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Conserved domains on  [gi|767922798|ref|XP_011531844|]
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serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A isoform X4 [Homo sapiens]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
26-315 3.02e-50

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 179.38  E-value: 3.02e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   26 AEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNV 105
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  106 NVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAA 185
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  186 ASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALcLELLV 265
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 767922798  266 GNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPL 315
Cdd:COG0666   240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
512-749 7.41e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.56  E-value: 7.41e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  512 DMLSDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGASILVKDYiLKRT 591
Cdd:COG0666    44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGET 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  592 PIHAAATNGHSECLRLLIGNaepqNA-VDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGH 670
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEA----GAdVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767922798  671 EECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAasmdANPATADNHGYTALHWACYNGHETCVELLLE 749
Cdd:COG0666   199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG----ADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
709-953 1.35e-33

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.23  E-value: 1.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  709 ALLQSAASMDANPATADNHGYTALHWACYNGHETCVELLLEQEVF-QKTEGNAFSPLHCAVINDNEGAAEMLIDtLGASi 787
Cdd:COG0666    35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADiNAKDDGGNTLLHAAARNGDLEIVKLLLE-AGAD- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  788 VNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSsASAELTLQDNSKNTALH 867
Cdd:COG0666   113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLH 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  868 LACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADC 947
Cdd:COG0666   192 LAAENGHLEIVKLLLEAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268

                  ....*.
gi 767922798  948 LALILA 953
Cdd:COG0666   269 KLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
197-475 9.39e-33

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.92  E-value: 9.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  197 LLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSK 276
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  277 DGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGF 356
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  357 SDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASV 436
Cdd:COG0666   166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767922798  437 NDLDERGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDK 475
Cdd:COG0666   246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
26-315 3.02e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 179.38  E-value: 3.02e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   26 AEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNV 105
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  106 NVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAA 185
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  186 ASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALcLELLV 265
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 767922798  266 GNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPL 315
Cdd:COG0666   240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
6-273 1.50e-38

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 149.43  E-value: 1.50e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798    6 LRDQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLH-----RAVASCSEEAVQVLLKHSADVNARDKNWQ 80
Cdd:PHA03100   28 NDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   81 TPLHIAAANKavkcaealvpllsnvnvsdragrtalhhaafSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHI-- 158
Cdd:PHA03100  108 TPLLYAISKK-------------------------------SNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdl 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  159 EVVKLLVSHGAEVTCKDKksytplhaaassgmisvVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVN 238
Cdd:PHA03100  157 KILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPN 219
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767922798  239 QKNEKGFTPLHFAAASTHGALcLELLVGNGADVNM 273
Cdd:PHA03100  220 LVNKYGDTPLHIAILNNNKEI-FKLLLNNGPSIKT 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
512-749 7.41e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.56  E-value: 7.41e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  512 DMLSDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGASILVKDYiLKRT 591
Cdd:COG0666    44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGET 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  592 PIHAAATNGHSECLRLLIGNaepqNA-VDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGH 670
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEA----GAdVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767922798  671 EECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAasmdANPATADNHGYTALHWACYNGHETCVELLLE 749
Cdd:COG0666   199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG----ADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
709-953 1.35e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.23  E-value: 1.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  709 ALLQSAASMDANPATADNHGYTALHWACYNGHETCVELLLEQEVF-QKTEGNAFSPLHCAVINDNEGAAEMLIDtLGASi 787
Cdd:COG0666    35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADiNAKDDGGNTLLHAAARNGDLEIVKLLLE-AGAD- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  788 VNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSsASAELTLQDNSKNTALH 867
Cdd:COG0666   113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLH 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  868 LACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADC 947
Cdd:COG0666   192 LAAENGHLEIVKLLLEAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268

                  ....*.
gi 767922798  948 LALILA 953
Cdd:COG0666   269 KLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
197-475 9.39e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.92  E-value: 9.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  197 LLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSK 276
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  277 DGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGF 356
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  357 SDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASV 436
Cdd:COG0666   166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767922798  437 NDLDERGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDK 475
Cdd:COG0666   246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
PHA03095 PHA03095
ankyrin-like protein; Provisional
191-447 4.15e-31

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 128.22  E-value: 4.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  191 ISVVKYLLDLGVDMNEPNAYGNTPLHV--ACYNGQDV-VVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGN 267
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLylHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  268 GADVNMKSKDGKTPLH--MTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGH---ELLiNTLITSGADTAKRGI 342
Cdd:PHA03095  107 GADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGADVYAVDD 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  343 HGMFPLHLAALS--GFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLL--NTGADFNKKDKFGRSPLHYAA 418
Cdd:PHA03095  186 RFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPllIAGISINARNRYGQTPLHYAA 265
                         250       260       270
                  ....*....|....*....|....*....|
gi 767922798  419 ANCNyQCLFA-LVGSGASVNDLDERGCTPL 447
Cdd:PHA03095  266 VFNN-PRACRrLIALGADINAVSSDGNTPL 294
PHA02874 PHA02874
ankyrin repeat protein; Provisional
526-835 8.40e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 102.73  E-value: 8.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  526 LHLAAYHGHHQALEVLVQS---LLDLDVRNSSgrTPLDLAAFKGHVECVDVLINQGASIlvkDYILKRTP--IHAAATNG 600
Cdd:PHA02874    5 LRMCIYSGDIEAIEKIIKNkgnCINISVDETT--TPLIDAIRSGDAKIVELFIKHGADI---NHINTKIPhpLLTAIKIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  601 HSECLRLLIgnaepQNAVDIQdgngqtplMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQH 680
Cdd:PHA02874   80 AHDIIKLLI-----DNGVDTS--------ILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEY 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  681 GAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAASMDANpataDNHGYTALHWACYNGHETCVELLLEQ--EVFQKTEg 758
Cdd:PHA02874  147 GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK----DNNGESPLHNAAEYGDYACIKLLIDHgnHIMNKCK- 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767922798  759 NAFSPLHCAVINdNEGAAEMLIDTlgASIvNATDSKGRTPLH-AAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMA 835
Cdd:PHA02874  222 NGFTPLHNAIIH-NRSAIELLINN--ASI-NDQDIDGSTPLHhAINPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
116-208 7.59e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 7.59e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   116 LHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHgAEVTCKDKKsYTPLHAAASSGMISVVK 195
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 767922798   196 YLLDLGVDMNEPN 208
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
625-954 4.25e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 91.62  E-value: 4.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  625 GQTPLMLSVLNGHTDC---VYSLLNKGANVDAKDKWGRTALH---RGAVTghEECVDALLQHGAKCLLRDSRGRTPIH-- 696
Cdd:PHA03095   47 GKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHlylYNATT--LDVIKLLIKAGADVNAKDKVGRTPLHvy 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  697 LSAACGHIGVLGALLQsaasMDANPATADNHGYTalhwacynghetcvellleqevfqktegnafsPLHCAVINdnegaa 776
Cdd:PHA03095  125 LSGFNINPKVIRLLLR----KGADVNALDLYGMT--------------------------------PLAVLLKS------ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  777 emlidtlgasiVNATdskgrtplhaaaftdhVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNT--VEMLVSsASAE 854
Cdd:PHA03095  163 -----------RNAN----------------VELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRAriVRELIR-AGCD 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  855 LTLQDNSKNTALHLACSKGHETSALLI--LEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGY 932
Cdd:PHA03095  215 PAATDMLGNTPLHSMATGSSCKRSLVLplLIAGIS---INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGN 291
                         330       340
                  ....*....|....*....|..
gi 767922798  933 TPALACAPNKDVaDCLALILAT 954
Cdd:PHA03095  292 TPLSLMVRNNNG-RAVRAALAK 312
Ank_2 pfam12796
Ankyrin repeats (3 copies);
593-688 2.48e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 2.48e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   593 IHAAATNGHSECLRLLIgnaEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKgANVDAKDKwGRTALHRGAVTGHEE 672
Cdd:pfam12796    1 LHLAAKNGNLELVKLLL---ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE 75
                           90
                   ....*....|....*.
gi 767922798   673 CVDALLQHGAKCLLRD 688
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
799-892 1.75e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.75e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   799 LHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSASAELtlqDNSKNTALHLACSKGHETSA 878
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 767922798   879 LLILEKITDRNLIN 892
Cdd:pfam12796   78 KLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
46-231 5.52e-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: 76.20  E-value: 5.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   46 WLTPLHRAVASCSEEAVQVLLK-HSADVNARDKNWQTPLHIAAANKAVKCAEAL---VPLLSNVNV-SD-RAGRTALHHA 119
Cdd:cd22192    17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLmeaAPELVNEPMtSDlYQGETALHIA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  120 AFSGHGEMVKLLLSRGANIN-------AFDKKDRRAIHW-------AAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAA 185
Cdd:cd22192    97 VVNQNLNLVRELIARGADVVspratgtFFRPGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767922798  186 ASSGMISVVKYLLDLGVDMNE----------PNAYGNTPLHVACYNGQDVVVNELI 231
Cdd:cd22192   177 VLQPNKTFACQMYDLILSYDKeddlqpldlvPNNQGLTPFKLAAKEGNIVMFQHLV 232
Ank_2 pfam12796
Ankyrin repeats (3 copies);
282-374 9.68e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 9.68e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   282 LHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGAdtAKRGIHGMFPLHLAALSGFSDCCR 361
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 767922798   362 KLLSSGFDIDTPD 374
Cdd:pfam12796   79 LLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
557-697 1.58e-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: 61.95  E-value: 1.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  557 TPLDLAAFKGHVECVDVLINQGASILVKDYILKRTPIHAAATNGHSECLRLLIGNA-----EPQNAVDIQdgnGQTPLML 631
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelvnEPMTSDLYQ---GETALHI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  632 SVLNGHTDCVYSLLNKGANV--------------DAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHL 697
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
546-769 4.43e-08

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 57.40  E-value: 4.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   546 LDLDVRNSSGRTPLDLAAFKG-HVECVDVLINQGASILVKDyilkrTPIHAAATNGH---SECLRLLIGNAE----PQNA 617
Cdd:TIGR00870   43 LNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGD-----TLLHAISLEYVdavEAILLHLLAAFRksgpLELA 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   618 VDIQDGN---GQTPLMLSVLNGHTDCVYSLLNKGANVDAKDK--------------WGRTALHRGAVTGHEECVDALLQH 680
Cdd:TIGR00870  118 NDQYTSEftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSED 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   681 GAKCLLRDSRGRTPIHLSAACGHIGVLGALL-----QSAASMDANPATAD------NH-GYTALHWACYNGHETCVELLL 748
Cdd:TIGR00870  198 PADILTADSLGNTLLHLLVMENEFKAEYEELscqmyNFALSLLDKLRDSKelevilNHqGLTPLKLAAKEGRIVLFRLKL 277
                          250       260
                   ....*....|....*....|..
gi 767922798   749 EQEVFQKT-EGNAFSPLHCAVI 769
Cdd:TIGR00870  278 AIKYKQKKfVAWPNGQQLLSLY 299
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
677-850 6.58e-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: 56.56  E-value: 6.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  677 LLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAASMDANPATADNH-GYTALHWACYNGHETCVELLLEQ----- 750
Cdd:cd22192    37 LKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDLYqGETALHIAVVNQNLNLVRELIARgadvv 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  751 ------EVFQKTEGNAF----SPLHCAVINDNEGAAEMLIDTlGASIVnATDSKGRTPLHAAAF----TDHVECLQLLLS 816
Cdd:cd22192   117 spratgTFFRPGPKNLIyygeHPLSFAACVGNEEIVRLLIEH-GADIR-AQDSLGNTVLHILVLqpnkTFACQMYDLILS 194
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 767922798  817 HNAQVNSV------DSTGKTPLMMAAENGQTNTVEMLVSS 850
Cdd:cd22192   195 YDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQHLVQK 234
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
39-219 1.70e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 55.47  E-value: 1.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798    39 VNAKDSKWLTPLHRAVA-SCSEEAVQVLLKHSADVNARDknwqTPLHIAAANKAVKCAEALVPLLSN---------VNVS 108
Cdd:TIGR00870   45 INCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAISLEYVDAVEAILLHLLAAfrksgplelANDQ 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   109 DR----AGRTALHHAAFSGHGEMVKLLLSRGANINA------FDKKDRRA--------IHWAAYMGHIEVVKLLVSHGAE 170
Cdd:TIGR00870  121 YTseftPGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDsfyhgespLNAAACLGSPSIVALLSEDPAD 200
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767922798   171 VTCKDKKSYTPLHAAA------------SSGMISVVKYLLDLGVDMNE----PNAYGNTPLHVAC 219
Cdd:TIGR00870  201 ILTADSLGNTLLHLLVmenefkaeyeelSCQMYNFALSLLDKLRDSKEleviLNHQGLTPLKLAA 265
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
246-451 1.39e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.32  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  246 TPLhFAAASTHGALCLE-LLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGA-----VIDCEDKNGNTPLHIAA 319
Cdd:cd22192    19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPelvnePMTSDLYQGETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  320 RYGHELLINTLITSGADTAKRGIHGMFplhlaalsgFSDCCRKLLSsgfdidtpddFGRTCLHAAAAGGNLECLNLLLNT 399
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSPRATGTF---------FRPGPKNLIY----------YGEHPLSFAACVGNEEIVRLLIEH 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767922798  400 GADFNKKDKFGRSPLHYAA--ANCNYQC-----LFALVGSGASVNdLD----ERGCTPLHYAA 451
Cdd:cd22192   159 GADIRAQDSLGNTVLHILVlqPNKTFACqmydlILSYDKEDDLQP-LDlvpnNQGLTPFKLAA 220
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
112-140 1.87e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 1.87e-05
                            10        20
                    ....*....|....*....|....*....
gi 767922798    112 GRTALHHAAFSGHGEMVKLLLSRGANINA 140
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
794-822 5.48e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 5.48e-04
                            10        20
                    ....*....|....*....|....*....
gi 767922798    794 KGRTPLHAAAFTDHVECLQLLLSHNAQVN 822
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
310-336 1.10e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 1.10e-03
                            10        20
                    ....*....|....*....|....*..
gi 767922798    310 NGNTPLHIAARYGHELLINTLITSGAD 336
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
727-749 1.27e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 1.27e-03
                            10        20
                    ....*....|....*....|...
gi 767922798    727 HGYTALHWACYNGHETCVELLLE 749
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLD 23
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
363-543 4.38e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.83  E-value: 4.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   363 LLSSGFDIDTpddfGRTCLHAA-----------------AAGGNLECLNLLLNTGADFNkkdkFGRSPLHYAAANCNYQC 425
Cdd:TIGR00870   72 LLNLSCRGAV----GDTLLHAIsleyvdaveaillhllaAFRKSGPLELANDQYTSEFT----PGITALHLAAHRQNYEI 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   426 LFALVGSGASVN--------------DLDERGCTPLH-YAATSDTDgkCLEYLLRNDANPGIRDKQGYNAVH-------Y 483
Cdd:TIGR00870  144 VKLLLERGASVParacgdffvksqgvDSFYHGESPLNaAACLGSPS--IVALLSEDPADILTADSLGNTLLHllvmeneF 221
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767922798   484 SAAYGH--RLCLQLIasetpLDVLMETSGTDMLSDSDNRATISPLHLAAYHGHHQALEVLVQ 543
Cdd:TIGR00870  222 KAEYEElsCQMYNFA-----LSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
738-918 9.10e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.06  E-value: 9.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   738 NGHETCVELLLEQEVFQKTEGNAfspLHCAVINDnEGAAEMLI--------DTLGASIVNATD----SKGRTPLHAAAFT 805
Cdd:TIGR00870   63 NENLELTELLLNLSCRGAVGDTL---LHAISLEY-VDAVEAILlhllaafrKSGPLELANDQYtsefTPGITALHLAAHR 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   806 DHVECLQLLLSHNAQVNS------------VDST--GKTPLMMAAENGQTNTVEMLvSSASAELTLQDNSKNTALHL--- 868
Cdd:TIGR00870  139 QNYEIVKLLLERGASVPAracgdffvksqgVDSFyhGESPLNAAACLGSPSIVALL-SEDPADILTADSLGNTLLHLlvm 217
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   869 ---------ACSKGHETSALLILEKITD-RNLINATNAALQTPLHVAARNGLTMVVQELL 918
Cdd:TIGR00870  218 enefkaeyeELSCQMYNFALSLLDKLRDsKELEVILNHQGLTPLKLAAKEGRIVLFRLKL 277
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
26-315 3.02e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 179.38  E-value: 3.02e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   26 AEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNV 105
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  106 NVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAA 185
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  186 ASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALcLELLV 265
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLL 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 767922798  266 GNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPL 315
Cdd:COG0666   240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-280 1.28e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 174.76  E-value: 1.28e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798    1 MAFLKLRDQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQ 80
Cdd:COG0666     9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   81 TPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEV 160
Cdd:COG0666    89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  161 VKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQK 240
Cdd:COG0666   169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 767922798  241 NEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSKDGKT 280
Cdd:COG0666   249 DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
PHA03100 PHA03100
ankyrin repeat protein; Provisional
6-273 1.50e-38

