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Conserved domains on  [gi|1953334645|ref|XP_038288164|]
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serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A isoform X5 [Canis lupus familiaris]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
31-287 2.59e-50

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 179.38  E-value: 2.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  31 LEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANI 110
Cdd:COG0666    34 LLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 111 NAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVA 190
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 191 CYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTII 270
Cdd:COG0666   194 AENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
                         250
                  ....*....|....*..
gi 1953334645 271 QSGAVIDCEDKNGNTPL 287
Cdd:COG0666   273 LALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
546-870 6.75e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 6.75e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 546 LINQGASILVKDYILKRTPIHAAATNGHSECLRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDA 625
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 626 KDKWGRTALHRGAVTGHEECVDALLQHGAKCLFRDSRGRTPIHLSAACGHIGVLGALLQSAASVDAnpaiADNHGYTALH 705
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA----QDNDGNTPLH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 706 WACYNGHETCVELLLEQevfqktegnafsplhcavindneGAaemlidtlgasIVNATDSKGRTPLHAAAFTDHVECLQL 785
Cdd:COG0666   159 LAAANGNLEIVKLLLEA-----------------------GA-----------DVNARDNDGETPLHLAAENGHLEIVKL 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 786 LLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVsSASADLTLQDNSKNTALHLACSKGHETSALLILEKITDRNLINA 865
Cdd:COG0666   205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL-EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283

                  ....*
gi 1953334645 866 TNAAL 870
Cdd:COG0666   284 DLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
169-447 4.56e-33

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 129.69  E-value: 4.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 169 LLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSK 248
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 249 DGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGF 328
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 329 SDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASV 408
Cdd:COG0666   166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1953334645 409 NDLDERGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDK 447
Cdd:COG0666   246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
Ank_4 pfam13637
Ankyrin repeats (many copies);
496-547 2.01e-10

Ankyrin repeats (many copies);


:

Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.90  E-value: 2.01e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953334645 496 SPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLI 547
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
861-906 2.79e-03

Ankyrin repeats (many copies);


:

Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 2.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1953334645 861 NLINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTP 906
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
31-287 2.59e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 179.38  E-value: 2.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  31 LEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANI 110
Cdd:COG0666    34 LLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 111 NAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVA 190
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 191 CYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTII 270
Cdd:COG0666   194 AENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
                         250
                  ....*....|....*..
gi 1953334645 271 QSGAVIDCEDKNGNTPL 287
Cdd:COG0666   273 LALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
546-870 6.75e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 6.75e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 546 LINQGASILVKDYILKRTPIHAAATNGHSECLRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDA 625
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 626 KDKWGRTALHRGAVTGHEECVDALLQHGAKCLFRDSRGRTPIHLSAACGHIGVLGALLQSAASVDAnpaiADNHGYTALH 705
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA----QDNDGNTPLH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 706 WACYNGHETCVELLLEQevfqktegnafsplhcavindneGAaemlidtlgasIVNATDSKGRTPLHAAAFTDHVECLQL 785
Cdd:COG0666   159 LAAANGNLEIVKLLLEA-----------------------GA-----------DVNARDNDGETPLHLAAENGHLEIVKL 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 786 LLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVsSASADLTLQDNSKNTALHLACSKGHETSALLILEKITDRNLINA 865
Cdd:COG0666   205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL-EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283

                  ....*
gi 1953334645 866 TNAAL 870
Cdd:COG0666   284 DLLTL 288
PHA03100 PHA03100
ankyrin repeat protein; Provisional
34-245 7.67e-36

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 141.34  E-value: 7.67e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  34 VQVLLKHSADVNARDKNWQTPLHIAAANKAV-----KCAEALVPLLSNVNVSDRAGRTALHHAAF--SGHGEMVKLLLSR 106
Cdd:PHA03100   51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDN 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 107 GANINAFDKKDRRAIHWAAYMGHI--EVVKLLVAHGAEVTCKDKksytplhaaassgmisvVKYLLDLGVDMNEPNAYGN 184
Cdd:PHA03100  131 GANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGF 193
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953334645 185 TPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNM 245
Cdd:PHA03100  194 TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI-FKLLLNNGPSIKT 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
169-447 4.56e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 129.69  E-value: 4.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 169 LLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSK 248
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 249 DGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGF 328
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 329 SDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASV 408
Cdd:COG0666   166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1953334645 409 NDLDERGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDK 447
Cdd:COG0666   246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
PHA03095 PHA03095
ankyrin-like protein; Provisional
163-419 1.66e-31

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 129.37  E-value: 1.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 163 ISVVKYLLDLGVDMNEPNAYGNTPLHV--ACYNGQDV-VVNELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLVGN 239
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLylHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 240 GADVNMKSKDGKTPLH--MTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGH---ELLiNTLITSGADTAKRGI 314
Cdd:PHA03095  107 GADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGADVYAVDD 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 315 HGMFPLHLAALS--GFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLL--NTGADFNKKDKFGRSPLHYAA 390
Cdd:PHA03095  186 RFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPllIAGISINARNRYGQTPLHYAA 265
                         250       260       270
                  ....*....|....*....|....*....|
gi 1953334645 391 ANCNyQCLFA-LVGSGASVNDLDERGCTPL 419
Cdd:PHA03095  266 VFNN-PRACRrLIALGADINAVSSDGNTPL 294
PHA02874 PHA02874
ankyrin repeat protein; Provisional
498-807 2.32e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 101.19  E-value: 2.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 498 LHLAAYHGHHQALEVLVQS---LLDLDVRNSSgrTPLDLAAFKGHVECVDVLINQGASIlvkDYILKRTP--IHAAATNG 572
Cdd:PHA02874    5 LRMCIYSGDIEAIEKIIKNkgnCINISVDETT--TPLIDAIRSGDAKIVELFIKHGADI---NHINTKIPhpLLTAIKIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 573 HSECLRLLIGNAEPQNAVDIQDGNGQTplmlsvlnghtdcVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQH 652
Cdd:PHA02874   80 AHDIIKLLIDNGVDTSILPIPCIEKDM-------------IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEY 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 653 GAKCLFRDSRGRTPIHLSAACGHIGVLGALLQSAASVDANpaiaDNHGYTALHWACYNGHETCVELLLEQ--EVFQKTEg 730
Cdd:PHA02874  147 GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK----DNNGESPLHNAAEYGDYACIKLLIDHgnHIMNKCK- 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953334645 731 NAFSPLHCAVINdNEGAAEMLIDTlgASIvNATDSKGRTPLH-AAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMA 807
Cdd:PHA02874  222 NGFTPLHNAIIH-NRSAIELLINN--ASI-NDQDIDGSTPLHhAINPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
88-180 1.04e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.48  E-value: 1.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  88 LHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHgAEVTCKDKKsYTPLHAAASSGMISVVK 167
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1953334645 168 YLLDLGVDMNEPN 180
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
531-627 3.23e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 3.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 531 LDLAAFKGHVECVDVLINQGASILVKDyILKRTPIHAAATNGHSECLRLLIGNAEPQNavdiqDGNGQTPLMLSVLNGHT 610
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAARSGHL 74
                          90
                  ....*....|....*..
gi 1953334645 611 DCVYSLLNKGANVDAKD 627
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
254-346 1.06e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 254 LHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGAdtAKRGIHGMFPLHLAALSGFSDCCR 333
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1953334645 334 KLLSSGFDIDTPD 346
Cdd:pfam12796  79 LLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
7-203 1.45e-12

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 71.58  E-value: 1.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645   7 MKRELHcmllpILEMQK-SLNCLFY------LEAVQVLLK-HSADVNARDKNWQTPLHIAAANKAVKCAEAL---VPLLS 75
Cdd:cd22192     4 MLDELH-----LLQQKRiSESPLLLaakendVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLmeaAPELV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  76 NVNV-SD-RAGRTALHHAAFSGHGEMVKLLLSRGANIN-------AFDKKDRRAIHW-------AAYMGHIEVVKLLVAH 139
Cdd:cd22192    79 NEPMtSDlYQGETALHIAVVNQNLNLVRELIARGADVVspratgtFFRPGPKNLIYYgehplsfAACVGNEEIVRLLIEH 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953334645 140 GAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNE----------PNAYGNTPLHVACYNGQDVVVNELI 203
Cdd:cd22192   159 GADIRAQDSLGNTVLHILVLQPNKTFACQMYDLILSYDKeddlqpldlvPNNQGLTPFKLAAKEGNIVMFQHLV 232
Ank_4 pfam13637
Ankyrin repeats (many copies);
496-547 2.01e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.90  E-value: 2.01e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953334645 496 SPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLI 547
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
529-669 1.92e-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: 61.57  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 529 TPLDLAAFKGHVECVDVLINQGASILVKDYILKRTPIHAAATNGHSECLRLLIGNA-----EPQNAVDIQdgnGQTPLML 603
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelvnEPMTSDLYQ---GETALHI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 604 SVLNGHTDCVYSLLNKGANV--------------DAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLFRDSRGRTPIHL 669
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
518-741 4.46e-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: 4.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 518 LDLDVRNSSGRTPLDLAAFKG-HVECVDVLINQGASILVKDyilkrTPIHAAATNGH---SECLRLLIGNAE----PQNA 589
Cdd:TIGR00870  43 LNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGD-----TLLHAISLEYVdavEAILLHLLAAFRksgpLELA 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 590 VDIQDGN---GQTPLMLSVLNGHTDCVYSLLNKGANVDAKDK--------------WGRTALHRGAVTGHEECVDALLQH 652
Cdd:TIGR00870 118 NDQYTSEftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSED 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 653 GAKCLFRDSRGRTPIHLSA------------ACG-HIGVLGALLQSAASVDANpAIADNHGYTALHWACYNGHETCVELL 719
Cdd:TIGR00870 198 PADILTADSLGNTLLHLLVmenefkaeyeelSCQmYNFALSLLDKLRDSKELE-VILNHQGLTPLKLAAKEGRIVLFRLK 276
                         250       260
                  ....*....|....*....|...
gi 1953334645 720 LEQEVFQKT-EGNAFSPLHCAVI 741
Cdd:TIGR00870 277 LAIKYKQKKfVAWPNGQQLLSLY 299
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
218-423 1.36e-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: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 218 TPLhFAAASTHGALCLE-LLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGA-----VIDCEDKNGNTPLHIAA 291
Cdd:cd22192    19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPelvnePMTSDLYQGETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 292 RYGHELLINTLITSGADTAKRGIHGMFplhlaalsgFSDCCRKLLSsgfdidtpddFGRTCLHAAAAGGNLECLNLLLNT 371
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSPRATGTF---------FRPGPKNLIY----------YGEHPLSFAACVGNEEIVRLLIEH 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953334645 372 GADFNKKDKFGRSPLHYAA--ANCNYQC-----LFALVGSGASVNdLD----ERGCTPLHYAA 423
Cdd:cd22192   159 GADIRAQDSLGNTVLHILVlqPNKTFACqmydlILSYDKEDDLQP-LDlvpnNQGLTPFKLAA 220
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
31-191 1.42e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 52.39  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  31 LEAVQVLLKHSADVNARDknwqTPLHIAAANKAVKCAEALVPLLSN---------VNVSDR----AGRTALHHAAFSGHG 97
Cdd:TIGR00870  66 LELTELLLNLSCRGAVGD----TLLHAISLEYVDAVEAILLHLLAAfrksgplelANDQYTseftPGITALHLAAHRQNY 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  98 EMVKLLLSRGANINA------FDKKDRRA--------IHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAA----- 158
Cdd:TIGR00870 142 EIVKLLLERGASVPAracgdfFVKSQGVDsfyhgespLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenef 221
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1953334645 159 -------SSGMISVVKYLLDLGVDMNE----PNAYGNTPLHVAC 191
Cdd:TIGR00870 222 kaeyeelSCQMYNFALSLLDKLRDSKEleviLNHQGLTPLKLAA 265
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
84-112 2.09e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 2.09e-05
                           10        20
                   ....*....|....*....|....*....
gi 1953334645   84 GRTALHHAAFSGHGEMVKLLLSRGANINA 112
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
766-794 6.11e-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: 6.11e-04
                           10        20
                   ....*....|....*....|....*....
gi 1953334645  766 KGRTPLHAAAFTDHVECLQLLLSHNAQVN 794
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
282-308 1.28e-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: 1.28e-03
                           10        20
                   ....*....|....*....|....*..
gi 1953334645  282 NGNTPLHIAARYGHELLINTLITSGAD 308
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank_5 pfam13857
Ankyrin repeats (many copies);
861-906 2.79e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 2.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1953334645 861 NLINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTP 906
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
527-553 2.98e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 2.98e-03
                           10        20
                   ....*....|....*....|....*..
gi 1953334645  527 GRTPLDLAAFKGHVECVDVLINQGASI 553
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
335-515 4.42e-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: 4.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 335 LLSSGFDIDTpddfGRTCLHAA-----------------AAGGNLECLNLLLNTGADFNkkdkFGRSPLHYAAANCNYQC 397
Cdd:TIGR00870  72 LLNLSCRGAV----GDTLLHAIsleyvdaveaillhllaAFRKSGPLELANDQYTSEFT----PGITALHLAAHRQNYEI 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 398 LFALVGSGASVN--------------DLDERGCTPLH-YAATSDTDgkCLEYLLRNDANPGIRDKQGYNAVH-------Y 455
Cdd:TIGR00870 144 VKLLLERGASVParacgdffvksqgvDSFYHGESPLNaAACLGSPS--IVALLSEDPADILTADSLGNTLLHllvmeneF 221
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953334645 456 SAAYGH--RLCLQLIasetpLDVLMETSGTDMLNDSDNRATISPLHLAAYHGHHQALEVLVQ 515
Cdd:TIGR00870 222 KAEYEElsCQMYNFA-----LSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
31-287 2.59e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 179.38  E-value: 2.59e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  31 LEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANI 110
Cdd:COG0666    34 LLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 111 NAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVA 190
Cdd:COG0666   114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLA 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 191 CYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTII 270
Cdd:COG0666   194 AENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
                         250
                  ....*....|....*..
gi 1953334645 271 QSGAVIDCEDKNGNTPL 287
Cdd:COG0666   273 LALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
31-312 2.10e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 177.07  E-value: 2.10e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  31 LEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANI 110
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 111 NAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVA 190
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 191 CYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTII 270
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI-VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1953334645 271 QSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKR 312
Cdd:COG0666   240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
30-220 5.22e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.80  E-value: 5.22e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  30 YLEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGAN 109
Cdd:COG0666    99 DLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGAD 178
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 110 INAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHV 189
Cdd:COG0666   179 VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1953334645 190 ACYNGQDVVVNELIDCGANVNQKNEKGFTPL 220
Cdd:COG0666   259 AAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
98-419 5.47e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 5.47e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  98 EMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMN 177
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 178 EPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKskdgktplhmt 257
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI-VKLLLEAGADVNAQ----------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 258 alhgrfsrsqtiiqsgavidceDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLS 337
Cdd:COG0666   150 ----------------------DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 338 SGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCT 417
Cdd:COG0666   208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287

                  ..
gi 1953334645 418 PL 419
Cdd:COG0666   288 LL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
546-870 6.75e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 6.75e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 546 LINQGASILVKDYILKRTPIHAAATNGHSECLRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDA 625
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 626 KDKWGRTALHRGAVTGHEECVDALLQHGAKCLFRDSRGRTPIHLSAACGHIGVLGALLQSAASVDAnpaiADNHGYTALH 705
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA----QDNDGNTPLH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 706 WACYNGHETCVELLLEQevfqktegnafsplhcavindneGAaemlidtlgasIVNATDSKGRTPLHAAAFTDHVECLQL 785
Cdd:COG0666   159 LAAANGNLEIVKLLLEA-----------------------GA-----------DVNARDNDGETPLHLAAENGHLEIVKL 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 786 LLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVsSASADLTLQDNSKNTALHLACSKGHETSALLILEKITDRNLINA 865
Cdd:COG0666   205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL-EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283

                  ....*
gi 1953334645 866 TNAAL 870
Cdd:COG0666   284 DLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
577-907 1.90e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.40  E-value: 1.90e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 577 LRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKC 656
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 657 LFRDSRGRTPIHLSAACGHIGVLGALLQSAASVDAnpaiADNHGYTALHWACYNGHETCVELLLEQevfqktegnafspl 736
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA----RDKDGETPLHLAAYNGNLEIVKLLLEA-------------- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 737 hcavindnegaaemlidtlGASiVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTV 816
Cdd:COG0666   143 -------------------GAD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 817 EMLVsSASADLTLQDNSKNTALHLACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASV 896
Cdd:COG0666   203 KLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
                         330
                  ....*....|.
gi 1953334645 897 LAVDENGYTPA 907
Cdd:COG0666   279 AAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
451-698 1.47e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.09  E-value: 1.47e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 451 NAVHYSAAYGHRLCLQLIASETPLDVLMETSGTDMLNDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTP 530
Cdd:COG0666    44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 531 LDLAAFKGHVECVDVLINQGASILVKDyILKRTPIHAAATNGHSECLRLLIGNaepqNA-VDIQDGNGQTPLMLSVLNGH 609
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLEIVKLLLEA----GAdVNARDNDGETPLHLAAENGH 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 610 TDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLFRDSRGRTPIHLSAACGHIGVLGALLQSAASV 689
Cdd:COG0666   199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278

