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Conserved domains on  [gi|1370483583|ref|XP_024309190|]
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serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A isoform X8 [Homo sapiens]

Protein Classification

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

ankyrin repeat (ANK) domain-containing protein is involved in mediating protein-protein interactions

Gene Ontology:  GO:0005515
PubMed:  33435370|17176038

Graphical summary

 Zoom to residue level

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-287 2.91e-50

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 179.38  E-value: 2.91e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  25 LNFLFYLEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLL 104
Cdd:COG0666    28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 105 SRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGN 184
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 185 TPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSKDGKTPLHMTALHGRFS 264
Cdd:COG0666   188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266
                         250       260
                  ....*....|....*....|...
gi 1370483583 265 RSQTIIQSGAVIDCEDKNGNTPL 287
Cdd:COG0666   267 IVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
484-721 7.19e-39

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.64  E-value: 7.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 484 DMLSDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGASILVKDYiLKRT 563
Cdd:COG0666    44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGET 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 564 PIHAAATNGHSECLRLLIGNaepqNA-VDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGH 642
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEA----GAdVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483583 643 EECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAasmdANPATADNHGYTALHWACYNGHETCVELLLE 721
Cdd:COG0666   199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG----ADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
681-925 1.41e-34

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.31  E-value: 1.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 681 ALLQSAASMDANPATADNHGYTALHWACYNGHETCVELLLEQEVF-QKTEGNAFSPLHCAVINDNEGAAEMLIDtLGASi 759
Cdd:COG0666    35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADiNAKDDGGNTLLHAAARNGDLEIVKLLLE-AGAD- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 760 VNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSsASAELTLQDNSKNTALH 839
Cdd:COG0666   113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLH 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 840 LACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADC 919
Cdd:COG0666   192 LAAENGHLEIVKLLLEAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268

                  ....*.
gi 1370483583 920 LALILA 925
Cdd:COG0666   269 KLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
169-447 1.60e-33

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.23  E-value: 1.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 169 LLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSK 248
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 249 DGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGF 328
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 329 SDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASV 408
Cdd:COG0666   166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1370483583 409 NDLDERGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDK 447
Cdd:COG0666   246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-287 2.91e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 179.38  E-value: 2.91e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  25 LNFLFYLEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLL 104
Cdd:COG0666    28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 105 SRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGN 184
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 185 TPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSKDGKTPLHMTALHGRFS 264
Cdd:COG0666   188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266
                         250       260
                  ....*....|....*....|...
gi 1370483583 265 RSQTIIQSGAVIDCEDKNGNTPL 287
Cdd:COG0666   267 IVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
484-721 7.19e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.64  E-value: 7.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 484 DMLSDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGASILVKDYiLKRT 563
Cdd:COG0666    44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGET 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 564 PIHAAATNGHSECLRLLIGNaepqNA-VDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGH 642
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEA----GAdVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483583 643 EECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAasmdANPATADNHGYTALHWACYNGHETCVELLLE 721
Cdd:COG0666   199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG----ADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
PHA03100 PHA03100
ankyrin repeat protein; Provisional
34-245 1.46e-35

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 140.57  E-value: 1.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  34 VQVLLKHSADVNARDKNWQTPLHIAAANKAV-----KCAEALVPLLSNVNVSDRAGRTALHHAAF--SGHGEMVKLLLSR 106
Cdd:PHA03100   51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDN 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 107 GANINAFDKKDRRAIHWAAYMGHI--EVVKLLVSHGAEVTCKDKksytplhaaassgmisvVKYLLDLGVDMNEPNAYGN 184
Cdd:PHA03100  131 GANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGF 193
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370483583 185 TPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNM 245
Cdd:PHA03100  194 TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI-FKLLLNNGPSIKT 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
681-925 1.41e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.31  E-value: 1.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 681 ALLQSAASMDANPATADNHGYTALHWACYNGHETCVELLLEQEVF-QKTEGNAFSPLHCAVINDNEGAAEMLIDtLGASi 759
Cdd:COG0666    35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADiNAKDDGGNTLLHAAARNGDLEIVKLLLE-AGAD- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 760 VNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSsASAELTLQDNSKNTALH 839
Cdd:COG0666   113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLH 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 840 LACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADC 919
Cdd:COG0666   192 LAAENGHLEIVKLLLEAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268

                  ....*.
gi 1370483583 920 LALILA 925
Cdd:COG0666   269 KLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
169-447 1.60e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.23  E-value: 1.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 169 LLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSK 248
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 249 DGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGF 328
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 329 SDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASV 408
Cdd:COG0666   166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1370483583 409 NDLDERGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDK 447
Cdd:COG0666   246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
PHA03095 PHA03095
ankyrin-like protein; Provisional
163-419 2.60e-31

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 128.99  E-value: 2.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 163 ISVVKYLLDLGVDMNEPNAYGNTPLHV--ACYNGQDV-VVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGN 239
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLylHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 240 GADVNMKSKDGKTPLH--MTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGH---ELLiNTLITSGADTAKRGI 314
Cdd:PHA03095  107 GADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGADVYAVDD 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 315 HGMFPLHLAALS--GFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLL--NTGADFNKKDKFGRSPLHYAA 390
Cdd:PHA03095  186 RFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPllIAGISINARNRYGQTPLHYAA 265
                         250       260       270
                  ....*....|....*....|....*....|
gi 1370483583 391 ANCNyQCLFA-LVGSGASVNDLDERGCTPL 419
Cdd:PHA03095  266 VFNN-PRACRrLIALGADINAVSSDGNTPL 294
PHA02874 PHA02874
ankyrin repeat protein; Provisional
498-807 7.99e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 102.73  E-value: 7.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 498 LHLAAYHGHHQALEVLVQS---LLDLDVRNSSgrTPLDLAAFKGHVECVDVLINQGASIlvkDYILKRTP--IHAAATNG 572
Cdd:PHA02874    5 LRMCIYSGDIEAIEKIIKNkgnCINISVDETT--TPLIDAIRSGDAKIVELFIKHGADI---NHINTKIPhpLLTAIKIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 573 HSECLRLLIgnaepQNAVDIQdgngqtplMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQH 652
Cdd:PHA02874   80 AHDIIKLLI-----DNGVDTS--------ILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEY 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 653 GAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAASMDANpataDNHGYTALHWACYNGHETCVELLLEQ--EVFQKTEg 730
Cdd:PHA02874  147 GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK----DNNGESPLHNAAEYGDYACIKLLIDHgnHIMNKCK- 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370483583 731 NAFSPLHCAVINdNEGAAEMLIDTlgASIvNATDSKGRTPLH-AAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMA 807
Cdd:PHA02874  222 NGFTPLHNAIIH-NRSAIELLINN--ASI-NDQDIDGSTPLHhAINPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
88-180 5.35e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 5.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  88 LHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHgAEVTCKDKKsYTPLHAAASSGMISVVK 167
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1370483583 168 YLLDLGVDMNEPN 180
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
597-926 2.41e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 92.40  E-value: 2.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 597 GQTPLMLSVLNGHTDC---VYSLLNKGANVDAKDKWGRTALH---RGAVTghEECVDALLQHGAKCLLRDSRGRTPIH-- 668
Cdd:PHA03095   47 GKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHlylYNATT--LDVIKLLIKAGADVNAKDKVGRTPLHvy 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 669 LSAACGHIGVLGALLQsaasMDANPATADNHGYTalhwacynghetcvellleqevfqktegnafsPLHCAVINdnegaa 748
Cdd:PHA03095  125 LSGFNINPKVIRLLLR----KGADVNALDLYGMT--------------------------------PLAVLLKS------ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 749 emlidtlgasiVNATdskgrtplhaaaftdhVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNT--VEMLVSsASAE 826
Cdd:PHA03095  163 -----------RNAN----------------VELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRAriVRELIR-AGCD 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 827 LTLQDNSKNTALHLACSKGHETSALLI--LEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGY 904
Cdd:PHA03095  215 PAATDMLGNTPLHSMATGSSCKRSLVLplLIAGIS---INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGN 291
                         330       340
                  ....*....|....*....|..
gi 1370483583 905 TPALACAPNKDVaDCLALILAT 926
Cdd:PHA03095  292 TPLSLMVRNNNG-RAVRAALAK 312
Ank_2 pfam12796
Ankyrin repeats (3 copies);
565-660 1.75e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 565 IHAAATNGHSECLRLLIgnaEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKgANVDAKDKwGRTALHRGAVTGHEE 644
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL---ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE 75
                          90
                  ....*....|....*.
gi 1370483583 645 CVDALLQHGAKCLLRD 660
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
771-864 1.30e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 1.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 771 LHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSASAELtlqDNSKNTALHLACSKGHETSA 850
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 1370483583 851 LLILEKITDRNLIN 864
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
254-346 7.74e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.14  E-value: 7.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 254 LHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGAdtAKRGIHGMFPLHLAALSGFSDCCR 333
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1370483583 334 KLLSSGFDIDTPD 346
Cdd:pfam12796  79 LLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
31-203 1.70e-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: 71.20  E-value: 1.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  31 LEAVQVLLK-HSADVNARDKNWQTPLHIAAANKAVKCAEAL---VPLLSNVNV-SD-RAGRTALHHAAFSGHGEMVKLLL 104
Cdd:cd22192    30 VQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLmeaAPELVNEPMtSDlYQGETALHIAVVNQNLNLVRELI 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 105 SRGANIN-------AFDKKDRRAIHW-------AAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLL 170
Cdd:cd22192   110 ARGADVVspratgtFFRPGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMY 189
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1370483583 171 DLGVDMNE----------PNAYGNTPLHVACYNGQDVVVNELI 203
Cdd:cd22192   190 DLILSYDKeddlqpldlvPNNQGLTPFKLAAKEGNIVMFQHLV 232
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
529-669 1.52e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 61.95  E-value: 1.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 529 TPLDLAAFKGHVECVDVLINQGASILVKDYILKRTPIHAAATNGHSECLRLLIGNA-----EPQNAVDIQdgnGQTPLML 603
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelvnEPMTSDLYQ---GETALHI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 604 SVLNGHTDCVYSLLNKGANV--------------DAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHL 669
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
518-741 4.27e-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: 4.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 518 LDLDVRNSSGRTPLDLAAFKG-HVECVDVLINQGASILVKDyilkrTPIHAAATNGH---SECLRLLIGNAE----PQNA 589
Cdd:TIGR00870  43 LNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGD-----TLLHAISLEYVdavEAILLHLLAAFRksgpLELA 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 590 VDIQDGN---GQTPLMLSVLNGHTDCVYSLLNKGANVDAKDK--------------WGRTALHRGAVTGHEECVDALLQH 652
Cdd:TIGR00870 118 NDQYTSEftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSED 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 653 GAKCLLRDSRGRTPIHLSAACGHIGVLGALL-----QSAASMDANPATAD------NH-GYTALHWACYNGHETCVELLL 720
Cdd:TIGR00870 198 PADILTADSLGNTLLHLLVMENEFKAEYEELscqmyNFALSLLDKLRDSKelevilNHqGLTPLKLAAKEGRIVLFRLKL 277
                         250       260
                  ....*....|....*....|..
gi 1370483583 721 EQEVFQKT-EGNAFSPLHCAVI 741
Cdd:TIGR00870 278 AIKYKQKKfVAWPNGQQLLSLY 299
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
649-822 6.36e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.56  E-value: 6.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 649 LLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAASMDANPATADNH-GYTALHWACYNGHETCVELLLEQ----- 722
Cdd:cd22192    37 LKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDLYqGETALHIAVVNQNLNLVRELIARgadvv 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 723 ------EVFQKTEGNAF----SPLHCAVINDNEGAAEMLIDTlGASIVnATDSKGRTPLHAAAF----TDHVECLQLLLS 788
Cdd:cd22192   117 spratgTFFRPGPKNLIyygeHPLSFAACVGNEEIVRLLIEH-GADIR-AQDSLGNTVLHILVLqpnkTFACQMYDLILS 194
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1370483583 789 HNAQVNSV------DSTGKTPLMMAAENGQTNTVEMLVSS 822
Cdd:cd22192   195 YDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQHLVQK 234
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
31-191 1.16e-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: 52.78  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  31 LEAVQVLLKHSADVNARDknwqTPLHIAAANKAVKCAEALVPLLSN---------VNVSDR----AGRTALHHAAFSGHG 97
Cdd:TIGR00870  66 LELTELLLNLSCRGAVGD----TLLHAISLEYVDAVEAILLHLLAAfrksgplelANDQYTseftPGITALHLAAHRQNY 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  98 EMVKLLLSRGANINA------FDKKDRRA--------IHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAA----- 158
Cdd:TIGR00870 142 EIVKLLLERGASVPAracgdfFVKSQGVDsfyhgespLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenef 221
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1370483583 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 ...
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 1370483583 218 TPLhFAAASTHGALCLE-LLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGA-----VIDCEDKNGNTPLHIAA 291
Cdd:cd22192    19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPelvnePMTSDLYQGETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 292 RYGHELLINTLITSGADTAKRGIHGMFplhlaalsgFSDCCRKLLSsgfdidtpddFGRTCLHAAAAGGNLECLNLLLNT 371
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSPRATGTF---------FRPGPKNLIY----------YGEHPLSFAACVGNEEIVRLLIEH 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370483583 372 GADFNKKDKFGRSPLHYAA--ANCNYQC-----LFALVGSGASVNdLD----ERGCTPLHYAA 423
Cdd:cd22192   159 GADIRAQDSLGNTVLHILVlqPNKTFACqmydlILSYDKEDDLQP-LDlvpnNQGLTPFKLAA 220
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
84-112 1.72e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 1.72e-05
                           10        20
                   ....*....|....*....|....*....
gi 1370483583   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 5.12e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 5.12e-04
                           10        20
                   ....*....|....*....|....*....
gi 1370483583  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 1.04e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 1.04e-03
                           10        20
                   ....*....|....*....|....*..
gi 1370483583  282 NGNTPLHIAARYGHELLINTLITSGAD 308
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
699-721 1.20e-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: 1.20e-03
                           10        20
                   ....*....|....*....|...
gi 1370483583  699 HGYTALHWACYNGHETCVELLLE 721
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLD 23
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
335-515 4.20e-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: 41.22  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 335 LLSSGFDIDTpddfGRTCLHAA-----------------AAGGNLECLNLLLNTGADFNkkdkFGRSPLHYAAANCNYQC 397
Cdd:TIGR00870  72 LLNLSCRGAV----GDTLLHAIsleyvdaveaillhllaAFRKSGPLELANDQYTSEFT----PGITALHLAAHRQNYEI 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 398 LFALVGSGASVN--------------DLDERGCTPLH-YAATSDTDgkCLEYLLRNDANPGIRDKQGYNAVH-------Y 455
Cdd:TIGR00870 144 VKLLLERGASVParacgdffvksqgvDSFYHGESPLNaAACLGSPS--IVALLSEDPADILTADSLGNTLLHllvmeneF 221
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370483583 456 SAAYGH--RLCLQLIasetpLDVLMETSGTDMLSDSDNRATISPLHLAAYHGHHQALEVLVQ 515
Cdd:TIGR00870 222 KAEYEElsCQMYNFA-----LSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
710-890 8.81e-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: 8.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 710 NGHETCVELLLEQEVFQKTEGNAfspLHCAVINDnEGAAEMLI--------DTLGASIVNATD----SKGRTPLHAAAFT 777
Cdd:TIGR00870  63 NENLELTELLLNLSCRGAVGDTL---LHAISLEY-VDAVEAILlhllaafrKSGPLELANDQYtsefTPGITALHLAAHR 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 778 DHVECLQLLLSHNAQVNS------------VDST--GKTPLMMAAENGQTNTVEMLvSSASAELTLQDNSKNTALHL--- 840
Cdd:TIGR00870 139 QNYEIVKLLLERGASVPAracgdffvksqgVDSFyhGESPLNAAACLGSPSIVALL-SEDPADILTADSLGNTLLHLlvm 217
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 841 ---------ACSKGHETSALLILEKITD-RNLINATNAALQTPLHVAARNGLTMVVQELL 890
Cdd:TIGR00870 218 enefkaeyeELSCQMYNFALSLLDKLRDsKELEVILNHQGLTPLKLAAKEGRIVLFRLKL 277
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
25-287 2.91e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 179.38  E-value: 2.91e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  25 LNFLFYLEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLL 104
Cdd:COG0666    28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLL 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 105 SRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGN 184
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGE 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 185 TPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSKDGKTPLHMTALHGRFS 264
Cdd:COG0666   188 TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLLEAGADLNAKDKDGLTALLLAAAAGAAL 266
                         250       260
                  ....*....|....*....|...
gi 1370483583 265 RSQTIIQSGAVIDCEDKNGNTPL 287
Cdd:COG0666   267 IVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
31-312 2.78e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 176.68  E-value: 2.78e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  31 LEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANI 110
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 111 NAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVA 190
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 191 CYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTII 270
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI-VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1370483583 271 QSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKR 312
Cdd:COG0666   240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
484-721 7.19e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.64  E-value: 7.19e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 484 DMLSDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGASILVKDYiLKRT 563
Cdd:COG0666    44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGET 122
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 564 PIHAAATNGHSECLRLLIGNaepqNA-VDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGH 642
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEA----GAdVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH 198
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483583 643 EECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAasmdANPATADNHGYTALHWACYNGHETCVELLLE 721
Cdd:COG0666   199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG----ADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
98-419 9.99e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.17  E-value: 9.99e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  98 EMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMN 177
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 178 EPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKskdgktplhmt 257
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI-VKLLLEAGADVNAQ----------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 258 alhgrfsrsqtiiqsgavidceDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLS 337
Cdd:COG0666   150 ----------------------DNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 338 SGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCT 417
Cdd:COG0666   208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287