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 149.43  E-value: 1.50e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798    6 LRDQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLH-----RAVASCSEEAVQVLLKHSADVNARDKNWQ 80
Cdd:PHA03100   28 NDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   81 TPLHIAAANKavkcaealvpllsnvnvsdragrtalhhaafSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHI-- 158
Cdd:PHA03100  108 TPLLYAISKK-------------------------------SNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdl 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  159 EVVKLLVSHGAEVTCKDKksytplhaaassgmisvVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVN 238
Cdd:PHA03100  157 KILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPN 219
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 767922798  239 QKNEKGFTPLHFAAASTHGALcLELLVGNGADVNM 273
Cdd:PHA03100  220 LVNKYGDTPLHIAILNNNKEI-FKLLLNNGPSIKT 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
512-749 7.41e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.56  E-value: 7.41e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  512 DMLSDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGASILVKDYiLKRT 591
Cdd:COG0666    44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGET 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  592 PIHAAATNGHSECLRLLIGNaepqNA-VDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGH 670
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEA----GAdVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767922798  671 EECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAasmdANPATADNHGYTALHWACYNGHETCVELLLE 749
Cdd:COG0666   199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG----ADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
126-447 9.26e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.47  E-value: 9.26e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  126 EMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMN 205
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  206 EPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKskdgktplhmt 285
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI-VKLLLEAGADVNAQ----------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  286 alhgrfsrsqtiiqsgavidceDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLS 365
Cdd:COG0666   150 ----------------------DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  366 SGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCT 445
Cdd:COG0666   208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287

                  ..
gi 767922798  446 PL 447
Cdd:COG0666   288 LL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
574-898 1.66e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.70  E-value: 1.66e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  574 LINQGASILVKDYILKRTPIHAAATNGHSECLRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDA 653
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  654 KDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSaasmDANPATADNHGYTALH 733
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA----GADVNAQDNDGNTPLH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  734 WACYNGHETCVELLLEQevfqktegnafsplhcavindneGAaemlidtlgasIVNATDSKGRTPLHAAAFTDHVECLQL 813
Cdd:COG0666   159 LAAANGNLEIVKLLLEA-----------------------GA-----------DVNARDNDGETPLHLAAENGHLEIVKL 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  814 LLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVsSASAELTLQDNSKNTALHLACSKGHETSALLILEKITDRNLINA 893
Cdd:COG0666   205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL-EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283

                  ....*
gi 767922798  894 TNAAL 898
Cdd:COG0666   284 DLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
605-935 5.12e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.55  E-value: 5.12e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  605 LRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKC 684
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  685 LLRDSRGRTPIHLSAACGHIGVLGALLQSaasmDANPATADNHGYTALHWACYNGHETCVELLLEQevfqktegnafspl 764
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEA----GADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-------------- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  765 hcavindnegaaemlidtlGASiVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTV 844
Cdd:COG0666   143 -------------------GAD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  845 EMLVsSASAELTLQDNSKNTALHLACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASV 924
Cdd:COG0666   203 KLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
                         330
                  ....*....|.
gi 767922798  925 LAVDENGYTPA 935
Cdd:COG0666   279 AAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
479-726 7.65e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.78  E-value: 7.65e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  479 NAVHYSAAYGHRLCLQLIASETPLDVLMETSGTDMLSDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTP 558
Cdd:COG0666    44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  559 LDLAAFKGHVECVDVLINQGASILVKDyILKRTPIHAAATNGHSECLRLLIGNaepqNA-VDIQDGNGQTPLMLSVLNGH 637
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLEIVKLLLEA----GAdVNARDNDGETPLHLAAENGH 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  638 TDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAASM 717
Cdd:COG0666   199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278

                  ....*....
gi 767922798  718 DANPATADN 726
Cdd:COG0666   279 AAALLDLLT 287
PHA03095 PHA03095
ankyrin-like protein; Provisional
14-282 7.98e-36

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 142.47  E-value: 7.98e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   14 RTPLHAaaYLG-----DAEIIELLILSGARVNAKDSKWLTPLHRAV-ASCSEEAVQVLLKHSADVNARDKNWQTPLHIAA 87
Cdd:PHA03095   48 KTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLyNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   88 ANKAVkcaealvpllsnvnvsdragrtalhhaafsgHGEMVKLLLSRGANINAFDKKDRRAIHwaAYMGH----IEVVKL 163
Cdd:PHA03095  126 SGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMTPLA--VLLKSrnanVELLRL 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  164 LVSHGAEVTCKDKKSYTPLHAAASSGMIS--VVKYLLDLGVDMNEPNAYGNTPLHVACYNG--QDVVVNELIDCGAIVNQ 239
Cdd:PHA03095  173 LIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINA 252
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 767922798  240 KNEKGFTPLHFAAASTHGALCLELLVGnGADVNMKSKDGKTPL 282
Cdd:PHA03095  253 RNRYGQTPLHYAAVFNNPRACRRLIAL-GADINAVSSDGNTPL 294
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
709-953 1.35e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.23  E-value: 1.35e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  709 ALLQSAASMDANPATADNHGYTALHWACYNGHETCVELLLEQEVF-QKTEGNAFSPLHCAVINDNEGAAEMLIDtLGASi 787
Cdd:COG0666    35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADiNAKDDGGNTLLHAAARNGDLEIVKLLLE-AGAD- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  788 VNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSsASAELTLQDNSKNTALH 867
Cdd:COG0666   113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLH 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  868 LACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADC 947
Cdd:COG0666   192 LAAENGHLEIVKLLLEAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268

                  ....*.
gi 767922798  948 LALILA 953
Cdd:COG0666   269 KLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
197-475 9.39e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.92  E-value: 9.39e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  197 LLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSK 276
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  277 DGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGF 356
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  357 SDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASV 436
Cdd:COG0666   166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767922798  437 NDLDERGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDK 475
Cdd:COG0666   246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
PHA02876 PHA02876
ankyrin repeat protein; Provisional
9-336 3.49e-32

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 134.42  E-value: 3.49e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798    9 QDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNwqtpLHIAAA 88
Cdd:PHA02876  174 KDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLS----LLKAIR 249
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   89 NKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGH-GEMVKLLLSRGANINAFDKKDRRAIHWAAYMGH-IEVVKLLVS 166
Cdd:PHA02876  250 NEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIM 329
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  167 HGAEVTCKDKKSYTPLHAAAS-SGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGF 245
Cdd:PHA02876  330 LGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG 409
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  246 TPLHFAAASTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHG-RFSRSQTIIQSGAVIDCEDKNGNTPLHIAarYGHE 324
Cdd:PHA02876  410 TALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYH 487
                         330
                  ....*....|..
gi 767922798  325 LLINTLITSGAD 336
Cdd:PHA02876  488 GIVNILLHYGAE 499
PHA03095 PHA03095
ankyrin-like protein; Provisional
58-331 4.11e-32

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 131.30  E-value: 4.11e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   58 SEEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLL---SNVNVSDRAGRTALH-HAAFSGHGEMVKLLLS 133
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLeagADVNAPERCGFTPLHlYLYNATTLDVIKLLIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  134 RGANINAFDKKDRRAIHwaAYMG----HIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISV--VKYLLDLGVDMNEP 207
Cdd:PHA03095  106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  208 NAYGNTPLHVACYNGQD--VVVNELIDCGAIVNQKNEKGFTPLHFAAA-STHGALCLELLVGNGADVNMKSKDGKTPLHM 284
Cdd:PHA03095  184 DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 767922798  285 TALHGR---FSRsqtIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLI 331
Cdd:PHA03095  264 AAVFNNpraCRR---LIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA02874 PHA02874
ankyrin repeat protein; Provisional
22-339 1.91e-31

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 128.54  E-value: 1.91e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   22 YLGDAEIIELLILS-GARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQTPLHIA---AANKAVK---- 93
Cdd:PHA02874   10 YSGDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAikiGAHDIIKllid 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   94 ----CAEALVPLLSNvnvsdragrtalhhaafsghgEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGA 169
Cdd:PHA02874   90 ngvdTSILPIPCIEK---------------------DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  170 EVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLH 249
Cdd:PHA02874  149 DVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLH 228
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  250 faAASTHGALCLELLVgNGADVNMKSKDGKTPLHMtALHGRFSRS--QTIIQSGAVIDCEDKNGNTPLHIAARYGH---- 323
Cdd:PHA02874  229 --NAIIHNRSAIELLI-NNASINDQDIDGSTPLHH-AINPPCDIDiiDILLYHKADISIKDNKGENPIDTAFKYINkdpv 304
                         330
                  ....*....|....*...
gi 767922798  324 --ELLINTLITSGADTAK 339
Cdd:PHA02874  305 ikDIIANAVLIKEADKLK 322
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
709-953 2.40e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.68  E-value: 2.40e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  709 ALLQSAASMDANPATADNHGYTALHWACYNGHETCVELLLEQEVFQKTEGNAFSPLHCAVINDNEGAAEMLIDTLGASIv 788
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  789 NATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVsSASAELTLQDNSKNTALHL 868
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  869 ACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADCL 948
Cdd:COG0666   160 AAANGNLEIVKLLLEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                  ....*
gi 767922798  949 ALILA 953
Cdd:COG0666   237 LLLEA 241
PHA03095 PHA03095
ankyrin-like protein; Provisional
191-447 4.15e-31

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 128.22  E-value: 4.15e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  191 ISVVKYLLDLGVDMNEPNAYGNTPLHV--ACYNGQDV-VVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGN 267
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLylHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  268 GADVNMKSKDGKTPLH--MTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGH---ELLiNTLITSGADTAKRGI 342
Cdd:PHA03095  107 GADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGADVYAVDD 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  343 HGMFPLHLAALS--GFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLL--NTGADFNKKDKFGRSPLHYAA 418
Cdd:PHA03095  186 RFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPllIAGISINARNRYGQTPLHYAA 265
                         250       260       270
                  ....*....|....*....|....*....|
gi 767922798  419 ANCNyQCLFA-LVGSGASVNDLDERGCTPL 447
Cdd:PHA03095  266 VFNN-PRACRrLIALGADINAVSSDGNTPL 294
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
235-497 1.00e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.14  E-value: 1.00e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  235 AIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTP 314
Cdd:COG0666    11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  315 LHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLN 394
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  395 LLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLLRNDANPGIRD 474
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENG-NLEIVKLLLEAGADLNAKD 249
                         250       260
                  ....*....|....*....|...
gi 767922798  475 KQGYNAVHYSAAYGHRLCLQLIA 497
Cdd:COG0666   250 KDGLTALLLAAAAGAALIVKLLL 272
PHA03095 PHA03095
ankyrin-like protein; Provisional
158-426 1.37e-30

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 126.68  E-value: 1.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  158 IEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGM---ISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDV-VVNELIDC 233
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  234 GAIVNQKNEKGFTPLH--FAAASTHgALCLELLVGNGADVNMKSKDGKTPLHMtalhgrFSRS--------QTIIQSGAV 303
Cdd:PHA03095  107 GADVNAKDKVGRTPLHvyLSGFNIN-PKVIRLLLRKGADVNALDLYGMTPLAV------LLKSrnanvellRLLIDAGAD 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  304 IDCEDKNGNTPLHIAARYGH--ELLINTLITSGADTAKRGIHGMFPLHLAALsgFSDCCR----KLLSSGFDIDTPDDFG 377
Cdd:PHA03095  180 VYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNTPLHSMAT--GSSCKRslvlPLLIAGISINARNRYG 257
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 767922798  378 RTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCL 426
Cdd:PHA03095  258 QTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAV 306
PHA02876 PHA02876
ankyrin repeat protein; Provisional
127-447 1.50e-30