                  ....*....
gi 1953334645 690 DANPAIADN 698
Cdd:COG0666   279 AAALLDLLT 287
PHA03100 PHA03100
ankyrin repeat protein; Provisional
34-245 7.67e-36

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 141.34  E-value: 7.67e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  34 VQVLLKHSADVNARDKNWQTPLHIAAANKAV-----KCAEALVPLLSNVNVSDRAGRTALHHAAF--SGHGEMVKLLLSR 106
Cdd:PHA03100   51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDN 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 107 GANINAFDKKDRRAIHWAAYMGHI--EVVKLLVAHGAEVTCKDKksytplhaaassgmisvVKYLLDLGVDMNEPNAYGN 184
Cdd:PHA03100  131 GANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGF 193
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953334645 185 TPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNM 245
Cdd:PHA03100  194 TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI-FKLLLNNGPSIKT 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
484-769 4.33e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.47  E-value: 4.33e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 484 DMLNDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGASILVKDYILkRT 563
Cdd:COG0666    11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG-NT 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 564 PIHAAATNGHSECLRLLIGNAEPqnaVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHE 643
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 644 ECVDALLQHGAKCLFRDSRGRTPIHLSAACGHIGVLGALLQSaasvDANPAIADNHGYTALHWACYNGHETCVELLLEQE 723
Cdd:COG0666   167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA----GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1953334645 724 VFQKTEGNAFSPLHCAVINDNEGAAEMLIDTLGASIVNATDSKGRT 769
Cdd:COG0666   243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
681-925 8.86e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.70  E-value: 8.86e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 681 ALLQSAASVDANPAIADNHGYTALHWACYNGHETCVELLLEQEVF-QKTEGNAFSPLHCAVINDNEGAAEMLIDtLGASi 759
Cdd:COG0666    35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADiNAKDDGGNTLLHAAARNGDLEIVKLLLE-AGAD- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 760 VNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSsASADLTLQDNSKNTALH 839
Cdd:COG0666   113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLH 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 840 LACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADC 919
Cdd:COG0666   192 LAAENGHLEIVKLLLEAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268

                  ....*.
gi 1953334645 920 LALILA 925
Cdd:COG0666   269 KLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
169-447 4.56e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 129.69  E-value: 4.56e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 169 LLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSK 248
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 249 DGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGF 328
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 329 SDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASV 408
Cdd:COG0666   166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1953334645 409 NDLDERGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDK 447
Cdd:COG0666   246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
PHA03095 PHA03095
ankyrin-like protein; Provisional
30-303 5.15e-33

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 134.00  E-value: 5.15e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  30 YLEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLL---SNVNVSDRAGRTALH-HAAFSGHGEMVKLLLS 105
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLeagADVNAPERCGFTPLHlYLYNATTLDVIKLLIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 106 RGANINAFDKKDRRAIHwaAYMG----HIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISV--VKYLLDLGVDMNEP 179
Cdd:PHA03095  106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 180 NAYGNTPLHVACYNGQD--VVVNELIDCGANVNQKNEKGFTPLHFAAA-STHGALCLELLVGNGADVNMKSKDGKTPLHM 256
Cdd:PHA03095  184 DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953334645 257 TALHGR---FSRsqtIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLI 303
Cdd:PHA03095  264 AAVFNNpraCRR---LIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
681-925 1.45e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 128.15  E-value: 1.45e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 681 ALLQSAASVDANPAIADNHGYTALHWACYNGHETCVELLLEQEVFQKTEGNAFSPLHCAVINDNEGAAEMLIDTLGASIv 760
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 761 NATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSsASADLTLQDNSKNTALHL 840
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE-AGADVNAQDNDGNTPLHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 841 ACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADCL 920
Cdd:COG0666   160 AAANGNLEIVKLLLEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                  ....*
gi 1953334645 921 ALILA 925
Cdd:COG0666   237 LLLEA 241
PHA03095 PHA03095
ankyrin-like protein; Provisional
130-398 3.21e-32

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 131.69  E-value: 3.21e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 130 IEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGM---ISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDV-VVNELIDC 205
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 206 GANVNQKNEKGFTPLH--FAAASTHgALCLELLVGNGADVNMKSKDGKTPLHMtalhgrFSRS--------QTIIQSGAV 275
Cdd:PHA03095  107 GADVNAKDKVGRTPLHvyLSGFNIN-PKVIRLLLRKGADVNALDLYGMTPLAV------LLKSrnanvellRLLIDAGAD 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 276 IDCEDKNGNTPLHIAARYGH--ELLINTLITSGADTAKRGIHGMFPLHLAALsgFSDCCR----KLLSSGFDIDTPDDFG 349
Cdd:PHA03095  180 VYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNTPLHSMAT--GSSCKRslvlPLLIAGISINARNRYG 257
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1953334645 350 RTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCL 398
Cdd:PHA03095  258 QTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAV 306
PHA03095 PHA03095
ankyrin-like protein; Provisional
163-419 1.66e-31

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 129.37  E-value: 1.66e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 163 ISVVKYLLDLGVDMNEPNAYGNTPLHV--ACYNGQDV-VVNELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLVGN 239
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLylHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 240 GADVNMKSKDGKTPLH--MTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGH---ELLiNTLITSGADTAKRGI 314
Cdd:PHA03095  107 GADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGADVYAVDD 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 315 HGMFPLHLAALS--GFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLL--NTGADFNKKDKFGRSPLHYAA 390
Cdd:PHA03095  186 RFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPllIAGISINARNRYGQTPLHYAA 265
                         250       260       270
                  ....*....|....*....|....*....|
gi 1953334645 391 ANCNyQCLFA-LVGSGASVNDLDERGCTPL 419
Cdd:PHA03095  266 VFNN-PRACRrLIALGADINAVSSDGNTPL 294
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
207-469 4.35e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.91  E-value: 4.35e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 207 ANVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTP 286
Cdd:COG0666    11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 287 LHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLN 366
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 367 LLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLLRNDANPGIRD 446
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENG-NLEIVKLLLEAGADLNAKD 249
                         250       260
                  ....*....|....*....|...
gi 1953334645 447 KQGYNAVHYSAAYGHRLCLQLIA 469
Cdd:COG0666   250 KDGLTALLLAAAAGAALIVKLLL 272
PHA02876 PHA02876
ankyrin repeat protein; Provisional
99-419 2.18e-30

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 128.64  E-value: 2.18e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  99 MVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNE 178
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 179 P-----NAYGNTPLHVACYngqdvvvneLIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSKDGKTP 253
Cdd:PHA02876  240 NdlsllKAIRNEDLETSLL---------LYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETP 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 254 LHMTALHGRFSRS-QTIIQSGAVIDCEDKNGNTPLHIAA---RYGHELLinTLITSGADTAKRGIHGMFPLHLAALSGFS 329
Cdd:PHA02876  311 LYLMAKNGYDTENiRTLIMLGADVNAADRLYITPLHQAStldRNKDIVI--TLLELGANVNARDYCDKTPIHYAAVRNNV 388
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 330 DCCRKLLSSGFDIDTPDDFGRTCLHAAAAG-GNLECLNLLLNTGADFNKKDKFGRSPLHYAAA-NCNYQCLFALVGSGAS 407
Cdd:PHA02876  389 VIINTLLDYGADIEALSQKIGTALHFALCGtNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKkNCKLDVIEMLLDNGAD 468
                         330
                  ....*....|..
gi 1953334645 408 VNDLDERGCTPL 419
Cdd:PHA02876  469 VNAINIQNQYPL 480
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
233-531 4.57e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.21  E-value: 4.57e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 233 LELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKR 312
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 313 GIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAAN 392
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 393 CNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCLQLIASET 472
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENG-HLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953334645 473 PldvlmetsgtdmLNDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPL 531
Cdd:COG0666   243 A------------DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
14-214 8.48e-30

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 123.24  E-value: 8.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  14 MLLPILEMQKS-LNCLfyLEAVQVLLKHSADVNARDKNWQTPLHIAAANKavKCAEALVPLL----SNVNVSDRAGRTAL 88
Cdd:PHA03100   70 TPLHYLSNIKYnLTDV--KEIVKLLLEYGANVNAPDNNGITPLLYAISKK--SNSYSIVEYLldngANVNIKNSDGENLL 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  89 HHAAFSGHG--EMVKLLLSRGANINAfdkKDRraihwaaymghievVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVV 166
Cdd:PHA03100  146 HLYLESNKIdlKILKLLIDKGVDINA---KNR--------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFV 208
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1953334645 167 KYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNE 214
Cdd:PHA03100  209 KYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
296-634 1.94e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 119.29  E-value: 1.94e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 296 ELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADF 375
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 376 NKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLLRNDANPGIRDKQGYnavhy 455
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG-NLEIVKLLLEAGADVNAQDNDGN----- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 456 saayghrlclqliasetpldvlmetsgtdmlndsdnratiSPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAA 535
Cdd:COG0666   155 ----------------------------------------TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 536 FKGHVECVDVLINQGASILVKDYiLKRTPIHAAATNGHSECLRLLIGNAEpqnAVDIQDGNGQTPLMLSVLNGHTDCVYS 615
Cdd:COG0666   195 ENGHLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGA---DLNAKDKDGLTALLLAAAAGAALIVKL 270
                         330
                  ....*....|....*....
gi 1953334645 616 LLNKGANVDAKDKWGRTAL 634
Cdd:COG0666   271 LLLALLLLAAALLDLLTLL 289
PHA02874 PHA02874
ankyrin repeat protein; Provisional
34-311 2.46e-28

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 119.30  E-value: 2.46e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  34 VQVLLKHSADVNARDKNWQTPLHIA---AANKAVKcaealVPLLSNVNVSdragrtALHHAAFSGhgEMVKLLLSRGANI 110
Cdd:PHA02874   51 VELFIKHGADINHINTKIPHPLLTAikiGAHDIIK-----LLIDNGVDTS------ILPIPCIEK--DMIKTILDCGIDV 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 111 NAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVA 190
Cdd:PHA02874  118 NIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNA 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 191 CYNGQDVVVNELIDCGANVNQKNEKGFTPLHfaAASTHGALCLELLVgNGADVNMKSKDGKTPLHMtALHGRFSRS--QT 268
Cdd:PHA02874  198 AEYGDYACIKLLIDHGNHIMNKCKNGFTPLH--NAIIHNRSAIELLI-NNASINDQDIDGSTPLHH-AINPPCDIDiiDI 273
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1953334645 269 IIQSGAVIDCEDKNGNTPLHIAARYGH------ELLINTLITSGADTAK 311
Cdd:PHA02874  274 LLYHKADISIKDNKGENPIDTAFKYINkdpvikDIIANAVLIKEADKLK 322
PHA02874 PHA02874
ankyrin repeat protein; Provisional
93-487 2.70e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 116.22  E-value: 2.70e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  93 FSGHGEMV-KLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLD 171
Cdd:PHA02874   10 YSGDIEAIeKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 172 LGVDmnepnaygNTPLHVACYNGQdvVVNELIDCGANVNQKNEKGFTPLHFAAASthGAL-CLELLVGNGADVNMKSKDG 250
Cdd:PHA02874   90 NGVD--------TSILPIPCIEKD--MIKTILDCGIDVNIKDAELKTFLHYAIKK--GDLeSIKMLFEYGADVNIEDDNG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 251 KTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALsgfsd 330
Cdd:PHA02874  158 CYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII----- 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 331 ccrkllssgfdidtpddfgrtclhaaaaggnleclnlllntgadfnkkdkFGRSPLhyaaancnyqclfALVGSGASVND 410
Cdd:PHA02874  233 --------------------------------------------------HNRSAI-------------ELLINNASIND 249
                         330       340       350       360       370       380       390
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953334645 411 LDERGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCL--QLIASETPLDVLMETSGTDMLN 487
Cdd:PHA02874  250 QDIDGSTPLHHAINPPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVikDIIANAVLIKEADKLKDSDFLE 328
PHA02874 PHA02874
ankyrin repeat protein; Provisional
77-323 9.30e-26

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 111.59  E-value: 9.30e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  77 VNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAE-------------- 142
Cdd:PHA02874   28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsilpipciekdmi 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 143 ---------VTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKN 213
Cdd:PHA02874  108 ktildcgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 214 EKGFTPLHFAAASTHGAlCLELLVGNGADVNMKSKDGKTPLHMTALHGRfSRSQTIIQSgAVIDCEDKNGNTPLHIAARY 293
Cdd:PHA02874  188 NNGESPLHNAAEYGDYA-CIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAINP 264
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1953334645 294 GHEL-LINTLITSGADTAKRGIHGMFPLHLA 323
Cdd:PHA02874  265 PCDIdIIDILLYHKADISIKDNKGENPIDTA 295
PHA03100 PHA03100
ankyrin repeat protein; Provisional
130-344 6.34e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 108.98  E-value: 6.34e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 130 IEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLH---VACYNGQDVV--VNELID 204
Cdd:PHA03100   15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsNIKYNLTDVKeiVKLLLE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 205 CGANVNQKNEKGFTPLHFAAASTHGALCL-ELLVGNGADVNMKSKDGKTPLHMTA--LHGRFSRSQTIIQSGA------- 274
Cdd:PHA03100   95 YGANVNAPDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVdinaknr 174
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953334645 275 ---------VIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDT 344
Cdd:PHA03100  175 vnyllsygvPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
34-308 1.68e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 110.15  E-value: 1.68e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  34 VQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRA-----------------------------G 84
Cdd:PHA02876  194 VNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLSllkairnedletslllydagfsvnsiddcK 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  85 RTALHHAAFSGH-GEMVKLLLSRGANINAFDKKDRRAIHWAAYMGH-IEVVKLLVAHGAEVTCKDKKSYTPLHAAAS-SG 161
Cdd:PHA02876  274 NTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDR 353
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 162 MISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLVGNGA 241
Cdd:PHA02876  354 NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGA 433
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953334645 242 DVNMKSKDGKTPLHMTALHG-RFSRSQTIIQSGAVIDCEDKNGNTPLHIAarYGHELLINTLITSGAD 308
Cdd:PHA02876  434 NVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGAE 499
PHA02878 PHA02878
ankyrin repeat protein; Provisional
31-297 2.68e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 104.58  E-value: 2.68e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  31 LEAVQVLLKHSADVNARDKNWQTPLHIA--AANKavkcaEALVPLLSNVNVSD-----RAGRTALHHAAFsghgEMVK-L 102
Cdd:PHA02878   50 LDVVKSLLTRGHNVNQPDHRDLTPLHIIckEPNK-----LGMKEMIRSINKCSvfytlVAIKDAFNNRNV----EIFKiI 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 103 LLSRGANINAFDKKDRRAIHWAAYMgHIEVVKLLVAHGAEVTCKDK-KSYTPLHAAASSGMISVVKYLLDLGVDMNEPNA 181
Cdd:PHA02878  121 LTNRYKNIQTIDLVYIDKKSKDDII-EAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 182 YGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSK-DGKTPLHMtALH 260
Cdd:PHA02878  200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHS-SIK 278
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1953334645 261 GRfSRSQTIIQSGAVIDCEDKNGNTPLHIAA--RYGHEL 297
Cdd:PHA02878  279 SE-RKLKLLLEYGADINSLNSYKLTPLSSAVkqYLCINI 316
PHA02874 PHA02874
ankyrin repeat protein; Provisional
498-807 2.32e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 101.19  E-value: 2.32e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 498 LHLAAYHGHHQALEVLVQS---LLDLDVRNSSgrTPLDLAAFKGHVECVDVLINQGASIlvkDYILKRTP--IHAAATNG 572
Cdd:PHA02874    5 LRMCIYSGDIEAIEKIIKNkgnCINISVDETT--TPLIDAIRSGDAKIVELFIKHGADI---NHINTKIPhpLLTAIKIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 573 HSECLRLLIGNAEPQNAVDIQDGNGQTplmlsvlnghtdcVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQH 652
Cdd:PHA02874   80 AHDIIKLLIDNGVDTSILPIPCIEKDM-------------IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEY 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 653 GAKCLFRDSRGRTPIHLSAACGHIGVLGALLQSAASVDANpaiaDNHGYTALHWACYNGHETCVELLLEQ--EVFQKTEg 730
Cdd:PHA02874  147 GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK----DNNGESPLHNAAEYGDYACIKLLIDHgnHIMNKCK- 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953334645 731 NAFSPLHCAVINdNEGAAEMLIDTlgASIvNATDSKGRTPLH-AAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMA 807
Cdd:PHA02874  222 NGFTPLHNAIIH-NRSAIELLINN--ASI-NDQDIDGSTPLHhAINPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
88-180 1.04e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.48  E-value: 1.04e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  88 LHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHgAEVTCKDKKsYTPLHAAASSGMISVVK 167
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1953334645 168 YLLDLGVDMNEPN 180
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
55-147 1.52e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 1.52e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  55 LHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRgANINAFDkKDRRAIHWAAYMGHIEVVK 134
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1953334645 135 LLVAHGAEVTCKD 147
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
121-213 1.61e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 1.61e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 121 IHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLgVDMNEPNaYGNTPLHVACYNGQDVVVN 200
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1953334645 201 ELIDCGANVNQKN 213
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
646-926 2.79e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 95.09  E-value: 2.79e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 646 VDALLQHGAKCLFRDSRGRTPIHLSAACGH---IGVLGALLQSAASVDAnpaiADNHGYTALH-WACYNGHETCVELLLE 721
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNA----PERCGFTPLHlYLYNATTLDVIKLLIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 722 QEV-FQKTEGNAFSPLH--CAVINDNEGAAEMLIDtLGASiVNATDSKGRTPLHAA-AFTD-HVECLQLLLSHNAQVNSI 796
Cdd:PHA03095  106 AGAdVNAKDKVGRTPLHvyLSGFNINPKVIRLLLR-KGAD-VNALDLYGMTPLAVLlKSRNaNVELLRLLIDAGADVYAV 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 797 DSSGKTPLMMAAENGQTNT--VEMLVSsASADLTLQDNSKNTALHLACSKGHETSALLI--LEKITDrnlINATNAALQT 872
Cdd:PHA03095  184 DDRFRSLLHHHLQSFKPRAriVRELIR-AGCDPAATDMLGNTPLHSMATGSSCKRSLVLplLIAGIS---INARNRYGQT 259
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953334645 873 PLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVaDCLALILAT 926
Cdd:PHA03095  260 PLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNG-RAVRAALAK 312
Ank_2 pfam12796
Ankyrin repeats (3 copies);
30-114 2.41e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 2.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  30 YLEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLsNVNVSDRaGRTALHHAAFSGHGEMVKLLLSRGAN 109
Cdd:pfam12796   9 NLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVKLLLEKGAD 86