                  ..
gi 1370483583 418 PL 419
Cdd:COG0666   288 LL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
546-870 1.44e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.79  E-value: 1.44e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 546 LINQGASILVKDYILKRTPIHAAATNGHSECLRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDA 625
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 626 KDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSaasmDANPATADNHGYTALH 705
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA----GADVNAQDNDGNTPLH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 706 WACYNGHETCVELLLEQevfqktegnafsplhcavindneGAaemlidtlgasIVNATDSKGRTPLHAAAFTDHVECLQL 785
Cdd:COG0666   159 LAAANGNLEIVKLLLEA-----------------------GA-----------DVNARDNDGETPLHLAAENGHLEIVKL 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 786 LLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVsSASAELTLQDNSKNTALHLACSKGHETSALLILEKITDRNLINA 865
Cdd:COG0666   205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL-EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283

                  ....*
gi 1370483583 866 TNAAL 870
Cdd:COG0666   284 DLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
577-907 4.36e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.63  E-value: 4.36e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 577 LRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKC 656
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 657 LLRDSRGRTPIHLSAACGHIGVLGALLQSaasmDANPATADNHGYTALHWACYNGHETCVELLLEQevfqktegnafspl 736
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEA----GADVNARDKDGETPLHLAAYNGNLEIVKLLLEA-------------- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 737 hcavindnegaaemlidtlGASiVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTV 816
Cdd:COG0666   143 -------------------GAD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 817 EMLVsSASAELTLQDNSKNTALHLACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASV 896
Cdd:COG0666   203 KLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
                         330
                  ....*....|.
gi 1370483583 897 LAVDENGYTPA 907
Cdd:COG0666   279 AAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
451-698 7.89e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.86  E-value: 7.89e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 451 NAVHYSAAYGHRLCLQLIASETPLDVLMETSGTDMLSDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTP 530
Cdd:COG0666    44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETP 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 531 LDLAAFKGHVECVDVLINQGASILVKDyILKRTPIHAAATNGHSECLRLLIGNaepqNA-VDIQDGNGQTPLMLSVLNGH 609
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGADVNAQD-NDGNTPLHLAAANGNLEIVKLLLEA----GAdVNARDNDGETPLHLAAENGH 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 610 TDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAASM 689
Cdd:COG0666   199 LEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278

                  ....*....
gi 1370483583 690 DANPATADN 698
Cdd:COG0666   279 AAALLDLLT 287
PHA03100 PHA03100
ankyrin repeat protein; Provisional
34-245 1.46e-35

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 140.57  E-value: 1.46e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  34 VQVLLKHSADVNARDKNWQTPLHIAAANKAV-----KCAEALVPLLSNVNVSDRAGRTALHHAAF--SGHGEMVKLLLSR 106
Cdd:PHA03100   51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDN 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 107 GANINAFDKKDRRAIHWAAYMGHI--EVVKLLVSHGAEVTCKDKksytplhaaassgmisvVKYLLDLGVDMNEPNAYGN 184
Cdd:PHA03100  131 GANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGF 193
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370483583 185 TPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNM 245
Cdd:PHA03100  194 TPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI-FKLLLNNGPSIKT 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
681-925 1.41e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.31  E-value: 1.41e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 681 ALLQSAASMDANPATADNHGYTALHWACYNGHETCVELLLEQEVF-QKTEGNAFSPLHCAVINDNEGAAEMLIDtLGASi 759
Cdd:COG0666    35 LLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADiNAKDDGGNTLLHAAARNGDLEIVKLLLE-AGAD- 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 760 VNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSsASAELTLQDNSKNTALH 839
Cdd:COG0666   113 VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLH 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 840 LACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADC 919
Cdd:COG0666   192 LAAENGHLEIVKLLLEAGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIV 268

                  ....*.
gi 1370483583 920 LALILA 925
Cdd:COG0666   269 KLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
169-447 1.60e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.23  E-value: 1.60e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 169 LLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSK 248
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 249 DGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGF 328
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 329 SDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASV 408
Cdd:COG0666   166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1370483583 409 NDLDERGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDK 447
Cdd:COG0666   246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
PHA03095 PHA03095
ankyrin-like protein; Provisional
30-254 8.49e-33

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 133.23  E-value: 8.49e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  30 YLEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVkcaEALVPLL----SNVNVSDRAGRTALH-HAA-FSGHGEMVKLL 103
Cdd:PHA03095   62 VKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATT---LDVIKLLikagADVNAKDKVGRTPLHvYLSgFNINPKVIRLL 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 104 LSRGANINAFDKKDRRAIHwaAYMGH----IEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMIS--VVKYLLDLGVDMN 177
Cdd:PHA03095  139 LRKGADVNALDLYGMTPLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPA 216
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483583 178 EPNAYGNTPLHVACYNG--QDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGnGADVNMKSKDGKTPL 254
Cdd:PHA03095  217 ATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIAL-GADINAVSSDGNTPL 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
30-303 1.48e-32

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 132.46  E-value: 1.48e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  30 YLEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLL---SNVNVSDRAGRTALH-HAAFSGHGEMVKLLLS 105
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLeagADVNAPERCGFTPLHlYLYNATTLDVIKLLIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 106 RGANINAFDKKDRRAIHwaAYMG----HIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISV--VKYLLDLGVDMNEP 179
Cdd:PHA03095  106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 180 NAYGNTPLHVACYNGQD--VVVNELIDCGAIVNQKNEKGFTPLHFAAA-STHGALCLELLVGNGADVNMKSKDGKTPLHM 256
Cdd:PHA03095  184 DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370483583 257 TALHGR---FSRsqtIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLI 303
Cdd:PHA03095  264 AAVFNNpraCRR---LIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
681-925 3.45e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.38  E-value: 3.45e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 681 ALLQSAASMDANPATADNHGYTALHWACYNGHETCVELLLEQEVFQKTEGNAFSPLHCAVINDNEGAAEMLIDTLGASIv 760
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI- 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 761 NATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVsSASAELTLQDNSKNTALHL 840
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLL-EAGADVNAQDNDGNTPLHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 841 ACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADCL 920
Cdd:COG0666   160 AAANGNLEIVKLLLEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                  ....*
gi 1370483583 921 ALILA 925
Cdd:COG0666   237 LLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
207-469 1.54e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.45  E-value: 1.54e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 207 AIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTP 286
Cdd:COG0666    11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 287 LHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLN 366
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 367 LLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLLRNDANPGIRD 446
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENG-NLEIVKLLLEAGADLNAKD 249
                         250       260
                  ....*....|....*....|...
gi 1370483583 447 KQGYNAVHYSAAYGHRLCLQLIA 469
Cdd:COG0666   250 KDGLTALLLAAAAGAALIVKLLL 272
PHA03095 PHA03095
ankyrin-like protein; Provisional
163-419 2.60e-31

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 128.99  E-value: 2.60e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 163 ISVVKYLLDLGVDMNEPNAYGNTPLHV--ACYNGQDV-VVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGN 239
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLylHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 240 GADVNMKSKDGKTPLH--MTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGH---ELLiNTLITSGADTAKRGI 314
Cdd:PHA03095  107 GADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanvELL-RLLIDAGADVYAVDD 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 315 HGMFPLHLAALS--GFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLL--NTGADFNKKDKFGRSPLHYAA 390
Cdd:PHA03095  186 RFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPllIAGISINARNRYGQTPLHYAA 265
                         250       260       270
                  ....*....|....*....|....*....|
gi 1370483583 391 ANCNyQCLFA-LVGSGASVNDLDERGCTPL 419
Cdd:PHA03095  266 VFNN-PRACRrLIALGADINAVSSDGNTPL 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
130-398 8.70e-31

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 127.45  E-value: 8.70e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 130 IEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGM---ISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDV-VVNELIDC 205
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 206 GAIVNQKNEKGFTPLH--FAAASTHgALCLELLVGNGADVNMKSKDGKTPLHMtalhgrFSRSQTI--------IQSGAV 275
Cdd:PHA03095  107 GADVNAKDKVGRTPLHvyLSGFNIN-PKVIRLLLRKGADVNALDLYGMTPLAV------LLKSRNAnvellrllIDAGAD 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 276 IDCEDKNGNTPLHIAARYGH--ELLINTLITSGADTAKRGIHGMFPLHLAALsgFSDCCR----KLLSSGFDIDTPDDFG 349
Cdd:PHA03095  180 VYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLGNTPLHSMAT--GSSCKRslvlPLLIAGISINARNRYG 257
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*....
gi 1370483583 350 RTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCL 398
Cdd:PHA03095  258 QTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAV 306
PHA02876 PHA02876
ankyrin repeat protein; Provisional
99-419 1.43e-30

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 129.03  E-value: 1.43e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  99 MVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNE 178
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINK 239
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 179 P-----NAYGNTPLHVACYngqdvvvneLIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSKDGKTP 253
Cdd:PHA02876  240 NdlsllKAIRNEDLETSLL---------LYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETP 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 254 LHMTALHGRFSRS-QTIIQSGAVIDCEDKNGNTPLHIAA---RYGHELLinTLITSGADTAKRGIHGMFPLHLAALSGFS 329
Cdd:PHA02876  311 LYLMAKNGYDTENiRTLIMLGADVNAADRLYITPLHQAStldRNKDIVI--TLLELGANVNARDYCDKTPIHYAAVRNNV 388
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 330 DCCRKLLSSGFDIDTPDDFGRTCLHAAAAG-GNLECLNLLLNTGADFNKKDKFGRSPLHYAAA-NCNYQCLFALVGSGAS 407
Cdd:PHA02876  389 VIINTLLDYGADIEALSQKIGTALHFALCGtNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKkNCKLDVIEMLLDNGAD 468
                         330
                  ....*....|..
gi 1370483583 408 VNDLDERGCTPL 419
Cdd:PHA02876  469 VNAINIQNQYPL 480
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
233-531 1.54e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.37  E-value: 1.54e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 233 LELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKR 312
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 313 GIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAAN 392
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 393 CNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCLQLIASET 472
Cdd:COG0666   164 GNLEIVKLLLEAGADVNARDNDGETPLHLAAENG-HLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483583 473 PLDvlmetsgtdmlsDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPL 531
Cdd:COG0666   243 ADL------------NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
296-634 5.37e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.83  E-value: 5.37e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 296 ELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADF 375
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 376 NKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLLRNDANPGIRDKQGYnavhy 455
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG-NLEIVKLLLEAGADVNAQDNDGN----- 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 456 saayghrlclqliasetpldvlmetsgtdmlsdsdnratiSPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAA 535
Cdd:COG0666   155 ----------------------------------------TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 536 FKGHVECVDVLINQGASILVKDYiLKRTPIHAAATNGHSECLRLLIGNAEpqnAVDIQDGNGQTPLMLSVLNGHTDCVYS 615
Cdd:COG0666   195 ENGHLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGA---DLNAKDKDGLTALLLAAAAGAALIVKL 270
                         330
                  ....*....|....*....
gi 1370483583 616 LLNKGANVDAKDKWGRTAL 634
Cdd:COG0666   271 LLLALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
31-214 1.65e-29

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 122.47  E-value: 1.65e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  31 LEAVQVLLKHSADVNARDKNWQTPLHIAAANKavKCAEALVPLL----SNVNVSDRAGRTALHHAAFSGHG--EMVKLLL 104
Cdd:PHA03100   86 KEIVKLLLEYGANVNAPDNNGITPLLYAISKK--SNSYSIVEYLldngANVNIKNSDGENLLHLYLESNKIdlKILKLLI 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 105 SRGANINAfdkKDRraihwaaymghievVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGN 184
Cdd:PHA03100  164 DKGVDINA---KNR--------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226
                         170       180       190
                  ....*....|....*....|....*....|
gi 1370483583 185 TPLHVACYNGQDVVVNELIDCGAIVNQKNE 214
Cdd:PHA03100  227 TPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02874 PHA02874
ankyrin repeat protein; Provisional
34-311 1.75e-27

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 116.60  E-value: 1.75e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  34 VQVLLKHSADVNARDKNWQTPLHIA---AANKAVK--------CAEALVPLLSNvnvsdragrtalhhaafsghgEMVKL 102
Cdd:PHA02874   51 VELFIKHGADINHINTKIPHPLLTAikiGAHDIIKllidngvdTSILPIPCIEK---------------------DMIKT 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 103 LLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAY 182
Cdd:PHA02874  110 ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 183 GNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHfaAASTHGALCLELLVgNGADVNMKSKDGKTPLHMtALHGR 262
Cdd:PHA02874  190 GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLH--NAIIHNRSAIELLI-NNASINDQDIDGSTPLHH-AINPP 265
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370483583 263 FSRS--QTIIQSGAVIDCEDKNGNTPLHIAARYGH------ELLINTLITSGADTAK 311
Cdd:PHA02874  266 CDIDiiDILLYHKADISIKDNKGENPIDTAFKYINkdpvikDIIANAVLIKEADKLK 322
PHA02874 PHA02874
ankyrin repeat protein; Provisional
93-463 1.02e-26

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 114.29  E-value: 1.02e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  93 FSGHGEMV-KLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLD 171
Cdd:PHA02874   10 YSGDIEAIeKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 172 LGVDmnepnaygNTPLHVACYNGQdvVVNELIDCGAIVNQKNEKGFTPLHFAAASthGAL-CLELLVGNGADVNMKSKDG 250
Cdd:PHA02874   90 NGVD--------TSILPIPCIEKD--MIKTILDCGIDVNIKDAELKTFLHYAIKK--GDLeSIKMLFEYGADVNIEDDNG 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 251 KTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALsgfsd 330
Cdd:PHA02874  158 CYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII----- 232
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 331 ccrkllssgfdidtpddfgrtclhaaaaggnleclnlllntgadfnkkdkFGRSPLhyaaancnyqclfALVGSGASVND 410
Cdd:PHA02874  233 --------------------------------------------------HNRSAI-------------ELLINNASIND 249
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370483583 411 LDERGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRL 463
Cdd:PHA02874  250 QDIDGSTPLHHAINPPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKD 302
PHA02874 PHA02874
ankyrin repeat protein; Provisional
77-323 4.11e-26