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 129.03  E-value: 1.50e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  127 MVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNE 206
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  207 P-----NAYGNTPLHVACYngqdvvvneLIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSKDGKTP 281
Cdd:PHA02876  240 NdlsllKAIRNEDLETSLL---------LYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETP 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  282 LHMTALHGRFSRS-QTIIQSGAVIDCEDKNGNTPLHIAA---RYGHELLinTLITSGADTAKRGIHGMFPLHLAALSGFS 357
Cdd:PHA02876  311 LYLMAKNGYDTENiRTLIMLGADVNAADRLYITPLHQAStldRNKDIVI--TLLELGANVNARDYCDKTPIHYAAVRNNV 388
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  358 DCCRKLLSSGFDIDTPDDFGRTCLHAAAAG-GNLECLNLLLNTGADFNKKDKFGRSPLHYAAA-NCNYQCLFALVGSGAS 435
Cdd:PHA02876  389 VIINTLLDYGADIEALSQKIGTALHFALCGtNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKkNCKLDVIEMLLDNGAD 468
                         330
                  ....*....|..
gi 767922798  436 VNDLDERGCTPL 447
Cdd:PHA02876  469 VNAINIQNQYPL 480
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
261-559 9.12e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.06  E-value: 9.12e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  261 LELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKR 340
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  341 GIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAAN 420
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  421 CNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCLQLIASET 500
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENG-HLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767922798  501 PLDvlmetsgtdmlsDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPL 559
Cdd:COG0666   243 ADL------------NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
324-662 4.47e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.13  E-value: 4.47e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  324 ELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADF 403
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  404 NKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLLRNDANPGIRDKQGYnavhy 483
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG-NLEIVKLLLEAGADVNAQDNDGN----- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  484 saayghrlclqliasetpldvlmetsgtdmlsdsdnratiSPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAA 563
Cdd:COG0666   155 ----------------------------------------TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  564 FKGHVECVDVLINQGASILVKDYiLKRTPIHAAATNGHSECLRLLIGNAEpqnAVDIQDGNGQTPLMLSVLNGHTDCVYS 643
Cdd:COG0666   195 ENGHLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGA---DLNAKDKDGLTALLLAAAAGAALIVKL 270
                         330
                  ....*....|....*....
gi 767922798  644 LLNKGANVDAKDKWGRTAL 662
Cdd:COG0666   271 LLLALLLLAAALLDLLTLL 289
PHA02878 PHA02878
ankyrin repeat protein; Provisional
47-325 3.67e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 110.35  E-value: 3.67e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   47 LTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQTPLHIA--AANKavkcaEALVPLLSNVNVSD-----RAGRTALHHA 119
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckEPNK-----LGMKEMIRSINKCSvfytlVAIKDAFNNR 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  120 AFsghgEMVK-LLLSRGANINAFDKKDRRAIHWAAYMgHIEVVKLLVSHGAEVTCKDK-KSYTPLHAAASSGMISVVKYL 197
Cdd:PHA02878  113 NV----EIFKiILTNRYKNIQTIDLVYIDKKSKDDII-EAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELL 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  198 LDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSK- 276
Cdd:PHA02878  188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYi 267
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767922798  277 DGKTPLHMtALHGRfSRSQTIIQSGAVIDCEDKNGNTPLHIAA--RYGHEL 325
Cdd:PHA02878  268 LGLTALHS-SIKSE-RKLKLLLEYGADINSLNSYKLTPLSSAVkqYLCINI 316
PHA03100 PHA03100
ankyrin repeat protein; Provisional
158-372 7.16e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 108.60  E-value: 7.16e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  158 IEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLH---VACYNGQDVV--VNELID 232
Cdd:PHA03100   15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsNIKYNLTDVKeiVKLLLE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  233 CGAIVNQKNEKGFTPLHFAAASTHGALCL-ELLVGNGADVNMKSKDGKTPLHMtAL---HGRFSRSQTIIQSGA------ 302
Cdd:PHA03100   95 YGANVNAPDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHL-YLesnKIDLKILKLLIDKGVdinakn 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  303 ----------VIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDT 372
Cdd:PHA03100  174 rvnyllsygvPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02874 PHA02874
ankyrin repeat protein; Provisional
526-835 8.40e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 102.73  E-value: 8.40e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  526 LHLAAYHGHHQALEVLVQS---LLDLDVRNSSgrTPLDLAAFKGHVECVDVLINQGASIlvkDYILKRTP--IHAAATNG 600
Cdd:PHA02874    5 LRMCIYSGDIEAIEKIIKNkgnCINISVDETT--TPLIDAIRSGDAKIVELFIKHGADI---NHINTKIPhpLLTAIKIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  601 HSECLRLLIgnaepQNAVDIQdgngqtplMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQH 680
Cdd:PHA02874   80 AHDIIKLLI-----DNGVDTS--------ILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEY 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  681 GAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAASMDANpataDNHGYTALHWACYNGHETCVELLLEQ--EVFQKTEg 758
Cdd:PHA02874  147 GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK----DNNGESPLHNAAEYGDYACIKLLIDHgnHIMNKCK- 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767922798  759 NAFSPLHCAVINdNEGAAEMLIDTlgASIvNATDSKGRTPLH-AAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMA 835
Cdd:PHA02874  222 NGFTPLHNAIIH-NRSAIELLINN--ASI-NDQDIDGSTPLHhAINPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02874 PHA02874
ankyrin repeat protein; Provisional
213-491 1.29e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 101.96  E-value: 1.29e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  213 TPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLhFAAASTHGALCLELLVGNGADVNMkskdgktpLHMTALHGRFS 292
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPL-LTAIKIGAHDIIKLLIDNGVDTSI--------LPIPCIEKDMI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  293 RsqTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDT 372
Cdd:PHA02874  108 K--TILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  373 PDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAanCNYQCLFALVGSGASVNDLDERGCTPLHYAAT 452
Cdd:PHA02874  186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI--IHNRSAIELLINNASINDQDIDGSTPLHHAIN 263
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 767922798  453 SDTDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRL 491
Cdd:PHA02874  264 PPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKD 302
Ank_2 pfam12796
Ankyrin repeats (3 copies);
116-208 7.59e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 7.59e-21
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   116 LHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHgAEVTCKDKKsYTPLHAAASSGMISVVK 195
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 767922798   196 YLLDLGVDMNEPN 208
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
83-175 1.05e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.48  E-value: 1.05e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798    83 LHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRgANINAFDkKDRRAIHWAAYMGHIEVVK 162
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 767922798   163 LLVSHGAEVTCKD 175
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
16-289 1.28e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 96.49  E-value: 1.28e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   16 PLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLK------------------HSADVNA--- 74
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcsvfytlvaikdafNNRNVEIfki 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   75 ----RDKNWQTP--LHIAAANKAVKCAEALVPLL----SNVNVSDR-AGRTALHHAAFSGHGEMVKLLLSRGANINAFDK 143
Cdd:PHA02878  120 iltnRYKNIQTIdlVYIDKKSKDDIIEAEITKLLlsygADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  144 KDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGM-ISVVKYLLDLGVDMN-EPNAYGNTPLHVACYN 221
Cdd:PHA02878  200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKdYDILKLLLEHGVDVNaKSYILGLTALHSSIKS 279
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767922798  222 GQdvVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSKDGKTPL----HMTALHG 289
Cdd:PHA02878  280 ER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISNICLLKRIKPDIKNSEgfidNMDCITS 349
Ank_2 pfam12796
Ankyrin repeats (3 copies);
149-241 1.04e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.78  E-value: 1.04e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   149 IHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLgVDMNEPNaYGNTPLHVACYNGQDVVVN 228
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 767922798   229 ELIDCGAIVNQKN 241
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
625-954 4.25e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 91.62  E-value: 4.25e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  625 GQTPLMLSVLNGHTDC---VYSLLNKGANVDAKDKWGRTALH---RGAVTghEECVDALLQHGAKCLLRDSRGRTPIH-- 696
Cdd:PHA03095   47 GKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHlylYNATT--LDVIKLLIKAGADVNAKDKVGRTPLHvy 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  697 LSAACGHIGVLGALLQsaasMDANPATADNHGYTalhwacynghetcvellleqevfqktegnafsPLHCAVINdnegaa 776
Cdd:PHA03095  125 LSGFNINPKVIRLLLR----KGADVNALDLYGMT--------------------------------PLAVLLKS------ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  777 emlidtlgasiVNATdskgrtplhaaaftdhVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNT--VEMLVSsASAE 854
Cdd:PHA03095  163 -----------RNAN----------------VELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRAriVRELIR-AGCD 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  855 LTLQDNSKNTALHLACSKGHETSALLI--LEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGY 932
Cdd:PHA03095  215 PAATDMLGNTPLHSMATGSSCKRSLVLplLIAGIS---INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGN 291
                         330       340
                  ....*....|....*....|..
gi 767922798  933 TPALACAPNKDVaDCLALILAT 954
Cdd:PHA03095  292 TPLSLMVRNNNG-RAVRAALAK 312
PHA02874 PHA02874
ankyrin repeat protein; Provisional
4-206 1.70e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 89.25  E-value: 1.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798    4 LKLRDQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQTPL 83
Cdd:PHA02874  115 IDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   84 HIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFsgHGEMVKLLLSRGANINAFDKKDRRAIHWA-AYMGHIEVVK 162
Cdd:PHA02874  195 HNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAiNPPCDIDIID 272
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 767922798  163 LLVSHGAEVTCKDKKSYTPLHAAASS-GMISVVKYLLDLGVDMNE 206
Cdd:PHA02874  273 ILLYHKADISIKDNKGENPIDTAFKYiNKDPVIKDIIANAVLIKE 317
PHA02875 PHA02875
ankyrin repeat protein; Provisional
14-238 2.19e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 88.89  E-value: 2.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   14 RTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVK 93
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   94 CAEALvpLLSNVNVSD---RAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAE 170
Cdd:PHA02875   83 AVEEL--LDLGKFADDvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767922798  171 VTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDmnePNAYGNTP-LHVACY---NGQDVVVNELIDCGAIVN 238
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN---IDYFGKNGcVAALCYaieNNKIDIVRLFIKRGADCN 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
593-688 2.48e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 2.48e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   593 IHAAATNGHSECLRLLIgnaEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKgANVDAKDKwGRTALHRGAVTGHEE 672
Cdd:pfam12796    1 LHLAAKNGNLELVKLLL---ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE 75
                           90
                   ....*....|....*.
gi 767922798   673 CVDALLQHGAKCLLRD 688
Cdd:pfam12796   76 IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
559-655 3.04e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 3.04e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   559 LDLAAFKGHVECVDVLINQGASILVKDyILKRTPIHAAATNGHSECLRLLIGNAEPQNavdiqDGNGQTPLMLSVLNGHT 638
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAARSGHL 74
                           90
                   ....*....|....*..
gi 767922798   639 DCVYSLLNKGANVDAKD 655
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
547-827 4.79e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 88.54  E-value: 4.79e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  547 DLDVRNSSGRTPLDLAAFKGHVECVDV---LINQGASILVKDyILKRTPIHAAATNGHSE-CLRLLIGNaepqNA-VDIQ 621
Cdd:PHA03095   39 DVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPE-RCGFTPLHLYLYNATTLdVIKLLIKA----GAdVNAK 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  622 DGNGQTPL--MLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALH----RGAVTghEECVDALLQHGAKCLLRDSRGRTPI 695
Cdd:PHA03095  114 DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvllkSRNAN--VELLRLLIDAGADVYAVDDRFRSLL 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  696 HLSAACGHI--GVLGALLQSAASmdanPATADNHGYTALHWACYngHETCVELLLEQEVFQKTEGNA-----FSPLHCAV 768
Cdd:PHA03095  192 HHHLQSFKPraRIVRELIRAGCD----PAATDMLGNTPLHSMAT--GSSCKRSLVLPLLIAGISINArnrygQTPLHYAA 265
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767922798  769 INDNEGAAEMLIdTLGASIvNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDST 827
Cdd:PHA03095  266 VFNNPRACRRLI-ALGADI-NAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAAT 322
Ank_2 pfam12796
Ankyrin repeats (3 copies);
182-274 7.53e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 7.53e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   182 LHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIvnQKNEKGFTPLHFAAASTHGAlCL 261
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLE-IV 77
                           90
                   ....*....|...
gi 767922798   262 ELLVGNGADVNMK 274
Cdd:pfam12796   78 KLLLEKGADINVK 90
PHA02876 PHA02876
ankyrin repeat protein; Provisional
400-749 8.53e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 88.58  E-value: 8.53e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  400 GADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLLRNDANPGIRDKQGYN 479
Cdd:PHA02876  168 GADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSK-NIDTIKAIIDNRSNINKNDLSLLK 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  480 AVHYSAAyghrlclqliasETPLdvLMETSGTDMLSDSDNRATisPLHLAAyhgHHQALEVLVQSLL----DLDVRNSSG 555
Cdd:PHA02876  247 AIRNEDL------------ETSL--LLYDAGFSVNSIDDCKNT--PLHHAS---QAPSLSRLVPKLLergaDVNAKNIKG 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  556 RTPLDLAAFKGH-VECVDVLINQGASILVKDYiLKRTPIHAAATnghseclrllignaepqnavdiqdgngqtplmlsvL 634
Cdd:PHA02876  308 ETPLYLMAKNGYdTENIRTLIMLGADVNAADR-LYITPLHQAST-----------------------------------L 351
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  635 NGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLsAACGHIGVLGalLQSA 714
Cdd:PHA02876  352 DRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHF-ALCGTNPYMS--VKTL 428
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 767922798  715 ASMDANPATADNHGYTALHWACYNGHE-TCVELLLE 749
Cdd:PHA02876  429 IDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLD 464
Ank_2 pfam12796
Ankyrin repeats (3 copies);
17-142 1.32e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 1.32e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798    17 LHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHsADVNARDKnwqtplhiaaankavkcae 96
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN------------------- 60
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 767922798    97 alvpllsnvnvsdraGRTALHHAAFSGHGEMVKLLLSRGANINAFD 142
Cdd:pfam12796   61 ---------------GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
361-729 3.63e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.46  E-value: 3.63e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  361 RKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECL---NLLLNTGADFNKKDKFGRSPLH-YAAANCNYQCLFALVGSGASV 436
Cdd:PHA03095   31 RRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADV 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  437 NDLDERGCTPLH-YAATSDTDGKCLEYLLRNDANPGIRDKqgynavhysaaYGHrlclqliaseTPLDVLMetsgtdmls 515
Cdd:PHA03095  111 NAKDKVGRTPLHvYLSGFNINPKVIRLLLRKGADVNALDL-----------YGM----------TPLAVLL--------- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  516 dSDNRATISPLHLaayhghhqalevLVQSLLDLDVRNSSGRTPLD--LAAFKGHVECVDVLINQGASILVKDyILKRTPI 593
Cdd:PHA03095  161 -KSRNANVELLRL------------LIDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATD-MLGNTPL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  594 HAAATngHSECLRLLIGNaepqnavdiqdgngqtplmlsvlnghtdcvysLLNKGANVDAKDKWGRTALHRGAVTGHEEC 673
Cdd:PHA03095  227 HSMAT--GSSCKRSLVLP--------------------------------LLIAGISINARNRYGQTPLHYAAVFNNPRA 272
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767922798  674 VDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQ---SAASMDANPATADNHGY 729
Cdd:PHA03095  273 CRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAknpSAETVAATLNTASVAGG 331
Ank_2 pfam12796
Ankyrin repeats (3 copies);
799-892 1.75e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 1.75e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   799 LHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSASAELtlqDNSKNTALHLACSKGHETSA 878
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 767922798   879 LLILEKITDRNLIN 892
Cdd:pfam12796   78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
629-720 7.67e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.61  E-value: 7.67e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   629 LMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAkcLLRDSRGRTPIHLSAACGHIGVLG 708
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|..
gi 767922798   709 ALLQSAASMDAN 720
Cdd:pfam12796   79 LLLEKGADINVK 90
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
503-682 1.23e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 81.84  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  503 DVLMETSGTDmlsdsDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGASIL 582
Cdd:PLN03192  511 DLLGDNGGEH-----DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH 585
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  583 VKDyILKRTPIHAAATNGHSECLRLLIGNA---EPQNAVDIqdgngqtpLMLSVLNGHTDCVYSLLNKGANVDAKDKWGR 659
Cdd:PLN03192  586 IRD-ANGNTALWNAISAKHHKIFRILYHFAsisDPHAAGDL--------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656
                         170       180
                  ....*....|....*....|...
gi 767922798  660 TALHRGAVTGHEECVDALLQHGA 682
Cdd:PLN03192  657 TALQVAMAEDHVDMVRLLIMNGA 679
Ank_2 pfam12796
Ankyrin repeats (3 copies);
732-825 2.97e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 2.97e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   732 LHWACYNGHETCVELLLEQEV-FQKTEGNAFSPLHCAVINDNEGAAEMLIDTLGASIVNatdsKGRTPLHAAAFTDHVEC 810
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD----NGRTALHYAARSGHLEI 76
                           90
                   ....*....|....*
gi 767922798   811 LQLLLSHNAQVNSVD 825
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
181-495 3.89e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 79.15  E-value: 3.89e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  181 PLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIdcgAIVNQ--------------------- 239
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKcsvfytlvaikdafnnrnvei 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  240 ---------KNEKGFTPLHFAAASTHGAL---CLELLVGNGADVNMKSKD-GKTPLHMTALHGRFSRSQTIIQSGAVIDC 306
Cdd:PHA02878  117 fkiiltnryKNIQTIDLVYIDKKSKDDIIeaeITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNI 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  307 EDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFS-DCCRKLLSSGFDIDTpddfgrtclhaaa 385
Cdd:PHA02878  197 PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNA------------- 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  386 aggnleclnlllntgadfnKKDKFGRSPLHYAAAncNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDGKCLEYL-- 463
Cdd:PHA02878  264 -------------------KSYILGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILis 322
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 767922798  464 ---LRNDANPGIRDKQGYnAVHYSAAYGHRLCLQL 495
Cdd:PHA02878  323 nicLLKRIKPDIKNSEGF-IDNMDCITSNKRLNQI 356
PHA02878 PHA02878
ankyrin repeat protein; Provisional
2-167 3.93e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 79.15  E-value: 3.93e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798    2 AFLKLRDQDNEKrTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQT 81
Cdd:PHA02878  158 ADINMKDRHKGN-TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNT 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   82 PLHIAAAnkAVKCAEALVPLL---SNVNV-SDRAGRTALHHAAFSghGEMVKLLLSRGANINAFDKKDRRAIHWAA--YM 155
Cdd:PHA02878  237 PLHISVG--YCKDYDILKLLLehgVDVNAkSYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVkqYL 312
                         170
                  ....*....|..
gi 767922798  156 GhIEVVKLLVSH 167
Cdd:PHA02878  313 C-INIGRILISN 323
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
8-173 5.23e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 79.91  E-value: 5.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798    8 DQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQTPLHIAA 87
Cdd:PLN03192  520 HDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAI 599
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   88 ANKAVKCAEALVPLLSnvnVSD-RAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVS 166
Cdd:PLN03192  600 SAKHHKIFRILYHFAS---ISDpHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM 676

                  ....*..
gi 767922798  167 HGAEVTC 173
Cdd:PLN03192  677 NGADVDK 683
PHA03100 PHA03100
ankyrin repeat protein; Provisional
744-930 5.57e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.55  E-value: 5.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  744 VELLLEQ--EVFQKTEGNaFSPLH-----CAVINDNEGAAEMLIDtLGASIvNATDSKGRTPLHAAAFT--DHVECLQLL 814
Cdd:PHA03100   51 VKILLDNgaDINSSTKNN-STPLHylsniKYNLTDVKEIVKLLLE-YGANV-NAPDNNGITPLLYAISKksNSYSIVEYL 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  815 LSHNAQVNSVDSTGKTPLMMAAENG------------------QTNTVEMLVSSASaELTLQDNSKNTALHLACSKGHET 876
Cdd:PHA03100  128 LDNGANVNIKNSDGENLLHLYLESNkidlkilkllidkgvdinAKNRVNYLLSYGV-PINIKDVYGFTPLHYAVYNNNPE 206
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767922798  877 SALLILEKITDRNLINATNaalQTPLHVAARNGLTMVVQELLGKGASVLAVDEN 930
Cdd:PHA03100  207 FVKYLLDLGANPNLVNKYG---DTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02876 PHA02876
ankyrin repeat protein; Provisional
644-936 5.91e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 79.34  E-value: 5.91e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  644 LLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAASMDANPAT 723
Cdd:PHA02876  164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLS 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  724 -------------------------ADNHGYTALHWACYNGH-ETCVELLLEQEVFQKTEG-NAFSPLHCAVINDNEGAA 776
Cdd:PHA02876  244 llkairnedletslllydagfsvnsIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNiKGETPLYLMAKNGYDTEN 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  777 EMLIDTLGASiVNATDSKGRTPLHAAAFTD-HVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSAsAEL 855
Cdd:PHA02876  324 IRTLIMLGAD-VNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG-ADI 401
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  856 TLQDNSKNTALHLACskgHETSALLILEKITDRNL-INATNAALQTPLHVAARNGLTM-VVQELLGKGASVLAVDENGYT 933
Cdd:PHA02876  402 EALSQKIGTALHFAL---CGTNPYMSVKTLIDRGAnVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAINIQNQY 478