                  ....*
gi 1953334645 110 INAFD 114
Cdd:pfam12796  87 INVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
531-627 3.23e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 3.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 531 LDLAAFKGHVECVDVLINQGASILVKDyILKRTPIHAAATNGHSECLRLLIGNAEPQNavdiqDGNGQTPLMLSVLNGHT 610
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAARSGHL 74
                          90
                  ....*....|....*..
gi 1953334645 611 DCVYSLLNKGANVDAKD 627
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
32-261 4.61e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 88.40  E-value: 4.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  32 EAVQVLLKHSADVNARDKNW-QTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANI 110
Cdd:PHA02878  148 EITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 111 NAfdkkdrraihwaaymghievvkllvahgaevtcKDKKSYTPLHAAASSGM-ISVVKYLLDLGVDMN-EPNAYGNTPLH 188
Cdd:PHA02878  228 DA---------------------------------RDKCGNTPLHISVGYCKdYDILKLLLEHGVDVNaKSYILGLTALH 274
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953334645 189 VACYNGQdvVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSKDGKTPL----HMTALHG 261
Cdd:PHA02878  275 SSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISNICLLKRIKPDIKNSEgfidNMDCITS 349
Ank_2 pfam12796
Ankyrin repeats (3 copies);
565-660 5.20e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 5.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 565 IHAAATNGHSECLRLLIgnaEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKgANVDAKDKwGRTALHRGAVTGHEE 644
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL---ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE 75
                          90
                  ....*....|....*.
gi 1953334645 645 CVDALLQHGAKCLFRD 660
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
154-246 6.08e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 6.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 154 LHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCgANVNQKNEkGFTPLHFAAASTHGAlCL 233
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE-IV 77
                          90
                  ....*....|...
gi 1953334645 234 ELLVGNGADVNMK 246
Cdd:pfam12796  78 KLLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
519-799 1.53e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 86.62  E-value: 1.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 519 DLDVRNSSGRTPLDLAAFKGHVECVDV---LINQGASILVKDyILKRTPIHAAATNGHSE-CLRLLIGNaepqNA-VDIQ 593
Cdd:PHA03095   39 DVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPE-RCGFTPLHLYLYNATTLdVIKLLIKA----GAdVNAK 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 594 DGNGQTPL--MLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALH----RGAVTghEECVDALLQHGAKCLFRDSRGRTPI 667
Cdd:PHA03095  114 DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvllkSRNAN--VELLRLLIDAGADVYAVDDRFRSLL 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 668 HLSAACGHI--GVLGALLQSAASvdanPAIADNHGYTALHWACYngHETCVELLLEQEVFQKTEGNA-----FSPLHCAV 740
Cdd:PHA03095  192 HHHLQSFKPraRIVRELIRAGCD----PAATDMLGNTPLHSMAT--GSSCKRSLVLPLLIAGISINArnrygQTPLHYAA 265
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953334645 741 INDNEGAAEMLIdTLGASIvNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSS 799
Cdd:PHA03095  266 VFNNPRACRRLI-ALGADI-NAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAAT 322
PHA02878 PHA02878
ankyrin repeat protein; Provisional
153-356 1.60e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 86.86  E-value: 1.60e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 153 PLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVAC------------------------------YNGQDV----- 197
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnklgmkemirsinkcsvfytlvaikdaFNNRNVeifki 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 198 -----------------------------VVNELIDCGANVNQKNE-KGFTPLHFAAASTHGALcLELLVGNGADVNMKS 247
Cdd:PHA02878  120 iltnrykniqtidlvyidkkskddiieaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRL-TELLLSYGANVNIPD 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 248 KDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHEL-LINTLITSGAD-TAKRGIHGMFPLHLAAL 325
Cdd:PHA02878  199 KTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYdILKLLLEHGVDvNAKSYILGLTALHSSIK 278
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1953334645 326 SgfSDCCRKLLSSGFDIDTPDDFGRTCLHAA 356
Cdd:PHA02878  279 S--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02874 PHA02874
ankyrin repeat protein; Provisional
15-223 2.19e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 85.79  E-value: 2.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  15 LLPILEMQKslnclfylEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFS 94
Cdd:PHA02874   96 ILPIPCIEK--------DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKH 167
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  95 GHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMiSVVKYLLDlGV 174
Cdd:PHA02874  168 NFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLIN-NA 245
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953334645 175 DMNEPNAYGNTPLHVACYNGQDV-VVNELIDCGANVNQKNEKGFTPLHFA 223
Cdd:PHA02874  246 SINDQDIDGSTPLHHAINPPCDIdIIDILLYHKADISIKDNKGENPIDTA 295
PHA02875 PHA02875
ankyrin repeat protein; Provisional
32-210 5.07e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 84.66  E-value: 5.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  32 EAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALvpLLSNVNVSD---RAGRTALHHAAFSGHGEMVKLLLSRGA 108
Cdd:PHA02875   49 EAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL--LDLGKFADDvfyKDGMTPLHLATILKKLDIMKLLIARGA 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 109 NINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDmnePNAYGNTP-L 187
Cdd:PHA02875  127 DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN---IDYFGKNGcV 203
                         170       180
                  ....*....|....*....|....*.
gi 1953334645 188 HVACY---NGQDVVVNELIDCGANVN 210
Cdd:PHA02875  204 AALCYaieNNKIDIVRLFIKRGADCN 229
PHA02876 PHA02876
ankyrin repeat protein; Provisional
372-721 7.11e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 85.50  E-value: 7.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 372 GADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLLRNDANPGIRDKQGYN 451
Cdd:PHA02876  168 GADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSK-NIDTIKAIIDNRSNINKNDLSLLK 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 452 AVHYSAAyghrlclqliasETPLdvLMETSGTDMLNDSDNRATisPLHLAAyhgHHQALEVLVQSLL----DLDVRNSSG 527
Cdd:PHA02876  247 AIRNEDL------------ETSL--LLYDAGFSVNSIDDCKNT--PLHHAS---QAPSLSRLVPKLLergaDVNAKNIKG 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 528 RTPLDLAAFKGH-VECVDVLINQGASILVKDYiLKRTPIHAAATnghseclrllignaepqnavdiqdgngqtplmlsvL 606
Cdd:PHA02876  308 ETPLYLMAKNGYdTENIRTLIMLGADVNAADR-LYITPLHQAST-----------------------------------L 351
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 607 NGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLFRDSRGRTPIHLsAACGH--IGVLGALLQ 684
Cdd:PHA02876  352 DRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHF-ALCGTnpYMSVKTLID 430
                         330       340       350
                  ....*....|....*....|....*....|....*...
gi 1953334645 685 SAASVDANpaiaDNHGYTALHWACYNGHE-TCVELLLE 721
Cdd:PHA02876  431 RGANVNSK----NKDLSTPLHYACKKNCKlDVIEMLLD 464
Ank_2 pfam12796
Ankyrin repeats (3 copies);
771-864 1.20e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 1.20e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 771 LHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSSASADLtlqDNSKNTALHLACSKGHETSA 850
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 1953334645 851 LLILEKITDRNLIN 864
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
333-691 1.54e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.54  E-value: 1.54e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 333 RKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECL---NLLLNTGADFNKKDKFGRSPLH-YAAANCNYQCLFALVGSGASV 408
Cdd:PHA03095   31 RRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADV 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 409 NDLDERGCTPLH-YAATSDTDGKCLEYLLRNDANPGIRDKqgynavhysaaYGHrlclqliaseTPLDVLMetsgtdmln 487
Cdd:PHA03095  111 NAKDKVGRTPLHvYLSGFNINPKVIRLLLRKGADVNALDL-----------YGM----------TPLAVLL--------- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 488 dSDNRATISPLHLaayhghhqalevLVQSLLDLDVRNSSGRTPLD--LAAFKGHVECVDVLINQGASILVKDyILKRTPI 565
Cdd:PHA03095  161 -KSRNANVELLRL------------LIDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATD-MLGNTPL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 566 HAAATngHSECLRLLIGNaepqnavdiqdgngqtplmlsvlnghtdcvysLLNKGANVDAKDKWGRTALHRGAVTGHEEC 645
Cdd:PHA03095  227 HSMAT--GSSCKRSLVLP--------------------------------LLIAGISINARNRYGQTPLHYAAVFNNPRA 272
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*.
gi 1953334645 646 VDALLQHGAKCLFRDSRGRTPIHLSAACGHIGVLGALLQSAASVDA 691
Cdd:PHA03095  273 CRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAET 318
Ank_2 pfam12796
Ankyrin repeats (3 copies);
601-692 4.45e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 4.45e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 601 LMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAkcLFRDSRGRTPIHLSAACGHIGVLG 680
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|..
gi 1953334645 681 ALLQSAASVDAN 692
Cdd:pfam12796  79 LLLEKGADINVK 90
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
475-654 1.17e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 81.84  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 475 DVLMETSGTDmlndsDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGASIL 554
Cdd:PLN03192  511 DLLGDNGGEH-----DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH 585
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 555 VKDyILKRTPIHAAATNGHSECLRLLIGNA---EPQNAVDIqdgngqtpLMLSVLNGHTDCVYSLLNKGANVDAKDKWGR 631
Cdd:PLN03192  586 IRD-ANGNTALWNAISAKHHKIFRILYHFAsisDPHAAGDL--------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656
                         170       180
                  ....*....|....*....|...
gi 1953334645 632 TALHRGAVTGHEECVDALLQHGA 654
Cdd:PLN03192  657 TALQVAMAEDHVDMVRLLIMNGA 679
Ank_2 pfam12796
Ankyrin repeats (3 copies);
704-797 2.80e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 2.80e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 704 LHWACYNGHETCVELLLEQEV-FQKTEGNAFSPLHCAVINDNEGAAEMLIDTLGASIVNatdsKGRTPLHAAAFTDHVEC 782
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD----NGRTALHYAARSGHLEI 76
                          90
                  ....*....|....*
gi 1953334645 783 LQLLLSHNAQVNSID 797
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
716-902 1.12e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.40  E-value: 1.12e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 716 VELLLEQ--EVFQKTEGNaFSPLH-----CAVINDNEGAAEMLIDtLGASIvNATDSKGRTPLHAAAFT--DHVECLQLL 786
Cdd:PHA03100   51 VKILLDNgaDINSSTKNN-STPLHylsniKYNLTDVKEIVKLLLE-YGANV-NAPDNNGITPLLYAISKksNSYSIVEYL 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 787 LSHNAQVNSIDSSGKTPLMMAAENG------------------QTNTVEMLVSSASaDLTLQDNSKNTALHLACSKGHET 848
Cdd:PHA03100  128 LDNGANVNIKNSDGENLLHLYLESNkidlkilkllidkgvdinAKNRVNYLLSYGV-PINIKDVYGFTPLHYAVYNNNPE 206
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953334645 849 SALLILEKITDRNLINATNaalQTPLHVAARNGLTMVVQELLGKGASVLAVDEN 902
Cdd:PHA03100  207 FVKYLLDLGANPNLVNKYG---DTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA03100 PHA03100
ankyrin repeat protein; Provisional
371-591 2.64e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 76.24  E-value: 2.64e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 371 TGADFNKKDKFGRSPLHYAA-----ANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSD-TDGKCLEYLLRNDANPGI 444
Cdd:PHA03100   57 NGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKsNSYSIVEYLLDNGANVNI 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 445 RDKQGYNAVHYSAAYGHRlclqliasETPLDVLMETSGTDMlnDSDNRatisplhlaayhghhqaLEVLVQSLLDLDVRN 524
Cdd:PHA03100  137 KNSDGENLLHLYLESNKI--------DLKILKLLIDKGVDI--NAKNR-----------------VNYLLSYGVPINIKD 189
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953334645 525 SSGRTPLDLAAFKGHVECVDVLINQGASILVKDYILKrTPIHAAATNGHSECLRLLIGNAEPQNAVD 591
Cdd:PHA03100  190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD-TPLHIAILNNNKEIFKLLLNNGPSIKTII 255
PHA02875 PHA02875
ankyrin repeat protein; Provisional
53-245 3.05e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.18  E-value: 3.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  53 TPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANIN-AFDKKDRRAIHWAAYMGHIE 131
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLD 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 132 VVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQ 211
Cdd:PHA02875  117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDY 196
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1953334645 212 KNEKGFTPLHFAAASTHGALCLELLVGNGADVNM 245
Cdd:PHA02875  197 FGKNGCVAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA03100 PHA03100
ankyrin repeat protein; Provisional
599-829 9.73e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 74.32  E-value: 9.73e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 599 TPLMLSVLNGHT-----DCVYSLLNKGANVDAKDKWGRTALHRGAVT--GHEECVDALLQHGAKCLFRDSRGRTPIHLSA 671
Cdd:PHA03100   70 TPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYL 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 672 ACGHI--GVLGALLQSAASVDAnpaiadnhgytalhwacynghETCVELLLEQEV-FQKTEGNAFSPLHCAVINDNEGAA 748
Cdd:PHA03100  150 ESNKIdlKILKLLIDKGVDINA---------------------KNRVNYLLSYGVpINIKDVYGFTPLHYAVYNNNPEFV 208
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 749 EMLIDtLGASIvNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSgktpLMMAAEN--GQTNTVEMLVSSASAD 826
Cdd:PHA03100  209 KYLLD-LGANP-NLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET----LLYFKDKdlNTITKIKMLKKSIMYM 282