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 112.75  E-value: 4.11e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  77 VNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAE-------------- 142
Cdd:PHA02874   28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsilpipciekdmi 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 143 ---------VTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKN 213
Cdd:PHA02874  108 ktildcgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 214 EKGFTPLHFAAASTHGAlCLELLVGNGADVNMKSKDGKTPLHMTALHGRfSRSQTIIQSgAVIDCEDKNGNTPLHIAARY 293
Cdd:PHA02874  188 NNGESPLHNAAEYGDYA-CIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLHHAINP 264
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1370483583 294 GHEL-LINTLITSGADTAKRGIHGMFPLHLA 323
Cdd:PHA02874  265 PCDIdIIDILLYHKADISIKDNKGENPIDTA 295
PHA03100 PHA03100
ankyrin repeat protein; Provisional
130-344 7.90e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 108.60  E-value: 7.90e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 130 IEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLH---VACYNGQDVV--VNELID 204
Cdd:PHA03100   15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsNIKYNLTDVKeiVKLLLE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 205 CGAIVNQKNEKGFTPLHFAAASTHGALCL-ELLVGNGADVNMKSKDGKTPLHMtAL---HGRFSRSQTIIQSGA------ 274
Cdd:PHA03100   95 YGANVNAPDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHL-YLesnKIDLKILKLLIDKGVdinakn 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 275 ----------VIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDT 344
Cdd:PHA03100  174 rvnyllsygvPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
34-308 2.02e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 109.77  E-value: 2.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  34 VQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRA-----------------------------G 84
Cdd:PHA02876  194 VNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLSllkairnedletslllydagfsvnsiddcK 273
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  85 RTALHHAAFSGH-GEMVKLLLSRGANINAFDKKDRRAIHWAAYMGH-IEVVKLLVSHGAEVTCKDKKSYTPLHAAAS-SG 161
Cdd:PHA02876  274 NTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDR 353
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 162 MISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGA 241
Cdd:PHA02876  354 NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGA 433
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370483583 242 DVNMKSKDGKTPLHMTALHG-RFSRSQTIIQSGAVIDCEDKNGNTPLHIAarYGHELLINTLITSGAD 308
Cdd:PHA02876  434 NVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGAE 499
PHA02874 PHA02874
ankyrin repeat protein; Provisional
498-807 7.99e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 102.73  E-value: 7.99e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 498 LHLAAYHGHHQALEVLVQS---LLDLDVRNSSgrTPLDLAAFKGHVECVDVLINQGASIlvkDYILKRTP--IHAAATNG 572
Cdd:PHA02874    5 LRMCIYSGDIEAIEKIIKNkgnCINISVDETT--TPLIDAIRSGDAKIVELFIKHGADI---NHINTKIPhpLLTAIKIG 79
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 573 HSECLRLLIgnaepQNAVDIQdgngqtplMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQH 652
Cdd:PHA02874   80 AHDIIKLLI-----DNGVDTS--------ILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEY 146
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 653 GAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAASMDANpataDNHGYTALHWACYNGHETCVELLLEQ--EVFQKTEg 730
Cdd:PHA02874  147 GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK----DNNGESPLHNAAEYGDYACIKLLIDHgnHIMNKCK- 221
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370483583 731 NAFSPLHCAVINdNEGAAEMLIDTlgASIvNATDSKGRTPLH-AAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMA 807
Cdd:PHA02874  222 NGFTPLHNAIIH-NRSAIELLINN--ASI-NDQDIDGSTPLHhAINPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA02878 PHA02878
ankyrin repeat protein; Provisional
31-297 1.02e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 103.04  E-value: 1.02e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  31 LEAVQVLLKHSADVNARDKNWQTPLHIA--AANKavkcaEALVPLLSNVNVSD-----RAGRTALHHAAFsghgEMVK-L 102
Cdd:PHA02878   50 LDVVKSLLTRGHNVNQPDHRDLTPLHIIckEPNK-----LGMKEMIRSINKCSvfytlVAIKDAFNNRNV----EIFKiI 120
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 103 LLSRGANINAFDKKDRRAIHWAAYMgHIEVVKLLVSHGAEVTCKDK-KSYTPLHAAASSGMISVVKYLLDLGVDMNEPNA 181
Cdd:PHA02878  121 LTNRYKNIQTIDLVYIDKKSKDDII-EAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 182 YGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSK-DGKTPLHMtALH 260
Cdd:PHA02878  200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHS-SIK 278
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1370483583 261 GRfSRSQTIIQSGAVIDCEDKNGNTPLHIAA--RYGHEL 297
Cdd:PHA02878  279 SE-RKLKLLLEYGADINSLNSYKLTPLSSAVkqYLCINI 316
Ank_2 pfam12796
Ankyrin repeats (3 copies);
88-180 5.35e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 5.35e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  88 LHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHgAEVTCKDKKsYTPLHAAASSGMISVVK 167
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1370483583 168 YLLDLGVDMNEPN 180
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
55-147 7.38e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 7.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  55 LHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRgANINAFDkKDRRAIHWAAYMGHIEVVK 134
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1370483583 135 LLVSHGAEVTCKD 147
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
121-213 7.62e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 7.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 121 IHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDlGVDMNEPNaYGNTPLHVACYNGQDVVVN 200
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1370483583 201 ELIDCGAIVNQKN 213
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
597-926 2.41e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 92.40  E-value: 2.41e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 597 GQTPLMLSVLNGHTDC---VYSLLNKGANVDAKDKWGRTALH---RGAVTghEECVDALLQHGAKCLLRDSRGRTPIH-- 668
Cdd:PHA03095   47 GKTPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHlylYNATT--LDVIKLLIKAGADVNAKDKVGRTPLHvy 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 669 LSAACGHIGVLGALLQsaasMDANPATADNHGYTalhwacynghetcvellleqevfqktegnafsPLHCAVINdnegaa 748
Cdd:PHA03095  125 LSGFNINPKVIRLLLR----KGADVNALDLYGMT--------------------------------PLAVLLKS------ 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 749 emlidtlgasiVNATdskgrtplhaaaftdhVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNT--VEMLVSsASAE 826
Cdd:PHA03095  163 -----------RNAN----------------VELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRAriVRELIR-AGCD 214
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 827 LTLQDNSKNTALHLACSKGHETSALLI--LEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGY 904
Cdd:PHA03095  215 PAATDMLGNTPLHSMATGSSCKRSLVLplLIAGIS---INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGN 291
                         330       340
                  ....*....|....*....|..
gi 1370483583 905 TPALACAPNKDVaDCLALILAT 926
Cdd:PHA03095  292 TPLSLMVRNNNG-RAVRAALAK 312
Ank_2 pfam12796
Ankyrin repeats (3 copies);
30-114 1.65e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.65e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  30 YLEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLsNVNVSDRaGRTALHHAAFSGHGEMVKLLLSRGAN 109
Cdd:pfam12796   9 NLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVKLLLEKGAD 86

                  ....*
gi 1370483583 110 INAFD 114
Cdd:pfam12796  87 INVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
565-660 1.75e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 565 IHAAATNGHSECLRLLIgnaEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKgANVDAKDKwGRTALHRGAVTGHEE 644
Cdd:pfam12796   1 LHLAAKNGNLELVKLLL---ENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE 75
                          90
                  ....*....|....*.
gi 1370483583 645 CVDALLQHGAKCLLRD 660
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
531-627 2.30e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 2.30e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 531 LDLAAFKGHVECVDVLINQGASILVKDyILKRTPIHAAATNGHSECLRLLIGNAEPQNavdiqDGNGQTPLMLSVLNGHT 610
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAARSGHL 74
                          90
                  ....*....|....*..
gi 1370483583 611 DCVYSLLNKGANVDAKD 627
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
519-799 2.95e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 88.93  E-value: 2.95e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 519 DLDVRNSSGRTPLDLAAFKGHVECVDV---LINQGASILVKDyILKRTPIHAAATNGHSE-CLRLLIGNaepqNA-VDIQ 593
Cdd:PHA03095   39 DVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPE-RCGFTPLHLYLYNATTLdVIKLLIKA----GAdVNAK 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 594 DGNGQTPL--MLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALH----RGAVTghEECVDALLQHGAKCLLRDSRGRTPI 667
Cdd:PHA03095  114 DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvllkSRNAN--VELLRLLIDAGADVYAVDDRFRSLL 191
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 668 HLSAACGHI--GVLGALLQSAAsmdaNPATADNHGYTALHWACYngHETCVELLLEQEVFQKTEGNA-----FSPLHCAV 740
Cdd:PHA03095  192 HHHLQSFKPraRIVRELIRAGC----DPAATDMLGNTPLHSMAT--GSSCKRSLVLPLLIAGISINArnrygQTPLHYAA 265
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483583 741 INDNEGAAEMLIdTLGASIvNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDST 799
Cdd:PHA03095  266 VFNNPRACRRLI-ALGADI-NAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAAT 322
Ank_2 pfam12796
Ankyrin repeats (3 copies);
154-246 5.90e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 5.90e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 154 LHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIvnQKNEKGFTPLHFAAASTHGAlCL 233
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLE-IV 77
                          90
                  ....*....|...
gi 1370483583 234 ELLVGNGADVNMK 246
Cdd:pfam12796  78 KLLLEKGADINVK 90
PHA02876 PHA02876
ankyrin repeat protein; Provisional
372-721 7.97e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 88.58  E-value: 7.97e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 372 GADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLLRNDANPGIRDKQGYN 451
Cdd:PHA02876  168 GADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSK-NIDTIKAIIDNRSNINKNDLSLLK 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 452 AVHYSAAyghrlclqliasETPLdvLMETSGTDMLSDSDNRATisPLHLAAyhgHHQALEVLVQSLL----DLDVRNSSG 527
Cdd:PHA02876  247 AIRNEDL------------ETSL--LLYDAGFSVNSIDDCKNT--PLHHAS---QAPSLSRLVPKLLergaDVNAKNIKG 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 528 RTPLDLAAFKGH-VECVDVLINQGASILVKDYiLKRTPIHAAATnghseclrllignaepqnavdiqdgngqtplmlsvL 606
Cdd:PHA02876  308 ETPLYLMAKNGYdTENIRTLIMLGADVNAADR-LYITPLHQAST-----------------------------------L 351
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 607 NGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLsAACGHIGVLGalLQSA 686
Cdd:PHA02876  352 DRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHF-ALCGTNPYMS--VKTL 428
                         330       340       350
                  ....*....|....*....|....*....|....*.
gi 1370483583 687 ASMDANPATADNHGYTALHWACYNGHE-TCVELLLE 721
Cdd:PHA02876  429 IDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLD 464
PHA02878 PHA02878
ankyrin repeat protein; Provisional
32-261 1.08e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 87.24  E-value: 1.08e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  32 EAVQVLLKHSADVNARDKNW-QTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANI 110
Cdd:PHA02878  148 EITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 111 NAFDKKDRRAIHWA-AYMGHIEVVKLLVSHGAEVTCKdkksytplhaaassgmisvvKYLLDLgvdmnepnaygnTPLHV 189
Cdd:PHA02878  228 DARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAK--------------------SYILGL------------TALHS 275
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370483583 190 ACYNGQdvVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKSKDGKTPL----HMTALHG 261
Cdd:PHA02878  276 SIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISNICLLKRIKPDIKNSEgfidNMDCITS 349
PHA03095 PHA03095
ankyrin-like protein; Provisional
333-701 2.34e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 86.23  E-value: 2.34e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 333 RKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECL---NLLLNTGADFNKKDKFGRSPLH-YAAANCNYQCLFALVGSGASV 408
Cdd:PHA03095   31 RRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADV 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 409 NDLDERGCTPLH-YAATSDTDGKCLEYLLRNDANPGIRDKqgynavhysaaYGHrlclqliaseTPLDVLMetsgtdmls 487
Cdd:PHA03095  111 NAKDKVGRTPLHvYLSGFNINPKVIRLLLRKGADVNALDL-----------YGM----------TPLAVLL--------- 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 488 dSDNRATISPLHLaayhghhqalevLVQSLLDLDVRNSSGRTPLD--LAAFKGHVECVDVLINQGASILVKDyILKRTPI 565
Cdd:PHA03095  161 -KSRNANVELLRL------------LIDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATD-MLGNTPL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 566 HAAATngHSECLRLLIGNaepqnavdiqdgngqtplmlsvlnghtdcvysLLNKGANVDAKDKWGRTALHRGAVTGHEEC 645
Cdd:PHA03095  227 HSMAT--GSSCKRSLVLP--------------------------------LLIAGISINARNRYGQTPLHYAAVFNNPRA 272
                         330       340       350       360       370
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483583 646 VDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQ---SAASMDANPATADNHGY 701
Cdd:PHA03095  273 CRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAknpSAETVAATLNTASVAGG 331
PHA02874 PHA02874
ankyrin repeat protein; Provisional
32-223 6.45e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 84.63  E-value: 6.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  32 EAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANIN 111
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 112 AFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMiSVVKYLLDlGVDMNEPNAYGNTPLHVAC 191
Cdd:PHA02874  185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLIN-NASINDQDIDGSTPLHHAI 262
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1370483583 192 YNGQDV-VVNELIDCGAIVNQKNEKGFTPLHFA 223
Cdd:PHA02874  263 NPPCDIdIIDILLYHKADISIKDNKGENPIDTA 295
PHA02875 PHA02875
ankyrin repeat protein; Provisional
32-210 1.22e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 83.50  E-value: 1.22e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  32 EAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALvpLLSNVNVSD---RAGRTALHHAAFSGHGEMVKLLLSRGA 108
Cdd:PHA02875   49 EAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEEL--LDLGKFADDvfyKDGMTPLHLATILKKLDIMKLLIARGA 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 109 NINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDmnePNAYGNTP-L 187
Cdd:PHA02875  127 DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN---IDYFGKNGcV 203
                         170       180
                  ....*....|....*....|....*.
gi 1370483583 188 HVACY---NGQDVVVNELIDCGAIVN 210
Cdd:PHA02875  204 AALCYaieNNKIDIVRLFIKRGADCN 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
771-864 1.30e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 1.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 771 LHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSASAELtlqDNSKNTALHLACSKGHETSA 850
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL---KDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 1370483583 851 LLILEKITDRNLIN 864
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
601-692 5.62e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.00  E-value: 5.62e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 601 LMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAkcLLRDSRGRTPIHLSAACGHIGVLG 680
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|..
gi 1370483583 681 ALLQSAASMDAN 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 1370483583 475 DVLMETSGTDmlsdsDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGASIL 554
Cdd:PLN03192  511 DLLGDNGGEH-----DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH 585
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 555 VKDyILKRTPIHAAATNGHSECLRLLIGNA---EPQNAVDIqdgngqtpLMLSVLNGHTDCVYSLLNKGANVDAKDKWGR 631
Cdd:PLN03192  586 IRD-ANGNTALWNAISAKHHKIFRILYHFAsisDPHAAGDL--------LCTAAKRNDLTAMKELLKQGLNVDSEDHQGA 656
                         170       180
                  ....*....|....*....|...
gi 1370483583 632 TALHRGAVTGHEECVDALLQHGA 654
Cdd:PLN03192  657 TALQVAMAEDHVDMVRLLIMNGA 679
PHA02874 PHA02874
ankyrin repeat protein; Provisional
6-211 1.28e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 80.39  E-value: 1.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583   6 TMKSEPHCTPQLTLEMQKSLNFLFY------LEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNV 79
Cdd:PHA02874  106 MIKTILDCGIDVNIKDAELKTFLHYaikkgdLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  80 SDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHwAAYMGHIEVVKLLVSHgAEVTCKDKKSYTPLHAAAS 159
Cdd:PHA02874  186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLH-NAIIHNRSAIELLINN-ASINDQDIDGSTPLHHAIN 263
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370483583 160 SGM-ISVVKYLLDLGVDMNEPNAYGNTPLHVAC-YNGQDVVVNELIDCGAIVNQ 211
Cdd:PHA02874  264 PPCdIDIIDILLYHKADISIKDNKGENPIDTAFkYINKDPVIKDIIANAVLIKE 317
Ank_2 pfam12796
Ankyrin repeats (3 copies);
704-797 2.13e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 2.13e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 704 LHWACYNGHETCVELLLEQEV-FQKTEGNAFSPLHCAVINDNEGAAEMLIDTLGASIVNatdsKGRTPLHAAAFTDHVEC 782
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD----NGRTALHYAARSGHLEI 76
                          90
                  ....*....|....*
gi 1370483583 783 LQLLLSHNAQVNSVD 797
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
153-467 3.81e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 79.15  E-value: 3.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 153 PLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIdcgAIVNQ--------------------- 211
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKcsvfytlvaikdafnnrnvei 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 212 ---------KNEKGFTPLHFAAASTHGAL---CLELLVGNGADVNMKSKD-GKTPLHMTALHGRFSRSQTIIQSGAVIDC 278
Cdd:PHA02878  117 fkiiltnryKNIQTIDLVYIDKKSKDDIIeaeITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNI 196
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 279 EDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFS-DCCRKLLSSGFDIDTpddfgrtclhaaa 357
Cdd:PHA02878  197 PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLLLEHGVDVNA------------- 263
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 358 aggnleclnlllntgadfnKKDKFGRSPLHYAAAncNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDGKCLEYL-- 435
Cdd:PHA02878  264 -------------------KSYILGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILis 322
                         330       340       350
                  ....*....|....*....|....*....|....*
gi 1370483583 436 ---LRNDANPGIRDKQGYnAVHYSAAYGHRLCLQL 467
Cdd:PHA02878  323 nicLLKRIKPDIKNSEGF-IDNMDCITSNKRLNQI 356
PHA02876 PHA02876
ankyrin repeat protein; Provisional
616-908 5.48e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 79.34  E-value: 5.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 616 LLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAASMDANPAT 695
Cdd:PHA02876  164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLS 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 696 -------------------------ADNHGYTALHWACYNGH-ETCVELLLEQEVFQKTEG-NAFSPLHCAVINDNEGAA 748
Cdd:PHA02876  244 llkairnedletslllydagfsvnsIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNiKGETPLYLMAKNGYDTEN 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 749 EMLIDTLGASiVNATDSKGRTPLHAAAFTD-HVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSAsAEL 827
Cdd:PHA02876  324 IRTLIMLGAD-VNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG-ADI 401
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 828 TLQDNSKNTALHLACskgHETSALLILEKITDRNL-INATNAALQTPLHVAARNGLTM-VVQELLGKGASVLAVDENGYT 905
Cdd:PHA02876  402 EALSQKIGTALHFAL---CGTNPYMSVKTLIDRGAnVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAINIQNQY 478