                  ...
gi 767922798  934 PAL 936
Cdd:PHA02876  479 PLL 481
PHA02874 PHA02874
ankyrin repeat protein; Provisional
282-619 9.74e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 77.70  E-value: 9.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  282 LHMTALHGRFSRSQTIIQS-GAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCC 360
Cdd:PHA02874    5 LRMCIYSGDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDII 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  361 RKLLSSGFDI------DTPDDFGRTCLHaaaaggnleclnlllnTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGA 434
Cdd:PHA02874   85 KLLIDNGVDTsilpipCIEKDMIKTILD----------------CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  435 SVNDLDERGCTPLHYAATSDTdGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCLQLIAsetpldvlmeTSGTDML 514
Cdd:PHA02874  149 DVNIEDDNGCYPIHIAIKHNF-FDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI----------DHGNHIM 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  515 SDSDNRATisPLHLAAYHgHHQALEVLVQSlLDLDVRNSSGRTPLDLA-AFKGHVECVDVLINQGASILVKDYiLKRTPI 593
Cdd:PHA02874  218 NKCKNGFT--PLHNAIIH-NRSAIELLINN-ASINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKDN-KGENPI 292
                         330       340
                  ....*....|....*....|....*..
gi 767922798  594 HAAATN-GHSECLRLLIGNAEPQNAVD 619
Cdd:PHA02874  293 DTAFKYiNKDPVIKDIIANAVLIKEAD 319
PHA02876 PHA02876
ankyrin repeat protein; Provisional
164-690 1.13e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 78.57  E-value: 1.13e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  164 LVSHGAEvTCKDKK-SYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYG-NTPLHVACY--NGQDVVVNELIDCGAIVNQ 239
Cdd:PHA02876   27 LHKHGAN-QCENESiPFTAIHQALQLRQIDIVEEIIQQNPELIYITDHKcHSTLHTICIipNVMDIVISLTLDCDIILDI 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  240 KNEKGFTPLHfaaasTHGALCLELLVG--NGADVNMkSKDGKTPLHMTALHGRFSRSQTIIQSgavidcedkngntplhi 317
Cdd:PHA02876  106 KYASIILNKH-----KLDEACIHILKEaiSGNDIHY-DKINESIEYMKLIKERIQQDELLIAE----------------- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  318 aaryghellinTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLL 397
Cdd:PHA02876  163 -----------MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  398 NTGADFNKKDkfgrSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDKQG 477
Cdd:PHA02876  232 DNRSNINKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKG 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  478 YNAVHYSAAYGHRlclqliaSETPLDVLMEtsGTDMlsDSDNRATISPLHLAAYHGHHQALEVLVQSL-LDLDVRNSSGR 556
Cdd:PHA02876  308 ETPLYLMAKNGYD-------TENIRTLIML--GADV--NAADRLYITPLHQASTLDRNKDIVITLLELgANVNARDYCDK 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  557 TPLDLAAFKGHVECVDVLINQGASILVKDYILKrTPIHAA--ATNGHSECLRLLIGNAEpqnaVDIQDGNGQTPLMLSVL 634
Cdd:PHA02876  377 TPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFAlcGTNPYMSVKTLIDRGAN----VNSKNKDLSTPLHYACK 451
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767922798  635 NG-HTDCVYSLLNKGANVDAKDKWGRTALHrgAVTGHEECVDALLQHGAKclLRDSR 690
Cdd:PHA02876  452 KNcKLDVIEMLLDNGADVNAINIQNQYPLL--IALEYHGIVNILLHYGAE--LRDSR 504
PHA03100 PHA03100
ankyrin repeat protein; Provisional
399-656 1.29e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.40  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  399 TGADFNKKDKFGRSPLHYAA-----ANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSD-TDGKCLEYLLRNDANPGI 472
Cdd:PHA03100   57 NGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKsNSYSIVEYLLDNGANVNI 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  473 RDKQGYNAVHYSAAYGHRlclqliasETPLDVLMETSGTDMlsDSDNRatisplhlaayhghhqaLEVLVQSLLDLDVRN 552
Cdd:PHA03100  137 KNSDGENLLHLYLESNKI--------DLKILKLLIDKGVDI--NAKNR-----------------VNYLLSYGVPINIKD 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  553 SSGRTPLDLAAFKGHVECVDVLINQGASIlvkdyilkrtpihaaatnghseclrllignaepqNAVDIqdgNGQTPLMLS 632
Cdd:PHA03100  190 VYGFTPLHYAVYNNNPEFVKYLLDLGANP----------------------------------NLVNK---YGDTPLHIA 232
                         250       260
                  ....*....|....*....|....
gi 767922798  633 VLNGHTDCVYSLLNKGANVDAKDK 656
Cdd:PHA03100  233 ILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02798 PHA02798
ankyrin-like protein; Provisional
27-282 4.24e-14

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 76.03  E-value: 4.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   27 EIIELLILSGARVNAKDSKWLTPLHRAVASCSE-----EAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPL 101
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFM 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  102 LSN---VNVSDRAGRTALHHAAFSGHG---EMVKLLLSRGANINAFDkkdrraiHWAAYmghievvkllvshgAEVTCKD 175
Cdd:PHA02798  132 IENgadTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHN-------NKEKY--------------DTLHCYF 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  176 KKSYTPLHAaassgmiSVVKYLLDLGVDMNEPNAYGNTP----LHVACYNGQDVVVN--ELIDCGAIVNQKNEKGFTPLH 249
Cdd:PHA02798  191 KYNIDRIDA-------DILKLFVDNGFIINKENKSHKKKfmeyLNSLLYDNKRFKKNilDFIFSYIDINQVDELGFNPLY 263
                         250       260       270
                  ....*....|....*....|....*....|...
gi 767922798  250 FAAASTHGALClELLVGNGADVNMKSKDGKTPL 282
Cdd:PHA02798  264 YSVSHNNRKIF-EYLLQLGGDINIITELGNTCL 295
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
46-231 5.52e-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: 76.20  E-value: 5.52e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   46 WLTPLHRAVASCSEEAVQVLLK-HSADVNARDKNWQTPLHIAAANKAVKCAEAL---VPLLSNVNV-SD-RAGRTALHHA 119
Cdd:cd22192    17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLmeaAPELVNEPMtSDlYQGETALHIA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  120 AFSGHGEMVKLLLSRGANIN-------AFDKKDRRAIHW-------AAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAA 185
Cdd:cd22192    97 VVNQNLNLVRELIARGADVVspratgtFFRPGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767922798  186 ASSGMISVVKYLLDLGVDMNE----------PNAYGNTPLHVACYNGQDVVVNELI 231
Cdd:cd22192   177 VLQPNKTFACQMYDLILSYDKeddlqpldlvPNNQGLTPFKLAAKEGNIVMFQHLV 232
PHA02798 PHA02798
ankyrin-like protein; Provisional
50-336 6.74e-14

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 75.64  E-value: 6.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   50 LHRAvaSCSEEAVQVLLKHSADVNARDKNWQTPLhiaaankavkCAealvpLLSNVnvsdRAGRTALhhaafsghgEMVK 129
Cdd:PHA02798   44 LQRD--SPSTDIVKLFINLGANVNGLDNEYSTPL----------CT-----ILSNI----KDYKHML---------DIVK 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  130 LLLSRGANINAFDKKDRRAIHWA---AYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGM---ISVVKYLLDLGVD 203
Cdd:PHA02798   94 ILIENGADINKKNSDGETPLYCLlsnGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVD 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  204 MNE-PNAYGNTPLHvaCYNGQDV------VVNELIDCGAIVNQKNEkgftplhfAAASTHGALCLELLVGNGA------- 269
Cdd:PHA02798  174 INThNNKEKYDTLH--CYFKYNIdridadILKLFVDNGFIINKENK--------SHKKKFMEYLNSLLYDNKRfkknild 243
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767922798  270 ------DVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGAD 336
Cdd:PHA02798  244 fifsyiDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
PHA03100 PHA03100
ankyrin repeat protein; Provisional
584-851 3.06e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.16  E-value: 3.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  584 KDYILKRTPIHAAATNGHseclrllignaepqnAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALH 663
Cdd:PHA03100    9 KSRIIKVKNIKYIIMEDD---------------LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLH 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  664 RGAVTGHE-----ECVDALLQHGAKCLLRDSRGRTPIHLSAAC--GHIGVLGALLQSAAsmDANPATADnhGYTALHWA- 735
Cdd:PHA03100   74 YLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGA--NVNIKNSD--GENLLHLYl 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  736 --CYNGHETcVELLLEqevfqktegnafsplHCAVINdNEGAAEMLIdTLGASIvNATDSKGRTPLHAAAFTDHVECLQL 813
Cdd:PHA03100  150 esNKIDLKI-LKLLID---------------KGVDIN-AKNRVNYLL-SYGVPI-NIKDVYGFTPLHYAVYNNNPEFVKY 210
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 767922798  814 LLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSA 851
Cdd:PHA03100  211 LLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248
PHA02875 PHA02875
ankyrin repeat protein; Provisional
185-369 6.91e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 71.95  E-value: 6.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  185 AASSGMISVVKYLLDLGVDMN--------------------------EPNAYGN-------TPLHVACYNGQDVVVNELI 231
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNfeiydgispiklamkfrdseaikllmKHGAIPDvkypdieSELHDAVEEGDVKAVEELL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  232 DCGAIVNQK-NEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKN 310
Cdd:PHA02875   89 DLGKFADDVfYKDGMTPLHLATILKKLDI-MKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  311 GNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFS-DCCRKLLSSGFD 369
Cdd:PHA02875  168 GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGAD 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
832-928 7.82e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.14  E-value: 7.82e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   832 LMMAAENGQTNTVEMLVSSaSAELTLQDNSKNTALHLACSKGHETSALLILEKItDRNLINATNaalqTPLHVAARNGLT 911
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDNGR----TALHYAARSGHL 74
                           90
                   ....*....|....*..
gi 767922798   912 MVVQELLGKGASVLAVD 928
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
675-929 8.59e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 72.40  E-value: 8.59e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  675 DALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAAsmDANPATADnhGYTALHWACYNGHETCVELLLEQEvfQ 754
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGA--DVNIIALD--DLSVLECAVDSKNIDTIKAIIDNR--S 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  755 KTEGNAFSPLHcAVINDNEGAAEMLIDTlGASiVNATDSKGRTPLHAAAFTDHVECL-QLLLSHNAQVNSVDSTGKTPLM 833
Cdd:PHA02876  236 NINKNDLSLLK-AIRNEDLETSLLLYDA-GFS-VNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLY 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  834 MAAENG-QTNTVEMLVSSAsAELTLQDNSKNTALHLACSKGHETSALLILEKITDRnlINATNAALQTPLHVAARNGLTM 912
Cdd:PHA02876  313 LMAKNGyDTENIRTLIMLG-ADVNAADRLYITPLHQASTLDRNKDIVITLLELGAN--VNARDYCDKTPIHYAAVRNNVV 389
                         250
                  ....*....|....*..
gi 767922798  913 VVQELLGKGASVLAVDE 929
Cdd:PHA02876  390 IINTLLDYGADIEALSQ 406
PHA02874 PHA02874
ankyrin repeat protein; Provisional
509-695 8.77e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 71.53  E-value: 8.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  509 SGTDMlsDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGASILVKDYIL 588
Cdd:PHA02874  113 CGIDV--NIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  589 KrTPIHAAATNGHSECLRLLIGNAepqNAVDIQDGNGQTPLMLSVLngHTDCVYSLLNKGANVDAKDKWGRTALHRG-AV 667
Cdd:PHA02874  191 E-SPLHNAAEYGDYACIKLLIDHG---NHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAiNP 264
                         170       180
                  ....*....|....*....|....*...
gi 767922798  668 TGHEECVDALLQHGAKCLLRDSRGRTPI 695
Cdd:PHA02874  265 PCDIDIIDILLYHKADISIKDNKGENPI 292
Ank_2 pfam12796
Ankyrin repeats (3 copies);
282-374 9.68e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 9.68e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   282 LHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGAdtAKRGIHGMFPLHLAALSGFSDCCR 361
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 767922798   362 KLLSSGFDIDTPD 374
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
7-76 9.97e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 9.97e-13
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798     7 RDQDNEKRTPLHAAAYLGDAEIIELLiLSGARVNAKDSKWlTPLHRAVASCSEEAVQVLLKHSADVNARD 76
Cdd:pfam12796   24 NLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDNGR-TALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02798 PHA02798
ankyrin-like protein; Provisional
158-384 2.70e-12

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 70.25  E-value: 2.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  158 IEVVKLLVSHGAEVTCKDKKSYTPLHAAASS-----GMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGqdvVVNEL-- 230
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPLYCLLSNG---YINNLei 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  231 ----IDCGAIVNQKNEKGFTPLHFAAASTHGAL--CLELLVGNGADVNMKSKDGKtplhMTALHGRFSRS---------Q 295
Cdd:PHA02798  128 llfmIENGADTTLLDKDGFTMLQVYLQSNHHIDieIIKLLLEKGVDINTHNNKEK----YDTLHCYFKYNidridadilK 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  296 TIIQSGAVIDCEDKNGNTPLhiaARYGHELLINT---------LITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSS 366
Cdd:PHA02798  204 LFVDNGFIINKENKSHKKKF---MEYLNSLLYDNkrfkknildFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQL 280
                         250
                  ....*....|....*...
gi 767922798  367 GFDIDTPDDFGRTCLHAA 384
Cdd:PHA02798  281 GGDINIITELGNTCLFTA 298
Ank_2 pfam12796
Ankyrin repeats (3 copies);
348-440 3.15e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 3.15e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   348 LHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTgADFNKKDKfGRSPLHYAAANCNYQCLF 427
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 767922798   428 ALVGSGASVNDLD 440
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
5-140 1.08e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.51  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798    5 KLRDQDNEKRTPLH--AAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQV--LLKHSADVNARDKNWQ 80
Cdd:PHA03095  179 DVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQ 258
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767922798   81 TPLHIAAA-NKAVKCAEaLVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINA 140
Cdd:PHA03095  259 TPLHYAAVfNNPRACRR-LIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAET 318
Ank_4 pfam13637
Ankyrin repeats (many copies);
112-165 1.11e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.75  E-value: 1.11e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767922798   112 GRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLV 165
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
569-833 1.41e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 67.68  E-value: 1.41e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  569 ECVDVLINQGASILVKDYILKrTPIHAAATNGHSECLRLLIgnaEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKG 648
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELK-TFLHYAIKKGDLESIKMLF---EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  649 ANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAkcllrdsrgrtpiHLSAACghigvlgallqsaasmdanpatadNHG 728
Cdd:PHA02874  181 AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN-------------HIMNKC------------------------KNG 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  729 YTALHWAC-YNghETCVELLLEQEVFQKTEGNAFSPLHCAVindNEGAAEMLIDTL--GASIVNATDSKGRTPLHAA-AF 804
Cdd:PHA02874  224 FTPLHNAIiHN--RSAIELLINNASINDQDIDGSTPLHHAI---NPPCDIDIIDILlyHKADISIKDNKGENPIDTAfKY 298
                         250       260
                  ....*....|....*....|....*....
gi 767922798  805 TDHVECLQLLLSHNAQVNSVDSTGKTPLM 833
Cdd:PHA02874  299 INKDPVIKDIIANAVLIKEADKLKDSDFL 327
Ank_2 pfam12796
Ankyrin repeats (3 copies);
248-336 1.56e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 1.56e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   248 LHFAAASTHgALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSgAVIDCEDkNGNTPLHIAARYGHELLI 327
Cdd:pfam12796    1 LHLAAKNGN-LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                   ....*....
gi 767922798   328 NTLITSGAD 336
Cdd:pfam12796   78 KLLLEKGAD 86
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
601-810 4.76e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.82  E-value: 4.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  601 HSECLRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQH 680
Cdd:PLN03192  501 HKELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKH 580
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  681 GAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAASMDANPA---------------------------TADNHGYTALH 733
Cdd:PLN03192  581 ACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAgdllctaakrndltamkellkqglnvdSEDHQGATALQ 660
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  734 WACYNGHETCVELLLEQ--EVFQKTEGNAFSPLHC-AVINDNE-GAAEMLIDTLGASIVNATDSKGRTPLHAAAFTDHVE 809
Cdd:PLN03192  661 VAMAEDHVDMVRLLIMNgaDVDKANTDDDFSPTELrELLQKRElGHSITIVDSVPADEPDLGRDGGSRPGRLQGTSSDNQ 740

                  .
gi 767922798  810 C 810
Cdd:PLN03192  741 C 741
Ank_2 pfam12796
Ankyrin repeats (3 copies);
215-308 4.92e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.13  E-value: 4.92e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   215 LHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLvgNGADVNMKSkDGKTPLHMTALHGRFSRS 294
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL--EHADVNLKD-NGRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 767922798   295 QTIIQSGAVIDCED 308
Cdd:pfam12796   78 KLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
146-198 5.58e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 5.58e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767922798   146 RRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLL 198
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02989 PHA02989
ankyrin repeat protein; Provisional
27-289 9.72e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 65.53  E-value: 9.72e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   27 EIIELLILSGARVNAKdSKWLTPL-----HRAVASCS-EEAVQVLLKHSADVNARDKNWQTPlhiaaankavkcaeaLVP 100
Cdd:PHA02989   51 KIVKLLIDNGADVNYK-GYIETPLcavlrNREITSNKiKKIVKLLLKFGADINLKTFNGVSP---------------IVC 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  101 LLSNVNVSDRagrtalhhaafsghgEMVKLLLSRGANINafDKKDRRA-----IHWAAYMGHIEVVKLLVSHGaeVTCKD 175
Cdd:PHA02989  115 FIYNSNINNC---------------DMLRFLLSKGINVN--DVKNSRGynllhMYLESFSVKKDVIKILLSFG--VNLFE 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  176 KKSY---TPLHAAASSGM----ISVVKYLLDLGVDMNEPNAYGNTPL------HVACYNGQDVVVNeLIDCGAIVNQKNE 242
Cdd:PHA02989  176 KTSLyglTPMNIYLRNDIdvisIKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLN-FILKYIKINKKDK 254
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*...
gi 767922798  243 KGFTPLHFAA-ASTHGALCLELLVGNgaDVNMKSKDGKTPLHMTALHG 289
Cdd:PHA02989  255 KGFNPLLISAkVDNYEAFNYLLKLGD--DIYNVSKDGDTVLTYAIKHG 300
Ank_4 pfam13637
Ankyrin repeats (many copies);
524-575 1.97e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.90  E-value: 1.97e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767922798   524 SPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLI 575
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
788-948 4.90e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.06  E-value: 4.90e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  788 VNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSAsAELTLQDNSKNTALH 867
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLH 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  868 LACSKGHETSALLILEKITdrNLINATNAALqTPLHVAARNGLTMVvqELLGKGASVLAVDENGYTP---ALACAPNKDV 944
Cdd:PHA02874  196 NAAEYGDYACIKLLIDHGN--HIMNKCKNGF-TPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPlhhAINPPCDIDI 270

                  ....
gi 767922798  945 ADCL 948
Cdd:PHA02874  271 IDIL 274
PHA03100 PHA03100
ankyrin repeat protein; Provisional
538-719 5.79e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 62.76  E-value: 5.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  538 LEVLVQSLLDLDVRNSSGRTPLDLAAFK--GHVECVDVLINQGASILVKDYILKrTPIHAAATNGH--SECLRLLIgnae 613
Cdd:PHA03100   89 VKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGE-NLLHLYLESNKidLKILKLLI---- 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  614 pQNAVDIqdgngqtplmlsvlNGhTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRT 693
Cdd:PHA03100  164 -DKGVDI--------------NA-KNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
                         170       180
                  ....*....|....*....|....*.
gi 767922798  694 PIHLSAACGHIGVLGALLQSAASMDA 719
Cdd:PHA03100  228 PLHIAILNNNKEIFKLLLNNGPSIKT 253
Ank_4 pfam13637
Ankyrin repeats (many copies);
179-223 5.89e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 5.89e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 767922798   179 YTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQ 223
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
Ank_2 pfam12796
Ankyrin repeats (3 copies);
414-498 5.92e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.05  E-value: 5.92e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   414 LHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDgKCLEYLLRNdANPGIRDkQGYNAVHYSAAYGHRLCL 493
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHL-EIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                   ....*
gi 767922798   494 QLIAS 498
Cdd:pfam12796   78 KLLLE 82
PHA02878 PHA02878
ankyrin repeat protein; Provisional
662-934 6.12e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 6.12e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  662 LHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLsaACGHIGVLGA--LLQSAasmdanpaTADNHGYT--ALHWACY 737
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHI--ICKEPNKLGMkeMIRSI--------NKCSVFYTlvAIKDAFN 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  738 NGHETCVELLLeqevFQKTEGNAFSPLHCAVINDNEGAAEMLIDTL----GASIVNATDSKGRTPLHAAAFTDHVECLQL 813
Cdd:PHA02878  111 NRNVEIFKIIL----TNRYKNIQTIDLVYIDKKSKDDIIEAEITKLllsyGADINMKDRHKGNTALHYATENKDQRLTEL 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  814 LLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSAsAELTLQDNSKNTALHLACSKGHETSAL-LILEKITDrnlIN 892
Cdd:PHA02878  187 LLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHISVGYCKDYDILkLLLEHGVD---VN 262
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 767922798  893 ATNAALQ-TPLHVAARNglTMVVQELLGKGASVLAVDENGYTP 934
Cdd:PHA02878  263 AKSYILGlTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTP 303
PHA02876 PHA02876
ankyrin repeat protein; Provisional
776-941 8.55e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.77  E-value: 8.55e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  776 AEMLIDtlGASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSAS--- 852
Cdd:PHA02876  161 AEMLLE--GGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSnin 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  853 -AELTLQDNSKNTALhlacskghETSALLILEKITdrnlINATNAALQTPLHVAARN-GLTMVVQELLGKGASVLAVDEN 930
Cdd:PHA02876  239 kNDLSLLKAIRNEDL--------ETSLLLYDAGFS----VNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIK 306
                         170
                  ....*....|.
gi 767922798  931 GYTPALACAPN 941
Cdd:PHA02876  307 GETPLYLMAKN 317
PHA02875 PHA02875
ankyrin repeat protein; Provisional
258-472 9.01e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.93  E-value: 9.01e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  258 ALCLELLVGN----------GADVNMKSKDGKTPLHMTAlhgRFSRSQTI---IQSGAVIDCEDKNGNTPLHIAARYGHE 324
Cdd:PHA02875    5 ALCDAILFGEldiarrlldiGINPNFEIYDGISPIKLAM---KFRDSEAIkllMKHGAIPDVKYPDIESELHDAVEEGDV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  325 LLINTLITSGA---DTAKRgiHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGA 401
Cdd:PHA02875   82 KAVEELLDLGKfadDVFYK--DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767922798  402 DFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDGKCLEYLLRNDANPGI 472
Cdd:PHA02875  160 CLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA02878 PHA02878
ankyrin repeat protein; Provisional
518-749 9.61e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.20  E-value: 9.61e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  518 DNRATiSPLHLAAYHGHHQALEVLVQSLLDLDVRNSsgRTPLDLAAFKGHVECVD-VLINQGASILVKDYILKRTPIHAA 596
Cdd:PHA02878   67 DHRDL-TPLHIICKEPNKLGMKEMIRSINKCSVFYT--LVAIKDAFNNRNVEIFKiILTNRYKNIQTIDLVYIDKKSKDD 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  597 ATNghSECLRLLIGNAEPQNAVDIQDGNgqTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDA 676
Cdd:PHA02878  144 IIE--AEITKLLLSYGADINMKDRHKGN--TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHI 219
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767922798  677 LLQHGAKCLLRDSRGRTPIHLSAA-CGHIGVLGALLQSAASMDANPATAdnhGYTALHWACYNghETCVELLLE 749
Cdd:PHA02878  220 LLENGASTDARDKCGNTPLHISVGyCKDYDILKLLLEHGVDVNAKSYIL---GLTALHSSIKS--ERKLKLLLE 288
Ank_4 pfam13637
Ankyrin repeats (many copies);
46-99 9.99e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 9.99e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767922798    46 WLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALV 99
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02859 PHA02859
ankyrin repeat protein; Provisional
44-222 1.45e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 59.06  E-value: 1.45e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   44 SKWLTPLHRAVASCSEEAVQvllKHSADVNARDKNWQTPLHIAAANKAV--KCAEALVPLLSNVNVSDRA-GRTALHHAA 120
Cdd:PHA02859   19 YRYCNPLFYYVEKDDIEGVK---KWIKFVNDCNDLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRDnNLSALHHYL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  121 FSGHG---EMVKLLLSRGANINAFDKKDRRAIHwaAYMGH----IEVVKLLVSHGAEVTCKDKK------SYTPLHAAAS 187
Cdd:PHA02859   96 SFNKNvepEILKILIDSGSSITEEDEDGKNLLH--MYMCNfnvrINVIKLLIDSGVSFLNKDFDnnnilySYILFHSDKK 173
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 767922798  188 sgmisVVKYLLDLGVDMNEPNAYGNTPLHVACYNG 222
Cdd:PHA02859  174 -----IFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
PHA02946 PHA02946
ankyin-like protein; Provisional
21-248 1.48e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 61.61  E-value: 1.48e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   21 AYLG----DAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQTPLHIAAAnkavkcae 96
Cdd:PHA02946   43 AYCGikglDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSG-------- 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   97 alvpllSNVNVSDRagrtalhhaafsghgemVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDK 176
Cdd:PHA02946  115 ------TDDEVIER-----------------INLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDK 171
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767922798  177 --KSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNG-QDVVVNELIDCGAIVNQKNEKGFTPL 248
Cdd:PHA02946  172 fgKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTvKNVDIINLLLPSTDVNKQNKFGDSPL 246
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
557-697 1.58e-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: 61.95  E-value: 1.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  557 TPLDLAAFKGHVECVDVLINQGASILVKDYILKRTPIHAAATNGHSECLRLLIGNA-----EPQNAVDIQdgnGQTPLML 631
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelvnEPMTSDLYQ---GETALHI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  632 SVLNGHTDCVYSLLNKGANV--------------DAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHL 697
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
Ank_2 pfam12796
Ankyrin repeats (3 copies);
447-552 1.75e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.51  E-value: 1.75e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   447 LHYAATSDtDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCLQLIASETPLDvlMETSGTdmlsdsdnratiSPL 526
Cdd:pfam12796    1 LHLAAKNG-NLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN--LKDNGR------------TAL 65
                           90       100
                   ....*....|....*....|....*.
gi 767922798   527 HLAAYHGHHQALEVLVQSLLDLDVRN 552
Cdd:pfam12796   66 HYAARSGHLEIVKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
555-750 1.86e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.16  E-value: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  555 GRTPLDLAAFKGHVECVDVLINQGASILVKdYILKRTPIHAAATNGHSECLRLLIGNAEPQNAVDIQDGNgqTPLMLSVL 634
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVK-YPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGM--TPLHLATI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  635 NGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSA 714
Cdd:PHA02875  112 LKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 767922798  715 ASMDanpATADNHGYTALHWACYNGHETCVELLLEQ 750
Cdd:PHA02875  192 ANID---YFGKNGCVAALCYAIENNKIDIVRLFIKR 224
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
180-317 2.76e-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: 61.18  E-value: 2.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  180 TPLHAAASSGMISVVKYLLDL-GVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCG-AIVNQKNE----KGFTPLHFAAA 253
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApELVNEPMTsdlyQGETALHIAVV 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767922798  254 STHGALcLELLVGNGADVN---------MKSKD-----GKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHI 317
Cdd:cd22192    99 NQNLNL-VRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
116-198 3.41e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.68  E-value: 3.41e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  116 LHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVK 195
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                  ...
gi 767922798  196 YLL 198
Cdd:PTZ00322  166 LLS 168
PHA02878 PHA02878
ankyrin repeat protein; Provisional
429-634 3.72e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.28  E-value: 3.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  429 LVGSGASVNDLDE-RGCTPLHYAATsDTDGKCLEYLLRNDANPGIRDKqgynavhysaayghrlclqliasetpldvlme 507
Cdd:PHA02878  153 LLSYGADINMKDRhKGNTALHYATE-NKDQRLTELLLSYGANVNIPDK-------------------------------- 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  508 tsgtdmlsdSDNratiSPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAfkGHVECVDV---LINQGASILVK 584
Cdd:PHA02878  200 ---------TNN----SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYCKDYDIlklLLEHGVDVNAK 264
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767922798  585 DYILKRTPIHAAAtngHSE-CLRLLIGNAEPQNAVDIQDgngQTPLMLSVL 634
Cdd:PHA02878  265 SYILGLTALHSSI---KSErKLKLLLEYGADINSLNSYK---LTPLSSAVK 309
Ank_4 pfam13637
Ankyrin repeats (many copies);
81-132 9.04e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 9.04e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767922798    81 TPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLL 132
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
795-848 1.02e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 1.02e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767922798   795 GRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLV 848
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
119-277 1.29e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 59.11  E-value: 1.29e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  119 AAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLL 198
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767922798  199 DLGvDMNEPNAYGNTpLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSKD 277
Cdd:PLN03192  612 HFA-SISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDM-VRLLIMNGADVDKANTD 687
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
751-862 2.02e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.37  E-value: 2.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  751 EVFQKTEGNAFSPLHCAVIND--NEGAAEMLI----------DTLGASIV-------NATDSKGRTPLHAAAFTDHVECL 811
Cdd:PTZ00322   52 EALEATENKDATPDHNLTTEEviDPVVAHMLTvelcqlaasgDAVGARILltggadpNCRDYDGRTPLHIACANGHVQVV 131
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767922798  812 QLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSASAELTLQDNSK 862
Cdd:PTZ00322  132 RVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAK 182
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
417-665 2.02e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.34  E-value: 2.02e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  417 AAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDgKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHrlclqli 496
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYE-DCVLVLLKHACNVHIRDANGNTALWNAISAKH------- 603
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  497 asETPLDVLMETSgtdmlSDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLIN 576
Cdd:PLN03192  604 --HKIFRILYHFA-----SISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM 676
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  577 QGASIlvkdyilkrtpIHAAATNGHS-ECLRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCvySLLNKGANvdaKD 655
Cdd:PLN03192  677 NGADV-----------DKANTDDDFSpTELRELLQKRELGHSITIVDSVPADEPDLGRDGGSRPG--RLQGTSSD---NQ 740
                         250
                  ....*....|
gi 767922798  656 KWGRTALHRG 665
Cdd:PLN03192  741 CRPRVSIYKG 750
Ank_4 pfam13637
Ankyrin repeats (many copies);
14-66 2.71e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 2.71e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767922798    14 RTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLL 66
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
555-609 2.81e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 2.81e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767922798   555 GRTPLDLAAFKGHVECVDVLINQGASILVKDYiLKRTPIHAAATNGHSECLRLLI 609
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
764-934 3.39e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 3.39e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  764 LHCAVINDNEGAAEMLIDtLGASiVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNT 843
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFE-YGAD-VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  844 VEMLVSSASaELTLQDNSKNTALHLACSkgHETSALLILekITDRNlINATNAALQTPLHVAARNGLTM-VVQELLGKGA 922
Cdd:PHA02874  206 IKLLIDHGN-HIMNKCKNGFTPLHNAII--HNRSAIELL--INNAS-INDQDIDGSTPLHHAINPPCDIdIIDILLYHKA 279
                         170
                  ....*....|..
gi 767922798  923 SVLAVDENGYTP 934
Cdd:PHA02874  280 DISIKDNKGENP 291
PHA02875 PHA02875
ankyrin repeat protein; Provisional
732-904 3.43e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.92  E-value: 3.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  732 LHWACYNGHETCVELLLE-----QEVFQKtEGNafSPLHCAVINDNEGAAEMLIDTLGASIVNATDSKgrTPLHAAAFTD 806
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDlgkfaDDVFYK-DGM--TPLHLATILKKLDIMKLLIARGADPDIPNTDKF--SPLHLAVMMG 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  807 HVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSASAELTLQDNSKNTALHLACSKGHETSALLILEKIT 886
Cdd:PHA02875  147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGA 226
                         170
                  ....*....|....*...
gi 767922798  887 DRNLINATNAALQTPLHV 904
Cdd:PHA02875  227 DCNIMFMIEGEECTILDM 244
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
55-133 4.39e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 4.39e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767922798   55 ASCSEEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLS 133
Cdd:PTZ00322   91 ASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
546-769 4.43e-08

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 57.40  E-value: 4.43e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   546 LDLDVRNSSGRTPLDLAAFKG-HVECVDVLINQGASILVKDyilkrTPIHAAATNGH---SECLRLLIGNAE----PQNA 617
Cdd:TIGR00870   43 LNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGD-----TLLHAISLEYVdavEAILLHLLAAFRksgpLELA 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   618 VDIQDGN---GQTPLMLSVLNGHTDCVYSLLNKGANVDAKDK--------------WGRTALHRGAVTGHEECVDALLQH 680
Cdd:TIGR00870  118 NDQYTSEftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSED 197
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   681 GAKCLLRDSRGRTPIHLSAACGHIGVLGALL-----QSAASMDANPATAD------NH-GYTALHWACYNGHETCVELLL 748
Cdd:TIGR00870  198 PADILTADSLGNTLLHLLVMENEFKAEYEELscqmyNFALSLLDKLRDSKelevilNHqGLTPLKLAAKEGRIVLFRLKL 277
                          250       260
                   ....*....|....*....|..
gi 767922798   749 EQEVFQKT-EGNAFSPLHCAVI 769
Cdd:TIGR00870  278 AIKYKQKKfVAWPNGQQLLSLY 299
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
161-233 4.95e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 4.95e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767922798  161 VKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDC 233
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
155-346 5.57e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.19  E-value: 5.57e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  155 MGHIEVVKLLVSHGAEVTckDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCG 234
Cdd:PLN03192  504 LHDLNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  235 AIVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSkdGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTP 314
Cdd:PLN03192  582 CNVHIRDANGNTALWNAISAKHHKI-FRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
                         170       180       190
                  ....*....|....*....|....*....|..
gi 767922798  315 LHIAARYGHELLINTLITSGADTAKRGIHGMF 346
Cdd:PLN03192  659 LQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
251-405 6.22e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.80  E-value: 6.22e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  251 AAASTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTL 330
Cdd:PLN03192  531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767922798  331 --ITSGADTAKRGIhgmfPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNK 405
Cdd:PLN03192  611 yhFASISDPHAAGD----LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
677-850 6.58e-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: 56.56  E-value: 6.58e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  677 LLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAASMDANPATADNH-GYTALHWACYNGHETCVELLLEQ----- 750
Cdd:cd22192    37 LKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDLYqGETALHIAVVNQNLNLVRELIARgadvv 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  751 ------EVFQKTEGNAF----SPLHCAVINDNEGAAEMLIDTlGASIVnATDSKGRTPLHAAAF----TDHVECLQLLLS 816
Cdd:cd22192   117 spratgTFFRPGPKNLIyygeHPLSFAACVGNEEIVRLLIEH-GADIR-AQDSLGNTVLHILVLqpnkTFACQMYDLILS 194
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 767922798  817 HNAQVNSV------DSTGKTPLMMAAENGQTNTVEMLVSS 850
Cdd:cd22192   195 YDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
658-711 6.60e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 6.60e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767922798   658 GRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALL 711
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
792-920 9.15e-08