                  ...
gi 1953334645 827 LTL 829
Cdd:PHA03100  283 FLL 285
PHA02876 PHA02876
ankyrin repeat protein; Provisional
296-689 1.23e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 75.10  E-value: 1.23e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 296 ELLI-NTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGAD 374
Cdd:PHA02876  157 ELLIaEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSN 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 375 FNKKDkfgrSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDKQGynavh 454
Cdd:PHA02876  237 INKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKG----- 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 455 ysaayghrlclqliasETPLdVLMETSGTDMLNdsdnratisplhlaayhghhqaLEVLVQSLLDLDVRNSSGRTPLDLA 534
Cdd:PHA02876  308 ----------------ETPL-YLMAKNGYDTEN----------------------IRTLIMLGADVNAADRLYITPLHQA 348
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 535 A-FKGHVECVDVLINQGASILVKDYiLKRTPIHAAATNGHSECLRLLIGNAEPQNAVDIQDGN-------GQTPLMlsvl 606
Cdd:PHA02876  349 StLDRNKDIVITLLELGANVNARDY-CDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTalhfalcGTNPYM---- 423
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 607 nghtdCVYSLLNKGANVDAKDKWGRTALHRGAVTGHE-ECVDALLQHGAKCLFRDSRGRTPihLSAACGHIGVLGALLQS 685
Cdd:PHA02876  424 -----SVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYP--LLIALEYHGIVNILLHY 496

                  ....
gi 1953334645 686 AASV 689
Cdd:PHA02876  497 GAEL 500
Ank_2 pfam12796
Ankyrin repeats (3 copies);
804-900 3.88e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.91  E-value: 3.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 804 LMMAAENGQTNTVEMLVSSaSADLTLQDNSKNTALHLACSKGHETSALLILEKItDRNLINATNaalqTPLHVAARNGLT 883
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDNGR----TALHYAARSGHL 74
                          90
                  ....*....|....*..
gi 1953334645 884 MVVQELLGKGASVLAVD 900
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
PHA02798 PHA02798
ankyrin-like protein; Provisional
31-254 4.67e-13

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 72.56  E-value: 4.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  31 LEAVQVLLKHSADVNARDKNWQTPLhiaaankavkCAealvpLLSNVnvsdRAGRTALhhaafsghgEMVKLLLSRGANI 110
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPL----------CT-----ILSNI----KDYKHML---------DIVKILIENGADI 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 111 NAFDKKDRRAIHWA---AYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGM---ISVVKYLLDLGVDMNE-PNAYG 183
Cdd:PHA02798  103 NKKNSDGETPLYCLlsnGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINThNNKEK 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 184 NTPLHvaCY------------------NG--------------QDVVVNELIDCGA-------------NVNQKNEKGFT 218
Cdd:PHA02798  183 YDTLH--CYfkynidridadilklfvdNGfiinkenkshkkkfMEYLNSLLYDNKRfkknildfifsyiDINQVDELGFN 260
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1953334645 219 PLHFAAASTHGALClELLVGNGADVNMKSKDGKTPL 254
Cdd:PHA02798  261 PLYYSVSHNNRKIF-EYLLQLGGDINIITELGNTCL 295
PHA02876 PHA02876
ankyrin repeat protein; Provisional
544-896 4.77e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 73.17  E-value: 4.77e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 544 DVLINQGASILVKDyILKRTPIHAAATNGHSECLRLLIGNAEPQNAVDIqdgNGQTPLMLSVLNGHTDCVYSLLNKGANV 623
Cdd:PHA02876  162 EMLLEGGADVNAKD-IYCITPIHYAAERGNAKMVNLLLSYGADVNIIAL---DDLSVLECAVDSKNIDTIKAIIDNRSNI 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 624 DAKDkwgrTALHRGAVTGHEECVDALLQHGAKCLFRDSRGRTPIHLSAACGHIGVL-GALLQSAASVDANpaiaDNHGYT 702
Cdd:PHA02876  238 NKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAK----NIKGET 309
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 703 ALHWACYNGHET--CVELLLEQEVFQKTEGNAFSPLHCAVINDNEGAAEMLIDTLGASiVNATDSKGRTPLHAAAFTDHV 780
Cdd:PHA02876  310 PLYLMAKNGYDTenIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITLLELGAN-VNARDYCDKTPIHYAAVRNNV 388
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 781 ECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSSASADLTLQDNSKNTALHLACSKGHETSAL-LILEKITD 859
Cdd:PHA02876  389 VIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLDVIeMLLDNGAD 468
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1953334645 860 RNLINATNaalQTPLHVAArnGLTMVVQELLGKGASV 896
Cdd:PHA02876  469 VNAINIQN---QYPLLIAL--EYHGIVNILLHYGAEL 500
PHA03100 PHA03100
ankyrin repeat protein; Provisional
735-913 5.88e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.01  E-value: 5.88e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 735 PLHCAVINDNEGAAEMLIDTlGASIvNATDSKGRTPLH-----AAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAE 809
Cdd:PHA03100   38 PLYLAKEARNIDVVKILLDN-GADI-NSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAIS 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 810 N--GQTNTVEMLVSSAsADLTLQDNSKNTALHLACSKGHETSAL--LILEKITDRNL-------------INATNAALQT 872
Cdd:PHA03100  116 KksNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDLKIlkLLIDKGVDINAknrvnyllsygvpINIKDVYGFT 194
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1953334645 873 PLHVAARNGLTMVVQELLGKGASVLAVDENGYTPA-LACAPN 913
Cdd:PHA03100  195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLhIAILNN 236
PHA02876 PHA02876
ankyrin repeat protein; Provisional
647-901 7.78e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 72.40  E-value: 7.78e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 647 DALLQHGAKCLFRDSRGRTPIHLSAACGHIGVLGALLQSAASVDanpaIADNHGYTALHWACYNGHETCVELLLEQEvfQ 726
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVN----IIALDDLSVLECAVDSKNIDTIKAIIDNR--S 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 727 KTEGNAFSPLHcAVINDNEGAAEMLIDTlGASiVNATDSKGRTPLHAAAFTDHVECL-QLLLSHNAQVNSIDSSGKTPLM 805
Cdd:PHA02876  236 NINKNDLSLLK-AIRNEDLETSLLLYDA-GFS-VNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLY 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 806 MAAENG-QTNTVEMLVSSAsADLTLQDNSKNTALHLACSKGHETSALLILEKITDRnlINATNAALQTPLHVAARNGLTM 884
Cdd:PHA02876  313 LMAKNGyDTENIRTLIMLG-ADVNAADRLYITPLHQASTLDRNKDIVITLLELGAN--VNARDYCDKTPIHYAAVRNNVV 389
                         250
                  ....*....|....*..
gi 1953334645 885 VVQELLGKGASVLAVDE 901
Cdd:PHA02876  390 IINTLLDYGADIEALSQ 406
Ank_2 pfam12796
Ankyrin repeats (3 copies);
254-346 1.06e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 1.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 254 LHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGAdtAKRGIHGMFPLHLAALSGFSDCCR 333
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1953334645 334 KLLSSGFDIDTPD 346
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
157-341 1.38e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.79  E-value: 1.38e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 157 AASSGMISVVKYLLDLGVDMN--------------------------EPNAYGN-------TPLHVACYNGQDVVVNELI 203
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNfeiydgispiklamkfrdseaikllmKHGAIPDvkypdieSELHDAVEEGDVKAVEELL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 204 DCGANVNQK-NEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKN 282
Cdd:PHA02875   89 DLGKFADDVfYKDGMTPLHLATILKKLDI-MKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 283 GNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFS-DCCRKLLSSGFD 341
Cdd:PHA02875  168 GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGAD 227
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
7-203 1.45e-12

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 71.58  E-value: 1.45e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645   7 MKRELHcmllpILEMQK-SLNCLFY------LEAVQVLLK-HSADVNARDKNWQTPLHIAAANKAVKCAEAL---VPLLS 75
Cdd:cd22192     4 MLDELH-----LLQQKRiSESPLLLaakendVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLmeaAPELV 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  76 NVNV-SD-RAGRTALHHAAFSGHGEMVKLLLSRGANIN-------AFDKKDRRAIHW-------AAYMGHIEVVKLLVAH 139
Cdd:cd22192    79 NEPMtSDlYQGETALHIAVVNQNLNLVRELIARGADVVspratgtFFRPGPKNLIYYgehplsfAACVGNEEIVRLLIEH 158
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953334645 140 GAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNE----------PNAYGNTPLHVACYNGQDVVVNELI 203
Cdd:cd22192   159 GADIRAQDSLGNTVLHILVLQPNKTFACQMYDLILSYDKeddlqpldlvPNNQGLTPFKLAAKEGNIVMFQHLV 232
PHA02798 PHA02798
ankyrin-like protein; Provisional
130-356 1.67e-12

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 71.02  E-value: 1.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 130 IEVVKLLVAHGAEVTCKDKKSYTPLHAAASS-----GMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGqdvVVNEL-- 202
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPLYCLLSNG---YINNLei 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 203 ----IDCGANVNQKNEKGFTPLHFAAASTHGAL--CLELLVGNGADVNMKSKDGKtplhMTALHGRFSRS---------Q 267
Cdd:PHA02798  128 llfmIENGADTTLLDKDGFTMLQVYLQSNHHIDieIIKLLLEKGVDINTHNNKEK----YDTLHCYFKYNidridadilK 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 268 TIIQSGAVIDCEDKNGNTPLhiaARYGHELLINT---------LITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSS 338
Cdd:PHA02798  204 LFVDNGFIINKENKSHKKKF---MEYLNSLLYDNkrfkknildFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQL 280
                         250
                  ....*....|....*...
gi 1953334645 339 GFDIDTPDDFGRTCLHAA 356
Cdd:PHA02798  281 GGDINIITELGNTCLFTA 298
PHA02874 PHA02874
ankyrin repeat protein; Provisional
481-667 1.83e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 70.76  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 481 SGTDMlnDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGASILVKDYIL 560
Cdd:PHA02874  113 CGIDV--NIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 561 KrTPIHAAATNGHSECLRLLIGNAepqNAVDIQDGNGQTPLMLSVLngHTDCVYSLLNKGANVDAKDKWGRTALHRG-AV 639
Cdd:PHA02874  191 E-SPLHNAAEYGDYACIKLLIDHG---NHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAiNP 264
                         170       180
                  ....*....|....*....|....*...
gi 1953334645 640 TGHEECVDALLQHGAKCLFRDSRGRTPI 667
Cdd:PHA02874  265 PCDIDIIDILLYHKADISIKDNKGENPI 292
PHA03100 PHA03100
ankyrin repeat protein; Provisional
611-823 3.01e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 69.69  E-value: 3.01e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 611 DCVYSLLNKGANVDAKDKWGRTALHRGAVTGHE-----ECVDALLQHGAKCLFRDSRGRTPIHLSAAC--GHIGVLGALL 683
Cdd:PHA03100   49 DVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLL 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 684 QSAASVDanpaIADNHGYTALHWA---CYNGHETcVELLLEqevfqktegnafsplHCAVINdNEGAAEMLIdTLGASIv 760
Cdd:PHA03100  129 DNGANVN----IKNSDGENLLHLYlesNKIDLKI-LKLLID---------------KGVDIN-AKNRVNYLL-SYGVPI- 185
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953334645 761 NATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSSA 823
Cdd:PHA03100  186 NIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248
Ank_2 pfam12796
Ankyrin repeats (3 copies);
320-412 3.37e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 3.37e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 320 LHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTgADFNKKDKfGRSPLHYAAANCNYQCLF 399
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1953334645 400 ALVGSGASVNDLD 412
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
187-280 7.29e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 7.29e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 187 LHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLvgNGADVNMKSkDGKTPLHMTALHGRFSRS 266
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL--EHADVNLKD-NGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 1953334645 267 QTIIQSGAVIDCED 280
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
486-721 9.40e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.37  E-value: 9.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 486 LNDSDNRATiSPLHLAAYHGHHQALEVLVQSLLDLDVRNSsgRTPLDLAAFKGHVECVD-VLINQGASILVKDYILKRTP 564
Cdd:PHA02878   63 VNQPDHRDL-TPLHIICKEPNKLGMKEMIRSINKCSVFYT--LVAIKDAFNNRNVEIFKiILTNRYKNIQTIDLVYIDKK 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 565 IHAAATNghSECLRLLIGNAEPQNAVDIQDGNgqTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEE 644
Cdd:PHA02878  140 SKDDIIE--AEITKLLLSYGADINMKDRHKGN--TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKP 215
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953334645 645 CVDALLQHGAKCLFRDSRGRTPIHLSAA-CGHIGVLGALLQSAASVDANPAIAdnhGYTALHWACYNghETCVELLLE 721
Cdd:PHA02878  216 IVHILLENGASTDARDKCGNTPLHISVGyCKDYDILKLLLEHGVDVNAKSYIL---GLTALHSSIKS--ERKLKLLLE 288
Ank_4 pfam13637
Ankyrin repeats (many copies);
84-137 1.17e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 1.17e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953334645  84 GRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLV 137
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
220-308 1.62e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 1.62e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 220 LHFAAASTHgALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSgAVIDCEDkNGNTPLHIAARYGHELLI 299
Cdd:pfam12796   1 LHLAAKNGN-LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                  ....*....
gi 1953334645 300 NTLITSGAD 308
Cdd:pfam12796  78 KLLLEKGAD 86
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
37-182 2.44e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.97  E-value: 2.44e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  37 LLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKK 116
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG 623
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953334645 117 DrrAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAY 182
Cdd:PLN03192  624 D--LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
573-782 4.63e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.82  E-value: 4.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 573 HSECLRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQH 652
Cdd:PLN03192  501 HKELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKH 580
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 653 GAKCLFRDSRGRTPIHLSAACGH-------------------------------IGVLGALLQSAASVDANpaiaDNHGY 701
Cdd:PLN03192  581 ACNVHIRDANGNTALWNAISAKHhkifrilyhfasisdphaagdllctaakrndLTAMKELLKQGLNVDSE----DHQGA 656
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 702 TALHWACYNGHETCVELLLEQ--EVFQKTEGNAFSPLHC-AVINDNE-GAAEMLIDTLGASIVNATDSKGRTPLHAAAFT 777
Cdd:PLN03192  657 TALQVAMAEDHVDMVRLLIMNgaDVDKANTDDDFSPTELrELLQKRElGHSITIVDSVPADEPDLGRDGGSRPGRLQGTS 736

                  ....*
gi 1953334645 778 DHVEC 782
Cdd:PLN03192  737 SDNQC 741
Ank_4 pfam13637
Ankyrin repeats (many copies);
118-170 4.87e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.83  E-value: 4.87e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1953334645 118 RRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLL 170
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
614-913 6.21e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.24  E-value: 6.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 614 YSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLF-RDSRGRTPIHLsaacghIGVLGALLQSAASVDAN 692
Cdd:PHA02876   25 YDLHKHGANQCENESIPFTAIHQALQLRQIDIVEEIIQQNPELIYiTDHKCHSTLHT------ICIIPNVMDIVISLTLD 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 693 PAIADNHGYTALHWACYNGHETCVELLleqevfqkTEGNAFSPLHCAVIN---------------DNEGAAEMLIDtlGA 757
Cdd:PHA02876   99 CDIILDIKYASIILNKHKLDEACIHIL--------KEAISGNDIHYDKINesieymklikeriqqDELLIAEMLLE--GG 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 758 SIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSSAS----ADLTLQDNS 833
Cdd:PHA02876  169 ADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSninkNDLSLLKAI 248
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 834 KNTALhlacskghETSALLILEKITdrnlINATNAALQTPLHVAARN-GLTMVVQELLGKGASVLAVDENGYTPALACAP 912
Cdd:PHA02876  249 RNEDL--------ETSLLLYDAGFS----VNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAK 316

