----QVEVVRCLLRNGA 495
Cdd:PHA02798   131 mIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNidriDADILKLFVDNGF 210

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  496 LVDARAREEQT-------PLHIASRLGKTEIVQLLLQHMahpDAATTN--GYTPLHISAREGQVDVASVLLEAGAAHSLA 566
Cdd:PHA02798   211 IINKENKSHKKkfmeylnSLLYDNKRFKKNILDFIFSYI---DINQVDelGFNPLYYSVSHNNRKIFEYLLQLGGDINII 287

                          250
                   ....*....|.
gi 1039763615  567 TKKGFTPLHVA 577
Cdd:PHA02798   288 TELGNTCLFTA 298
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 669-697 4.92e-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: 4.92e-03
                           10        20
                   ....*....|....*....|....*....
gi 1039763615  669 GVTPLHLASQEGHTDMVTLLLDKGANIHM 697
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 371-400 5.02e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 5.02e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1039763615  371 DYLTALHVAAHCGHYRVTKLLLDKRANPNA 400
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 636-789 5.05e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 42.86  E-value: 5.05e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  636 GYTPLHIAAKKNQMQIASTLLNYGAETNTVTKQ--------------GVTPLHLASQEGHTDMVTLLLD---KGANIHMS 698
Cdd:cd22193     76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLEnehQPADIEAQ 155

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  699 TKSGLTSLHLAaqedkVNVADiltkHGADRDAYTKlgytplivachygnvKMVNFLLKQGANVNAKTK-------NGYTP 771
Cdd:cd22193    156 DSRGNTVLHAL-----VTVAD----NTKENTKFVT---------------RMYDMILIRGAKLCPTVEleeirnnDGLTP 211

                          170
                   ....*....|....*...
gi 1039763615  772 LHQAAQQGHTHIINVLLQ 789
Cdd:cd22193    212 LQLAAKMGKIEILKYILQ 229
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 304-429 5.12e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 40.63  E-value: 5.12e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  304 RDGLTPLHCAARSGhdQVVELLLERKAP-------LLARTKNGLSPLHMAAQGDHV---ECVKHLLQYKAPVD-DVTLDY 372
Cdd:PHA02736    15 IEGENILHYLCRNG--GVTDLLAFKNAIsdenrylVLEYNRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINgKERVFG 92

                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039763615  373 LTALHVAAHCGHYRVTKLLLdKRANPNARALNGF--TPLHIACKKNRIKVMELLVKYGA 429
Cdd:PHA02736    93 NTPLHIAVYTQNYELATWLC-NQPGVNMEILNYAfkTPYYVACERHDAKMMNILRAKGA 150
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 78-106 5.22e-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: 5.22e-03
                            10        20
                    ....*....|....*....|....*....
gi 1039763615    78 NGLNALHLAAKEGHVGLVQELLGRGSSVD 106
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02741 PHA02741
hypothetical protein; Provisional
 631-732 5.32e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 40.80  E-value: 5.32e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  631 ATAKNGYTPLHIAAKKNQMQIASTLLNY----GAETNTVTK-QGVTPLHLASQEGHTDMVTLLLDK-GANIHMSTKSGLT 704
Cdd:PHA02741    55 ATDDAGQMCIHIAAEKHEAQLAAEIIDHlielGADINAQEMlEGDTALHLAAHRRDHDLAEWLCCQpGIDLHFCNADNKS 134

                           90       100
                   ....*....|....*....|....*...
gi 1039763615  705 SLHLAAQEDKVNVADILTKHGADRDAYT 732
Cdd:PHA02741   135 PFELAIDNEDVAMMQILREIVATSRGFS 162
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 536-561 6.03e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 6.03e-03
                           10        20
                   ....*....|....*....|....*..
gi 1039763615  536 NGYTPLHISA-REGQVDVASVLLEAGA 561
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGA 27
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 539-675 6.77e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.96  E-value: 6.77e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  539 TPLH--ISAREGQVDVASVLLEAGAAHSLATK-KGFTPLHVAAKYG---SLDVAKLLLQRRAAADSAGKNGLTPLHVaaH 612
Cdd:PHA02859    53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRdNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHM--Y 130