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: 56.31  E-value: 9.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  792 DSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDST--------------GKTPLMMAAENGQTNTVEMLVSSASAELTL 857
Cdd:cd22194   138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITS 217
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767922798  858 QDNSKNTALHLAC-----SKGHETSAL----LILEKITDRNLINATNAALQTPLHVAARNGLTMVVQELLGK 920
Cdd:cd22194   218 QDSRGNTVLHALVtvaedSKTQNDFVKrmydMILLKSENKNLETIRNNEGLTPLQLAAKMGKAEILKYILSR 289
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
764-920 1.05e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 55.79  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  764 LHCAVINDNEGAAEMLIDTLGASIVNATDS---KGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDST------------- 827
Cdd:cd22192    55 LHVAALYDNLEAAVVLMEAAPELVNEPMTSdlyQGETALHIAVVNQNLNLVRELIARGADVVSPRATgtffrpgpknliy 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  828 -GKTPLMMAAENGQTNTVEMLVsSASAELTLQDNSKNTALHLACSKGHETSA------LLILEK-ITDRNLINATNAALQ 899
Cdd:cd22192   135 yGEHPLSFAACVGNEEIVRLLI-EHGADIRAQDSLGNTVLHILVLQPNKTFAcqmydlILSYDKeDDLQPLDLVPNNQGL 213
                         170       180
                  ....*....|....*....|.
gi 767922798  900 TPLHVAARNGLTMVVQELLGK 920
Cdd:cd22192   214 TPFKLAAKEGNIVMFQHLVQK 234
PHA02875 PHA02875
ankyrin repeat protein; Provisional
789-951 1.16e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.38  E-value: 1.16e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  789 NATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSASAELTLQDNSKNTALHL 868
Cdd:PHA02875   29 NFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  869 AC-SKGHETSALLILEKiTDRNLINATNAalqTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADC 947
Cdd:PHA02875  109 ATiLKKLDIMKLLIARG-ADPDIPNTDKF---SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAIC 184

                  ....
gi 767922798  948 LALI 951
Cdd:PHA02875  185 KMLL 188
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
17-233 1.43e-07

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 55.69  E-value: 1.43e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   17 LHAaaYLG----DAEIIELLILSGARVNAKDSKWLTPLHRAV--ASCSEEAVQVLLKHSADVNARDKNWQTPL--HIAAA 88
Cdd:PHA02716  181 LHA--YLGnmyvDIDILEWLCNNGVNVNLQNNHLITPLHTYLitGNVCASVIKKIIELGGDMDMKCVNGMSPImtYIINI 258
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   89 -----------------NKAVKCAEAL---VPLLSNVNVS---------------DRAGRTALHHAAFSGH--GEMVKLL 131
Cdd:PHA02716  259 dninpeitniyiesldgNKVKNIPMILhsyITLARNIDISvvysflqpgvklhykDSAGRTCLHQYILRHNisTDIIKLL 338
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  132 LSRGANINAFDKKDRRAIHwaAYMGHIEVVKLLVSHgaevTCKDKKsytplhaaassgmISVVKYLLDLGVDMNEPNAYG 211
Cdd:PHA02716  339 HEYGNDLNEPDNIGNTVLH--TYLSMLSVVNILDPE----TDNDIR-------------LDVIQCLISLGADITAVNCLG 399
                         250       260
                  ....*....|....*....|..
gi 767922798  212 NTPLHVACYNGQDVVVNELIDC 233
Cdd:PHA02716  400 YTPLTSYICTAQNYMYYDIIDC 421
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
39-219 1.70e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 55.47  E-value: 1.70e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798    39 VNAKDSKWLTPLHRAVA-SCSEEAVQVLLKHSADVNARDknwqTPLHIAAANKAVKCAEALVPLLSN---------VNVS 108
Cdd:TIGR00870   45 INCPDRLGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAISLEYVDAVEAILLHLLAAfrksgplelANDQ 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   109 DR----AGRTALHHAAFSGHGEMVKLLLSRGANINA------FDKKDRRA--------IHWAAYMGHIEVVKLLVSHGAE 170
Cdd:TIGR00870  121 YTseftPGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDsfyhgespLNAAACLGSPSIVALLSEDPAD 200
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767922798   171 VTCKDKKSYTPLHAAA------------SSGMISVVKYLLDLGVDMNE----PNAYGNTPLHVAC 219
Cdd:TIGR00870  201 ILTADSLGNTLLHLLVmenefkaeyeelSCQMYNFALSLLDKLRDSKEleviLNHQGLTPLKLAA 265
PHA02798 PHA02798
ankyrin-like protein; Provisional
226-472 2.51e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 54.46  E-value: 2.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  226 VVNELIDCGAIVNQKNEKGFTPLHFAAAS----THGALCLELLVGNGADVNMKSKDGKTPLHmTALHGRFSRSQTI---- 297
Cdd:PHA02798   53 IVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHMLDIVKILIENGADINKKNSDGETPLY-CLLSNGYINNLEIllfm 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  298 IQSGAVIDCEDKNGNTPLHIAARYGHELLINTLitsgadtakrgihgmfplhlaalsgfsdccRKLLSSGFDIDTPDD-F 376
Cdd:PHA02798  132 IENGADTTLLDKDGFTMLQVYLQSNHHIDIEII------------------------------KLLLEKGVDINTHNNkE 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  377 GRTCLHAAAAGGNLECLNLLLN----TGADFNKKDKFGRS-------PLHYAAANCNYQcLFALVGSGASVNDLDERGCT 445
Cdd:PHA02798  182 KYDTLHCYFKYNIDRIDADILKlfvdNGFIINKENKSHKKkfmeylnSLLYDNKRFKKN-ILDFIFSYIDINQVDELGFN 260
                         250       260
                  ....*....|....*....|....*..
gi 767922798  446 PLHYAATSDTDgKCLEYLLRNDANPGI 472
Cdd:PHA02798  261 PLYYSVSHNNR-KIFEYLLQLGGDINI 286
PHA02875 PHA02875
ankyrin repeat protein; Provisional
762-953 2.82e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.23  E-value: 2.82e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  762 SPLHCAVINDNEGAAEMLIDtLGASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQT 841
Cdd:PHA02875   70 SELHDAVEEGDVKAVEELLD-LGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  842 NTVEMLVSsasaeltlqdnskntalHLACskghetsallilekitdrnlINATNAALQTPLHVAARNGLTMVVQELLGKG 921
Cdd:PHA02875  149 KGIELLID-----------------HKAC--------------------LDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
                         170       180       190
                  ....*....|....*....|....*....|..
gi 767922798  922 ASVLAVDENGYTPALACAPNKDVADCLALILA 953
Cdd:PHA02875  192 ANIDYFGKNGCVAALCYAIENNKIDIVRLFIK 223
Ank_4 pfam13637
Ankyrin repeats (many copies);
410-464 2.84e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 2.84e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767922798   410 GRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLL 464
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG-NVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
624-871 2.97e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.23  E-value: 2.97e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  624 NGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAkcLLRD---SRGRTPIHLSAA 700
Cdd:PHA02875   34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK--FADDvfyKDGMTPLHLATI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  701 CGHIGVLGALLQSAASMDAnPATadnhgytalhwacynghetcvellleqevfqktegNAFSPLHCAVINDNEGAAEMLI 780
Cdd:PHA02875  112 LKKLDIMKLLIARGADPDI-PNT-----------------------------------DKFSPLHLAVMMGDIKGIELLI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  781 DTlgASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLM-MAAENGQTNTVEMLVS--SASAELTL 857
Cdd:PHA02875  156 DH--KACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKrgADCNIMFM 233
                         250
                  ....*....|....
gi 767922798  858 QDNSKNTALHLACS 871
Cdd:PHA02875  234 IEGEECTILDMICN 247
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
774-934 3.01e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 3.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  774 GAAEMLIDTLGASI-VNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSAS 852
Cdd:PLN03192  536 GNAALLEELLKAKLdPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS 615
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  853 AeltlqdNSKNTALHLACSKGHETSaLLILEKITDRNL-INATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVD-EN 930
Cdd:PLN03192  616 I------SDPHAAGDLLCTAAKRND-LTAMKELLKQGLnVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDD 688

                  ....
gi 767922798  931 GYTP 934
Cdd:PLN03192  689 DFSP 692
PHA02859 PHA02859
ankyrin repeat protein; Provisional
178-336 3.57e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 52.13  E-value: 3.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  178 SYT-PLHAAASSGMISVVKYLLDLgvdMNEPNAYGNTPLHvACYNGQDVVVNE---LIDCGAIVNQK-NEKGFTPLHFAA 252
Cdd:PHA02859   20 RYCnPLFYYVEKDDIEGVKKWIKF---VNDCNDLYETPIF-SCLEKDKVNVEIlkfLIENGADVNFKtRDNNLSALHHYL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  253 ASTHGAL--CLELLVGNGADVNMKSKDGKTPLH--MTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLI- 327
Cdd:PHA02859   96 SFNKNVEpeILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKKIf 175

                  ....*....
gi 767922798  328 NTLITSGAD 336
Cdd:PHA02859  176 DFLTSLGID 184
PHA03100 PHA03100
ankyrin repeat protein; Provisional
15-78 4.31e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.52  E-value: 4.31e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767922798   15 TPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKN 78
Cdd:PHA03100  194 TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02874 PHA02874
ankyrin repeat protein; Provisional
775-934 6.44e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 6.44e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  775 AAEMLIDTLGaSIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVssasae 854
Cdd:PHA02874   16 AIEKIIKNKG-NCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI------ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  855 ltlqDNSKNTA-LHLACSKGHETSAllILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYT 933
Cdd:PHA02874   89 ----DNGVDTSiLPIPCIEKDMIKT--ILDCGID---VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCY 159

                  .
gi 767922798  934 P 934
Cdd:PHA02874  160 P 160
Ank_4 pfam13637
Ankyrin repeats (many copies);
762-815 8.78e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 8.78e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767922798   762 SPLHCAVINDNEGAAEMLIDTlGASIvNATDSKGRTPLHAAAFTDHVECLQLLL 815
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEK-GADI-NAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
253-322 1.25e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 1.25e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  253 ASTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYG 322
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
246-451 1.39e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.32  E-value: 1.39e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  246 TPLhFAAASTHGALCLE-LLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGA-----VIDCEDKNGNTPLHIAA 319
Cdd:cd22192    19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPelvnePMTSDLYQGETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  320 RYGHELLINTLITSGADTAKRGIHGMFplhlaalsgFSDCCRKLLSsgfdidtpddFGRTCLHAAAAGGNLECLNLLLNT 399
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSPRATGTF---------FRPGPKNLIY----------YGEHPLSFAACVGNEEIVRLLIEH 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767922798  400 GADFNKKDKFGRSPLHYAA--ANCNYQC-----LFALVGSGASVNdLD----ERGCTPLHYAA 451
Cdd:cd22192   159 GADIRAQDSLGNTVLHILVlqPNKTFACqmydlILSYDKEDDLQP-LDlvpnNQGLTPFKLAA 220
Ank_4 pfam13637
Ankyrin repeats (many copies);
627-678 1.78e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 1.78e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767922798   627 TPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALL 678
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
590-645 2.14e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 2.14e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767922798   590 RTPIHAAATNGHSECLRLLIGNAEPqnaVDIQDGNGQTPLMLSVLNGHTDCVYSLL 645
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
830-924 2.71e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.17  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  830 TPLMMAAENGQTNTVEMLVSSASAELTLQDNSKNTALHLACSKGHETSALLILEkiTDRNLIN-ATNAAL---QTPLHVA 905
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNePMTSDLyqgETALHIA 96
                          90
                  ....*....|....*....
gi 767922798  906 ARNGLTMVVQELLGKGASV 924
Cdd:cd22192    97 VVNQNLNLVRELIARGADV 115
Ank_5 pfam13857
Ankyrin repeats (many copies);
164-218 3.54e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 3.54e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767922798   164 LVSHG-AEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVA 218
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
162-346 3.98e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 50.78  E-value: 3.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  162 KLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDM-NEP---NAY-GNTPLHVACYNGQDVVVNELIDCGAI 236
Cdd:cd22192    35 KLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvNEPmtsDLYqGETALHIAVVNQNLNLVRELIARGAD 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  237 VN---------QKNEK-----GFTPLHFAAASTHGALcLELLVGNGADVNMKSKDGKTPLHMTALhgrfsrsqtiiQSGA 302
Cdd:cd22192   115 VVspratgtffRPGPKnliyyGEHPLSFAACVGNEEI-VRLLIEHGADIRAQDSLGNTVLHILVL-----------QPNK 182
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767922798  303 VIDCE--------DKNGN-------------TPLHIAARYGHELLINTLITSgadtaKRGIHGMF 346
Cdd:cd22192   183 TFACQmydlilsyDKEDDlqpldlvpnnqglTPFKLAAKEGNIVMFQHLVQK-----RRHIQWTY 242
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
666-748 4.36e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 4.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  666 AVTGHEECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQsaasMDANPATADNHGYTALHWACYNGHETCVE 745
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLE----FGADPTLLDKDGKTPLELAEENGFREVVQ 165

                  ...
gi 767922798  746 LLL 748
Cdd:PTZ00322  166 LLS 168
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
112-143 5.55e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.82  E-value: 5.55e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 767922798   112 GRTALHHAAFS-GHGEMVKLLLSRGANINAFDK 143
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
347-388 5.89e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 5.89e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 767922798   347 PLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGG 388
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG 45
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
80-231 5.93e-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: 50.26  E-value: 5.93e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   80 QTPLHIAAANKAVKCAEALVPLLSNVNVSDRA--------------GRTALHHAAFSGHGEMVKLLLSRGANINA----- 140
Cdd:cd21882    27 KTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAratgr 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  141 -FDKKDRRAIHW-------AAYMGHIEVVKLLVSHGAE---VTCKDKKSYTPLHA---------AASSGMISVVKYLLDL 200
Cdd:cd21882   107 fFRKSPGNLFYFgelplslAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHAlvlqadntpENSAFVCQMYNLLLSY 186
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 767922798  201 G------VDMNE-PNAYGNTPLHVACYNGQDVVVNELI 231
Cdd:cd21882   187 GahldptQQLEEiPNHQGLTPLKLAAVEGKIVMFQHIL 224
Ank_5 pfam13857
Ankyrin repeats (many copies);
230-284 6.70e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 6.70e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 767922798   230 LIDCGAI-VNQKNEKGFTPLHFAAasTHGAL-CLELLVGNGADVNMKSKDGKTPLHM 284
Cdd:pfam13857    1 LLEHGPIdLNRLDGEGYTPLHVAA--KYGALeIVRVLLAYGVDLNLKDEEGLTALDL 55
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
24-98 6.79e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 6.79e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767922798   24 GDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEAL 98
Cdd:PTZ00322   93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_4 pfam13637
Ankyrin repeats (many copies);
280-331 9.08e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 9.08e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767922798   280 TPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLI 331
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
411-629 1.01e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.22  E-value: 1.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  411 RSPLHYAAANCNYQCLFALVGSGASVND-LDERGCTPLHYAaTSDTDGKCLEYLLRNDANPGIrdkqgynavhysaaygh 489
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADDvFYKDGMTPLHLA-TILKKLDIMKLLIARGADPDI----------------- 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  490 rlclqliasetpldvlmetSGTDmlsdsdnraTISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVE 569
Cdd:PHA02875  131 -------------------PNTD---------KFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIA 182
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767922798  570 CVDVLINQGASIlvkDYILKRTPIHA---AATNGHSECLRLLIGNAEPQNAVDIQDGNGQTPL 629
Cdd:PHA02875  183 ICKMLLDSGANI---DYFGKNGCVAAlcyAIENNKIDIVRLFIKRGADCNIMFMIEGEECTIL 242
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
667-841 1.03e-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: 1.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  667 VTGHEECVDALLQHGAKclLRDSRGRTPIHLSAACGHIGVLGA---LLQSAASMDAN------PATADNH-GYTALHWAC 736
Cdd:cd21882     4 LLGLLECLRWYLTDSAY--QRGATGKTCLHKAALNLNDGVNEAimlLLEAAPDSGNPkelvnaPCTDEFYqGQTALHIAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  737 YNGHETCVELLLEQ----------EVFQKTEGNAF----SPLHCAVINDNEGAAEMLIDTlGASI--VNATDSKGRTPLH 800
Cdd:cd21882    82 ENRNLNLVRLLVENgadvsaratgRFFRKSPGNLFyfgeLPLSLAACTNQEEIVRLLLEN-GAQPaaLEAQDSLGNTVLH 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 767922798  801 A-----------AAFTDHVecLQLLLSHNAQVNSVDS-------TGKTPLMMAAENGQT 841
Cdd:cd21882   161 AlvlqadntpenSAFVCQM--YNLLLSYGAHLDPTQQleeipnhQGLTPLKLAAVEGKI 217
Ank_5 pfam13857
Ankyrin repeats (many copies);
65-119 1.14e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.14e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767922798    65 LLKH-SADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHA 119
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
696-836 1.35e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 1.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  696 HLSAACGHIGVLgALLQSAAsmdaNPATADNHGYTALHWACYNGHETCVELLLEqevfqktegnafsplhcavindnega 775
Cdd:PTZ00322   88 QLAASGDAVGAR-ILLTGGA----DPNCRDYDGRTPLHIACANGHVQVVRVLLE-------------------------- 136
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767922798  776 aemlidtLGASiVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGK-------------TPLMMAA 836
Cdd:PTZ00322  137 -------FGAD-PTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAKpdsftgkppsledSPISSHH 202
PHA03095 PHA03095
ankyrin-like protein; Provisional
10-115 1.44e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.87  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   10 DNEKRTPLHAAAYLGD--AEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQTPLHIAA 87
Cdd:PHA03095  219 DMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMV 298
                          90       100
                  ....*....|....*....|....*...
gi 767922798   88 ANKAVKCAEALVPLLSNVNVSDRAGRTA 115
Cdd:PHA03095  299 RNNNGRAVRAALAKNPSAETVAATLNTA 326
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
112-140 1.87e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 1.87e-05
                            10        20
                    ....*....|....*....|....*....
gi 767922798    112 GRTALHHAAFSGHGEMVKLLLSRGANINA 140
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
297-376 2.01e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 2.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  297 IIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLS---SGFDIDT- 372
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRhsqCHFELGAn 180