                  .
gi 1953334645 913 N 913
Cdd:PHA02876  317 N 317
Ank_4 pfam13637
Ankyrin repeats (many copies);
496-547 2.01e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.90  E-value: 2.01e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953334645 496 SPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLI 547
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
484-691 2.39e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.92  E-value: 2.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 484 DMLNDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHV-----ECVDVLINQGASILVKDY 558
Cdd:PHA03100   25 DDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDN 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 559 IlKRTPIHAAATN--GHSECLRLLIGNAEPQNAVDiqdGNGQTPLMLSVLNGHTDC------------------VYSLLN 618
Cdd:PHA03100  105 N-GITPLLYAISKksNSYSIVEYLLDNGANVNIKN---SDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLS 180
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953334645 619 KGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLFRDSRGRTPIHLSAACGHIGVLGALLQSAASVDA 691
Cdd:PHA03100  181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
30-178 3.19e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 63.93  E-value: 3.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  30 YLEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEM-VKLLLSRGA 108
Cdd:PHA02876  354 NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGA 433
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953334645 109 NINAFDKKDRRAIHWAAYMG-HIEVVKLLVAHGAEVTCKDKKSYTPLHAAAssGMISVVKYLLDLGVDMNE 178
Cdd:PHA02876  434 NVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAELRD 502
Ank_4 pfam13637
Ankyrin repeats (many copies);
151-195 6.01e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 6.01e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1953334645 151 YTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQ 195
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
Ank_2 pfam12796
Ankyrin repeats (3 copies);
386-470 6.21e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 6.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 386 LHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDgKCLEYLLRNdANPGIRDkQGYNAVHYSAAYGHRLCL 465
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHL-EIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                  ....*
gi 1953334645 466 QLIAS 470
Cdd:pfam12796  78 KLLLE 82
PHA02878 PHA02878
ankyrin repeat protein; Provisional
186-479 7.21e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.59  E-value: 7.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 186 PLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLvgngadvNMKSKDgKTPLHMTALHGRFSR 265
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI-------RSINKC-SVFYTLVAIKDAFNN 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 266 SQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITsgadtakrgihgmfplhlaalsgfsdccRKLLSSGFDIDTP 345
Cdd:PHA02878  112 RNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEIT----------------------------KLLLSYGADINMK 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 346 D-DFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAAT 424
Cdd:PHA02878  164 DrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVG 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953334645 425 SDTDGKCLEYLLRNDANPGIRDK-QGYNAVHYSaayghrlclqlIASETPLDVLME 479
Cdd:PHA02878  244 YCKDYDILKLLLEHGVDVNAKSYiLGLTALHSS-----------IKSERKLKLLLE 288
PHA02874 PHA02874
ankyrin repeat protein; Provisional
760-920 7.39e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.29  E-value: 7.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 760 VNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSSAsADLTLQDNSKNTALH 839
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLH 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 840 LACSKGHETSALLILEKITdrNLINATNAALqTPLHVAARNGLTMVvqELLGKGASVLAVDENGYTP---ALACAPNKDV 916
Cdd:PHA02874  196 NAAEYGDYACIKLLIDHGN--HIMNKCKNGF-TPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPlhhAINPPCDIDI 270

                  ....
gi 1953334645 917 ADCL 920
Cdd:PHA02874  271 IDIL 274
PHA02875 PHA02875
ankyrin repeat protein; Provisional
198-444 7.43e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.32  E-value: 7.43e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 198 VVNELIDCGANVNQKNEKGFTPLHFAAaSTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVI- 276
Cdd:PHA02875   17 IARRLLDIGINPNFEIYDGISPIKLAM-KFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAd 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 277 DCEDKNGNTPLHiaaryghellintlitsgadtakrgihgmfplhLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAA 356
Cdd:PHA02875   96 DVFYKDGMTPLH---------------------------------LATILKKLDIMKLLIARGADPDIPNTDKFSPLHLA 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 357 AAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDGKCLEYLL 436
Cdd:PHA02875  143 VMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFI 222

                  ....*...
gi 1953334645 437 RNDANPGI 444
Cdd:PHA02875  223 KRGADCNI 230
Ank_2 pfam12796
Ankyrin repeats (3 copies);
419-524 1.08e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 1.08e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 419 LHYAATSDtDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCLQLIASEtpldvlmetsgtDMLNDSDNRATisPL 498
Cdd:pfam12796   1 LHLAAKNG-NLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH------------ADVNLKDNGRT--AL 65
                          90       100
                  ....*....|....*....|....*.
gi 1953334645 499 HLAAYHGHHQALEVLVQSLLDLDVRN 524
Cdd:pfam12796  66 HYAARSGHLEIVKLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
91-249 1.11e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 62.58  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  91 AAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLL 170
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953334645 171 DLGvDMNEPNAYGNTpLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSKD 249
Cdd:PLN03192  612 HFA-SISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDM-VRLLIMNGADVDKANTD 687
PHA02875 PHA02875
ankyrin repeat protein; Provisional
527-722 1.82e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.16  E-value: 1.82e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 527 GRTPLDLAAFKGHVECVDVLINQGASILVKdYILKRTPIHAAATNGHSECLRLLIGNAEPQNAVDIQDGNgqTPLMLSVL 606
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVK-YPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGM--TPLHLATI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 607 NGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLFRDSRGRTPIHLSAACGHIGVLGALLQSA 686
Cdd:PHA02875  112 LKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1953334645 687 ASVDanpAIADNHGYTALHWACYNGHETCVELLLEQ 722
Cdd:PHA02875  192 ANID---YFGKNGCVAALCYAIENNKIDIVRLFIKR 224
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
529-669 1.92e-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: 61.57  E-value: 1.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 529 TPLDLAAFKGHVECVDVLINQGASILVKDYILKRTPIHAAATNGHSECLRLLIGNA-----EPQNAVDIQdgnGQTPLML 603
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelvnEPMTSDLYQ---GETALHI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 604 SVLNGHTDCVYSLLNKGANV--------------DAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLFRDSRGRTPIHL 669
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
PHA02878 PHA02878
ankyrin repeat protein; Provisional
634-906 2.17e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.05  E-value: 2.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 634 LHRGAVTGHEECVDALLQHGAKCLFRDSRGRTPIHLsaACGHIGVLGA--LLQSAasvdanpaIADNHGYT--ALHWACY 709
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHI--ICKEPNKLGMkeMIRSI--------NKCSVFYTlvAIKDAFN 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 710 NGHETCVELLLeqevFQKTEGNAFSPLHCAVINDNEGAAEMLIDTL----GASIVNATDSKGRTPLHAAAFTDHVECLQL 785
Cdd:PHA02878  111 NRNVEIFKIIL----TNRYKNIQTIDLVYIDKKSKDDIIEAEITKLllsyGADINMKDRHKGNTALHYATENKDQRLTEL 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 786 LLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSSAsADLTLQDNSKNTALHLACSKGHETSAL-LILEKITDrnlIN 864
Cdd:PHA02878  187 LLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHISVGYCKDYDILkLLLEHGVD---VN 262
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1953334645 865 ATNAALQ-TPLHVAARNglTMVVQELLGKGASVLAVDENGYTP 906
Cdd:PHA02878  263 AKSYILGlTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTP 303
PHA02875 PHA02875
ankyrin repeat protein; Provisional
31-142 3.35e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.00  E-value: 3.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  31 LEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANI 110
Cdd:PHA02875  115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1953334645 111 NAFDKK-DRRAIHWAAYMGHIEVVKLLVAHGAE 142
Cdd:PHA02875  195 DYFGKNgCVAALCYAIENNKIDIVRLFIKRGAD 227
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
127-318 3.55e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.04  E-value: 3.55e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 127 MGHIEVVKLLVAHGAEVTckDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCG 206
Cdd:PLN03192  504 LHDLNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 207 ANVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSkdGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTP 286
Cdd:PLN03192  582 CNVHIRDANGNTALWNAISAKHHKI-FRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1953334645 287 LHIAARYGHELLINTLITSGADTAKRGIHGMF 318
Cdd:PLN03192  659 LQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
PHA02946 PHA02946
ankyin-like protein; Provisional
34-220 3.73e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 60.07  E-value: 3.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  34 VQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHG--EMVKLLLSRGANIN 111
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEviERINLLVQYGAKIN 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 112 AFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDK--KSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHV 189
Cdd:PHA02946  135 NSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKfgKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHI 214
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1953334645 190 ACYNG-QDVVVNELIDCGANVNQKNEKGFTPL 220
Cdd:PHA02946  215 VCSKTvKNVDIINLLLPSTDVNKQNKFGDSPL 246
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
88-170 3.80e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.68  E-value: 3.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  88 LHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVK 167
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                  ...
gi 1953334645 168 YLL 170
Cdd:PTZ00322  166 LLS 168
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
152-289 4.85e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 60.03  E-value: 4.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 152 TPLHAAASSGMISVVKYLLDL-GVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAN-VNQKNE----KGFTPLHFAAA 225
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTsdlyQGETALHIAVV 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953334645 226 STHGALcLELLVGNGADVN---------MKSKD-----GKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHI 289
Cdd:cd22192    99 NQNLNL-VRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
723-834 4.87e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.30  E-value: 4.87e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 723 EVFQKTEGNAFSPLHCAVIND--NEGAAEMLI----------DTLGASIV-------NATDSKGRTPLHAAAFTDHVECL 783
Cdd:PTZ00322   52 EALEATENKDATPDHNLTTEEviDPVVAHMLTvelcqlaasgDAVGARILltggadpNCRDYDGRTPLHIACANGHVQVV 131
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953334645 784 QLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSSASADLTLQDNSK 834
Cdd:PTZ00322  132 RVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAK 182
Ank_4 pfam13637
Ankyrin repeats (many copies);
767-820 9.23e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 9.23e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953334645 767 GRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLV 820
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
53-104 9.60e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 9.60e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953334645  53 TPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLL 104
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
631-876 9.83e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.85  E-value: 9.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 631 RTALHRGAVTGHEECVDALLQHGAKCLFRDSRGRTPIHLSAACGHIGVLGALLQSAASVDAN-PAIAdnhgyTALHWACY 709
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKyPDIE-----SELHDAVE 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 710 NGHETCVELLLE-----QEVFQKtEGNafSPLHCAVINDNEGAAEMLIDTLGASIVNATDSKgrTPLHAAAFTDHVECLQ 784
Cdd:PHA02875   78 EGDVKAVEELLDlgkfaDDVFYK-DGM--TPLHLATILKKLDIMKLLIARGADPDIPNTDKF--SPLHLAVMMGDIKGIE 152
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 785 LLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSSASADLTLQDNSKNTALHLACSKGHETSALLILEKITDRNLIN 864
Cdd:PHA02875  153 LLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
                         250
                  ....*....|..
gi 1953334645 865 ATNAALQTPLHV 876
Cdd:PHA02875  233 MIEGEECTILDM 244
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
30-145 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 1953334645  30 YLEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSnvnVSD-RAGRTALHHAAFSGHGEMVKLLLSRGA 108
Cdd:PLN03192  570 YEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS---ISDpHAAGDLLCTAAKRNDLTAMKELLKQGL 646
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1953334645 109 NINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTC 145
Cdd:PLN03192  647 NVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
Ank_4 pfam13637
Ankyrin repeats (many copies);
527-581 2.82e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 2.82e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1953334645 527 GRTPLDLAAFKGHVECVDVLINQGASILVKDYiLKRTPIHAAATNGHSECLRLLI 581
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
764-892 2.83e-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: 57.85  E-value: 2.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 764 DSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSS--------------GKTPLMMAAENGQTNTVEMLVSSASADLTL 829
Cdd:cd22194   138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITS 217
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953334645 830 QDNSKNTALHLAC-----SKGHETSAL----LILEKITDRNLINATNAALQTPLHVAARNGLTMVVQELLGK 892
Cdd:cd22194   218 QDSRGNTVLHALVtvaedSKTQNDFVKrmydMILLKSENKNLETIRNNEGLTPLQLAAKMGKAEILKYILSR 289
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
389-637 3.45e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.57  E-value: 3.45e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 389 AAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDgKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHrlclqli 468
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYE-DCVLVLLKHACNVHIRDANGNTALWNAISAKH------- 603
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 469 asETPLDVLMETSGTdmlndSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLIN 548
Cdd:PLN03192  604 --HKIFRILYHFASI-----SDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM 676
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 549 QGASIlvkdyilkrtpIHAAATNGHS-ECLRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCvySLLNKGANvdaKD 627
Cdd:PLN03192  677 NGADV-----------DKANTDDDFSpTELRELLQKRELGHSITIVDSVPADEPDLGRDGGSRPG--RLQGTSSD---NQ 740
                         250
                  ....*....|
gi 1953334645 628 KWGRTALHRG 637
Cdd:PLN03192  741 CRPRVSIYKG 750
PHA02874 PHA02874
ankyrin repeat protein; Provisional
736-906 3.51e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.90  E-value: 3.51e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 736 LHCAVINDNEGAAEMLIDtLGASiVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNT 815
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFE-YGAD-VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 816 VEMLVSSASaDLTLQDNSKNTALHLACSkgHETSALLILekITDRNlINATNAALQTPLHVAARNGLTM-VVQELLGKGA 894
Cdd:PHA02874  206 IKLLIDHGN-HIMNKCKNGFTPLHNAII--HNRSAIELL--INNAS-INDQDIDGSTPLHHAINPPCDIdIIDILLYHKA 279
                         170
                  ....*....|..
gi 1953334645 895 SVLAVDENGYTP 906
Cdd:PHA02874  280 DISIKDNKGENP 291
PHA02859 PHA02859
ankyrin repeat protein; Provisional
150-308 4.42e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 54.44  E-value: 4.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 150 SYT-PLHAAASSGMISVVKYLLDLgvdMNEPNAYGNTPLHvACYNGQDVVVNE---LIDCGANVNQK-NEKGFTPLHFAA 224
Cdd:PHA02859   20 RYCnPLFYYVEKDDIEGVKKWIKF---VNDCNDLYETPIF-SCLEKDKVNVEIlkfLIENGADVNFKtRDNNLSALHHYL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 225 ASTHGAL--CLELLVGNGADVNMKSKDGKTPLH--MTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLI- 299
Cdd:PHA02859   96 SFNKNVEpeILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKKIf 175

                  ....*....
gi 1953334645 300 NTLITSGAD 308
Cdd:PHA02859  176 DFLTSLGID 184
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
518-741 4.46e-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: 4.46e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 518 LDLDVRNSSGRTPLDLAAFKG-HVECVDVLINQGASILVKDyilkrTPIHAAATNGH---SECLRLLIGNAE----PQNA 589
Cdd:TIGR00870  43 LNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGD-----TLLHAISLEYVdavEAILLHLLAAFRksgpLELA 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 590 VDIQDGN---GQTPLMLSVLNGHTDCVYSLLNKGANVDAKDK--------------WGRTALHRGAVTGHEECVDALLQH 652
Cdd:TIGR00870 118 NDQYTSEftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSED 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 653 GAKCLFRDSRGRTPIHLSA------------ACG-HIGVLGALLQSAASVDANpAIADNHGYTALHWACYNGHETCVELL 719
Cdd:TIGR00870 198 PADILTADSLGNTLLHLLVmenefkaeyeelSCQmYNFALSLLDKLRDSKELE-VILNHQGLTPLKLAAKEGRIVLFRLK 276
                         250       260
                  ....*....|....*....|...
gi 1953334645 720 LEQEVFQKT-EGNAFSPLHCAVI 741
Cdd:TIGR00870 277 LAIKYKQKKfVAWPNGQQLLSLY 299
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
223-377 5.85e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.80  E-value: 5.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 223 AAASTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTL 302
Cdd:PLN03192  531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953334645 303 --ITSGADTAKRGIhgmfPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNK 377
Cdd:PLN03192  611 yhFASISDPHAAGD----LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
PHA02859 PHA02859
ankyrin repeat protein; Provisional
26-194 6.13e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 54.05  E-value: 6.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  26 NCLFY------LEAVQvllKHSADVNARDKNWQTPLHIAAANKAV--KCAEALVPLLSNVNVSDRA-GRTALHHAAFSGH 96
Cdd:PHA02859   23 NPLFYyvekddIEGVK---KWIKFVNDCNDLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRDnNLSALHHYLSFNK 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  97 G---EMVKLLLSRGANINAFDKKDRRAIHwaAYMGH----IEVVKLLVAHGAEVTCKDKK------SYTPLHAAASsgmi 163
Cdd:PHA02859  100 NvepEILKILIDSGSSITEEDEDGKNLLH--MYMCNfnvrINVIKLLIDSGVSFLNKDFDnnnilySYILFHSDKK---- 173
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1953334645 164 sVVKYLLDLGVDMNEPNAYGNTPLHVACYNG 194
Cdd:PHA02859  174 -IFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
PHA02798 PHA02798
ankyrin-like protein; Provisional
198-422 6.53e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 56.38  E-value: 6.53e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 198 VVNELIDCGANVNQKNEKGFTPLHFAAAS----THGALCLELLVGNGADVNMKSKDGKTPLHmTALHGRFSRSQTI---- 269
Cdd:PHA02798   53 IVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHMLDIVKILIENGADINKKNSDGETPLY-CLLSNGYINNLEIllfm 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 270 IQSGAVIDCEDKNGNTPLHIAARYGHEL---LINTLITSGADTAKRG-------IHGMFPLHLAALSgfSDCCRKLLSSG 339
Cdd:PHA02798  132 IENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDINTHNnkekydtLHCYFKYNIDRID--ADILKLFVDNG 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 340 FDIDTPDDFGRTCLHAAAAGGNLECLNLLLN------TGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDE 413
Cdd:PHA02798  210 FIINKENKSHKKKFMEYLNSLLYDNKRFKKNildfifSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITE 289

                  ....*....
gi 1953334645 414 RGCTPLHYA 422
Cdd:PHA02798  290 LGNTCLFTA 298
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
34-105 6.56e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 6.56e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953334645  34 VQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLS 105
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PHA02875 PHA02875
ankyrin repeat protein; Provisional
761-923 7.71e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.77  E-value: 7.71e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 761 NATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSSAS--ADLTLQDNskNTAL 838
Cdd:PHA02875   29 NFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfaDDVFYKDG--MTPL 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 839 HLAC-SKGHETSALLILEKiTDRNLINATNAalqTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVA 917
Cdd:PHA02875  107 HLATiLKKLDIMKLLIARG-ADPDIPNTDKF---SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIA 182