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1039763615  613 YDNQKVAL----LLLEKGASPHATAKNGYTPLH--IAAKKNQmQIASTLLNYGAETNTVTKQGVTPLHL 675
Cdd:PHA02859   131 MCNFNVRInvikLLIDSGVSFLNKDFDNNNILYsyILFHSDK-KIFDFLTSLGIDINETNKSGYNCYDL 198
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 635-664 6.81e-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: 36.85  E-value: 6.81e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1039763615  635 NGYTPLHIAAKKNQMQIASTLLNYGAETNT 664
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 76-169 7.13e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 40.24  E-value: 7.13e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615   76 NQNGLNALHLAAKEGHVGLVQE---LLGRGSSVDSATKK-GNTALHIASLAGQAEVVKVLVKE-GANINAQSQNGFTPLY 150
Cdd:PHA02736    52 NRHGKQCVHIVSNPDKADPQEKlklLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYY 131

                           90
                   ....*....|....*....
gi 1039763615  151 MAAQENHIDVVKYLLENGA 169
Cdd:PHA02736   132 VACERHDAKMMNILRAKGA 150
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 638-771 7.28e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.96  E-value: 7.28e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  638 TPLH--IAAKKNQMQIASTLLNYGAETNTVTK-QGVTPLH--LASQEG-HTDMVTLLLDKGANIHMSTKSGLTSLH--LA 709
Cdd:PHA02859    53 TPIFscLEKDKVNVEILKFLIENGADVNFKTRdNNLSALHhyLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHmyMC 132

                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039763615  710 AQEDKVNVADILTKHGA-----DRDAYTKLgYTPLIvacHYGNVKMVNFLLKQGANVNAKTKNGYTP 771
Cdd:PHA02859   133 NFNVRINVIKLLIDSGVsflnkDFDNNNIL-YSYIL---FHSDKKIFDFLTSLGIDINETNKSGYNC 195
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 240-426 7.37e-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: 7.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  240 GFTPLHIAA---HYGNVNVATLLLNRGAAVDFTAR-----------NGITPLHVASKRGNTNMVKLLLDRGGQIDAKTRD 305
Cdd:cd21882     26 GKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSARATG 105

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615  306 -------------GLTPLHCAARSGHDQVVELLLErkapllartkNGLSPLHMAAQGDHVECVKHLL--QYKAPVDD--- 367
Cdd:cd21882    106 rffrkspgnlfyfGELPLSLAACTNQEEIVRLLLE----------NGAQPAALEAQDSLGNTVLHALvlQADNTPENsaf 175

                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1039763615  368 VTLDYLTALHVAAHCGHYRVTKLLldkranPNARalnGFTPLHIACKKNRIKVMELLVK 426
Cdd:cd21882    176 VCQMYNLLLSYGAHLDPTQQLEEI------PNHQ---GLTPLKLAAVEGKIVMFQHILQ 225
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 736-805 8.20e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.96  E-value: 8.20e-03
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039763615  736 YTPLIVAC---HYGNVKMVNFLLKQGANVNAKTK-NGYTPLH---QAAQQGHTHIINVLLQHGAKPNATTANGNTAL 805
Cdd:PHA02859    51 YETPIFSClekDKVNVEILKFLIENGADVNFKTRdNNLSALHhylSFNKNVEPEILKILIDSGSSITEEDEDGKNLL 127
PHA03095 PHA03095
ankyrin-like protein; Provisional
 748-805 9.37e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.93  E-value: 9.37e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1039763615  748 VKMVNFLLKQGANVNAKTKNGYTPLHQAAQQGH---THIINVLLQHGAKPNATTANGNTAL 805
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPL 87
PRK10263 PRK10263
DNA translocase FtsK; Provisional
 2369-2737 9.83e-03