                  ....*.
gi 767922798  373 --PDDF 376
Cdd:PTZ00322  181 akPDSF 186
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
15-152 2.09e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.47  E-value: 2.09e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   15 TPLHAAAYLGDAEIIELLILSGARVNA---------KDSKWLT-----PLHRAVASCSEEAVQVLLKHSADVNARDKNWQ 80
Cdd:cd22192    91 TALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   81 TPLHIAA--ANKAVKCAE-----ALVPLLSNVNVS---DRAGRTALHHAAFSGHGEMVKLLLSRganinafdkkdRRAIH 150
Cdd:cd22192   171 TVLHILVlqPNKTFACQMydlilSYDKEDDLQPLDlvpNNQGLTPFKLAAKEGNIVMFQHLVQK-----------RRHIQ 239

                  ..
gi 767922798  151 WA 152
Cdd:cd22192   240 WT 241
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
445-647 2.15e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.47  E-value: 2.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  445 TPLHYAAtSDTDGKCLEYLLR-NDANPGIRDKQGYNAVHYSAAYGHRLCLQLIASETPLDVLMETSgtdmlsdSDNRATI 523
Cdd:cd22192    19 SPLLLAA-KENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMT-------SDLYQGE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  524 SPLHLAAYHGHhqalEVLVQSLLD--LDVRNSS----------------GRTPLDLAAFKGHVECVDVLINQGASILVKD 585
Cdd:cd22192    91 TALHIAVVNQN----LNLVRELIArgADVVSPRatgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767922798  586 YiLKRTPIHAAAT--NGHSECLRL-LIGNAEP---QNAVD-IQDGNGQTPLMLSVLNGHTDCVYSLLNK 647
Cdd:cd22192   167 S-LGNTVLHILVLqpNKTFACQMYdLILSYDKeddLQPLDlVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
377-430 2.40e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 2.40e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767922798   377 GRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALV 430
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
84-170 2.47e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 2.47e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   84 HIAAANKAVKcAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKL 163
Cdd:PTZ00322   88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                  ....*..
gi 767922798  164 LVSHGAE 170
Cdd:PTZ00322  167 LSRHSQC 173
Ank_5 pfam13857
Ankyrin repeats (many copies);
615-663 2.68e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 2.68e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 767922798   615 QNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALH 663
Cdd:pfam13857    6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
186-292 2.73e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 2.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  186 ASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALcLELLV 265
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV-VQLLS 168
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 767922798  266 GN-------GADVNMKSKDGKTPLH----MTALHGRFS 292
Cdd:PTZ00322  169 RHsqchfelGANAKPDSFTGKPPSLedspISSHHPDFS 206
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
261-447 3.20e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 47.98  E-value: 3.20e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  261 LELLVGNGADVNMKSKDGKTPLHMTALHGRFSRS--QTIIQSGAVIDCEDKNGNTPLH---IAARYGHELLINTLITSGA 335
Cdd:PHA02716  195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASviKKIIELGGDMDMKCVNGMSPIMtyiINIDNINPEITNIYIESLD 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  336 DTAKRGIHGMFPLHLAALSGFS-DCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECL--NLLLNTGADFNKKDKFGRS 412
Cdd:PHA02716  275 GNKVKNIPMILHSYITLARNIDiSVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNISTDiiKLLHEYGNDLNEPDNIGNT 354
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 767922798  413 PLHYAAA--------------NCNYQCLFALVGSGASVNDLDERGCTPL 447
Cdd:PHA02716  355 VLHTYLSmlsvvnildpetdnDIRLDVIQCLISLGADITAVNCLGYTPL 403
Ank_4 pfam13637
Ankyrin repeats (many copies);
311-364 3.85e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 3.85e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767922798   311 GNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLL 364
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
112-140 4.23e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.47  E-value: 4.23e-05
                           10        20
                   ....*....|....*....|....*....
gi 767922798   112 GRTALHHAAFSGHGEMVKLLLSRGANINA 140
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
691-748 4.87e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 4.87e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 767922798   691 GRTPIHLSAACGHIGVLGALLQSAASMDAnpatADNHGYTALHWACYNGHETCVELLL 748
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINA----VDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
522-632 4.92e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 4.92e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  522 TISPLHLAAyHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGA--SILVKDyilKRTPIHAAATN 599
Cdd:PTZ00322   83 TVELCQLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAdpTLLDKD---GKTPLELAEEN 158
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 767922798  600 GHSECLRLLIG----------NAEPQNAVDIQDGNGQTPLMLS 632
Cdd:PTZ00322  159 GFREVVQLLSRhsqchfelgaNAKPDSFTGKPPSLEDSPISSH 201
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
781-952 5.21e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 5.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  781 DTLGASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSAsAELTLQDN 860
Cdd:PLN03192  511 DLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDA 589
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  861 SKNTALHLACSKGHETsallILEKITDRNLINATNAALQTPLHVAARNGLTMvVQELLGKGASVLAVDENGYTpALACAP 940
Cdd:PLN03192  590 NGNTALWNAISAKHHK----IFRILYHFASISDPHAAGDLLCTAAKRNDLTA-MKELLKQGLNVDSEDHQGAT-ALQVAM 663
                         170
                  ....*....|..
gi 767922798  941 NKDVADCLALIL 952
Cdd:PLN03192  664 AEDHVDMVRLLI 675
PHA02946 PHA02946
ankyin-like protein; Provisional
362-482 5.31e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.97  E-value: 5.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  362 KLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCN--YQCLFALVGSGASVND- 438
Cdd:PHA02946   57 ELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNs 136
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 767922798  439 LDERGCTPLhyAATSDTDGKCLEYLLRNDANPGIRDKQGYNAVH 482
Cdd:PHA02946  137 VDEEGCGPL--LACTDPSERVFKKIMSIGFEARIVDKFGKNHIH 178
Ank_4 pfam13637
Ankyrin repeats (many copies);
211-265 5.93e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 5.93e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 767922798   211 GNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGAlCLELLV 265
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
246-298 6.87e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 6.87e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 767922798   246 TPLHFAAASTHGAlCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTII 298
Cdd:pfam13637    3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
10-139 7.24e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.52  E-value: 7.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   10 DNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNArdknwqtplhiaaan 89
Cdd:PHA02875  132 NTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDY--------------- 196
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 767922798   90 kavkcaealvpllsnvnVSDRAGRTALHHAAFSGHGEMVKLLLSRGANIN 139
Cdd:PHA02875  197 -----------------FGKNGCVAALCYAIENNKIDIVRLFIKRGADCN 229
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
350-569 8.71e-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: 46.41  E-value: 8.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  350 LAALSGFSDCCRKLLSSgfDIDTPDDFGRTCLHAAA---AGGNLECLNLLLNTGADFNKKDKF-----------GRSPLH 415
Cdd:cd21882     1 LEELLGLLECLRWYLTD--SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELvnapctdefyqGQTALH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  416 YAAANCNYQCLFALVGSGASVND------LDERGCT-------PLHYAATSDTDgKCLEYLLRNDANP---GIRDKQGYN 479
Cdd:cd21882    79 IAIENRNLNLVRLLVENGADVSAratgrfFRKSPGNlfyfgelPLSLAACTNQE-EIVRLLLENGAQPaalEAQDSLGNT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  480 AVHysaayghrlCLQLIASETPLDVLMETSGTDMLsdsdnratispLHLAAYHGHHQALEvlvqslldlDVRNSSGRTPL 559
Cdd:cd21882   158 VLH---------ALVLQADNTPENSAFVCQMYNLL-----------LSYGAHLDPTQQLE---------EIPNHQGLTPL 208
                         250
                  ....*....|
gi 767922798  560 DLAAFKGHVE 569
Cdd:cd21882   209 KLAAVEGKIV 218
PHA02798 PHA02798
ankyrin-like protein; Provisional
618-838 1.13e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.98  E-value: 1.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  618 VDIQDGNGQTPL--MLSVL---NGHTDCVYSLLNKGANVDAKDKWGRTA----LHRGAVTgHEECVDALLQHGAKCLLRD 688
Cdd:PHA02798   64 VNGLDNEYSTPLctILSNIkdyKHMLDIVKILIENGADINKKNSDGETPlyclLSNGYIN-NLEILLFMIENGADTTLLD 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  689 SRGRTPIHLSAACGH---IGVLGALLQSAasMDANpaTADN-HGYTALHwaCYNGHE------TCVELLLEQ----EVFQ 754
Cdd:PHA02798  143 KDGFTMLQVYLQSNHhidIEIIKLLLEKG--VDIN--THNNkEKYDTLH--CYFKYNidridaDILKLFVDNgfiiNKEN 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  755 KTEGNAFSPLHCAVINDNEGAAEMLIDTLGASI-VNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLM 833
Cdd:PHA02798  217 KSHKKKFMEYLNSLLYDNKRFKKNILDFIFSYIdINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLF 296

                  ....*
gi 767922798  834 MAAEN 838
Cdd:PHA02798  297 TAFEN 301
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
611-720 1.27e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 1.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  611 NAEPQNAVDiqdgngQTPL-MLSV------LNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAK 683
Cdd:PTZ00322   67 NLTTEEVID------PVVAhMLTVelcqlaASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAD 140
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 767922798  684 CLLRDSRGRTPIHLSAACGHIGVLGALL---QSAASMDAN 720
Cdd:PTZ00322  141 PTLLDKDGKTPLELAEENGFREVVQLLSrhsQCHFELGAN 180
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
349-465 1.39e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 1.39e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  349 HLAALSGFSDccrKLLSSGFDIDTPDDFGRTCLHAA-------AAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANC 421
Cdd:PTZ00322   50 HLEALEATEN---KDATPDHNLTTEEVIDPVVAHMLtvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANG 126
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 767922798  422 NYQCLFALVGSGASVNDLDERGCTPLHYAATSDTdGKCLEYLLR 465
Cdd:PTZ00322  127 HVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF-REVVQLLSR 169
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
794-825 1.69e-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: 1.69e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 767922798   794 KGRTPLHAAA-FTDHVECLQLLLSHNAQVNSVD 825
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
836-931 1.73e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 1.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  836 AENGQTNTVEMLVSSAsAELTLQDNSKNTALHLACSKGHETSALLILEKITDRNLINATNaalQTPLHVAARNGLTMVVQ 915
Cdd:PTZ00322   90 AASGDAVGARILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDG---KTPLELAEENGFREVVQ 165
                          90
                  ....*....|....*.
gi 767922798  916 ELLGKGASVLAVDENG 931
Cdd:PTZ00322  166 LLSRHSQCHFELGANA 181
Ank_5 pfam13857
Ankyrin repeats (many copies);
197-251 3.38e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 3.38e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767922798   197 LLDLG-VDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFA 251
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
784-835 3.52e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 3.52e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767922798   784 GASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMA 835
Cdd:pfam13857    5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
179-206 3.73e-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: 38.72  E-value: 3.73e-04
                            10        20
                    ....*....|....*....|....*...
gi 767922798    179 YTPLHAAASSGMISVVKYLLDLGVDMNE 206
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
512-562 3.77e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 3.77e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767922798   512 DMLSDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLA 562
Cdd:pfam13857    6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
624-656 3.82e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.81  E-value: 3.82e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 767922798   624 NGQTPLMLSVL-NGHTDCVYSLLNKGANVDAKDK 656
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
37-86 4.37e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 4.37e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 767922798    37 ARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQTPLHIA 86
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
206-322 4.42e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 44.36  E-value: 4.42e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  206 EPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQK----------NEKGF----TPLHFAAASTHGALcLELLVGNGAD- 270
Cdd:cd22194   136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkyKHEGFyfgeTPLALAACTNQPEI-VQLLMEKESTd 214
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767922798  271 VNMKSKDGKTPLHMTALHGRFSRSQT--IIQSGAVI--DCEDKN--------GNTPLHIAARYG 322
Cdd:cd22194   215 ITSQDSRGNTVLHALVTVAEDSKTQNdfVKRMYDMIllKSENKNletirnneGLTPLQLAAKMG 278
PHA02859 PHA02859
ankyrin repeat protein; Provisional
400-482 4.64e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.50  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  400 GADFNKKDK-FGRSPLHYAAA---NCNYQCLFALVGSGASVNDLDERGCTPLH-YAATSDTDGKCLEYLLRNDANPGIRD 474
Cdd:PHA02859   76 GADVNFKTRdNNLSALHHYLSfnkNVEPEILKILIDSGSSITEEDEDGKNLLHmYMCNFNVRINVIKLLIDSGVSFLNKD 155

                  ....*...
gi 767922798  475 KQGYNAVH 482
Cdd:PHA02859  156 FDNNNILY 163
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
349-443 4.76e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 4.76e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  349 HLAAlSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFA 428
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
                          90
                  ....*....|....*
gi 767922798  429 LVGSGASVNDLDERG 443
Cdd:PTZ00322  167 LSRHSQCHFELGANA 181
Ank_5 pfam13857
Ankyrin repeats (many copies);
131-185 4.78e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 4.78e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767922798   131 LLSRG-ANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAA 185
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02884 PHA02884
ankyrin repeat protein; Provisional
27-167 4.78e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 43.43  E-value: 4.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   27 EIIELLILSGARVNAK----DSKWLTPLHRAVASCSEEAVQVLLKHSADVNARDKNWQ-TPLHIAAANKAVKCAEALVPL 101
Cdd:PHA02884   47 DIIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSY 126
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767922798  102 LSNVNVSDRAGRTALHHAAFSGHGEMVKLLlsRGANINAFDKKDRRaihwaaYMGHIEVVKLLVSH 167
Cdd:PHA02884  127 GADINIQTNDMVTPIELALMICNNFLAFMI--CDNEISNFYKHPKK------ILINFDILKILVSH 184
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
442-475 5.08e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 5.08e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 767922798   442 RGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDK 475
Cdd:pfam00023    1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
794-822 5.48e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 5.48e-04
                            10        20
                    ....*....|....*....|....*....
gi 767922798    794 KGRTPLHAAAFTDHVECLQLLLSHNAQVN 822
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
210-238 6.73e-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: 37.95  E-value: 6.73e-04
                            10        20
                    ....*....|....*....|....*....
gi 767922798    210 YGNTPLHVACYNGQDVVVNELIDCGAIVN 238
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
112-252 7.31e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.59  E-value: 7.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  112 GRTALHHAAFSGHGEMVKLLLSRGANINA------FDKKDRraiHWAAYMGHievvkllvshgaevtckdkksyTPLHAA 185
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNAhakgvfFNPKYK---HEGFYFGE----------------------TPLALA 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  186 ASSGMISVVKYLLDlgvdmNEPNAY------GNTPLH----VA-CYNGQDVVVNELID-----CG--AIVNQKNEKGFTP 247
Cdd:cd22194   196 ACTNQPEIVQLLME-----KESTDItsqdsrGNTVLHalvtVAeDSKTQNDFVKRMYDmillkSEnkNLETIRNNEGLTP 270

                  ....*
gi 767922798  248 LHFAA 252
Cdd:cd22194   271 LQLAA 275
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
10-69 8.08e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 8.08e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   10 DNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEEAVQVLLKHS 69
Cdd:PTZ00322  112 DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHS 171
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
243-276 9.26e-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: 37.65  E-value: 9.26e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 767922798   243 KGFTPLHFAAASTHGALCLELLVGNGADVNMKSK 276
Cdd:pfam00023    1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
126-348 1.04e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 42.98  E-value: 1.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  126 EMVKLLLSRG-ANINAFDKKDRRAIhWAAYMGH----IEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMI--SVVKYLL 198
Cdd:PHA02716  156 DLIKYMVDVGiVNLNYVCKKTGYGI-LHAYLGNmyvdIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNVcaSVIKKII 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  199 DLGVDMNEPNAYGNTPLHVACYNGQDV---VVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKS 275
Cdd:PHA02716  235 ELGGDMDMKCVNGMSPIMTYIINIDNInpeITNIYIESLDGNKVKNIPMILHSYITLARNIDISVVYSFLQPGVKLHYKD 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  276 KDGKTPLHMTALHGRFSRS--QTIIQSGAVIDCEDKNGNTPLH-------IAARYGHEL-------LINTLITSGADTAK 339
Cdd:PHA02716  315 SAGRTCLHQYILRHNISTDiiKLLHEYGNDLNEPDNIGNTVLHtylsmlsVVNILDPETdndirldVIQCLISLGADITA 394