                  ....*.
gi 1953334645 918 DCLALI 923
Cdd:PHA02875  183 ICKMLL 188
PHA02989 PHA02989
ankyrin repeat protein; Provisional
34-271 8.00e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 55.90  E-value: 8.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  34 VQVLLKHSADVNARDKNWQTPLhiaaankavkcaealVPLLSNVNVSDRagrtalhhaafsghgEMVKLLLSRGANINaf 113
Cdd:PHA02989   91 VKLLLKFGADINLKTFNGVSPI---------------VCFIYNSNINNC---------------DMLRFLLSKGINVN-- 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 114 DKKDRRA-----IHWAAYMGHIEVVKLLVAHGaeVTCKDKKSY---TPLHAAASSGM----ISVVKYLLDLGVDMNEPNA 181
Cdd:PHA02989  139 DVKNSRGynllhMYLESFSVKKDVIKILLSFG--VNLFEKTSLyglTPMNIYLRNDIdvisIKVIKYLIKKGVNIETNNN 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 182 YGNTPL------HVACYNGQDVVVNeLIDCGANVNQKNEKGFTPLHFAA-ASTHGALCLELLVGNgaDVNMKSKDGKTPL 254
Cdd:PHA02989  217 GSESVLesfldnNKILSKKEFKVLN-FILKYIKINKKDKKGFNPLLISAkVDNYEAFNYLLKLGD--DIYNVSKDGDTVL 293
                         250
                  ....*....|....*..
gi 1953334645 255 HMTALHGRFSRSQTIIQ 271
Cdd:PHA02989  294 TYAIKHGNIDMLNRILQ 310
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
133-205 1.03e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 1.03e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953334645 133 VKLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDC 205
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02875 PHA02875
ankyrin repeat protein; Provisional
674-925 1.70e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.61  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 674 GHIGVLGALLQSAAsvdaNPAIADNHGYTALHWACYNGHETCVELLLEQEVFQKTEG-NAFSPLHCAVINDNEGAAEMLI 752
Cdd:PHA02875   13 GELDIARRLLDIGI----NPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYpDIESELHDAVEEGDVKAVEELL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 753 DtLGASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSsasadltlqdn 832
Cdd:PHA02875   89 D-LGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLID----------- 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 833 skntalHLACskghetsallilekitdrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAP 912
Cdd:PHA02875  157 ------HKAC--------------------LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAI 210
                         250
                  ....*....|...
gi 1953334645 913 NKDVADCLALILA 925
Cdd:PHA02875  211 ENNKIDIVRLFIK 223
PHA02875 PHA02875
ankyrin repeat protein; Provisional
596-819 2.37e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.23  E-value: 2.37e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 596 NGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGA---KCLFRDsrGRTPIHLSAA 672
Cdd:PHA02875   34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 673 CGHIGVLGALLQSAasvdANPAIADNHGYTALHWACYNGHETCVELLLEQEVFQKTE-GNAFSPLHCAVINDNEGAAEML 751
Cdd:PHA02875  112 LKKLDIMKLLIARG----ADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEdCCGCTPLIIAMAKGDIAICKML 187
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1953334645 752 IDTlGASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNsidssgktpLMMAAENGQTNTVEML 819
Cdd:PHA02875  188 LDS-GANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCN---------IMFMIEGEECTILDMI 245
Ank_4 pfam13637
Ankyrin repeats (many copies);
630-683 2.39e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 2.39e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953334645 630 GRTALHRGAVTGHEECVDALLQHGAKCLFRDSRGRTPIHLSAACGHIGVLGALL 683
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
746-906 2.88e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 2.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 746 GAAEMLIDTLGASI-VNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSSAS 824
Cdd:PLN03192  536 GNAALLEELLKAKLdPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS 615
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 825 AdltlqdNSKNTALHLACSKGHETSaLLILEKITDRNL-INATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVD-EN 902
Cdd:PLN03192  616 I------SDPHAAGDLLCTAAKRND-LTAMKELLKQGLnVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDD 688

                  ....
gi 1953334645 903 GYTP 906
Cdd:PLN03192  689 DFSP 692
Ank_4 pfam13637
Ankyrin repeats (many copies);
382-436 3.02e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 3.02e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1953334645 382 GRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLL 436
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG-NVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
802-896 4.93e-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: 53.86  E-value: 4.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 802 TPLMMAAENGQTNTVEMLVSSASADLTLQDNSKNTALHLACSKGHETSALLILEkiTDRNLIN-ATNAAL---QTPLHVA 877
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNePMTSDLyqgETALHIA 96
                          90
                  ....*....|....*....
gi 1953334645 878 ARNGLTMVVQELLGKGASV 896
Cdd:cd22192    97 VVNQNLNLVRELIARGADV 115
PHA02874 PHA02874
ankyrin repeat protein; Provisional
747-906 5.80e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 5.80e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 747 AAEMLIDTLGaSIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVssasad 826
Cdd:PHA02874   16 AIEKIIKNKG-NCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI------ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 827 ltlqDNSKNTA-LHLACSKGHETSAllILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYT 905
Cdd:PHA02874   89 ----DNGVDTSiLPIPCIEKDMIKT--ILDCGID---VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCY 159

                  .
gi 1953334645 906 P 906
Cdd:PHA02874  160 P 160
Ank_4 pfam13637
Ankyrin repeats (many copies);
734-787 9.24e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 9.24e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953334645 734 SPLHCAVINDNEGAAEMLIDTlGASIvNATDSKGRTPLHAAAFTDHVECLQLLL 787
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEK-GADI-NAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
225-294 1.13e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 1.13e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 225 ASTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYG 294
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
218-423 1.36e-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: 1.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 218 TPLhFAAASTHGALCLE-LLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGA-----VIDCEDKNGNTPLHIAA 291
Cdd:cd22192    19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPelvnePMTSDLYQGETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 292 RYGHELLINTLITSGADTAKRGIHGMFplhlaalsgFSDCCRKLLSsgfdidtpddFGRTCLHAAAAGGNLECLNLLLNT 371
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSPRATGTF---------FRPGPKNLIY----------YGEHPLSFAACVGNEEIVRLLIEH 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953334645 372 GADFNKKDKFGRSPLHYAA--ANCNYQC-----LFALVGSGASVNdLD----ERGCTPLHYAA 423
Cdd:cd22192   159 GADIRAQDSLGNTVLHILVlqPNKTFACqmydlILSYDKEDDLQP-LDlvpnNQGLTPFKLAA 220
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
31-191 1.42e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 52.39  E-value: 1.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  31 LEAVQVLLKHSADVNARDknwqTPLHIAAANKAVKCAEALVPLLSN---------VNVSDR----AGRTALHHAAFSGHG 97
Cdd:TIGR00870  66 LELTELLLNLSCRGAVGD----TLLHAISLEYVDAVEAILLHLLAAfrksgplelANDQYTseftPGITALHLAAHRQNY 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  98 EMVKLLLSRGANINA------FDKKDRRA--------IHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAAA----- 158
Cdd:TIGR00870 142 EIVKLLLERGASVPAracgdfFVKSQGVDsfyhgespLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenef 221
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1953334645 159 -------SSGMISVVKYLLDLGVDMNE----PNAYGNTPLHVAC 191
Cdd:TIGR00870 222 kaeyeelSCQMYNFALSLLDKLRDSKEleviLNHQGLTPLKLAA 265
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
699-892 1.76e-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: 51.94  E-value: 1.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 699 HGYTALHWACYNGHETCVELLLEQE---VFQKTEGNAF---SPLHCAVINDNEGAAEMLIDTlGASIVN--ATDS---KG 767
Cdd:cd22192    50 LGETALHVAALYDNLEAAVVLMEAApelVNEPMTSDLYqgeTALHIAVVNQNLNLVRELIAR-GADVVSprATGTffrPG 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 768 RT--------PLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMaaengqtntvemlvssasadLTLQDNSKntalh 839
Cdd:cd22192   129 PKnliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI--------------------LVLQPNKT----- 183
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953334645 840 LACskgHETSALLILEK-ITDRNLINATNAALQTPLHVAARNGLTMVVQELLGK 892
Cdd:cd22192   184 FAC---QMYDLILSYDKeDDLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
599-650 1.85e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 1.85e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953334645 599 TPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALL 650
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
711-895 1.92e-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: 51.80  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 711 GHETCVELLLEQEVFQKTEGNAfSPLHCAVINDNEG---AAEMLIDTLGAS-----IVNA--TDS--KGRTPLHAAAFTD 778
Cdd:cd21882     6 GLLECLRWYLTDSAYQRGATGK-TCLHKAALNLNDGvneAIMLLLEAAPDSgnpkeLVNApcTDEfyQGQTALHIAIENR 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 779 HVECLQLLLSHNAQVNSIDSS-------------GKTPLMMAAENGQTNTVEMLVSSAS--ADLTLQDNSKNTALH---L 840
Cdd:cd21882    85 NLNLVRLLVENGADVSARATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAqpAALEAQDSLGNTVLHalvL 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953334645 841 ACSKGHETSA--------LLILEKITD--RNLINATNAALQTPLHVAARNGLTMVVQELLGKGAS 895
Cdd:cd21882   165 QADNTPENSAfvcqmynlLLSYGAHLDptQQLEEIPNHQGLTPLKLAAVEGKIVMFQHILQREFS 229
Ank_5 pfam13857
Ankyrin repeats (many copies);
136-190 2.13e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 2.13e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953334645 136 LVAHG-AEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVA 190
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
562-617 2.19e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 2.19e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953334645 562 RTPIHAAATNGHSECLRLLIGNAEPqnaVDIQDGNGQTPLMLSVLNGHTDCVYSLL 617
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
202-256 2.72e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 2.72e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953334645 202 LIDCG-ANVNQKNEKGFTPLHFAAasTHGAL-CLELLVGNGADVNMKSKDGKTPLHM 256
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAA--KYGALeIVRVLLAYGVDLNLKDEEGLTALDL 55
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
134-318 3.41e-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: 3.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 134 KLLVAHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDM-NEP---NAY-GNTPLHVACYNGQDVVVNELIDCGAN 208
Cdd:cd22192    35 KLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvNEPmtsDLYqGETALHIAVVNQNLNLVRELIARGAD 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 209 VN---------QKNEK-----GFTPLHFAAASTHGALcLELLVGNGADVNMKSKDGKTPLHMTALhgrfsrsqtiiQSGA 274
Cdd:cd22192   115 VVspratgtffRPGPKnliyyGEHPLSFAACVGNEEI-VRLLIEHGADIRAQDSLGNTVLHILVL-----------QPNK 182
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953334645 275 VIDCE--------DKNGN-------------TPLHIAARYGHELLINTLITSgadtaKRGIHGMF 318
Cdd:cd22192   183 TFACQmydlilsyDKEDDlqpldlvpnnqglTPFKLAAKEGNIVMFQHLVQK-----RRHIQWTY 242
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
638-720 3.74e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 3.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 638 AVTGHEECVDALLQHGAKCLFRDSRGRTPIHLSAACGHIGVLGALLQsaasVDANPAIADNHGYTALHWACYNGHETCVE 717
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLE----FGADPTLLDKDGKTPLELAEENGFREVVQ 165

                  ...
gi 1953334645 718 LLL 720
Cdd:PTZ00322  166 LLS 168
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
84-115 5.51e-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: 5.51e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1953334645  84 GRTALHHAAFS-GHGEMVKLLLSRGANINAFDK 115
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
319-360 6.08e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 6.08e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1953334645 319 PLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGG 360
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG 45
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
158-264 6.85e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 6.85e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 158 ASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGALcLELLV 237
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV-VQLLS 168
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1953334645 238 GN-------GADVNMKSKDGKTPLH----MTALHGRFS 264
Cdd:PTZ00322  169 RHsqchfelGANAKPDSFTGKPPSLedspISSHHPDFS 206
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
52-203 7.10e-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: 49.88  E-value: 7.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  52 QTPLHIAAANKAVKCAEALVPLLSNVNVSDRA--------------GRTALHHAAFSGHGEMVKLLLSRGANINA----- 112
Cdd:cd21882    27 KTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAratgr 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 113 -FDKKDRRAIHW-------AAYMGHIEVVKLLVAHGAE---VTCKDKKSYTPLHA---------AASSGMISVVKYLLDL 172
Cdd:cd21882   107 fFRKSPGNLFYFgelplslAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHAlvlqadntpENSAFVCQMYNLLLSY 186
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1953334645 173 G------VDMNE-PNAYGNTPLHVACYNGQDVVVNELI 203
Cdd:cd21882   187 GahldptQQLEEiPNHQGLTPLKLAAVEGKIVMFQHIL 224
Ank_4 pfam13637
Ankyrin repeats (many copies);
252-303 9.18e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 9.18e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953334645 252 TPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLI 303
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
183-237 9.27e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 9.27e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1953334645 183 GNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTHGAlCLELLV 237
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
639-813 1.18e-05

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 49.11  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 639 VTGHEECVDALLQHGAKClfRDSRGRTPIHLSAACGHIGVLGA---LLQSAASVDANPAIADN-------HGYTALHWAC 708
Cdd:cd21882     4 LLGLLECLRWYLTDSAYQ--RGATGKTCLHKAALNLNDGVNEAimlLLEAAPDSGNPKELVNApctdefyQGQTALHIAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 709 YNGHETCVELLLEQ----------EVFQKTEGNAF----SPLHCAVINDNEGAAEMLIDTlGASI--VNATDSKGRTPLH 772
Cdd:cd21882    82 ENRNLNLVRLLVENgadvsaratgRFFRKSPGNLFyfgeLPLSLAACTNQEEIVRLLLEN-GAQPaaLEAQDSLGNTVLH 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1953334645 773 A-----------AAFTDHVecLQLLLSHNAQVNSIDS-------SGKTPLMMAAENGQT 813
Cdd:cd21882   161 AlvlqadntpenSAFVCQM--YNLLLSYGAHLDPTQQleeipnhQGLTPLKLAAVEGKI 217
Ank_5 pfam13857
Ankyrin repeats (many copies);
37-91 1.19e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.19e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953334645  37 LLKH-SADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHA 91
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
383-601 1.22e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.83  E-value: 1.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 383 RSPLHYAAANCNYQCLFALVGSGASVND-LDERGCTPLHYAaTSDTDGKCLEYLLRNDANPGIrdkqgynavhysaaygh 461
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADDvFYKDGMTPLHLA-TILKKLDIMKLLIARGADPDI----------------- 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 462 rlclqliasetpldvlmetSGTDmlndsdnraTISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVE 541
Cdd:PHA02875  131 -------------------PNTD---------KFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIA 182
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953334645 542 CVDVLINQGASIlvkDYILKRTPIHA---AATNGHSECLRLLIGNAEPQNAVDIQDGNGQTPL 601
Cdd:PHA02875  183 ICKMLLDSGANI---DYFGKNGCVAAlcyAIENNKIDIVRLFIKRGADCNIMFMIEGEECTIL 242
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
668-808 1.85e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 1.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 668 HLSAACGHIGVLgALLQSAAsvdaNPAIADNHGYTALHWACYNGHETCVELLLEqevfqktegnafsplhcavindnega 747
Cdd:PTZ00322   88 QLAASGDAVGAR-ILLTGGA----DPNCRDYDGRTPLHIACANGHVQVVRVLLE-------------------------- 136
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953334645 748 aemlidtLGASiVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGK-------------TPLMMAA 808
Cdd:PTZ00322  137 -------FGAD-PTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAKpdsftgkppsledSPISSHH 202
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
269-348 1.86e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 1.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 269 IIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLS---SGFDIDT- 344
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRhsqCHFELGAn 180