DNA translocase FtsK; Provisional


Pssm-ID: 236669 [Multi-domain]  Cd Length: 1355  Bit Score: 41.99  E-value: 9.83e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 2369 ESQLPLVSSAFKTQSESETQESLTPSEVTKPFP-PSDASVKTAEGTEPKPQGAIRSPQGLELPlpnrDSEVLSPMADESL 2447
Cdd:PRK10263   402 QPQQPYYAPAAEQPAQQPYYAPAPEQPAQQPYYaPAPEQPVAGNAWQAEEQQSTFAPQSTYQT----EQTYQQPAAQEPL 477

                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 2448 -----AVSHKDSLEASPVLEDNSSHKTP----DSLEPSPLKEspcRDSL------------ESSPVEPKMKAGILPSHFP 2506
Cdd:PRK10263   478 yqqpqPVEQQPVVEPEPVVEETKPARPPlyyfEEVEEKRARE---REQLaawyqpipepvkEPEPIKSSLKAPSVAAVPP 554

                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 2507 LPAAIAKTDLVAEVASMRSRLLRDPDGSAEDDSLEQTSLMESSGKSPLSPDTPSSEEVsyEVTPKPSDSS----TPKPAV 2582
Cdd:PRK10263   555 VEAAAAVSPLASGVKKATLATGAAATVAAPVFSLANSGGPRPQVKEGIGPQLPRPKRI--RVPTRRELASygikLPSQRA 632

                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 2583 IHECAEEDDSENGEKKRFTPEEEMFKMVTkiktfDELEQE--AKQKRDYKKEPRQDGSSSASDpdADYSAEVNDEKQMAG 2660
Cdd:PRK10263   633 AEEKAREAQRNQYDSGDQYNDDEIDAMQQ-----DELARQfaQTQQQRYGEQYQHDVPVNAED--ADAAAEAELARQFAQ 705

                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1039763615 2661 TEGE---GEVPvlvtSENRKVSSSSSESEPELTQLSKGADSGLLTEPVIRVQPPSPLPSSIDSNSSPEeatqfQPIVPKQ 2737
Cdd:PRK10263   706 TQQQrysGEQP----AGANPFSLDDFEFSPMKALLDDGPHEPLFTPIVEPVQQPQQPVAPQQQYQQPQ-----QPVAPQP 776
Death_TNFR1 cd08313
Death domain of Tumor Necrosis Factor Receptor 1; Death Domain (DD) found in tumor necrosis ...
 3596-3662 9.93e-03

Death domain of Tumor Necrosis Factor Receptor 1; Death Domain (DD) found in tumor necrosis factor receptor-1 (TNFR-1). TNFR-1 has many names including TNFRSF1A, CD120a, p55, p60, and TNFR60. It activates two major intracellular signaling pathways that lead to the activation of the transcription factor NF-kB and the induction of cell death. Upon binding of its ligand TNF, TNFR-1 trimerizes which leads to the recruitment of an adaptor protein named TNFR-associated death domain protein (TRADD) through a DD/DD interaction. Mutations in the TNFRSF1A gene causes TNFR-associated periodic syndrome (TRAPS), a rare disorder characterized recurrent fever, myalgia, abdominal pain, conjunctivitis and skin eruptions. 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: 176729  Cd Length: 80  Bit Score: 37.75  E-value: 9.93e-03
                           10        20        30        40        50        60
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1039763615 3596 WTELARELDFTEEQIHQIRIENpNSLQDQSHALLKYWLERDGKHATDTILIECltKINRMDIVHLLE 3662
Cdd:cd08313     14 WKEFVRRLGLSDNEIERVELDH-RRCRDAQYQMLKVWKERGPRPYATLQHLLS--VLRDMELVGCAE 77
 
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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