                  ...
gi 1370483583 906 PAL 908
Cdd:PHA02876  479 PLL 481
PHA03100 PHA03100
ankyrin repeat protein; Provisional
716-902 5.86e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.17  E-value: 5.86e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 716 VELLLEQ--EVFQKTEGNaFSPLH-----CAVINDNEGAAEMLIDtLGASIvNATDSKGRTPLHAAAFT--DHVECLQLL 786
Cdd:PHA03100   51 VKILLDNgaDINSSTKNN-STPLHylsniKYNLTDVKEIVKLLLE-YGANV-NAPDNNGITPLLYAISKksNSYSIVEYL 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 787 LSHNAQVNSVDSTGKTPLMMAAENG------------------QTNTVEMLVSSASaELTLQDNSKNTALHLACSKGHET 848
Cdd:PHA03100  128 LDNGANVNIKNSDGENLLHLYLESNkidlkilkllidkgvdinAKNRVNYLLSYGV-PINIKDVYGFTPLHYAVYNNNPE 206
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370483583 849 SALLILEKITDRNLINATNaalQTPLHVAARNGLTMVVQELLGKGASVLAVDEN 902
Cdd:PHA03100  207 FVKYLLDLGANPNLVNKYG---DTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02874 PHA02874
ankyrin repeat protein; Provisional
254-591 9.29e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 77.70  E-value: 9.29e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 254 LHMTALHGRFSRSQTIIQS-GAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCC 332
Cdd:PHA02874    5 LRMCIYSGDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDII 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 333 RKLLSSGFDI------DTPDDFGRTCLHaaaaggnleclnlllnTGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGA 406
Cdd:PHA02874   85 KLLIDNGVDTsilpipCIEKDMIKTILD----------------CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGA 148
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 407 SVNDLDERGCTPLHYAATSDTdGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCLQLIAsetpldvlmeTSGTDML 486
Cdd:PHA02874  149 DVNIEDDNGCYPIHIAIKHNF-FDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI----------DHGNHIM 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 487 SDSDNRATisPLHLAAYHgHHQALEVLVQSlLDLDVRNSSGRTPLDLA-AFKGHVECVDVLINQGASILVKDYiLKRTPI 565
Cdd:PHA02874  218 NKCKNGFT--PLHNAIIH-NRSAIELLINN-ASINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKDN-KGENPI 292
                         330       340
                  ....*....|....*....|....*..
gi 1370483583 566 HAAATN-GHSECLRLLIGNAEPQNAVD 591
Cdd:PHA02874  293 DTAFKYiNKDPVIKDIIANAVLIKEAD 319
PHA02876 PHA02876
ankyrin repeat protein; Provisional
136-662 1.05e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 78.57  E-value: 1.05e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 136 LVSHGAEvTCKDKK-SYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYG-NTPLHVACY--NGQDVVVNELIDCGAIVNQ 211
Cdd:PHA02876   27 LHKHGAN-QCENESiPFTAIHQALQLRQIDIVEEIIQQNPELIYITDHKcHSTLHTICIipNVMDIVISLTLDCDIILDI 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 212 KNEKGFTPLHfaaasTHGALCLELLVG--NGADVNMkSKDGKTPLHMTALHGRFSRSQTIIQSgavidcedkngntplhi 289
Cdd:PHA02876  106 KYASIILNKH-----KLDEACIHILKEaiSGNDIHY-DKINESIEYMKLIKERIQQDELLIAE----------------- 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 290 aaryghellinTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLL 369
Cdd:PHA02876  163 -----------MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII 231
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 370 NTGADFNKKDkfgrSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDKQG 449
Cdd:PHA02876  232 DNRSNINKND----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKG 307
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 450 YNAVHYSAAYGHRlclqliaSETPLDVLMEtsGTDMlsDSDNRATISPLHLAAYHGHHQALEVLVQSL-LDLDVRNSSGR 528
Cdd:PHA02876  308 ETPLYLMAKNGYD-------TENIRTLIML--GADV--NAADRLYITPLHQASTLDRNKDIVITLLELgANVNARDYCDK 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 529 TPLDLAAFKGHVECVDVLINQGASILVKDYILKrTPIHAA--ATNGHSECLRLLIGNAEpqnaVDIQDGNGQTPLMLSVL 606
Cdd:PHA02876  377 TPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFAlcGTNPYMSVKTLIDRGAN----VNSKNKDLSTPLHYACK 451
                         490       500       510       520       530
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370483583 607 NG-HTDCVYSLLNKGANVDAKDKWGRTALHrgAVTGHEECVDALLQHGAKclLRDSR 662
Cdd:PHA02876  452 KNcKLDVIEMLLDNGADVNAINIQNQYPLL--IALEYHGIVNILLHYGAE--LRDSR 504
PHA03100 PHA03100
ankyrin repeat protein; Provisional
371-628 1.31e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.40  E-value: 1.31e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 371 TGADFNKKDKFGRSPLHYAA-----ANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSD-TDGKCLEYLLRNDANPGI 444
Cdd:PHA03100   57 NGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKsNSYSIVEYLLDNGANVNI 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 445 RDKQGYNAVHYSAAYGHRlclqliasETPLDVLMETSGTDMlsDSDNRatisplhlaayhghhqaLEVLVQSLLDLDVRN 524
Cdd:PHA03100  137 KNSDGENLLHLYLESNKI--------DLKILKLLIDKGVDI--NAKNR-----------------VNYLLSYGVPINIKD 189
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 525 SSGRTPLDLAAFKGHVECVDVLINQGASIlvkdyilkrtpihaaatnghseclrllignaepqNAVDIqdgNGQTPLMLS 604
Cdd:PHA03100  190 VYGFTPLHYAVYNNNPEFVKYLLDLGANP----------------------------------NLVNK---YGDTPLHIA 232
                         250       260
                  ....*....|....*....|....
gi 1370483583 605 VLNGHTDCVYSLLNKGANVDAKDK 628
Cdd:PHA03100  233 ILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02798 PHA02798
ankyrin-like protein; Provisional
31-308 1.27e-13

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 74.49  E-value: 1.27e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  31 LEAVQVLLKHSADVNARDKNWQTPLhiaaankavkCAealvpLLSNVnvsdRAGRTALhhaafsghgEMVKLLLSRGANI 110
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPL----------CT-----ILSNI----KDYKHML---------DIVKILIENGADI 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 111 NAFDKKDRRAIHWA---AYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGM---ISVVKYLLDLGVDMNE-PNAYG 183
Cdd:PHA02798  103 NKKNSDGETPLYCLlsnGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINThNNKEK 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 184 NTPLHvaCYNGQDV------VVNELIDCGAIVNQKNEkgftplhfAAASTHGALCLELLVGNGA-------------DVN 244
Cdd:PHA02798  183 YDTLH--CYFKYNIdridadILKLFVDNGFIINKENK--------SHKKKFMEYLNSLLYDNKRfkknildfifsyiDIN 252
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370483583 245 MKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGAD 308
Cdd:PHA02798  253 QVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
PHA03100 PHA03100
ankyrin repeat protein; Provisional
556-823 3.19e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.78  E-value: 3.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 556 KDYILKRTPIHAAATNGHseclrllignaepqnAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALH 635
Cdd:PHA03100    9 KSRIIKVKNIKYIIMEDD---------------LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLH 73
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 636 RGAVTGHE-----ECVDALLQHGAKCLLRDSRGRTPIHLSAAC--GHIGVLGALLQSAAsmDANPATADnhGYTALHWA- 707
Cdd:PHA03100   74 YLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGA--NVNIKNSD--GENLLHLYl 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 708 --CYNGHETcVELLLEqevfqktegnafsplHCAVINdNEGAAEMLIdTLGASIvNATDSKGRTPLHAAAFTDHVECLQL 785
Cdd:PHA03100  150 esNKIDLKI-LKLLID---------------KGVDIN-AKNRVNYLL-SYGVPI-NIKDVYGFTPLHYAVYNNNPEFVKY 210
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1370483583 786 LLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSA 823
Cdd:PHA03100  211 LLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248
Ank_2 pfam12796
Ankyrin repeats (3 copies);
804-900 5.89e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 5.89e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 804 LMMAAENGQTNTVEMLVSSaSAELTLQDNSKNTALHLACSKGHETSALLILEKItDRNLINATNaalqTPLHVAARNGLT 883
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDNGR----TALHYAARSGHL 74
                          90
                  ....*....|....*..
gi 1370483583 884 MVVQELLGKGASVLAVD 900
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
157-341 6.72e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 71.95  E-value: 6.72e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 157 AASSGMISVVKYLLDLGVDMN--------------------------EPNAYGN-------TPLHVACYNGQDVVVNELI 203
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNfeiydgispiklamkfrdseaikllmKHGAIPDvkypdieSELHDAVEEGDVKAVEELL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 204 DCGAIVNQK-NEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKN 282
Cdd:PHA02875   89 DLGKFADDVfYKDGMTPLHLATILKKLDI-MKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCC 167
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 283 GNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFS-DCCRKLLSSGFD 341
Cdd:PHA02875  168 GCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGAD 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
254-346 7.74e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.14  E-value: 7.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 254 LHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGAdtAKRGIHGMFPLHLAALSGFSDCCR 333
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1370483583 334 KLLSSGFDIDTPD 346
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
647-901 8.19e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 72.40  E-value: 8.19e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 647 DALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAAsmDANPATADnhGYTALHWACYNGHETCVELLLEQEvfQ 726
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGA--DVNIIALD--DLSVLECAVDSKNIDTIKAIIDNR--S 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 727 KTEGNAFSPLHcAVINDNEGAAEMLIDTlGASiVNATDSKGRTPLHAAAFTDHVECL-QLLLSHNAQVNSVDSTGKTPLM 805
Cdd:PHA02876  236 NINKNDLSLLK-AIRNEDLETSLLLYDA-GFS-VNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLY 312
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 806 MAAENG-QTNTVEMLVSSAsAELTLQDNSKNTALHLACSKGHETSALLILEKITDRnlINATNAALQTPLHVAARNGLTM 884
Cdd:PHA02876  313 LMAKNGyDTENIRTLIMLG-ADVNAADRLYITPLHQASTLDRNKDIVITLLELGAN--VNARDYCDKTPIHYAAVRNNVV 389
                         250
                  ....*....|....*..
gi 1370483583 885 VVQELLGKGASVLAVDE 901
Cdd:PHA02876  390 IINTLLDYGADIEALSQ 406
PHA02874 PHA02874
ankyrin repeat protein; Provisional
481-667 8.38e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 71.53  E-value: 8.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 481 SGTDMlsDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGASILVKDYIL 560
Cdd:PHA02874  113 CGIDV--NIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 561 KrTPIHAAATNGHSECLRLLIGNAepqNAVDIQDGNGQTPLMLSVLngHTDCVYSLLNKGANVDAKDKWGRTALHRG-AV 639
Cdd:PHA02874  191 E-SPLHNAAEYGDYACIKLLIDHG---NHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAiNP 264
                         170       180
                  ....*....|....*....|....*...
gi 1370483583 640 TGHEECVDALLQHGAKCLLRDSRGRTPI 667
Cdd:PHA02874  265 PCDIDIIDILLYHKADISIKDNKGENPI 292
PHA02875 PHA02875
ankyrin repeat protein; Provisional
53-245 1.26e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.79  E-value: 1.26e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  53 TPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANIN-AFDKKDRRAIHWAAYMGHIE 131
Cdd:PHA02875   37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLD 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 132 VVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQ 211
Cdd:PHA02875  117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDY 196
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1370483583 212 KNEKGFTPLHFAAASTHGALCLELLVGNGADVNM 245
Cdd:PHA02875  197 FGKNGCVAALCYAIENNKIDIVRLFIKRGADCNI 230
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
31-203 1.70e-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: 71.20  E-value: 1.70e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  31 LEAVQVLLK-HSADVNARDKNWQTPLHIAAANKAVKCAEAL---VPLLSNVNV-SD-RAGRTALHHAAFSGHGEMVKLLL 104
Cdd:cd22192    30 VQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLmeaAPELVNEPMtSDlYQGETALHIAVVNQNLNLVRELI 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 105 SRGANIN-------AFDKKDRRAIHW-------AAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLL 170
Cdd:cd22192   110 ARGADVVspratgtFFRPGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMY 189
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1370483583 171 DLGVDMNE----------PNAYGNTPLHVACYNGQDVVVNELI 203
Cdd:cd22192   190 DLILSYDKeddlqpldlvPNNQGLTPFKLAAKEGNIVMFQHLV 232
Ank_2 pfam12796
Ankyrin repeats (3 copies);
320-412 2.47e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.60  E-value: 2.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 320 LHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTgADFNKKDKfGRSPLHYAAANCNYQCLF 399
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1370483583 400 ALVGSGASVNDLD 412
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02798 PHA02798
ankyrin-like protein; Provisional
130-356 2.60e-12

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 70.25  E-value: 2.60e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 130 IEVVKLLVSHGAEVTCKDKKSYTPLHAAASS-----GMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGqdvVVNEL-- 202
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPLYCLLSNG---YINNLei 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 203 ----IDCGAIVNQKNEKGFTPLHFAAASTHGAL--CLELLVGNGADVNMKSKDGKtplhMTALHGRFSRS---------Q 267
Cdd:PHA02798  128 llfmIENGADTTLLDKDGFTMLQVYLQSNHHIDieIIKLLLEKGVDINTHNNKEK----YDTLHCYFKYNidridadilK 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 268 TIIQSGAVIDCEDKNGNTPLhiaARYGHELLINT---------LITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSS 338
Cdd:PHA02798  204 LFVDNGFIINKENKSHKKKF---MEYLNSLLYDNkrfkknildFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQL 280
                         250
                  ....*....|....*...
gi 1370483583 339 GFDIDTPDDFGRTCLHAA 356
Cdd:PHA02798  281 GGDINIITELGNTCLFTA 298
Ank_4 pfam13637
Ankyrin repeats (many copies);
84-137 9.16e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.75  E-value: 9.16e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370483583  84 GRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLV 137
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
220-308 1.22e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.67  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 220 LHFAAASTHgALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSgAVIDCEDkNGNTPLHIAARYGHELLI 299
Cdd:pfam12796   1 LHLAAKNGN-LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                  ....*....
gi 1370483583 300 NTLITSGAD 308
Cdd:pfam12796  78 KLLLEKGAD 86
PHA02874 PHA02874
ankyrin repeat protein; Provisional
541-805 1.37e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 67.68  E-value: 1.37e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 541 ECVDVLINQGASILVKDYILKrTPIHAAATNGHSECLRLLIgnaEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKG 620
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELK-TFLHYAIKKGDLESIKMLF---EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG 180
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 621 ANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAkcllrdsrgrtpiHLSAACghigvlgallqsaasmdanpatadNHG 700
Cdd:PHA02874  181 AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN-------------HIMNKC------------------------KNG 223
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 701 YTALHWAC-YNghETCVELLLEQEVFQKTEGNAFSPLHCAVindNEGAAEMLIDTL--GASIVNATDSKGRTPLHAA-AF 776
Cdd:PHA02874  224 FTPLHNAIiHN--RSAIELLINNASINDQDIDGSTPLHHAI---NPPCDIDIIDILlyHKADISIKDNKGENPIDTAfKY 298
                         250       260
                  ....*....|....*....|....*....
gi 1370483583 777 TDHVECLQLLLSHNAQVNSVDSTGKTPLM 805
Cdd:PHA02874  299 INKDPVIKDIIANAVLIKEADKLKDSDFL 327
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
37-182 2.04e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.97  E-value: 2.04e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  37 LLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKK 116
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG 623
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370483583 117 DrrAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAY 182
Cdd:PLN03192  624 D--LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
Ank_2 pfam12796
Ankyrin repeats (3 copies);
187-280 4.01e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.13  E-value: 4.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 187 LHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLvgNGADVNMKSkDGKTPLHMTALHGRFSRS 266
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL--EHADVNLKD-NGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 1370483583 267 QTIIQSGAVIDCED 280
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
573-782 4.39e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.20  E-value: 4.39e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 573 HSECLRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQH 652
Cdd:PLN03192  501 HKELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKH 580
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 653 GAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAASMDANPA---------------------------TADNHGYTALH 705
Cdd:PLN03192  581 ACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAgdllctaakrndltamkellkqglnvdSEDHQGATALQ 660
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 706 WACYNGHETCVELLLEQ--EVFQKTEGNAFSPLHC-AVINDNE-GAAEMLIDTLGASIVNATDSKGRTPLHAAAFTDHVE 781
Cdd:PLN03192  661 VAMAEDHVDMVRLLIMNgaDVDKANTDDDFSPTELrELLQKRElGHSITIVDSVPADEPDLGRDGGSRPGRLQGTSSDNQ 740

                  .
gi 1370483583 782 C 782
Cdd:PLN03192  741 C 741
Ank_4 pfam13637
Ankyrin repeats (many copies);
118-170 4.59e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.83  E-value: 4.59e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370483583 118 RRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLL 170
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
496-547 1.61e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.28  E-value: 1.61e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370483583 496 SPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLI 547
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
30-178 1.80e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.08  E-value: 1.80e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  30 YLEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEM-VKLLLSRGA 108
Cdd:PHA02876  354 NKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGA 433
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370483583 109 NINAFDKKDRRAIHWAAYMG-HIEVVKLLVSHGAEVTCKDKKSYTPLHAAAssGMISVVKYLLDLGVDMNE 178
Cdd:PHA02876  434 NVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAELRD 502
PHA02798 PHA02798
ankyrin-like protein; Provisional
8-254 2.77e-10