                  ....*....
gi 767922798  340 RGIHGMFPL 348
Cdd:PHA02716  395 VNCLGYTPL 403
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
590-696 1.06e-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: 42.94  E-value: 1.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  590 RTPIHAAATN---GHSECLRLLIgNAEPQNAVDIQDGN---------GQTPLMLSVLNGHTDCVYSLLNKGANVDAK--- 654
Cdd:cd21882    27 KTCLHKAALNlndGVNEAIMLLL-EAAPDSGNPKELVNapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSARatg 105
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767922798  655 ---DKWGRTALHRG-------AVTGHEECVDALLQHGAK---CLLRDSRGRTPIH 696
Cdd:cd21882   106 rffRKSPGNLFYFGelplslaACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLH 160
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
310-336 1.10e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 1.10e-03
                            10        20
                    ....*....|....*....|....*..
gi 767922798    310 NGNTPLHIAARYGHELLINTLITSGAD 336
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank_5 pfam13857
Ankyrin repeats (many copies);
6-53 1.11e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.11e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*...
gi 767922798     6 LRDQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRA 53
Cdd:pfam13857    9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
210-242 1.13e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 1.13e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 767922798   210 YGNTPLHVACY-NGQDVVVNELIDCGAIVNQKNE 242
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA02798 PHA02798
ankyrin-like protein; Provisional
777-892 1.26e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.51  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  777 EMLIDtLGASiVNATDSKGRTPL-----HAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVS-- 849
Cdd:PHA02798   55 KLFIN-LGAN-VNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFmi 132
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 767922798  850 SASAELTLQDNSKNTALHLACSKGHETSALLI---LEKITDRNLIN 892
Cdd:PHA02798  133 ENGADTTLLDKDGFTMLQVYLQSNHHIDIEIIkllLEKGVDINTHN 178
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
727-749 1.27e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 1.27e-03
                            10        20
                    ....*....|....*....|...
gi 767922798    727 HGYTALHWACYNGHETCVELLLE 749
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLD 23
PHA02736 PHA02736
Viral ankyrin protein; Provisional
109-219 1.36e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 40.24  E-value: 1.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  109 DRAGRTALHHaaFSGHGEMVKLLLSRGANINA-------FDKKDRRAIHWAAYMGHI---EVVKLLVSHGAEVTCKDKK- 177
Cdd:PHA02736   14 DIEGENILHY--LCRNGGVTDLLAFKNAISDEnrylvleYNRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKERVf 91
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 767922798  178 SYTPLHAAASSGMISVVKYLLDL-GVDMNEPNAYGNTPLHVAC 219
Cdd:PHA02736   92 GNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVAC 134
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
590-696 1.47e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.44  E-value: 1.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  590 RTPIHAAATNGhseCLRLLIgNAEPQNavdiQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDK------------- 656
Cdd:cd22194   114 RILLAFAEENG---ILDRFI-NAEYTE----EAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegf 185
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 767922798  657 -WGRTALHRGAVTGHEECVDALLQHGAKCL-LRDSRGRTPIH 696
Cdd:cd22194   186 yFGETPLALAACTNQPEIVQLLMEKESTDItSQDSRGNTVLH 227
Ank_5 pfam13857
Ankyrin repeats (many copies);
401-450 1.48e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 1.48e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 767922798   401 ADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYA 450
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
15-134 1.72e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.38  E-value: 1.72e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798    15 TPLHAAAYLGDAEIIELLILSGARVNAK------------DSKWLT--PLHRAVASCSEEAVQVLLKHSADVNARDKNWQ 80
Cdd:TIGR00870  130 TALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqgvDSFYHGesPLNAAACLGSPSIVALLSEDPADILTADSLGN 209
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798    81 TPLHIAAANKAVK---------CAEALVPLLSNVN-------VSDRAGRTALHHAAFSGHGEMVKLLLSR 134
Cdd:TIGR00870  210 TLLHLLVMENEFKaeyeelscqMYNFALSLLDKLRdskelevILNHQGLTPLKLAAKEGRIVLFRLKLAI 279
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
148-173 1.93e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 1.93e-03
                            10        20
                    ....*....|....*....|....*.
gi 767922798    148 AIHWAAYMGHIEVVKLLVSHGAEVTC 173
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
14-43 2.18e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 2.18e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 767922798    14 RTPLHAAAY-LGDAEIIELLILSGARVNAKD 43
Cdd:pfam00023    3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
863-918 2.22e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 2.22e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 767922798   863 NTALHLACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELL 918
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
644-697 2.26e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 2.26e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 767922798   644 LLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHL 697
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PHA02989 PHA02989
ankyrin repeat protein; Provisional
191-450 2.32e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 41.65  E-value: 2.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  191 ISVVKYLLDLGVDMNEpnAYGNTPLHVACYNGQDV---VVNELIDCGAIVNQKnekGF--TPL-----HFAAASTHGALC 260
Cdd:PHA02989   16 KNALEFLLRTGFDVNE--EYRGNSILLLYLKRKDVkikIVKLLIDNGADVNYK---GYieTPLcavlrNREITSNKIKKI 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  261 LELLVGNGADVNMKSKDGKTPLhMTALHG---------RFsrsqtIIQSGA-VIDCEDKNGNTPLHIaarYGHELLINT- 329
Cdd:PHA02989   91 VKLLLKFGADINLKTFNGVSPI-VCFIYNsninncdmlRF-----LLSKGInVNDVKNSRGYNLLHM---YLESFSVKKd 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  330 ----LITSGADT-AKRGIHGMFPLHLAALSGFS----DCCRKLLSSGFDIDTPDDFGRTCLHAAAagGNLECLNLLLNTG 400
Cdd:PHA02989  162 vikiLLSFGVNLfEKTSLYGLTPMNIYLRNDIDvisiKVIKYLIKKGVNIETNNNGSESVLESFL--DNNKILSKKEFKV 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 767922798  401 ADF-------NKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYA 450
Cdd:PHA02989  240 LNFilkyikiNKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
148-176 2.38e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 2.38e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 767922798   148 AIHWAAYM-GHIEVVKLLVSHGAEVTCKDK 176
Cdd:pfam00023    5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
144-254 2.64e-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: 41.72  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  144 KDRRAIHWAAYMGHIEVVKLLVSHGAEVTC-------KDKKSYT-------PLHAAASSGMISVVKYLLD---LGVDMNE 206
Cdd:cd22196    93 KGQTALHIAIERRNMHLVELLVQNGADVHArasgeffKKKKGGPgfyfgelPLSLAACTNQLDIVKFLLEnphSPADISA 172
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767922798  207 PNAYGNTPLHVACYNGQDVVVN---------ELIDCGAIVNQK-------NEKGFTPLHFAAAS 254
Cdd:cd22196   173 RDSMGNTVLHALVEVADNTPENtkfvtkmynEILILGAKIRPLlkleeitNKKGLTPLKLAAKT 236
Ank_5 pfam13857
Ankyrin repeats (many copies);
889-934 2.68e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 2.68e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 767922798   889 NLINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTP 934
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
555-581 2.69e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 2.69e-03
                            10        20
                    ....*....|....*....|....*..
gi 767922798    555 GRTPLDLAAFKGHVECVDVLINQGASI 581
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
555-585 2.93e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 2.93e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 767922798   555 GRTPLDLAAFK-GHVECVDVLINQGASILVKD 585
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
316-388 2.95e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 2.95e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767922798  316 HIAARyGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGG 388
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
Ank_5 pfam13857
Ankyrin repeats (many copies);
104-143 3.32e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 3.32e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|
gi 767922798   104 NVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDK 143
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDE 47
Ank_5 pfam13857
Ankyrin repeats (many copies);
434-483 3.49e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 3.49e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 767922798   434 ASVNDLDERGCTPLHYAAtSDTDGKCLEYLLRNDANPGIRDKQGYNAVHY 483
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAA-KYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
788-920 3.61e-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: 41.33  E-value: 3.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  788 VNA--TDS--KGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDST--------------GKTPLMMAAENGQTNTVEMLVS 849
Cdd:cd22196    83 VNAayTDSyyKGQTALHIAIERRNMHLVELLVQNGADVHARASGeffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLE 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  850 S--ASAELTLQDNSKNTALHLACS---------------------KGHETSALLILEKITDRNLInatnaalqTPLHVAA 906
Cdd:cd22196   163 NphSPADISARDSMGNTVLHALVEvadntpentkfvtkmyneiliLGAKIRPLLKLEEITNKKGL--------TPLKLAA 234
                         170
                  ....*....|....
gi 767922798  907 RNGLTMVVQELLGK 920
Cdd:cd22196   235 KTGKIGIFAYILGR 248
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
48-77 3.75e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 3.75e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 767922798    48 TPLHRAVASC-SEEAVQVLLKHSADVNARDK 77
Cdd:pfam00023    4 TPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
PHA02859 PHA02859
ankyrin repeat protein; Provisional
762-867 4.03e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.80  E-value: 4.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  762 SPLHCAVIND--NEGAAEMLIDTlGASIVNATDSKGRTPLHA-AAFTDHV--ECLQLLLSHNAQVNSVDSTGKTPLMMAA 836
Cdd:PHA02859   53 TPIFSCLEKDkvNVEILKFLIEN-GADVNFKTRDNNLSALHHyLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHMYM 131
                          90       100       110
                  ....*....|....*....|....*....|...
gi 767922798  837 ENGQTN--TVEMLVSSASAELTlQDNSKNTALH 867
Cdd:PHA02859  132 CNFNVRinVIKLLIDSGVSFLN-KDFDNNNILY 163
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
624-653 4.07e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 4.07e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 767922798    624 NGQTPLMLSVLNGHTDCVYSLLNKGANVDA 653
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
787-909 4.16e-03

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 40.99  E-value: 4.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  787 IVNA--TDS--KGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDST-------------GKTPLMMAAENGQTNTVEMLVS 849
Cdd:cd22197    82 LVNAqcTDEyyRGHSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELPLSLAACTKQWDVVNYLLE 161
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767922798  850 SAS--AELTLQDNSKNTALH---LACSKGHETSALL------ILEKITDRN----LINATNAALQTPLHVAARNG 909
Cdd:cd22197   162 NPHqpASLQAQDSLGNTVLHalvMIADNSPENSALVikmydgLLQAGARLCptvqLEEISNHEGLTPLKLAAKEG 236
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
363-543 4.38e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.83  E-value: 4.38e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   363 LLSSGFDIDTpddfGRTCLHAA-----------------AAGGNLECLNLLLNTGADFNkkdkFGRSPLHYAAANCNYQC 425
Cdd:TIGR00870   72 LLNLSCRGAV----GDTLLHAIsleyvdaveaillhllaAFRKSGPLELANDQYTSEFT----PGITALHLAAHRQNYEI 143
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   426 LFALVGSGASVN--------------DLDERGCTPLH-YAATSDTDgkCLEYLLRNDANPGIRDKQGYNAVH-------Y 483
Cdd:TIGR00870  144 VKLLLERGASVParacgdffvksqgvDSFYHGESPLNaAACLGSPS--IVALLSEDPADILTADSLGNTLLHllvmeneF 221
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767922798   484 SAAYGH--RLCLQLIasetpLDVLMETSGTDMLSDSDNRATISPLHLAAYHGHHQALEVLVQ 543
Cdd:TIGR00870  222 KAEYEElsCQMYNFA-----LSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
Ank_4 pfam13637
Ankyrin repeats (many copies);
900-951 4.97e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 4.97e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 767922798   900 TPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADCLALI 951
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02791 PHA02791
ankyrin-like protein; Provisional
724-893 5.16e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.03  E-value: 5.16e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  724 ADNHGYTALHWACYNGHETCVELLLEQEVFQKTEGNAFsPLH-CAVINDNEGAAEMLIDTLGASivnATDSKGRTPLHAA 802
Cdd:PHA02791   26 ADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF-PLHqAATLEDTKIVKILLFSGMDDS---QFDDKGNTALYYA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  803 AFTDHVECLQLLLSHNAQVNSVDSTG-KTPLMMAAENGQTNTVEMLVSSASAELTLQdnSKNTALHLACSKGHETSALLI 881
Cdd:PHA02791  102 VDSGNMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPSTFDLA--ILLSCIHITIKNGHVDMMILL 179
                         170
                  ....*....|..
gi 767922798  882 LEKITDRNLINA 893
Cdd:PHA02791  180 LDYMTSTNTNNS 191
PHA02884 PHA02884
ankyrin repeat protein; Provisional
193-287 5.98e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.97  E-value: 5.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  193 VVKYLLDLGVDMNEP-----NAYgNTPLHVACYNGQDVVVNELIDCGAIVNQ-KNEKGFTPLHFAAasTHGAL-CLELLV 265
Cdd:PHA02884   48 IIDAILKLGADPEAPfplseNSK-TNPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKITPLYISV--LHGCLkCLEILL 124
                          90       100
                  ....*....|....*....|..
gi 767922798  266 GNGADVNMKSKDGKTPLHMTAL 287
Cdd:PHA02884  125 SYGADINIQTNDMVTPIELALM 146
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
210-238 6.47e-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: 35.31  E-value: 6.47e-03
                           10        20
                   ....*....|....*....|....*....
gi 767922798   210 YGNTPLHVACYNGQDVVVNELIDCGAIVN 238
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_4 pfam13637
Ankyrin repeats (many copies);
830-875 6.69e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 6.69e-03
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 767922798   830 TPLMMAAENGQTNTVEMLVSSaSAELTLQDNSKNTALHLACSKGHE 875
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNV 47
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
310-336 7.65e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 7.65e-03
                           10        20
                   ....*....|....*....|....*..
gi 767922798   310 NGNTPLHIAARYGHELLINTLITSGAD 336
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
PHA02791 PHA02791
ankyrin-like protein; Provisional
69-247 8.91e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 39.25  E-value: 8.91e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   69 SADVNARDKNWQTPLHIAAANKAVKC------AEALVPLLSNvnvsdragRTALHHAAFSGHGEMVKLLLSRGANINAFD 142
Cdd:PHA02791   20 SKDAFKADVHGHSALYYAIADNNVRLvctllnAGALKNLLEN--------EFPLHQAATLEDTKIVKILLFSGMDDSQFD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  143 KKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSY-TPLHAAASSGMISVVKYLL-------DLGVDMnepnaygnTP 214
Cdd:PHA02791   92 DKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLseipstfDLAILL--------SC 163
                         170       180       190
                  ....*....|....*....|....*....|...
gi 767922798  215 LHVACYNGQDVVVNELIDCGAIVNQKNEKGFTP 247
Cdd:PHA02791  164 IHITIKNGHVDMMILLLDYMTSTNTNNSLLFIP 196
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
310-336 9.00e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 9.00e-03
                           10        20
                   ....*....|....*....|....*...
gi 767922798   310 NGNTPLHIAA-RYGHELLINTLITSGAD 336
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGAD 28
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
538-732 9.03e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 39.90  E-value: 9.03e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  538 LEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVeCVDVL---INQGASILVKdYILKRTPIHAAATNghseclrllIGNAEP 614
Cdd:PHA02716  195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNV-CASVIkkiIELGGDMDMK-CVNGMSPIMTYIIN---------IDNINP 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  615 Q--NA-VDIQDGNGQT--PLMLSVL-----NGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGH--EECVDALLQHGA 682
Cdd:PHA02716  264 EitNIyIESLDGNKVKniPMILHSYitlarNIDISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTDIIKLLHEYGN 343
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767922798  683 KCLLRDSRGRTPIH--LSAACG------------HIGVLGALLQSAASMDAnpatADNHGYTAL 732
Cdd:PHA02716  344 DLNEPDNIGNTVLHtyLSMLSVvnildpetdndiRLDVIQCLISLGADITA----VNCLGYTPL 403
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
738-918 9.10e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.06  E-value: 9.10e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   738 NGHETCVELLLEQEVFQKTEGNAfspLHCAVINDnEGAAEMLI--------DTLGASIVNATD----SKGRTPLHAAAFT 805
Cdd:TIGR00870   63 NENLELTELLLNLSCRGAVGDTL---LHAISLEY-VDAVEAILlhllaafrKSGPLELANDQYtsefTPGITALHLAAHR 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   806 DHVECLQLLLSHNAQVNS------------VDST--GKTPLMMAAENGQTNTVEMLvSSASAELTLQDNSKNTALHL--- 868
Cdd:TIGR00870  139 QNYEIVKLLLERGASVPAracgdffvksqgVDSFyhGESPLNAAACLGSPSIVALL-SEDPADILTADSLGNTLLHLlvm 217
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798   869 ---------ACSKGHETSALLILEKITD-RNLINATNAALQTPLHVAARNGLTMVVQELL 918
Cdd:TIGR00870  218 enefkaeyeELSCQMYNFALSLLDKLRDsKELEVILNHQGLTPLKLAAKEGRIVLFRLKL 277
Ank_4 pfam13637
Ankyrin repeats (many copies);
445-495 9.17e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 9.17e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 767922798   445 TPLHYAATSDtDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCLQL 495
Cdd:pfam13637    3 TALHAAAASG-HLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKL 52
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
491-574 9.18e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.88  E-value: 9.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  491 LClQLIASETPLDV-LMETSGTDMLS-DSDNRatiSPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHV 568
Cdd:PTZ00322   86 LC-QLAASGDAVGArILLTGGADPNCrDYDGR---TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161

                  ....*.
gi 767922798  569 ECVDVL 574
Cdd:PTZ00322  162 EVVQLL 167
PHA02736 PHA02736
Viral ankyrin protein; Provisional
206-335 9.63e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.93  E-value: 9.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  206 EPNAYGNTPLHVACYNGqDVV-----VNELIDCGA-IVNQKNEKGFTPLHFAAAS--THGALCLELLVGNGADVNMK-SK 276
Cdd:PHA02736   12 EPDIEGENILHYLCRNG-GVTdllafKNAISDENRyLVLEYNRHGKQCVHIVSNPdkADPQEKLKLLMEWGADINGKeRV 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767922798  277 DGKTPLHMTALHGRFSRSQTII-QSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGA 335
Cdd:PHA02736   91 FGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
 
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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