                  ....*.
gi 1953334645 345 --PDDF 348
Cdd:PTZ00322  181 akPDSF 186
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
417-619 2.07e-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: 2.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 417 TPLHYAAtSDTDGKCLEYLLR-NDANPGIRDKQGYNAVHYSAAYGHRLCLQLIASETPLDVLMETSgtdmlndSDNRATI 495
Cdd:cd22192    19 SPLLLAA-KENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMT-------SDLYQGE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 496 SPLHLAAYHGHhqalEVLVQSLLD--LDVRNSS----------------GRTPLDLAAFKGHVECVDVLINQGASILVKD 557
Cdd:cd22192    91 TALHIAVVNQN----LNLVRELIArgADVVSPRatgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953334645 558 YiLKRTPIHAAAT--NGHSECLRL-LIGNAEP---QNAVD-IQDGNGQTPLMLSVLNGHTDCVYSLLNK 619
Cdd:cd22192   167 S-LGNTVLHILVLqpNKTFACQMYdLILSYDKeddLQPLDlVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
84-112 2.09e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 2.09e-05
                           10        20
                   ....*....|....*....|....*....
gi 1953334645   84 GRTALHHAAFSGHGEMVKLLLSRGANINA 112
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
31-71 2.20e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 2.20e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1953334645  31 LEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALV 71
Cdd:pfam13637  14 LELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
663-720 2.20e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 2.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1953334645 663 GRTPIHLSAACGHIGVLGALLQSAASVDAnpaiADNHGYTALHWACYNGHETCVELLL 720
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINA----VDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
569-652 2.38e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 2.38e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 569 ATNGHSECLRLLI-GNAEPqnavDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVD 647
Cdd:PTZ00322   90 AASGDAVGARILLtGGADP----NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                  ....*
gi 1953334645 648 ALLQH 652
Cdd:PTZ00322  166 LLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
349-402 2.45e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 2.45e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953334645 349 GRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALV 402
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
590-810 2.61e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.91  E-value: 2.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 590 VDIQDGNGQTPL--MLSVL---NGHTDCVYSLLNKGANVDAKDKWGRTA----LHRGAVTgHEECVDALLQHGAKCLFRD 660
Cdd:PHA02798   64 VNGLDNEYSTPLctILSNIkdyKHMLDIVKILIENGADINKKNSDGETPlyclLSNGYIN-NLEILLFMIENGADTTLLD 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 661 SRGRTPIHLSAACGH---IGVLGALLQSAasVDANpAIADNHGYTALHwaCYNGHE------TCVELLLEQ----EVFQK 727
Cdd:PHA02798  143 KDGFTMLQVYLQSNHhidIEIIKLLLEKG--VDIN-THNNKEKYDTLH--CYFKYNidridaDILKLFVDNgfiiNKENK 217
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 728 TEGNAFSPLHCAVINDNEGAAEMLIDTLGASI-VNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMM 806
Cdd:PHA02798  218 SHKKKFMEYLNSLLYDNKRFKKNILDFIFSYIdINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFT 297

                  ....
gi 1953334645 807 AAEN 810
Cdd:PHA02798  298 AFEN 301
Ank_5 pfam13857
Ankyrin repeats (many copies);
587-635 2.73e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 2.73e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1953334645 587 QNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALH 635
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
198-419 2.94e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 47.98  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 198 VVNELIDCG-ANVNQK-NEKGFTPLHFAAASTHGAL-CLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRS--QTIIQS 272
Cdd:PHA02716  157 LIKYMVDVGiVNLNYVcKKTGYGILHAYLGNMYVDIdILEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASviKKIIEL 236
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 273 GAVIDCEDKNGNTPLH---IAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFS-DCCRKLLSSGFDIDTPDDF 348
Cdd:PHA02716  237 GGDMDMKCVNGMSPIMtyiINIDNINPEITNIYIESLDGNKVKNIPMILHSYITLARNIDiSVVYSFLQPGVKLHYKDSA 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 349 GRTCLHAAAAGGNLECL--NLLLNTGADFNKKDKFGRSPLHYAAA--------------NCNYQCLFALVGSGASVNDLD 412
Cdd:PHA02716  317 GRTCLHQYILRHNISTDiiKLLHEYGNDLNEPDNIGNTVLHTYLSmlsvvnildpetdnDIRLDVIQCLISLGADITAVN 396

                  ....*..
gi 1953334645 413 ERGCTPL 419
Cdd:PHA02716  397 CLGYTPL 403
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
808-903 3.24e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 3.24e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 808 AENGQTNTVEMLVSSAsADLTLQDNSKNTALHLACSKGHETSALLILEKITDRNLINATNaalQTPLHVAARNGLTMVVQ 887
Cdd:PTZ00322   90 AASGDAVGARILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDG---KTPLELAEENGFREVVQ 165
                          90
                  ....*....|....*.
gi 1953334645 888 ELLGKGASVLAVDENG 903
Cdd:PTZ00322  166 LLSRHSQCHFELGANA 181
Ank_4 pfam13637
Ankyrin repeats (many copies);
283-336 4.05e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 4.05e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953334645 283 GNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLL 336
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
169-223 4.13e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 4.13e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953334645 169 LLDLG-VDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFA 223
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02946 PHA02946
ankyin-like protein; Provisional
100-305 4.36e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.97  E-value: 4.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 100 VKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLH--AAASSGMISVVKYLLDLGVDMN 177
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYylSGTDDEVIERINLLVQYGAKIN 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 178 EP-NAYGNTPLhVACYNGQDVVVNELIDCGANVNQKNEKGFTPLHFAAASTH-GALCLELLVGNGADVNMKSKDGKTPLH 255
Cdd:PHA02946  135 NSvDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpKASTISWMMKLGISPSKPDHDGNTPLH 213
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953334645 256 MTAlhGRFSRSQTIIQ---SGAVIDCEDKNGNTPLHIAAR-YGHELLINTLITS 305
Cdd:PHA02946  214 IVC--SKTVKNVDIINlllPSTDVNKQNKFGDSPLTLLIKtLSPAHLINKLLST 265
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
494-604 4.64e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 4.64e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 494 TISPLHLAAyHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGA--SILVKDyilKRTPIHAAATN 571
Cdd:PTZ00322   83 TVELCQLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAdpTLLDKD---GKTPLELAEEN 158
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1953334645 572 GHSECLRLLIG----------NAEPQNAVDIQDGNGQTPLMLS 604
Cdd:PTZ00322  159 GFREVVQLLSRhsqchfelgaNAKPDSFTGKPPSLEDSPISSH 201
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
84-112 4.91e-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: 41.09  E-value: 4.91e-05
                          10        20
                  ....*....|....*....|....*....
gi 1953334645  84 GRTALHHAAFSGHGEMVKLLLSRGANINA 112
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
56-142 4.97e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 4.97e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  56 HIAAANKAVKcAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKL 135
Cdd:PTZ00322   88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                  ....*..
gi 1953334645 136 LVAHGAE 142
Cdd:PTZ00322  167 LSRHSQC 173
PHA03095 PHA03095
ankyrin-like protein; Provisional
34-112 5.62e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 5.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  34 VQVLLKHSADVNARDKNWQTPLHIAAA-NKAVKCAEaLVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINA 112
Cdd:PHA03095  240 VLPLLIAGISINARNRYGQTPLHYAAVfNNPRACRR-LIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAET 318
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
753-924 6.40e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 6.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 753 DTLGASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVSSAsADLTLQDN 832
Cdd:PLN03192  511 DLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDA 589
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 833 SKNTALHLACSKGHETsallILEKITDRNLINATNAALQTPLHVAARNGLTMvVQELLGKGASVLAVDENGYTpALACAP 912
Cdd:PLN03192  590 NGNTALWNAISAKHHK----IFRILYHFASISDPHAAGDLLCTAAKRNDLTA-MKELLKQGLNVDSEDHQGAT-ALQVAM 663
                         170
                  ....*....|..
gi 1953334645 913 NKDVADCLALIL 924
Cdd:PLN03192  664 AEDHVDMVRLLI 675
PHA02946 PHA02946
ankyin-like protein; Provisional
334-454 6.60e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.59  E-value: 6.60e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 334 KLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCN--YQCLFALVGSGASVND- 410
Cdd:PHA02946   57 ELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNs 136
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1953334645 411 LDERGCTPLhyAATSDTDGKCLEYLLRNDANPGIRDKQGYNAVH 454
Cdd:PHA02946  137 VDEEGCGPL--LACTDPSERVFKKIMSIGFEARIVDKFGKNHIH 178
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
178-294 6.66e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 46.68  E-value: 6.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 178 EPNAYGNTPLHVACYNGQDVVVNELIDCGANVNQK----------NEKGF----TPLHFAAASTHGALcLELLVGNGAD- 242
Cdd:cd22194   136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkyKHEGFyfgeTPLALAACTNQPEI-VQLLMEKESTd 214
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953334645 243 VNMKSKDGKTPLHMTALHGRFSRSQT--IIQSGAVI--DCEDKN--------GNTPLHIAARYG 294
Cdd:cd22194   215 ITSQDSRGNTVLHALVTVAEDSKTQNdfVKRMYDMIllKSENKNletirnneGLTPLQLAAKMG 278
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
182-210 7.05e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.65  E-value: 7.05e-05
                           10        20
                   ....*....|....*....|....*....
gi 1953334645  182 YGNTPLHVACYNGQDVVVNELIDCGANVN 210
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_4 pfam13637
Ankyrin repeats (many copies);
218-270 7.09e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 7.09e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1953334645 218 TPLHFAAASTHGAlCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTII 270
Cdd:pfam13637   3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
182-214 7.65e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 7.65e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1953334645 182 YGNTPLHVACY-NGQDVVVNELIDCGANVNQKNE 214
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
322-541 8.35e-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: 8.35e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 322 LAALSGFSDCCRKLLSSgfDIDTPDDFGRTCLHAAA---AGGNLECLNLLLNTGADFNKKDKF-----------GRSPLH 387
Cdd:cd21882     1 LEELLGLLECLRWYLTD--SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELvnapctdefyqGQTALH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 388 YAAANCNYQCLFALVGSGASVND------LDERGCT-------PLHYAATSDTDgKCLEYLLRNDANP---GIRDKQGYN 451
Cdd:cd21882    79 IAIENRNLNLVRLLVENGADVSAratgrfFRKSPGNlfyfgelPLSLAACTNQE-EIVRLLLENGAQPaalEAQDSLGNT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 452 AVHysaayghrlCLQLIASETPLDVLMETSGTDMLndsdnratispLHLAAYHGHHQALEvlvqslldlDVRNSSGRTPL 531
Cdd:cd21882   158 VLH---------ALVLQADNTPENSAFVCQMYNLL-----------LSYGAHLDPTQQLE---------EIPNHQGLTPL 208
                         250
                  ....*....|
gi 1953334645 532 DLAAFKGHVE 541
Cdd:cd21882   209 KLAAVEGKIV 218
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
599-822 1.25e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 45.77  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 599 TPLMLSVLNGHTDCVYSLL-NKGANVDAKDKWGRTALHRGAVTGHEECVDALLQhGAKCLFRDS------RGRTPIHLSA 671
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLME-AAPELVNEPmtsdlyQGETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 672 ACGHIGVLGALLQSAASVdANPAIAdnhGYtalhwacynghetcvellleqeVFQKTEGNAF----SPLHCAVINDNEGA 747
Cdd:cd22192    98 VNQNLNLVRELIARGADV-VSPRAT---GT----------------------FFRPGPKNLIyygeHPLSFAACVGNEEI 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 748 AEMLIDTlGASIVnATDSKGRTPLHAAAF----TDHVECLQLLLSHNAQVNSI------DSSGKTPLMMAAENGQTNTVE 817
Cdd:cd22192   152 VRLLIEH-GADIR-AQDSLGNTVLHILVLqpnkTFACQMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQ 229

                  ....*
gi 1953334645 818 MLVSS 822
Cdd:cd22192   230 HLVQK 234
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
321-437 1.31e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 1.31e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 321 HLAALSGFSDccrKLLSSGFDIDTPDDFGRTCLHAA-------AAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANC 393
Cdd:PTZ00322   50 HLEALEATEN---KDATPDHNLTTEEVIDPVVAHMLtvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANG 126
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1953334645 394 NYQCLFALVGSGASVNDLDERGCTPLHYAATSDTdGKCLEYLLR 437
Cdd:PTZ00322  127 HVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF-REVVQLLSR 169
Ank_5 pfam13857
Ankyrin repeats (many copies);
103-157 1.36e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 1.36e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953334645 103 LLSRG-ANINAFDKKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSYTPLHAA 157
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
756-807 2.29e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 2.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953334645 756 GASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMA 807
Cdd:pfam13857   5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
766-797 2.46e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 2.46e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1953334645 766 KGRTPLHAAA-FTDHVECLQLLLSHNAQVNSID 797
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
484-534 2.78e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 2.78e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953334645 484 DMLNDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLA 534
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
84-224 3.17e-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: 44.75  E-value: 3.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  84 GRTALHHAAFSGHGEMVKLLLSRGANINA------FDKKDRraiHWAAYMGHievvkllvahgaevtckdkksyTPLHAA 157
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNAhakgvfFNPKYK---HEGFYFGE----------------------TPLALA 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 158 ASSGMISVVKYLLDlgvdmNEPNAY------GNTPLH----VA-CYNGQDVVVNELIDC------GANVNQ-KNEKGFTP 219
Cdd:cd22194   196 ACTNQPEIVQLLME-----KESTDItsqdsrGNTVLHalvtVAeDSKTQNDFVKRMYDMillkseNKNLETiRNNEGLTP 270

                  ....*
gi 1953334645 220 LHFAA 224
Cdd:cd22194   271 LQLAA 275
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
596-628 3.83e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 3.83e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1953334645 596 NGQTPLMLSVL-NGHTDCVYSLLNKGANVDAKDK 628
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
151-178 4.13e-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: 4.13e-04
                           10        20
                   ....*....|....*....|....*...
gi 1953334645  151 YTPLHAAASSGMISVVKYLLDLGVDMNE 178
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
321-415 4.45e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 4.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 321 HLAAlSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFA 400
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
                          90
                  ....*....|....*
gi 1953334645 401 LVGSGASVNDLDERG 415
Cdd:PTZ00322  167 LSRHSQCHFELGANA 181
PHA02989 PHA02989
ankyrin repeat protein; Provisional
163-422 4.87e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 43.96  E-value: 4.87e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 163 ISVVKYLLDLGVDMNEpnAYGNTPLHVACYNGQDV---VVNELIDCGANVNQKnekGF--TPL-----HFAAASTHGALC 232
Cdd:PHA02989   16 KNALEFLLRTGFDVNE--EYRGNSILLLYLKRKDVkikIVKLLIDNGADVNYK---GYieTPLcavlrNREITSNKIKKI 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 233 LELLVGNGADVNMKSKDGKTPLhMTALHG---------RFsrsqtIIQSGA-VIDCEDKNGNTPLHIaarYGHELLINT- 301
Cdd:PHA02989   91 VKLLLKFGADINLKTFNGVSPI-VCFIYNsninncdmlRF-----LLSKGInVNDVKNSRGYNLLHM---YLESFSVKKd 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 302 ----LITSGADT-AKRGIHGMFPLHLAALSGFS----DCCRKLLSSGFDIDTPDDFGRTCLHAAAagGNLECLNLLLNTG 372
Cdd:PHA02989  162 vikiLLSFGVNLfEKTSLYGLTPMNIYLRNDIDvisiKVIKYLIKKGVNIETNNNGSESVLESFL--DNNKILSKKEFKV 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953334645 373 ADF-------NKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYA 422
Cdd:PHA02989  240 LNFilkyikiNKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
414-447 5.00e-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: 5.00e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1953334645 414 RGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDK 447
Cdd:pfam00023   1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
583-692 5.24e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 5.24e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 583 NAEPQNAVDiqdgngQTPL-MLSV------LNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAK 655
Cdd:PTZ00322   67 NLTTEEVID------PVVAhMLTVelcqlaASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAD 140
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1953334645 656 CLFRDSRGRTPIHLSAACGHIGVLGALL---QSAASVDAN 692
Cdd:PTZ00322  141 PTLLDKDGKTPLELAEENGFREVVQLLSrhsQCHFELGAN 180
PHA02798 PHA02798
ankyrin-like protein; Provisional
749-864 5.98e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.67  E-value: 5.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 749 EMLIDtLGASiVNATDSKGRTPL-----HAAAFTDHVECLQLLLSHNAQVNSIDSSGKTPLMMAAENGQTNTVEMLVS-- 821
Cdd:PHA02798   55 KLFIN-LGAN-VNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFmi 132
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1953334645 822 SASADLTLQDNSKNTALHLACSKGHETSALLI---LEKITDRNLIN 864
Cdd:PHA02798  133 ENGADTTLLDKDGFTMLQVYLQSNHHIDIEIIkllLEKGVDINTHN 178
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
766-794 6.11e-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: 6.11e-04
                           10        20
                   ....*....|....*....|....*....
gi 1953334645  766 KGRTPLHAAAFTDHVECLQLLLSHNAQVN 794
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02859 PHA02859
ankyrin repeat protein; Provisional
372-454 6.37e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.11  E-value: 6.37e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 372 GADFNKKDK-FGRSPLHYAAA---NCNYQCLFALVGSGASVNDLDERGCTPLH-YAATSDTDGKCLEYLLRNDANPGIRD 446
Cdd:PHA02859   76 GADVNFKTRdNNLSALHHYLSfnkNVEPEILKILIDSGSSITEEDEDGKNLLHmYMCNFNVRINVIKLLIDSGVSFLNKD 155