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 64.09  E-value: 2.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583   8 KSEPHCTPQLTLEMQKSLnflfyLEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSN---VNVSDRAG 84
Cdd:PHA02798   71 YSTPLCTILSNIKDYKHM-----LDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFMIENgadTTLLDKDG 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  85 RTALHHAAFSGHG---EMVKLLLSRGANINAFDkkdrraiHWAAYmghievvkllvshgAEVTCKDKKSYTPLHAaassg 161
Cdd:PHA02798  146 FTMLQVYLQSNHHidiEIIKLLLEKGVDINTHN-------NKEKY--------------DTLHCYFKYNIDRIDA----- 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 162 miSVVKYLLDLGVDMNEPNAYGNTP----LHVACYNGQDVVVN--ELIDCGAIVNQKNEKGFTPLHFAAASTHGALClEL 235
Cdd:PHA02798  200 --DILKLFVDNGFIINKENKSHKKKfmeyLNSLLYDNKRFKKNilDFIFSYIDINQVDELGFNPLYYSVSHNNRKIF-EY 276
                         250
                  ....*....|....*....
gi 1370483583 236 LVGNGADVNMKSKDGKTPL 254
Cdd:PHA02798  277 LLQLGGDINIITELGNTCL 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
386-470 4.73e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.05  E-value: 4.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 386 LHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDgKCLEYLLRNdANPGIRDkQGYNAVHYSAAYGHRLCL 465
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHL-EIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                  ....*
gi 1370483583 466 QLIAS 470
Cdd:pfam12796  78 KLLLE 82
PHA02874 PHA02874
ankyrin repeat protein; Provisional
760-920 4.73e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.06  E-value: 4.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 760 VNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSAsAELTLQDNSKNTALH 839
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLH 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 840 LACSKGHETSALLILEKITdrNLINATNAALqTPLHVAARNGLTMVvqELLGKGASVLAVDENGYTP---ALACAPNKDV 916
Cdd:PHA02874  196 NAAEYGDYACIKLLIDHGN--HIMNKCKNGF-TPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPlhhAINPPCDIDI 270

                  ....
gi 1370483583 917 ADCL 920
Cdd:PHA02874  271 IDIL 274
Ank_4 pfam13637
Ankyrin repeats (many copies);
151-195 4.85e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 4.85e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1370483583 151 YTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQ 195
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
PHA03100 PHA03100
ankyrin repeat protein; Provisional
510-691 5.89e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 62.76  E-value: 5.89e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 510 LEVLVQSLLDLDVRNSSGRTPLDLAAFK--GHVECVDVLINQGASILVKDYILKrTPIHAAATNGH--SECLRLLIgnae 585
Cdd:PHA03100   89 VKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGE-NLLHLYLESNKidLKILKLLI---- 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 586 pQNAVDIqdgngqtplmlsvlNGhTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRT 665
Cdd:PHA03100  164 -DKGVDI--------------NA-KNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
                         170       180
                  ....*....|....*....|....*.
gi 1370483583 666 PIHLSAACGHIGVLGALLQSAASMDA 691
Cdd:PHA03100  228 PLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02878 PHA02878
ankyrin repeat protein; Provisional
634-906 5.91e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 5.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 634 LHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLsaACGHIGVLGA--LLQSAasmdanpaTADNHGYT--ALHWACY 709
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHI--ICKEPNKLGMkeMIRSI--------NKCSVFYTlvAIKDAFN 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 710 NGHETCVELLLeqevFQKTEGNAFSPLHCAVINDNEGAAEMLIDTL----GASIVNATDSKGRTPLHAAAFTDHVECLQL 785
Cdd:PHA02878  111 NRNVEIFKIIL----TNRYKNIQTIDLVYIDKKSKDDIIEAEITKLllsyGADINMKDRHKGNTALHYATENKDQRLTEL 186
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 786 LLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSAsAELTLQDNSKNTALHLACSKGHETSAL-LILEKITDrnlIN 864
Cdd:PHA02878  187 LLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHISVGYCKDYDILkLLLEHGVD---VN 262
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1370483583 865 ATNAALQ-TPLHVAARNglTMVVQELLGKGASVLAVDENGYTP 906
Cdd:PHA02878  263 AKSYILGlTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTP 303
PHA02876 PHA02876
ankyrin repeat protein; Provisional
748-913 8.10e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.77  E-value: 8.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 748 AEMLIDtlGASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSAS--- 824
Cdd:PHA02876  161 AEMLLE--GGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSnin 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 825 -AELTLQDNSKNTALhlacskghETSALLILEKITdrnlINATNAALQTPLHVAARN-GLTMVVQELLGKGASVLAVDEN 902
Cdd:PHA02876  239 kNDLSLLKAIRNEDL--------ETSLLLYDAGFS----VNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIK 306
                         170
                  ....*....|.
gi 1370483583 903 GYTPALACAPN 913
Cdd:PHA02876  307 GETPLYLMAKN 317
PHA02875 PHA02875
ankyrin repeat protein; Provisional
230-444 8.47e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.93  E-value: 8.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 230 ALCLELLVGN----------GADVNMKSKDGKTPLHMTAlhgRFSRSQTI---IQSGAVIDCEDKNGNTPLHIAARYGHE 296
Cdd:PHA02875    5 ALCDAILFGEldiarrlldiGINPNFEIYDGISPIKLAM---KFRDSEAIkllMKHGAIPDVKYPDIESELHDAVEEGDV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 297 LLINTLITSGA---DTAKRgiHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGA 373
Cdd:PHA02875   82 KAVEELLDLGKfadDVFYK--DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1370483583 374 DFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDGKCLEYLLRNDANPGI 444
Cdd:PHA02875  160 CLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA02878 PHA02878
ankyrin repeat protein; Provisional
490-721 9.27e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.20  E-value: 9.27e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 490 DNRATiSPLHLAAYHGHHQALEVLVQSLLDLDVRNSsgRTPLDLAAFKGHVECVD-VLINQGASILVKDYILKRTPIHAA 568
Cdd:PHA02878   67 DHRDL-TPLHIICKEPNKLGMKEMIRSINKCSVFYT--LVAIKDAFNNRNVEIFKiILTNRYKNIQTIDLVYIDKKSKDD 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 569 ATNghSECLRLLIGNAEPQNAVDIQDGNgqTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDA 648
Cdd:PHA02878  144 IIE--AEITKLLLSYGADINMKDRHKGN--TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHI 219
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370483583 649 LLQHGAKCLLRDSRGRTPIHLSAA-CGHIGVLGALLQSAASMDANPATAdnhGYTALHWACYNghETCVELLLE 721
Cdd:PHA02878  220 LLENGASTDARDKCGNTPLHISVGyCKDYDILKLLLEHGVDVNAKSYIL---GLTALHSSIKS--ERKLKLLLE 288
PHA02875 PHA02875
ankyrin repeat protein; Provisional
31-142 1.26e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.55  E-value: 1.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  31 LEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANI 110
Cdd:PHA02875  115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1370483583 111 NAFDKK-DRRAIHWAAYMGHIEVVKLLVSHGAE 142
Cdd:PHA02875  195 DYFGKNgCVAALCYAIENNKIDIVRLFIKRGAD 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
419-524 1.36e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.89  E-value: 1.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 419 LHYAATSDtDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCLQLIASETPLDvlMETSGTdmlsdsdnratiSPL 498
Cdd:pfam12796   1 LHLAAKNG-NLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN--LKDNGR------------TAL 65
                          90       100
                  ....*....|....*....|....*.
gi 1370483583 499 HLAAYHGHHQALEVLVQSLLDLDVRN 524
Cdd:pfam12796  66 HYAARSGHLEIVKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
529-669 1.52e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 61.95  E-value: 1.52e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 529 TPLDLAAFKGHVECVDVLINQGASILVKDYILKRTPIHAAATNGHSECLRLLIGNA-----EPQNAVDIQdgnGQTPLML 603
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApelvnEPMTSDLYQ---GETALHI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 604 SVLNGHTDCVYSLLNKGANV--------------DAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHL 669
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
PHA02875 PHA02875
ankyrin repeat protein; Provisional
527-722 1.80e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.16  E-value: 1.80e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 527 GRTPLDLAAFKGHVECVDVLINQGASILVKdYILKRTPIHAAATNGHSECLRLLIGNAEPQNAVDIQDGNgqTPLMLSVL 606
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVK-YPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGM--TPLHLATI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 607 NGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSA 686
Cdd:PHA02875  112 LKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1370483583 687 ASMDanpATADNHGYTALHWACYNGHETCVELLLEQ 722
Cdd:PHA02875  192 ANID---YFGKNGCVAALCYAIENNKIDIVRLFIKR 224
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
152-289 2.66e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 61.18  E-value: 2.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 152 TPLHAAASSGMISVVKYLLDL-GVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCG-AIVNQKNE----KGFTPLHFAAA 225
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAApELVNEPMTsdlyQGETALHIAVV 98
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370483583 226 STHGALcLELLVGNGADVN---------MKSKD-----GKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHI 289
Cdd:cd22192    99 NQNLNL-VRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
88-170 3.37e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.68  E-value: 3.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  88 LHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVK 167
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                  ...
gi 1370483583 168 YLL 170
Cdd:PTZ00322  166 LLS 168
PHA02878 PHA02878
ankyrin repeat protein; Provisional
401-606 3.62e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.28  E-value: 3.62e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 401 LVGSGASVNDLDE-RGCTPLHYAATsDTDGKCLEYLLRNDANPGIRDKqgynavhysaayghrlclqliasetpldvlme 479
Cdd:PHA02878  153 LLSYGADINMKDRhKGNTALHYATE-NKDQRLTELLLSYGANVNIPDK-------------------------------- 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 480 tsgtdmlsdSDNratiSPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAfkGHVECVDV---LINQGASILVK 556
Cdd:PHA02878  200 ---------TNN----SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYCKDYDIlklLLEHGVDVNAK 264
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370483583 557 DYILKRTPIHAAAtngHSE-CLRLLIGNAEPQNAVDIQDgngQTPLMLSVL 606
Cdd:PHA02878  265 SYILGLTALHSSI---KSErKLKLLLEYGADINSLNSYK---LTPLSSAVK 309
PHA02946 PHA02946
ankyin-like protein; Provisional
34-220 6.07e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 59.68  E-value: 6.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  34 VQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHG--EMVKLLLSRGANIN 111
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEviERINLLVQYGAKIN 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 112 AFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDK--KSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHV 189
Cdd:PHA02946  135 NSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKfgKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHI 214
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1370483583 190 ACYNG-QDVVVNELIDCGAIVNQKNEKGFTPL 220
Cdd:PHA02946  215 VCSKTvKNVDIINLLLPSTDVNKQNKFGDSPL 246
Ank_4 pfam13637
Ankyrin repeats (many copies);
53-104 7.89e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 7.89e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370483583  53 TPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLL 104
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
767-820 8.53e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 8.53e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370483583 767 GRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLV 820
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
91-249 1.20e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 59.11  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  91 AAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLL 170
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483583 171 DLGvDMNEPNAYGNTpLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSKD 249
Cdd:PLN03192  612 HFA-SISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDM-VRLLIMNGADVDKANTD 687
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
30-145 1.87e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.34  E-value: 1.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  30 YLEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSnvnVSD-RAGRTALHHAAFSGHGEMVKLLLSRGA 108
Cdd:PLN03192  570 YEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS---ISDpHAAGDLLCTAAKRNDLTAMKELLKQGL 646
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1370483583 109 NINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTC 145
Cdd:PLN03192  647 NVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
389-637 1.97e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.34  E-value: 1.97e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 389 AAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDTDgKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHrlclqli 468
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYE-DCVLVLLKHACNVHIRDANGNTALWNAISAKH------- 603
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 469 asETPLDVLMETSgtdmlSDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLIN 548
Cdd:PLN03192  604 --HKIFRILYHFA-----SISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM 676
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 549 QGASIlvkdyilkrtpIHAAATNGHS-ECLRLLIGNAEPQNAVDIQDGNGQTPLMLSVLNGHTDCvySLLNKGANvdaKD 627
Cdd:PLN03192  677 NGADV-----------DKANTDDDFSpTELRELLQKRELGHSITIVDSVPADEPDLGRDGGSRPG--RLQGTSSD---NQ 740
                         250
                  ....*....|
gi 1370483583 628 KWGRTALHRG 637
Cdd:PLN03192  741 CRPRVSIYKG 750
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
723-834 1.98e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.37  E-value: 1.98e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 723 EVFQKTEGNAFSPLHCAVIND--NEGAAEMLI----------DTLGASIV-------NATDSKGRTPLHAAAFTDHVECL 783
Cdd:PTZ00322   52 EALEATENKDATPDHNLTTEEviDPVVAHMLTvelcqlaasgDAVGARILltggadpNCRDYDGRTPLHIACANGHVQVV 131
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370483583 784 QLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSASAELTLQDNSK 834
Cdd:PTZ00322  132 RVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAK 182
Ank_4 pfam13637
Ankyrin repeats (many copies);
527-581 2.34e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 2.34e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370483583 527 GRTPLDLAAFKGHVECVDVLINQGASILVKDYiLKRTPIHAAATNGHSECLRLLI 581
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
736-906 3.27e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.28  E-value: 3.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 736 LHCAVINDNEGAAEMLIDtLGASiVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNT 815
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFE-YGAD-VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 816 VEMLVSSASaELTLQDNSKNTALHLACSkgHETSALLILekITDRNlINATNAALQTPLHVAARNGLTM-VVQELLGKGA 894
Cdd:PHA02874  206 IKLLIDHGN-HIMNKCKNGFTPLHNAII--HNRSAIELL--INNAS-INDQDIDGSTPLHHAINPPCDIdIIDILLYHKA 279
                         170
                  ....*....|..
gi 1370483583 895 SVLAVDENGYTP 906
Cdd:PHA02874  280 DISIKDNKGENP 291
PHA02875 PHA02875
ankyrin repeat protein; Provisional
704-876 3.28e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.92  E-value: 3.28e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 704 LHWACYNGHETCVELLLE-----QEVFQKtEGNafSPLHCAVINDNEGAAEMLIDTLGASIVNATDSKgrTPLHAAAFTD 778
Cdd:PHA02875   72 LHDAVEEGDVKAVEELLDlgkfaDDVFYK-DGM--TPLHLATILKKLDIMKLLIARGADPDIPNTDKF--SPLHLAVMMG 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 779 HVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSASAELTLQDNSKNTALHLACSKGHETSALLILEKIT 858
Cdd:PHA02875  147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGA 226
                         170
                  ....*....|....*...
gi 1370483583 859 DRNLINATNAALQTPLHV 876
Cdd:PHA02875  227 DCNIMFMIEGEECTILDM 244
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
518-741 4.27e-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: 4.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 518 LDLDVRNSSGRTPLDLAAFKG-HVECVDVLINQGASILVKDyilkrTPIHAAATNGH---SECLRLLIGNAE----PQNA 589
Cdd:TIGR00870  43 LNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGD-----TLLHAISLEYVdavEAILLHLLAAFRksgpLELA 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 590 VDIQDGN---GQTPLMLSVLNGHTDCVYSLLNKGANVDAKDK--------------WGRTALHRGAVTGHEECVDALLQH 652
Cdd:TIGR00870 118 NDQYTSEftpGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSED 197
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 653 GAKCLLRDSRGRTPIHLSAACGHIGVLGALL-----QSAASMDANPATAD------NH-GYTALHWACYNGHETCVELLL 720
Cdd:TIGR00870 198 PADILTADSLGNTLLHLLVMENEFKAEYEELscqmyNFALSLLDKLRDSKelevilNHqGLTPLKLAAKEGRIVLFRLKL 277
                         250       260
                  ....*....|....*....|..
gi 1370483583 721 EQEVFQKT-EGNAFSPLHCAVI 741
Cdd:TIGR00870 278 AIKYKQKKfVAWPNGQQLLSLY 299
PHA02859 PHA02859
ankyrin repeat protein; Provisional
26-194 4.63e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 54.44  E-value: 4.63e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  26 NFLFY------LEAVQvllKHSADVNARDKNWQTPLHIAAANKAV--KCAEALVPLLSNVNVSDRA-GRTALHHAAFSGH 96
Cdd:PHA02859   23 NPLFYyvekddIEGVK---KWIKFVNDCNDLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRDnNLSALHHYLSFNK 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  97 G---EMVKLLLSRGANINAFDKKDRRAIHwaAYMGH----IEVVKLLVSHGAEVTCKDKK------SYTPLHAAASsgmi 163
Cdd:PHA02859  100 NvepEILKILIDSGSSITEEDEDGKNLLH--MYMCNfnvrINVIKLLIDSGVSFLNKDFDnnnilySYILFHSDKK---- 173
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1370483583 164 sVVKYLLDLGVDMNEPNAYGNTPLHVACYNG 194
Cdd:PHA02859  174 -IFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
133-205 4.86e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 4.86e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370483583 133 VKLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDC 205
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
127-318 5.19e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.19  E-value: 5.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 127 MGHIEVVKLLVSHGAEVTckDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCG 206
Cdd:PLN03192  504 LHDLNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 207 AIVNQKNEKGFTPLHFAAASTHGALcLELLVGNGADVNMKSkdGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTP 286
Cdd:PLN03192  582 CNVHIRDANGNTALWNAISAKHHKI-FRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1370483583 287 LHIAARYGHELLINTLITSGADTAKRGIHGMF 318
Cdd:PLN03192  659 LQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
PHA02989 PHA02989
ankyrin repeat protein; Provisional
34-271 5.19e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 56.67  E-value: 5.19e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  34 VQVLLKHSADVNARDKNWQTPLhiaaankavkcaealVPLLSNVNVSDRagrtalhhaafsghgEMVKLLLSRGANINaf 113
Cdd:PHA02989   91 VKLLLKFGADINLKTFNGVSPI---------------VCFIYNSNINNC---------------DMLRFLLSKGINVN-- 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 114 DKKDRRA-----IHWAAYMGHIEVVKLLVSHGaeVTCKDKKSY---TPLHAAASSGM----ISVVKYLLDLGVDMNEPNA 181
Cdd:PHA02989  139 DVKNSRGynllhMYLESFSVKKDVIKILLSFG--VNLFEKTSLyglTPMNIYLRNDIdvisIKVIKYLIKKGVNIETNNN 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 182 YGNTPL------HVACYNGQDVVVNeLIDCGAIVNQKNEKGFTPLHFAA-ASTHGALCLELLVGNgaDVNMKSKDGKTPL 254
Cdd:PHA02989  217 GSESVLesfldnNKILSKKEFKVLN-FILKYIKINKKDKKGFNPLLISAkVDNYEAFNYLLKLGD--DIYNVSKDGDTVL 293
                         250
                  ....*....|....*..
gi 1370483583 255 HMTALHGRFSRSQTIIQ 271
Cdd:PHA02989  294 TYAIKHGNIDMLNRILQ 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
630-683 5.54e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 5.54e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370483583 630 GRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALL 683
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
223-377 5.90e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.80  E-value: 5.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 223 AAASTHGALCLELLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTL 302
Cdd:PLN03192  531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370483583 303 --ITSGADTAKRGIhgmfPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNK 377
Cdd:PLN03192  611 yhFASISDPHAAGD----LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
649-822 6.36e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.56  E-value: 6.36e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 649 LLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQSAASMDANPATADNH-GYTALHWACYNGHETCVELLLEQ----- 722
Cdd:cd22192    37 LKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDLYqGETALHIAVVNQNLNLVRELIARgadvv 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 723 ------EVFQKTEGNAF----SPLHCAVINDNEGAAEMLIDTlGASIVnATDSKGRTPLHAAAF----TDHVECLQLLLS 788
Cdd:cd22192   117 spratgTFFRPGPKNLIyygeHPLSFAACVGNEEIVRLLIEH-GADIR-AQDSLGNTVLHILVLqpnkTFACQMYDLILS 194
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1370483583 789 HNAQVNSV------DSTGKTPLMMAAENGQTNTVEMLVSS 822
Cdd:cd22192   195 YDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQHLVQK 234
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
34-105 6.90e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 6.90e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370483583  34 VQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLS 105
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
764-892 9.21e-08

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 56.31  E-value: 9.21e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 764 DSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDST--------------GKTPLMMAAENGQTNTVEMLVSSASAELTL 829
Cdd:cd22194   138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITS 217
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370483583 830 QDNSKNTALHLAC-----SKGHETSAL----LILEKITDRNLINATNAALQTPLHVAARNGLTMVVQELLGK 892
Cdd:cd22194   218 QDSRGNTVLHALVtvaedSKTQNDFVKrmydMILLKSENKNLETIRNNEGLTPLQLAAKMGKAEILKYILSR 289
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
736-892 1.01e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 55.79  E-value: 1.01e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 736 LHCAVINDNEGAAEMLIDTLGASIVNATDS---KGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDST------------- 799
Cdd:cd22192    55 LHVAALYDNLEAAVVLMEAAPELVNEPMTSdlyQGETALHIAVVNQNLNLVRELIARGADVVSPRATgtffrpgpknliy 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 800 -GKTPLMMAAENGQTNTVEMLVsSASAELTLQDNSKNTALHLACSKGHETSA------LLILEK-ITDRNLINATNAALQ 871
Cdd:cd22192   135 yGEHPLSFAACVGNEEIVRLLI-EHGADIRAQDSLGNTVLHILVLQPNKTFAcqmydlILSYDKeDDLQPLDLVPNNQGL 213
                         170       180
                  ....*....|....*....|.
gi 1370483583 872 TPLHVAARNGLTMVVQELLGK 892
Cdd:cd22192   214 TPFKLAAKEGNIVMFQHLVQK 234
PHA02875 PHA02875
ankyrin repeat protein; Provisional
761-923 1.13e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.38  E-value: 1.13e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 761 NATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSASAELTLQDNSKNTALHL 840
Cdd:PHA02875   29 NFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHL 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 841 AC-SKGHETSALLILEKiTDRNLINATNAalqTPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADC 919
Cdd:PHA02875  109 ATiLKKLDIMKLLIARG-ADPDIPNTDKF---SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAIC 184

                  ....
gi 1370483583 920 LALI 923
Cdd:PHA02875  185 KMLL 188
Ank_4 pfam13637
Ankyrin repeats (many copies);
382-436 2.43e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 2.43e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370483583 382 GRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYAATSDtDGKCLEYLL 436
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG-NVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
734-925 2.78e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.23  E-value: 2.78e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 734 SPLHCAVINDNEGAAEMLIDtLGASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQT 813
Cdd:PHA02875   70 SELHDAVEEGDVKAVEELLD-LGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 814 NTVEMLVSsasaeltlqdnskntalHLACskghetsallilekitdrnlINATNAALQTPLHVAARNGLTMVVQELLGKG 893
Cdd:PHA02875  149 KGIELLID-----------------HKAC--------------------LDIEDCCGCTPLIIAMAKGDIAICKMLLDSG 191
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1370483583 894 ASVLAVDENGYTPALACAPNKDVADCLALILA 925
Cdd:PHA02875  192 ANIDYFGKNGCVAALCYAIENNKIDIVRLFIK 223
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
746-906 2.85e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 2.85e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 746 GAAEMLIDTLGASI-VNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSAS 824
Cdd:PLN03192  536 GNAALLEELLKAKLdPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS 615
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 825 AeltlqdNSKNTALHLACSKGHETSaLLILEKITDRNL-INATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVD-EN 902
Cdd:PLN03192  616 I------SDPHAAGDLLCTAAKRND-LTAMKELLKQGLnVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDD 688

                  ....
gi 1370483583 903 GYTP 906
Cdd:PLN03192  689 DFSP 692
PHA02875 PHA02875
ankyrin repeat protein; Provisional
596-843 2.92e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.84  E-value: 2.92e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 596 NGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAkcLLRD---SRGRTPIHLSAA 672
Cdd:PHA02875   34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK--FADDvfyKDGMTPLHLATI 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 673 CGHIGVLGALLQSAASMDAnPATadnhgytalhwacynghetcvellleqevfqktegNAFSPLHCAVINDNEGAAEMLI 752
Cdd:PHA02875  112 LKKLDIMKLLIARGADPDI-PNT-----------------------------------DKFSPLHLAVMMGDIKGIELLI 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 753 DTlgASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLM-MAAENGQTNTVEMLVS--SASAELTL 829
Cdd:PHA02875  156 DH--KACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKrgADCNIMFM 233
                         250
                  ....*....|....
gi 1370483583 830 QDNSKNTALHLACS 843
Cdd:PHA02875  234 IEGEECTILDMICN 247
PHA02859 PHA02859
ankyrin repeat protein; Provisional
150-308 4.57e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 51.74  E-value: 4.57e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 150 SYT-PLHAAASSGMISVVKYLLDLgvdMNEPNAYGNTPLHvACYNGQDVVVNE---LIDCGAIVNQK-NEKGFTPLHFAA 224
Cdd:PHA02859   20 RYCnPLFYYVEKDDIEGVKKWIKF---VNDCNDLYETPIF-SCLEKDKVNVEIlkfLIENGADVNFKtRDNNLSALHHYL 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 225 ASTHGAL--CLELLVGNGADVNMKSKDGKTPLH--MTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLI- 299
Cdd:PHA02859   96 SFNKNVEpeILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKKIf 175

                  ....*....
gi 1370483583 300 NTLITSGAD 308
Cdd:PHA02859  176 DFLTSLGID 184
PHA02798 PHA02798
ankyrin-like protein; Provisional
198-422 5.95e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 53.30  E-value: 5.95e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 198 VVNELIDCGAIVNQKNEKGFTPLHFAAAS----THGALCLELLVGNGADVNMKSKDGKTPLHmTALHGRFSRSQTI---- 269
Cdd:PHA02798   53 IVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHMLDIVKILIENGADINKKNSDGETPLY-CLLSNGYINNLEIllfm 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 270 IQSGAVIDCEDKNGNTPLHIAARYGHEL---LINTLITSGADTAKRG-------IHGMFPLHLAALSgfSDCCRKLLSSG 339
Cdd:PHA02798  132 IENGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDINTHNnkekydtLHCYFKYNIDRID--ADILKLFVDNG 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 340 FDIDTPDDFGRTCLHAAAAGGNLECLNLLLN------TGADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDE 413
Cdd:PHA02798  210 FIINKENKSHKKKFMEYLNSLLYDNKRFKKNildfifSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITE 289

                  ....*....
gi 1370483583 414 RGCTPLHYA 422
Cdd:PHA02798  290 LGNTCLFTA 298
PHA02874 PHA02874
ankyrin repeat protein; Provisional
747-906 6.22e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 6.22e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 747 AAEMLIDTLGaSIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVssasae 826
Cdd:PHA02874   16 AIEKIIKNKG-NCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI------ 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 827 ltlqDNSKNTA-LHLACSKGHETSAllILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELLGKGASVLAVDENGYT 905
Cdd:PHA02874   89 ----DNGVDTSiLPIPCIEKDMIKT--ILDCGID---VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCY 159

                  .
gi 1370483583 906 P 906
Cdd:PHA02874  160 P 160
Ank_4 pfam13637
Ankyrin repeats (many copies);
734-787 7.59e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 7.59e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370483583 734 SPLHCAVINDNEGAAEMLIDTlGASIvNATDSKGRTPLHAAAFTDHVECLQLLL 787
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEK-GADI-NAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
31-191 1.16e-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: 52.78  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  31 LEAVQVLLKHSADVNARDknwqTPLHIAAANKAVKCAEALVPLLSN---------VNVSDR----AGRTALHHAAFSGHG 97
Cdd:TIGR00870  66 LELTELLLNLSCRGAVGD----TLLHAISLEYVDAVEAILLHLLAAfrksgplelANDQYTseftPGITALHLAAHRQNY 141
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  98 EMVKLLLSRGANINA------FDKKDRRA--------IHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAAA----- 158
Cdd:TIGR00870 142 EIVKLLLERGASVPAracgdfFVKSQGVDsfyhgespLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVmenef 221
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1370483583 159 -------SSGMISVVKYLLDLGVDMNE----PNAYGNTPLHVAC 191
Cdd:TIGR00870 222 kaeyeelSCQMYNFALSLLDKLRDSKEleviLNHQGLTPLKLAA 265
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
225-294 1.22e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 1.22e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 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 1370483583 218 TPLhFAAASTHGALCLE-LLVGNGADVNMKSKDGKTPLHMTALHGRFSRSQTIIQSGA-----VIDCEDKNGNTPLHIAA 291
Cdd:cd22192    19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPelvnePMTSDLYQGETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 292 RYGHELLINTLITSGADTAKRGIHGMFplhlaalsgFSDCCRKLLSsgfdidtpddFGRTCLHAAAAGGNLECLNLLLNT 371
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSPRATGTF---------FRPGPKNLIY----------YGEHPLSFAACVGNEEIVRLLIEH 158
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370483583 372 GADFNKKDKFGRSPLHYAA--ANCNYQC-----LFALVGSGASVNdLD----ERGCTPLHYAA 423
Cdd:cd22192   159 GADIRAQDSLGNTVLHILVlqPNKTFACqmydlILSYDKEDDLQP-LDlvpnNQGLTPFKLAA 220
Ank_4 pfam13637
Ankyrin repeats (many copies);
599-650 1.55e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 1.55e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370483583 599 TPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALL 650
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
562-617 1.84e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 1.84e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370483583 562 RTPIHAAATNGHSECLRLLIGNAEPqnaVDIQDGNGQTPLMLSVLNGHTDCVYSLL 617
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
802-896 2.62e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.17  E-value: 2.62e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 802 TPLMMAAENGQTNTVEMLVSSASAELTLQDNSKNTALHLACSKGHETSALLILEkiTDRNLIN-ATNAAL---QTPLHVA 877
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNePMTSDLyqgETALHIA 96
                          90
                  ....*....|....*....
gi 1370483583 878 ARNGLTMVVQELLGKGASV 896
Cdd:cd22192    97 VVNQNLNLVRELIARGADV 115
Ank_5 pfam13857
Ankyrin repeats (many copies);
136-190 2.86e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 2.86e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370483583 136 LVSHG-AEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVA 190
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
134-318 3.84e-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: 3.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 134 KLLVSHGAEVTCKDKKSYTPLHAAASSGMISVVKYLLDLGVDM-NEP---NAY-GNTPLHVACYNGQDVVVNELIDCGAI 208
Cdd:cd22192    35 KLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvNEPmtsDLYqGETALHIAVVNQNLNLVRELIARGAD 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 209 VN---------QKNEK-----GFTPLHFAAASTHGALcLELLVGNGADVNMKSKDGKTPLHMTALhgrfsrsqtiiQSGA 274
Cdd:cd22192   115 VVspratgtffRPGPKnliyyGEHPLSFAACVGNEEI-VRLLIEHGADIRAQDSLGNTVLHILVL-----------QPNK 182
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370483583 275 VIDCE--------DKNGN-------------TPLHIAARYGHELLINTLITSgadtaKRGIHGMF 318
Cdd:cd22192   183 TFACQmydlilsyDKEDDlqpldlvpnnqglTPFKLAAKEGNIVMFQHLVQK-----RRHIQWTY 242
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
638-720 4.28e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 4.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 638 AVTGHEECVDALLQHGAKCLLRDSRGRTPIHLSAACGHIGVLGALLQsaasMDANPATADNHGYTALHWACYNGHETCVE 717
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLE----FGADPTLLDKDGKTPLELAEENGFREVVQ 165

                  ...
gi 1370483583 718 LLL 720
Cdd:PTZ00322  166 LLS 168
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
84-115 4.57e-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: 44.20  E-value: 4.57e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1370483583  84 GRTALHHAAFS-GHGEMVKLLLSRGANINAFDK 115
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
319-360 5.09e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 5.09e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1370483583 319 PLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGG 360
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG 45
Ank_5 pfam13857
Ankyrin repeats (many copies);
202-256 5.30e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 5.30e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370483583 202 LIDCGAI-VNQKNEKGFTPLHFAAasTHGAL-CLELLVGNGADVNMKSKDGKTPLHM 256
Cdd:pfam13857   1 LLEHGPIdLNRLDGEGYTPLHVAA--KYGALeIVRVLLAYGVDLNLKDEEGLTALDL 55
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
52-203 5.73e-06

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 50.26  E-value: 5.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  52 QTPLHIAAANKAVKCAEALVPLLSNVNVSDRA--------------GRTALHHAAFSGHGEMVKLLLSRGANINA----- 112
Cdd:cd21882    27 KTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAratgr 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 113 -FDKKDRRAIHW-------AAYMGHIEVVKLLVSHGAE---VTCKDKKSYTPLHA---------AASSGMISVVKYLLDL 172
Cdd:cd21882   107 fFRKSPGNLFYFgelplslAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHAlvlqadntpENSAFVCQMYNLLLSY 186
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1370483583 173 G------VDMNE-PNAYGNTPLHVACYNGQDVVVNELI 203
Cdd:cd21882   187 GahldptQQLEEiPNHQGLTPLKLAAVEGKIVMFQHIL 224
Ank_4 pfam13637
Ankyrin repeats (many copies);
252-303 7.69e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 7.69e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370483583 252 TPLHMTALHGRFSRSQTIIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLI 303
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
37-91 9.75e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 9.75e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370483583  37 LLKH-SADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHA 91
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
383-601 9.79e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.22  E-value: 9.79e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 383 RSPLHYAAANCNYQCLFALVGSGASVND-LDERGCTPLHYAaTSDTDGKCLEYLLRNDANPGIrdkqgynavhysaaygh 461
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADDvFYKDGMTPLHLA-TILKKLDIMKLLIARGADPDI----------------- 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 462 rlclqliasetpldvlmetSGTDmlsdsdnraTISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVE 541
Cdd:PHA02875  131 -------------------PNTD---------KFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIA 182
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370483583 542 CVDVLINQGASIlvkDYILKRTPIHA---AATNGHSECLRLLIGNAEPQNAVDIQDGNGQTPL 601
Cdd:PHA02875  183 ICKMLLDSGANI---DYFGKNGCVAAlcyAIENNKIDIVRLFIKRGADCNIMFMIEGEECTIL 242
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
639-813 1.00e-05

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 49.49  E-value: 1.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 639 VTGHEECVDALLQHGAKclLRDSRGRTPIHLSAACGHIGVLGA---LLQSAASMDAN------PATADNH-GYTALHWAC 708
Cdd:cd21882     4 LLGLLECLRWYLTDSAY--QRGATGKTCLHKAALNLNDGVNEAimlLLEAAPDSGNPkelvnaPCTDEFYqGQTALHIAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 709 YNGHETCVELLLEQ----------EVFQKTEGNAF----SPLHCAVINDNEGAAEMLIDTlGASI--VNATDSKGRTPLH 772
Cdd:cd21882    82 ENRNLNLVRLLVENgadvsaratgRFFRKSPGNLFyfgeLPLSLAACTNQEEIVRLLLEN-GAQPaaLEAQDSLGNTVLH 160
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483583 773 A-----------AAFTDHVecLQLLLSHNAQVNSVDS-------TGKTPLMMAAENGQT 813
Cdd:cd21882   161 AlvlqadntpenSAFVCQM--YNLLLSYGAHLDPTQQleeipnhQGLTPLKLAAVEGKI 217
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
668-808 1.31e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 668 HLSAACGHIGVLgALLQSAAsmdaNPATADNHGYTALHWACYNGHETCVELLLEqevfqktegnafsplhcavindnega 747
Cdd:PTZ00322   88 QLAASGDAVGAR-ILLTGGA----DPNCRDYDGRTPLHIACANGHVQVVRVLLE-------------------------- 136
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370483583 748 aemlidtLGASiVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGK-------------TPLMMAA 808
Cdd:PTZ00322  137 -------FGAD-PTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFELGANAKpdsftgkppsledSPISSHH 202
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
84-112 1.72e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 1.72e-05
                           10        20
                   ....*....|....*....|....*....
gi 1370483583   84 GRTALHHAAFSGHGEMVKLLLSRGANINA 112
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
31-71 1.88e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 1.88e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1370483583  31 LEAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALV 71
Cdd:pfam13637  14 LELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
269-348 1.96e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 1.96e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 269 IIQSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLS---SGFDIDT- 344
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRhsqCHFELGAn 180