                  ....*...
gi 1953334645 447 KQGYNAVH 454
Cdd:PHA02859  156 FDNNNILY 163
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
562-668 7.01e-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: 7.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 562 RTPIHAAATNGhseCLRLLIgNAEPQNavdiQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDK------------- 628
Cdd:cd22194   114 RILLAFAEENG---ILDRFI-NAEYTE----EAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegf 185
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1953334645 629 -WGRTALHRGAVTGHEECVDALLQHGAKCLF-RDSRGRTPIH 668
Cdd:cd22194   186 yFGETPLALAACTNQPEIVQLLMEKESTDITsQDSRGNTVLH 227
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
760-892 7.47e-04

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: 43.26  E-value: 7.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 760 VNA--TDS--KGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSS--------------GKTPLMMAAENGQTNTVEMLVS 821
Cdd:cd22196    83 VNAayTDSyyKGQTALHIAIERRNMHLVELLVQNGADVHARASGeffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLE 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 822 S--ASADLTLQDNSKNTALHLACS---------------------KGHETSALLILEKITDRNLInatnaalqTPLHVAA 878
Cdd:cd22196   163 NphSPADISARDSMGNTVLHALVEvadntpentkfvtkmyneiliLGAKIRPLLKLEEITNKKGL--------TPLKLAA 234
                         170
                  ....*....|....
gi 1953334645 879 RNGLTMVVQELLGK 892
Cdd:cd22196   235 KTGKIGIFAYILGR 248
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
98-320 7.48e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 43.36  E-value: 7.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  98 EMVKLLLSRG-ANINAFDKKDRRAIhWAAYMGH----IEVVKLLVAHGAEVTCKDKKSYTPLHAAASSGMIS--VVKYLL 170
Cdd:PHA02716  156 DLIKYMVDVGiVNLNYVCKKTGYGI-LHAYLGNmyvdIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNVCasVIKKII 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 171 DLGVDMNEPNAYGNTPLHVACYNGQDV---VVNELIDCGANVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKS 247
Cdd:PHA02716  235 ELGGDMDMKCVNGMSPIMTYIINIDNInpeITNIYIESLDGNKVKNIPMILHSYITLARNIDISVVYSFLQPGVKLHYKD 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 248 KDGKTPLHMTALHGRFSRS--QTIIQSGAVIDCEDKNGNTPLH-------IAARYGHEL-------LINTLITSGADTAK 311
Cdd:PHA02716  315 SAGRTCLHQYILRHNISTDiiKLLHEYGNDLNEPDNIGNTVLHtylsmlsVVNILDPETdndirldVIQCLISLGADITA 394

                  ....*....
gi 1953334645 312 RGIHGMFPL 320
Cdd:PHA02716  395 VNCLGYTPL 403
PHA02884 PHA02884
ankyrin repeat protein; Provisional
165-259 7.52e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 42.66  E-value: 7.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 165 VVKYLLDLGVDMNEP-----NAYgNTPLHVACYNGQDVVVNELIDCGANVNQ-KNEKGFTPLHFAAasTHGAL-CLELLV 237
Cdd:PHA02884   48 IIDAILKLGADPEAPfplseNSK-TNPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKITPLYISV--LHGCLkCLEILL 124
                          90       100
                  ....*....|....*....|..
gi 1953334645 238 GNGADVNMKSKDGKTPLHMTAL 259
Cdd:PHA02884  125 SYGADINIQTNDMVTPIELALM 146
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
215-248 9.28e-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: 9.28e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1953334645 215 KGFTPLHFAAASTHGALCLELLVGNGADVNMKSK 248
Cdd:pfam00023   1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
562-668 1.12e-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: 1.12e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 562 RTPIHAAATN---GHSECLRLLIgNAEPQNAVDIQDGN---------GQTPLMLSVLNGHTDCVYSLLNKGANVDAK--- 626
Cdd:cd21882    27 KTCLHKAALNlndGVNEAIMLLL-EAAPDSGNPKELVNapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSARatg 105
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1953334645 627 ---DKWGRTALHRG-------AVTGHEECVDALLQHGAK---CLFRDSRGRTPIH 668
Cdd:cd21882   106 rffRKSPGNLFYFGelplslaACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLH 160
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
182-210 1.14e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.14e-03
                          10        20
                  ....*....|....*....|....*....
gi 1953334645 182 YGNTPLHVACYNGQDVVVNELIDCGANVN 210
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
282-308 1.28e-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: 1.28e-03
                           10        20
                   ....*....|....*....|....*..
gi 1953334645  282 NGNTPLHIAARYGHELLINTLITSGAD 308
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
116-226 1.44e-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: 42.49  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 116 KDRRAIHWAAYMGHIEVVKLLVAHGAEVTC-------KDKKSYT-------PLHAAASSGMISVVKYLLD---LGVDMNE 178
Cdd:cd22196    93 KGQTALHIAIERRNMHLVELLVQNGADVHArasgeffKKKKGGPgfyfgelPLSLAACTNQLDIVKFLLEnphSPADISA 172
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953334645 179 PNAYGNTPLHVACYNGQDVVVN---------ELIDCGANVNQK-------NEKGFTPLHFAAAS 226
Cdd:cd22196   173 RDSMGNTVLHALVEVADNTPENtkfvtkmynEILILGAKIRPLlkleeitNKKGLTPLKLAAKT 236
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
699-721 1.45e-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: 1.45e-03
                           10        20
                   ....*....|....*....|...
gi 1953334645  699 HGYTALHWACYNGHETCVELLLE 721
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLD 23
Ank_5 pfam13857
Ankyrin repeats (many copies);
373-422 1.53e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 1.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953334645 373 ADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYA 422
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
81-205 1.84e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 42.21  E-value: 1.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  81 DRAGRTALHHAAFSGH--GEMVKLLLSRGANINAFDKKDRRAIHwaAYMGHIEVVKLLvahgaevtckDKKSYTPLHaaa 158
Cdd:PHA02716  314 DSAGRTCLHQYILRHNisTDIIKLLHEYGNDLNEPDNIGNTVLH--TYLSMLSVVNIL----------DPETDNDIR--- 378
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1953334645 159 ssgmISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDC 205
Cdd:PHA02716  379 ----LDVIQCLISLGADITAVNCLGYTPLTSYICTAQNYMYYDIIDC 421
PHA02736 PHA02736
Viral ankyrin protein; Provisional
81-191 2.02e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.86  E-value: 2.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  81 DRAGRTALHHaaFSGHGEMVKLLLSRGANINA-------FDKKDRRAIHWAAYMGHI---EVVKLLVAHGAEVTCKDKK- 149
Cdd:PHA02736   14 DIEGENILHY--LCRNGGVTDLLAFKNAISDEnrylvleYNRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKERVf 91
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1953334645 150 SYTPLHAAASSGMISVVKYLLDL-GVDMNEPNAYGNTPLHVAC 191
Cdd:PHA02736   92 GNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVAC 134
PHA02859 PHA02859
ankyrin repeat protein; Provisional
734-839 2.18e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 2.18e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 734 SPLHCAVIND--NEGAAEMLIDTlGASIVNATDSKGRTPLHA-AAFTDHV--ECLQLLLSHNAQVNSIDSSGKTPLMMAA 808
Cdd:PHA02859   53 TPIFSCLEKDkvNVEILKFLIEN-GADVNFKTRDNNLSALHHyLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHMYM 131
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1953334645 809 ENGQTN--TVEMLVSSASADLTlQDNSKNTALH 839
Cdd:PHA02859  132 CNFNVRinVIKLLIDSGVSFLN-KDFDNNNILY 163
Ank_4 pfam13637
Ankyrin repeats (many copies);
802-847 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
                  ....*....|....*....|....*....|....*....|....*.
gi 1953334645 802 TPLMMAAENGQTNTVEMLVSSaSADLTLQDNSKNTALHLACSKGHE 847
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNV 47
Ank_4 pfam13637
Ankyrin repeats (many copies);
835-890 2.26e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 2.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1953334645 835 NTALHLACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELL 890
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
861-906 2.79e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 2.79e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1953334645 861 NLINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTP 906
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
288-360 2.81e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 2.81e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953334645 288 HIAARyGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGG 360
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
527-557 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 1953334645 527 GRTPLDLAAFK-GHVECVDVLINQGASILVKD 557
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
527-553 2.98e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 2.98e-03
                           10        20
                   ....*....|....*....|....*..
gi 1953334645  527 GRTPLDLAAFKGHVECVDVLINQGASI 553
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_5 pfam13857
Ankyrin repeats (many copies);
76-115 3.30e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 3.30e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1953334645  76 NVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDK 115
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDE 47
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
759-881 3.54e-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: 41.38  E-value: 3.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 759 IVNA--TDS--KGRTPLHAAAFTDHVECLQLLLSHNAQVNSIDSS-------------GKTPLMMAAENGQTNTVEMLVS 821
Cdd:cd22197    82 LVNAqcTDEyyRGHSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELPLSLAACTKQWDVVNYLLE 161
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953334645 822 SAS--ADLTLQDNSKNTALH---LACSKGHETSALL------ILEKITDRN----LINATNAALQTPLHVAARNG 881
Cdd:cd22197   162 NPHqpASLQAQDSLGNTVLHalvMIADNSPENSALVikmydgLLQAGARLCptvqLEEISNHEGLTPLKLAAKEG 236
Ank_5 pfam13857
Ankyrin repeats (many copies);
406-455 3.57e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 3.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1953334645 406 ASVNDLDERGCTPLHYAAtSDTDGKCLEYLLRNDANPGIRDKQGYNAVHY 455
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAA-KYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
120-148 3.90e-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: 3.90e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1953334645 120 AIHWAAYM-GHIEVVKLLVAHGAEVTCKDK 148
Cdd:pfam00023   5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
335-515 4.42e-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: 4.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 335 LLSSGFDIDTpddfGRTCLHAA-----------------AAGGNLECLNLLLNTGADFNkkdkFGRSPLHYAAANCNYQC 397
Cdd:TIGR00870  72 LLNLSCRGAV----GDTLLHAIsleyvdaveaillhllaAFRKSGPLELANDQYTSEFT----PGITALHLAAHRQNYEI 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 398 LFALVGSGASVN--------------DLDERGCTPLH-YAATSDTDgkCLEYLLRNDANPGIRDKQGYNAVH-------Y 455
Cdd:TIGR00870 144 VKLLLERGASVParacgdffvksqgvDSFYHGESPLNaAACLGSPS--IVALLSEDPADILTADSLGNTLLHllvmeneF 221
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953334645 456 SAAYGH--RLCLQLIasetpLDVLMETSGTDMLNDSDNRATISPLHLAAYHGHHQALEVLVQ 515
Cdd:TIGR00870 222 KAEYEElsCQMYNFA-----LSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
596-625 4.50e-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: 4.50e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1953334645  596 NGQTPLMLSVLNGHTDCVYSLLNKGANVDA 625
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
84-226 4.53e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.93  E-value: 4.53e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  84 GRTALHHAAFSGHGEMVKLLLSRGANINA------FDKKDRRAihwAAYMGHievvkllvahgaevtckdkksyTPLHAA 157
Cdd:cd22193    76 GQTALHIAIERRQGDIVALLVENGADVHAhakgrfFQPKYQGE---GFYFGE----------------------LPLSLA 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 158 ASSGMISVVKYLLD---LGVDMNEPNAYGNTPLHVACYNGQDVVVN---------ELIDCGANVNQ-------KNEKGFT 218
Cdd:cd22193   131 ACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLHALVTVADNTKENtkfvtrmydMILIRGAKLCPtveleeiRNNDGLT 210

                  ....*...
gi 1953334645 219 PLHFAAAS 226
Cdd:cd22193   211 PLQLAAKM 218
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
120-145 5.01e-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: 35.26  E-value: 5.01e-03
                           10        20
                   ....*....|....*....|....*.
gi 1953334645  120 AIHWAAYMGHIEVVKLLVAHGAEVTC 145
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
872-923 5.13e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 5.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953334645 872 TPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADCLALI 923
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02791 PHA02791
ankyrin-like protein; Provisional
41-219 5.22e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.03  E-value: 5.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645  41 SADVNARDKNWQTPLHIAAANKAVKC------AEALVPLLSNvnvsdragRTALHHAAFSGHGEMVKLLLSRGANINAFD 114
Cdd:PHA02791   20 SKDAFKADVHGHSALYYAIADNNVRLvctllnAGALKNLLEN--------EFPLHQAATLEDTKIVKILLFSGMDDSQFD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 115 KKDRRAIHWAAYMGHIEVVKLLVAHGAEVTCKDKKSY-TPLHAAASSGMISVVKYLL-------DLGVDMnepnaygnTP 186
Cdd:PHA02791   92 DKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLseipstfDLAILL--------SC 163
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1953334645 187 LHVACYNGQDVVVNELIDCGANVNQKNEKGFTP 219
Cdd:PHA02791  164 IHITIKNGHVDMMILLLDYMTSTNTNNSLLFIP 196
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
710-890 7.30e-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: 7.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 710 NGHETCVELLLEQEVFQKTEGNAfspLHCAVINDnEGAAEMLI--------DTLGASIVNATD----SKGRTPLHAAAFT 777
Cdd:TIGR00870  63 NENLELTELLLNLSCRGAVGDTL---LHAISLEY-VDAVEAILlhllaafrKSGPLELANDQYtsefTPGITALHLAAHR 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 778 DHVECLQLLLSHNAQVNS------------IDS--SGKTPLMMAAENGQTNTVEMLvSSASADLTLQDNSKNTALHL--- 840
Cdd:TIGR00870 139 QNYEIVKLLLERGASVPAracgdffvksqgVDSfyHGESPLNAAACLGSPSIVALL-SEDPADILTADSLGNTLLHLlvm 217
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 841 ---------ACSKGHETSALLILEKITD-RNLINATNAALQTPLHVAARNGLTMVVQELL 890
Cdd:TIGR00870 218 enefkaeyeELSCQMYNFALSLLDKLRDsKELEVILNHQGLTPLKLAAKEGRIVLFRLKL 277
PHA02989 PHA02989
ankyrin repeat protein; Provisional
130-221 8.64e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 39.72  E-value: 8.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 130 IEVVKLLVAHGAEVtckDKKSY--TPLHAA------ASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNE 201
Cdd:PHA02989   50 IKIVKLLIDNGADV---NYKGYieTPLCAVlrnreiTSNKIKKIVKLLLKFGADINLKTFNGVSPIVCFIYNSNINNCDM 126
                          90       100
                  ....*....|....*....|....
gi 1953334645 202 L---IDCGANVNQ-KNEKGFTPLH 221
Cdd:PHA02989  127 LrflLSKGINVNDvKNSRGYNLLH 150
Ank_5 pfam13857
Ankyrin repeats (many copies);
786-841 8.66e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 8.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953334645 786 LLSH-NAQVNSIDSSGKTPLMMAAENGQTNTVEMLVsSASADLTLQDNSKNTALHLA 841
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
282-308 8.79e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 8.79e-03
                          10        20
                  ....*....|....*....|....*..
gi 1953334645 282 NGNTPLHIAARYGHELLINTLITSGAD 308
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
282-308 9.11e-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: 9.11e-03
                          10        20
                  ....*....|....*....|....*...
gi 1953334645 282 NGNTPLHIAA-RYGHELLINTLITSGAD 308
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGAD 28
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
510-704 9.52e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 39.90  E-value: 9.52e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 510 LEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVeCVDVL---INQGASILVKdYILKRTPIHAAATNghseclrllIGNAEP 586
Cdd:PHA02716  195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNV-CASVIkkiIELGGDMDMK-CVNGMSPIMTYIIN---------IDNINP 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953334645 587 Q--NA-VDIQDGNGQT--PLMLSVL-----NGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGH--EECVDALLQHGA 654
Cdd:PHA02716  264 EitNIyIESLDGNKVKniPMILHSYitlarNIDISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTDIIKLLHEYGN 343
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953334645 655 KCLFRDSRGRTPIH--LSAACG------------HIGVLGALLQSAASVDAnpaiADNHGYTAL 704
Cdd:PHA02716  344 DLNEPDNIGNTVLHtyLSMLSVvnildpetdndiRLDVIQCLISLGADITA----VNCLGYTPL 403
Ank_4 pfam13637
Ankyrin repeats (many copies);
417-467 9.55e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 9.55e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953334645 417 TPLHYAATSDtDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCLQL 467
Cdd:pfam13637   3 TALHAAAASG-HLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKL 52
 
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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