                  ....*.
gi 1370483583 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 1370483583 417 TPLHYAAtSDTDGKCLEYLLR-NDANPGIRDKQGYNAVHYSAAYGHRLCLQLIASETPLDVLMETSgtdmlsdSDNRATI 495
Cdd:cd22192    19 SPLLLAA-KENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMT-------SDLYQGE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 496 SPLHLAAYHGHhqalEVLVQSLLD--LDVRNSS----------------GRTPLDLAAFKGHVECVDVLINQGASILVKD 557
Cdd:cd22192    91 TALHIAVVNQN----LNLVRELIArgADVVSPRatgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370483583 558 YiLKRTPIHAAAT--NGHSECLRL-LIGNAEP---QNAVD-IQDGNGQTPLMLSVLNGHTDCVYSLLNK 619
Cdd:cd22192   167 S-LGNTVLHILVLqpNKTFACQMYdLILSYDKeddLQPLDlVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank_4 pfam13637
Ankyrin repeats (many copies);
349-402 2.12e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 2.12e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370483583 349 GRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFALV 402
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
587-635 2.31e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 2.31e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1370483583 587 QNAVDIQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDKWGRTALH 635
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
56-142 2.45e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 2.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  56 HIAAANKAVKcAEALVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKL 135
Cdd:PTZ00322   88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                  ....*..
gi 1370483583 136 LVSHGAE 142
Cdd:PTZ00322  167 LSRHSQC 173
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
158-264 2.62e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 2.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 158 ASSGMISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALcLELLV 237
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV-VQLLS 168
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1370483583 238 GN-------GADVNMKSKDGKTPLH----MTALHGRFS 264
Cdd:PTZ00322  169 RHsqchfelGANAKPDSFTGKPPSLedspISSHHPDFS 206
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
233-419 3.23e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 47.98  E-value: 3.23e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 233 LELLVGNGADVNMKSKDGKTPLHMTALHGRFSRS--QTIIQSGAVIDCEDKNGNTPLH---IAARYGHELLINTLITSGA 307
Cdd:PHA02716  195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASviKKIIELGGDMDMKCVNGMSPIMtyiINIDNINPEITNIYIESLD 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 308 DTAKRGIHGMFPLHLAALSGFS-DCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECL--NLLLNTGADFNKKDKFGRS 384
Cdd:PHA02716  275 GNKVKNIPMILHSYITLARNIDiSVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNISTDiiKLLHEYGNDLNEPDNIGNT 354
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1370483583 385 PLHYAAA--------------NCNYQCLFALVGSGASVNDLDERGCTPL 419
Cdd:PHA02716  355 VLHTYLSmlsvvnildpetdnDIRLDVIQCLISLGADITAVNCLGYTPL 403
Ank_4 pfam13637
Ankyrin repeats (many copies);
283-336 3.39e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 3.39e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370483583 283 GNTPLHIAARYGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLL 336
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
84-112 3.84e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.47  E-value: 3.84e-05
                          10        20
                  ....*....|....*....|....*....
gi 1370483583  84 GRTALHHAAFSGHGEMVKLLLSRGANINA 112
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
663-720 4.13e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 4.13e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370483583 663 GRTPIHLSAACGHIGVLGALLQSAASMDAnpatADNHGYTALHWACYNGHETCVELLL 720
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINA----VDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
34-112 4.73e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 4.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  34 VQVLLKHSADVNARDKNWQTPLHIAAA-NKAVKCAEaLVPLLSNVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINA 112
Cdd:PHA03095  240 VLPLLIAGISINARNRYGQTPLHYAAVfNNPRACRR-LIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAET 318
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
494-604 4.84e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 4.84e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 494 TISPLHLAAyHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVECVDVLINQGA--SILVKDyilKRTPIHAAATN 571
Cdd:PTZ00322   83 TVELCQLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAdpTLLDKD---GKTPLELAEEN 158
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1370483583 572 GHSECLRLLIG----------NAEPQNAVDIQDGNGQTPLMLS 604
Cdd:PTZ00322  159 GFREVVQLLSRhsqchfelgaNAKPDSFTGKPPSLEDSPISSH 201
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
753-924 4.91e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.56  E-value: 4.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 753 DTLGASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVSSAsAELTLQDN 832
Cdd:PLN03192  511 DLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDA 589
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 833 SKNTALHLACSKGHETsallILEKITDRNLINATNAALQTPLHVAARNGLTMvVQELLGKGASVLAVDENGYTpALACAP 912
Cdd:PLN03192  590 NGNTALWNAISAKHHK----IFRILYHFASISDPHAAGDLLCTAAKRNDLTA-MKELLKQGLNVDSEDHQGAT-ALQVAM 663
                         170
                  ....*....|..
gi 1370483583 913 NKDVADCLALIL 924
Cdd:PLN03192  664 AEDHVDMVRLLI 675
Ank_4 pfam13637
Ankyrin repeats (many copies);
183-237 5.17e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 5.17e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370483583 183 GNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTHGAlCLELLV 237
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
218-264 5.77e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 5.77e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1370483583 218 TPLHFAAASTHGAlCLELLVGNGADVNMKSKDGKTPLHMTALHGRFS 264
Cdd:pfam13637   3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVE 48
PHA02946 PHA02946
ankyin-like protein; Provisional
334-454 6.55e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.59  E-value: 6.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 334 KLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCN--YQCLFALVGSGASVND- 410
Cdd:PHA02946   57 ELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNs 136
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1370483583 411 LDERGCTPLhyAATSDTDGKCLEYLLRNDANPGIRDKQGYNAVH 454
Cdd:PHA02946  137 VDEEGCGPL--LACTDPSERVFKKIMSIGFEARIVDKFGKNHIH 178
PHA02946 PHA02946
ankyin-like protein; Provisional
100-305 6.66e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.59  E-value: 6.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 100 VKLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLH--AAASSGMISVVKYLLDLGVDMN 177
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYylSGTDDEVIERINLLVQYGAKIN 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 178 EP-NAYGNTPLhVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFAAASTH-GALCLELLVGNGADVNMKSKDGKTPLH 255
Cdd:PHA02946  135 NSvDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpKASTISWMMKLGISPSKPDHDGNTPLH 213
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370483583 256 MTAlhGRFSRSQTIIQ---SGAVIDCEDKNGNTPLHIAAR-YGHELLINTLITS 305
Cdd:PHA02946  214 IVC--SKTVKNVDIINlllPSTDVNKQNKFGDSPLTLLIKtLSPAHLINKLLST 265
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
322-541 8.42e-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: 8.42e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 322 LAALSGFSDCCRKLLSSgfDIDTPDDFGRTCLHAAA---AGGNLECLNLLLNTGADFNKKDKF-----------GRSPLH 387
Cdd:cd21882     1 LEELLGLLECLRWYLTD--SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELvnapctdefyqGQTALH 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 388 YAAANCNYQCLFALVGSGASVND------LDERGCT-------PLHYAATSDTDgKCLEYLLRNDANP---GIRDKQGYN 451
Cdd:cd21882    79 IAIENRNLNLVRLLVENGADVSAratgrfFRKSPGNlfyfgelPLSLAACTNQE-EIVRLLLENGAQPaalEAQDSLGNT 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 452 AVHysaayghrlCLQLIASETPLDVLMETSGTDMLsdsdnratispLHLAAYHGHHQALEvlvqslldlDVRNSSGRTPL 531
Cdd:cd21882   158 VLH---------ALVLQADNTPENSAFVCQMYNLL-----------LSYGAHLDPTQQLE---------EIPNHQGLTPL 208
                         250
                  ....*....|
gi 1370483583 532 DLAAFKGHVE 541
Cdd:cd21882   209 KLAAVEGKIV 218
PHA02798 PHA02798
ankyrin-like protein; Provisional
590-810 1.09e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.98  E-value: 1.09e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 590 VDIQDGNGQTPL--MLSVL---NGHTDCVYSLLNKGANVDAKDKWGRTA----LHRGAVTgHEECVDALLQHGAKCLLRD 660
Cdd:PHA02798   64 VNGLDNEYSTPLctILSNIkdyKHMLDIVKILIENGADINKKNSDGETPlyclLSNGYIN-NLEILLFMIENGADTTLLD 142
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 661 SRGRTPIHLSAACGH---IGVLGALLQSAasMDANpaTADN-HGYTALHwaCYNGHE------TCVELLLEQ----EVFQ 726
Cdd:PHA02798  143 KDGFTMLQVYLQSNHhidIEIIKLLLEKG--VDIN--THNNkEKYDTLH--CYFKYNidridaDILKLFVDNgfiiNKEN 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 727 KTEGNAFSPLHCAVINDNEGAAEMLIDTLGASI-VNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLM 805
Cdd:PHA02798  217 KSHKKKFMEYLNSLLYDNKRFKKNILDFIFSYIdINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLF 296

                  ....*
gi 1370483583 806 MAAEN 810
Cdd:PHA02798  297 TAFEN 301
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
583-692 1.25e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 1.25e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 583 NAEPQNAVDiqdgngQTPL-MLSV------LNGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAK 655
Cdd:PTZ00322   67 NLTTEEVID------PVVAhMLTVelcqlaASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAD 140
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1370483583 656 CLLRDSRGRTPIHLSAACGHIGVLGALL---QSAASMDAN 692
Cdd:PTZ00322  141 PTLLDKDGKTPLELAEENGFREVVQLLSrhsQCHFELGAN 180
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
766-797 1.41e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 1.41e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1370483583 766 KGRTPLHAAA-FTDHVECLQLLLSHNAQVNSVD 797
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
321-437 1.43e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 321 HLAALSGFSDccrKLLSSGFDIDTPDDFGRTCLHAA-------AAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANC 393
Cdd:PTZ00322   50 HLEALEATEN---KDATPDHNLTTEEVIDPVVAHMLtvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANG 126
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1370483583 394 NYQCLFALVGSGASVNDLDERGCTPLHYAATSDTdGKCLEYLLR 437
Cdd:PTZ00322  127 HVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF-REVVQLLSR 169
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
808-903 1.70e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 808 AENGQTNTVEMLVSSAsAELTLQDNSKNTALHLACSKGHETSALLILEKITDRNLINATNaalQTPLHVAARNGLTMVVQ 887
Cdd:PTZ00322   90 AASGDAVGARILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDG---KTPLELAEENGFREVVQ 165
                          90
                  ....*....|....*.
gi 1370483583 888 ELLGKGASVLAVDENG 903
Cdd:PTZ00322  166 LLSRHSQCHFELGANA 181
Ank_5 pfam13857
Ankyrin repeats (many copies);
169-223 2.92e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 2.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370483583 169 LLDLG-VDMNEPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQKNEKGFTPLHFA 223
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
756-807 3.16e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 3.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370483583 756 GASIVNATDSKGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMA 807
Cdd:pfam13857   5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
484-534 3.19e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 3.19e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370483583 484 DMLSDSDNRATISPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLA 534
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
596-628 3.31e-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: 3.31e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1370483583 596 NGQTPLMLSVL-NGHTDCVYSLLNKGANVDAKDK 628
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA02989 PHA02989
ankyrin repeat protein; Provisional
98-229 3.48e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 44.35  E-value: 3.48e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  98 EMVKLLLSRGANINAFDKKDRRAI------HWAAYMGHIEVVKLLVSHgAEVTCKDKKSYTPLHAAASSGMISVVKYLLD 171
Cdd:PHA02989  199 KVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLK 277
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370483583 172 LGVDMNEPNAYGNTPLHVACYNGQDVVVNElidcgaIVNQKNEKGFTPLHFAAASTHG 229
Cdd:PHA02989  278 LGDDIYNVSKDGDTVLTYAIKHGNIDMLNR------ILQLKPGKYLIKKTFEYFSEHG 329
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
151-178 3.53e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 3.53e-04
                           10        20
                   ....*....|....*....|....*...
gi 1370483583  151 YTPLHAAASSGMISVVKYLLDLGVDMNE 178
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
103-157 4.13e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 4.13e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370483583 103 LLSRG-ANINAFDKKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSYTPLHAA 157
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
414-447 4.44e-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: 4.44e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1370483583 414 RGCTPLHYAATSDTDGKCLEYLLRNDANPGIRDK 447
Cdd:pfam00023   1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
321-415 4.65e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 4.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 321 HLAAlSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGGNLECLNLLLNTGADFNKKDKFGRSPLHYAAANCNYQCLFA 400
Cdd:PTZ00322   88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
                          90
                  ....*....|....*
gi 1370483583 401 LVGSGASVNDLDERG 415
Cdd:PTZ00322  167 LSRHSQCHFELGANA 181
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
178-294 4.78e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.98  E-value: 4.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 178 EPNAYGNTPLHVACYNGQDVVVNELIDCGAIVNQK----------NEKGF----TPLHFAAASTHGALcLELLVGNGAD- 242
Cdd:cd22194   136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHakgvffnpkyKHEGFyfgeTPLALAACTNQPEI-VQLLMEKESTd 214
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370483583 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 ...
766-794 5.12e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 5.12e-04
                           10        20
                   ....*....|....*....|....*....
gi 1370483583  766 KGRTPLHAAAFTDHVECLQLLLSHNAQVN 794
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02859 PHA02859
ankyrin repeat protein; Provisional
372-454 5.16e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.50  E-value: 5.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 372 GADFNKKDK-FGRSPLHYAAA---NCNYQCLFALVGSGASVNDLDERGCTPLH-YAATSDTDGKCLEYLLRNDANPGIRD 446
Cdd:PHA02859   76 GADVNFKTRdNNLSALHHYLSfnkNVEPEILKILIDSGSSITEEDEDGKNLLHmYMCNFNVRINVIKLLIDSGVSFLNKD 155

                  ....*...
gi 1370483583 447 KQGYNAVH 454
Cdd:PHA02859  156 FDNNNILY 163
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
182-210 6.48e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 6.48e-04
                           10        20
                   ....*....|....*....|....*....
gi 1370483583  182 YGNTPLHVACYNGQDVVVNELIDCGAIVN 210
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
215-248 8.01e-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: 8.01e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1370483583 215 KGFTPLHFAAASTHGALCLELLVGNGADVNMKSK 248
Cdd:pfam00023   1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
84-224 8.18e-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: 43.21  E-value: 8.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  84 GRTALHHAAFSGHGEMVKLLLSRGANINA------FDKKDRraiHWAAYMGHievvkllvshgaevtckdkksyTPLHAA 157
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNAhakgvfFNPKYK---HEGFYFGE----------------------TPLALA 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 158 ASSGMISVVKYLLDlgvdmNEPNAY------GNTPLH----VA-CYNGQDVVVNELID-----CG--AIVNQKNEKGFTP 219
Cdd:cd22194   196 ACTNQPEIVQLLME-----KESTDItsqdsrGNTVLHalvtVAeDSKTQNDFVKRMYDmillkSEnkNLETIRNNEGLTP 270

                  ....*
gi 1370483583 220 LHFAA 224
Cdd:cd22194   271 LQLAA 275
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
182-214 9.94e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 9.94e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1370483583 182 YGNTPLHVACY-NGQDVVVNELIDCGAIVNQKNE 214
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
562-668 1.02e-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: 1.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 562 RTPIHAAATN---GHSECLRLLIgNAEPQNAVDIQDGN---------GQTPLMLSVLNGHTDCVYSLLNKGANVDAK--- 626
Cdd:cd21882    27 KTCLHKAALNlndGVNEAIMLLL-EAAPDSGNPKELVNapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSARatg 105
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370483583 627 ---DKWGRTALHRG-------AVTGHEECVDALLQHGAK---CLLRDSRGRTPIH 668
Cdd:cd21882   106 rffRKSPGNLFYFGelplslaACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLH 160
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
282-308 1.04e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 1.04e-03
                           10        20
                   ....*....|....*....|....*..
gi 1370483583  282 NGNTPLHIAARYGHELLINTLITSGAD 308
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
98-320 1.05e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 42.98  E-value: 1.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  98 EMVKLLLSRG-ANINAFDKKDRRAIhWAAYMGH----IEVVKLLVSHGAEVTCKDKKSYTPLHAAASSGMI--SVVKYLL 170
Cdd:PHA02716  156 DLIKYMVDVGiVNLNYVCKKTGYGI-LHAYLGNmyvdIDILEWLCNNGVNVNLQNNHLITPLHTYLITGNVcaSVIKKII 234
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 171 DLGVDMNEPNAYGNTPLHVACYNGQDV---VVNELIDCGAIVNQKNEKGFTPLHFAAASTHGALCLELLVGNGADVNMKS 247
Cdd:PHA02716  235 ELGGDMDMKCVNGMSPIMTYIINIDNInpeITNIYIESLDGNKVKNIPMILHSYITLARNIDISVVYSFLQPGVKLHYKD 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 248 KDGKTPLHMTALHGRFSRS--QTIIQSGAVIDCEDKNGNTPLH-------IAARYGHEL-------LINTLITSGADTAK 311
Cdd:PHA02716  315 SAGRTCLHQYILRHNISTDiiKLLHEYGNDLNEPDNIGNTVLHtylsmlsVVNILDPETdndirldVIQCLISLGADITA 394

                  ....*....
gi 1370483583 312 RGIHGMFPL 320
Cdd:PHA02716  395 VNCLGYTPL 403
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
699-721 1.20e-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: 1.20e-03
                           10        20
                   ....*....|....*....|...
gi 1370483583  699 HGYTALHWACYNGHETCVELLLE 721
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLD 23
PHA02798 PHA02798
ankyrin-like protein; Provisional
749-864 1.22e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.51  E-value: 1.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 749 EMLIDtLGASiVNATDSKGRTPL-----HAAAFTDHVECLQLLLSHNAQVNSVDSTGKTPLMMAAENGQTNTVEMLVS-- 821
Cdd:PHA02798   55 KLFIN-LGAN-VNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFmi 132
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1370483583 822 SASAELTLQDNSKNTALHLACSKGHETSALLI---LEKITDRNLIN 864
Cdd:PHA02798  133 ENGADTTLLDKDGFTMLQVYLQSNHHIDIEIIkllLEKGVDINTHN 178
Ank_5 pfam13857
Ankyrin repeats (many copies);
373-422 1.25e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 1.25e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370483583 373 ADFNKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYA 422
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02736 PHA02736
Viral ankyrin protein; Provisional
81-191 1.32e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 40.24  E-value: 1.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  81 DRAGRTALHHaaFSGHGEMVKLLLSRGANINA-------FDKKDRRAIHWAAYMGHI---EVVKLLVSHGAEVTCKDKK- 149
Cdd:PHA02736   14 DIEGENILHY--LCRNGGVTDLLAFKNAISDEnrylvleYNRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKERVf 91
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1370483583 150 SYTPLHAAASSGMISVVKYLLDL-GVDMNEPNAYGNTPLHVAC 191
Cdd:PHA02736   92 GNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVAC 134
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
81-205 1.48e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 42.59  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  81 DRAGRTALHHAAFSGH--GEMVKLLLSRGANINAFDKKDRRAIHwaAYMGHIEVVKLLVSHgaevTCKDKKsytplhaaa 158
Cdd:PHA02716  314 DSAGRTCLHQYILRHNisTDIIKLLHEYGNDLNEPDNIGNTVLH--TYLSMLSVVNILDPE----TDNDIR--------- 378
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1370483583 159 ssgmISVVKYLLDLGVDMNEPNAYGNTPLHVACYNGQDVVVNELIDC 205
Cdd:PHA02716  379 ----LDVIQCLISLGADITAVNCLGYTPLTSYICTAQNYMYYDIIDC 421
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
562-668 1.55e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.44  E-value: 1.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 562 RTPIHAAATNGhseCLRLLIgNAEPQNavdiQDGNGQTPLMLSVLNGHTDCVYSLLNKGANVDAKDK------------- 628
Cdd:cd22194   114 RILLAFAEENG---ILDRFI-NAEYTE----EAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegf 185
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1370483583 629 -WGRTALHRGAVTGHEECVDALLQHGAKCL-LRDSRGRTPIH 668
Cdd:cd22194   186 yFGETPLALAACTNQPEIVQLLMEKESTDItSQDSRGNTVLH 227
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
120-145 1.75e-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: 1.75e-03
                           10        20
                   ....*....|....*....|....*.
gi 1370483583  120 AIHWAAYMGHIEVVKLLVSHGAEVTC 145
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
835-890 1.86e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 1.86e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370483583 835 NTALHLACSKGHETSALLILEKITDrnlINATNAALQTPLHVAARNGLTMVVQELL 890
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
616-669 1.97e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 1.97e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370483583 616 LLNKGANVDAKDKWGRTALHRGAVTGHEECVDALLQHGAKCLLRDSRGRTPIHL 669
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
120-148 2.02e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 2.02e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1370483583 120 AIHWAAYM-GHIEVVKLLVSHGAEVTCKDK 148
Cdd:pfam00023   5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
861-906 2.40e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 2.40e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1370483583 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 2.52e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 2.52e-03
                           10        20
                   ....*....|....*....|....*..
gi 1370483583  527 GRTPLDLAAFKGHVECVDVLINQGASI 553
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
527-557 2.53e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 2.53e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1370483583 527 GRTPLDLAAFK-GHVECVDVLINQGASILVKD 557
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
116-226 2.55e-03

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 41.72  E-value: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 116 KDRRAIHWAAYMGHIEVVKLLVSHGAEVTC-------KDKKSYT-------PLHAAASSGMISVVKYLLD---LGVDMNE 178
Cdd:cd22196    93 KGQTALHIAIERRNMHLVELLVQNGADVHArasgeffKKKKGGPgfyfgelPLSLAACTNQLDIVKFLLEnphSPADISA 172
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370483583 179 PNAYGNTPLHVACYNGQDVVVN---------ELIDCGAIVNQK-------NEKGFTPLHFAAAS 226
Cdd:cd22196   173 RDSMGNTVLHALVEVADNTPENtkfvtkmynEILILGAKIRPLlkleeitNKKGLTPLKLAAKT 236
PHA02989 PHA02989
ankyrin repeat protein; Provisional
163-422 2.88e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 41.27  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 163 ISVVKYLLDLGVDMNEpnAYGNTPLHVACYNGQDV---VVNELIDCGAIVNQKnekGF--TPL-----HFAAASTHGALC 232
Cdd:PHA02989   16 KNALEFLLRTGFDVNE--EYRGNSILLLYLKRKDVkikIVKLLIDNGADVNYK---GYieTPLcavlrNREITSNKIKKI 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 233 LELLVGNGADVNMKSKDGKTPLhMTALHG---------RFsrsqtIIQSGA-VIDCEDKNGNTPLHIaarYGHELLINT- 301
Cdd:PHA02989   91 VKLLLKFGADINLKTFNGVSPI-VCFIYNsninncdmlRF-----LLSKGInVNDVKNSRGYNLLHM---YLESFSVKKd 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 302 ----LITSGADT-AKRGIHGMFPLHLAALSGFS----DCCRKLLSSGFDIDTPDDFGRTCLHAAAagGNLECLNLLLNTG 372
Cdd:PHA02989  162 vikiLLSFGVNLfEKTSLYGLTPMNIYLRNDIDvisiKVIKYLIKKGVNIETNNNGSESVLESFL--DNNKILSKKEFKV 239
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1370483583 373 ADF-------NKKDKFGRSPLHYAAANCNYQCLFALVGSGASVNDLDERGCTPLHYA 422
Cdd:PHA02989  240 LNFilkyikiNKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
288-360 2.88e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 2.88e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370483583 288 HIAARyGHELLINTLITSGADTAKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTPDDFGRTCLHAAAAGG 360
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
Ank_5 pfam13857
Ankyrin repeats (many copies);
76-115 2.93e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 2.93e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1370483583  76 NVNVSDRAGRTALHHAAFSGHGEMVKLLLSRGANINAFDK 115
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDE 47
Ank_5 pfam13857
Ankyrin repeats (many copies);
406-455 2.93e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 2.93e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370483583 406 ASVNDLDERGCTPLHYAAtSDTDGKCLEYLLRNDANPGIRDKQGYNAVHY 455
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAA-KYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
760-892 3.50e-03

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 41.33  E-value: 3.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 760 VNA--TDS--KGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDST--------------GKTPLMMAAENGQTNTVEMLVS 821
Cdd:cd22196    83 VNAayTDSyyKGQTALHIAIERRNMHLVELLVQNGADVHARASGeffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLE 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 822 S--ASAELTLQDNSKNTALHLACS---------------------KGHETSALLILEKITDRNLInatnaalqTPLHVAA 878
Cdd:cd22196   163 NphSPADISARDSMGNTVLHALVEvadntpentkfvtkmyneiliLGAKIRPLLKLEEITNKKGL--------TPLKLAA 234
                         170
                  ....*....|....
gi 1370483583 879 RNGLTMVVQELLGK 892
Cdd:cd22196   235 KTGKIGIFAYILGR 248
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
596-625 3.77e-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: 3.77e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1370483583  596 NGQTPLMLSVLNGHTDCVYSLLNKGANVDA 625
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
335-515 4.20e-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: 41.22  E-value: 4.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 335 LLSSGFDIDTpddfGRTCLHAA-----------------AAGGNLECLNLLLNTGADFNkkdkFGRSPLHYAAANCNYQC 397
Cdd:TIGR00870  72 LLNLSCRGAV----GDTLLHAIsleyvdaveaillhllaAFRKSGPLELANDQYTSEFT----PGITALHLAAHRQNYEI 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 398 LFALVGSGASVN--------------DLDERGCTPLH-YAATSDTDgkCLEYLLRNDANPGIRDKQGYNAVH-------Y 455
Cdd:TIGR00870 144 VKLLLERGASVParacgdffvksqgvDSFYHGESPLNaAACLGSPS--IVALLSEDPADILTADSLGNTLLHllvmeneF 221
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370483583 456 SAAYGH--RLCLQLIasetpLDVLMETSGTDMLSDSDNRATISPLHLAAYHGHHQALEVLVQ 515
Cdd:TIGR00870 222 KAEYEElsCQMYNFA-----LSLLDKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
759-881 4.35e-03

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 40.99  E-value: 4.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 759 IVNA--TDS--KGRTPLHAAAFTDHVECLQLLLSHNAQVNSVDST-------------GKTPLMMAAENGQTNTVEMLVS 821
Cdd:cd22197    82 LVNAqcTDEyyRGHSALHIAIEKRSLQCVKLLVENGADVHARACGrffqkkqgtcfyfGELPLSLAACTKQWDVVNYLLE 161
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370483583 822 SAS--AELTLQDNSKNTALH---LACSKGHETSALL------ILEKITDRN----LINATNAALQTPLHVAARNG 881
Cdd:cd22197   162 NPHqpASLQAQDSLGNTVLHalvMIADNSPENSALVikmydgLLQAGARLCptvqLEEISNHEGLTPLKLAAKEG 236
Ank_4 pfam13637
Ankyrin repeats (many copies);
872-923 4.51e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 4.51e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370483583 872 TPLHVAARNGLTMVVQELLGKGASVLAVDENGYTPALACAPNKDVADCLALI 923
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02859 PHA02859
ankyrin repeat protein; Provisional
734-839 4.86e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.42  E-value: 4.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 734 SPLHCAVIND--NEGAAEMLIDTlGASIVNATDSKGRTPLHA-AAFTDHV--ECLQLLLSHNAQVNSVDSTGKTPLMMAA 808
Cdd:PHA02859   53 TPIFSCLEKDkvNVEILKFLIEN-GADVNFKTRDNNLSALHHyLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHMYM 131
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1370483583 809 ENGQTN--TVEMLVSSASAELTlQDNSKNTALH 839
Cdd:PHA02859  132 CNFNVRinVIKLLIDSGVSFLN-KDFDNNNILY 163
PHA02791 PHA02791
ankyrin-like protein; Provisional
696-865 5.46e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.03  E-value: 5.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 696 ADNHGYTALHWACYNGHETCVELLLEQEVFQKTEGNAFsPLH-CAVINDNEGAAEMLIDTLGASivnATDSKGRTPLHAA 774
Cdd:PHA02791   26 ADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF-PLHqAATLEDTKIVKILLFSGMDDS---QFDDKGNTALYYA 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 775 AFTDHVECLQLLLSHNAQVNSVDSTG-KTPLMMAAENGQTNTVEMLVSSASAELTLQdnSKNTALHLACSKGHETSALLI 853
Cdd:PHA02791  102 VDSGNMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPSTFDLA--ILLSCIHITIKNGHVDMMILL 179
                         170
                  ....*....|..
gi 1370483583 854 LEKITDRNLINA 865
Cdd:PHA02791  180 LDYMTSTNTNNS 191
Ank_4 pfam13637
Ankyrin repeats (many copies);
802-847 5.72e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 5.72e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1370483583 802 TPLMMAAENGQTNTVEMLVSSaSAELTLQDNSKNTALHLACSKGHE 847
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNV 47
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
182-210 5.87e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 5.87e-03
                          10        20
                  ....*....|....*....|....*....
gi 1370483583 182 YGNTPLHVACYNGQDVVVNELIDCGAIVN 210
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
282-308 6.81e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 6.81e-03
                          10        20
                  ....*....|....*....|....*..
gi 1370483583 282 NGNTPLHIAARYGHELLINTLITSGAD 308
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
PHA02884 PHA02884
ankyrin repeat protein; Provisional
165-259 7.09e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.58  E-value: 7.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 165 VVKYLLDLGVDMNEP-----NAYgNTPLHVACYNGQDVVVNELIDCGAIVNQ-KNEKGFTPLHFAAasTHGAL-CLELLV 237
Cdd:PHA02884   48 IIDAILKLGADPEAPfplseNSK-TNPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKITPLYISV--LHGCLkCLEILL 124
                          90       100
                  ....*....|....*....|..
gi 1370483583 238 GNGADVNMKSKDGKTPLHMTAL 259
Cdd:PHA02884  125 SYGADINIQTNDMVTPIELALM 146
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
282-308 7.86e-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: 7.86e-03
                          10        20
                  ....*....|....*....|....*...
gi 1370483583 282 NGNTPLHIAA-RYGHELLINTLITSGAD 308
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGAD 28
Ank_4 pfam13637
Ankyrin repeats (many copies);
417-467 8.32e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 8.32e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1370483583 417 TPLHYAATSDtDGKCLEYLLRNDANPGIRDKQGYNAVHYSAAYGHRLCLQL 467
Cdd:pfam13637   3 TALHAAAASG-HLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKL 52
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
710-890 8.81e-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: 8.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 710 NGHETCVELLLEQEVFQKTEGNAfspLHCAVINDnEGAAEMLI--------DTLGASIVNATD----SKGRTPLHAAAFT 777
Cdd:TIGR00870  63 NENLELTELLLNLSCRGAVGDTL---LHAISLEY-VDAVEAILlhllaafrKSGPLELANDQYtsefTPGITALHLAAHR 138
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 778 DHVECLQLLLSHNAQVNS------------VDST--GKTPLMMAAENGQTNTVEMLvSSASAELTLQDNSKNTALHL--- 840
Cdd:TIGR00870 139 QNYEIVKLLLERGASVPAracgdffvksqgVDSFyhGESPLNAAACLGSPSIVALL-SEDPADILTADSLGNTLLHLlvm 217
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 841 ---------ACSKGHETSALLILEKITD-RNLINATNAALQTPLHVAARNGLTMVVQELL 890
Cdd:TIGR00870 218 enefkaeyeELSCQMYNFALSLLDKLRDsKELEVILNHQGLTPLKLAAKEGRIVLFRLKL 277
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
463-546 8.96e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.88  E-value: 8.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 463 LClQLIASETPLDV-LMETSGTDMLS-DSDNRatiSPLHLAAYHGHHQALEVLVQSLLDLDVRNSSGRTPLDLAAFKGHV 540
Cdd:PTZ00322   86 LC-QLAASGDAVGArILLTGGADPNCrDYDGR---TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161

                  ....*.
gi 1370483583 541 ECVDVL 546
Cdd:PTZ00322  162 EVVQLL 167
PHA02736 PHA02736
Viral ankyrin protein; Provisional
178-307 9.34e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.93  E-value: 9.34e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 178 EPNAYGNTPLHVACYNGqDVV-----VNELIDCGA-IVNQKNEKGFTPLHFAAAS--THGALCLELLVGNGADVNMK-SK 248
Cdd:PHA02736   12 EPDIEGENILHYLCRNG-GVTdllafKNAISDENRyLVLEYNRHGKQCVHIVSNPdkADPQEKLKLLMEWGADINGKeRV 90
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 249 DGKTPLHMTALHGRFSRSQTII-QSGAVIDCEDKNGNTPLHIAARYGHELLINTLITSGA 307
Cdd:PHA02736   91 FGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
510-704 9.36e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 39.90  E-value: 9.36e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 510 LEVLVQSLLDLDVRNSSGRTPLDLAAFKGHVeCVDVL---INQGASILVKdYILKRTPIHAAATNghseclrllIGNAEP 586
Cdd:PHA02716  195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNV-CASVIkkiIELGGDMDMK-CVNGMSPIMTYIIN---------IDNINP 263
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 587 Q--NA-VDIQDGNGQT--PLMLSVL-----NGHTDCVYSLLNKGANVDAKDKWGRTALHRGAVTGH--EECVDALLQHGA 654
Cdd:PHA02716  264 EitNIyIESLDGNKVKniPMILHSYitlarNIDISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTDIIKLLHEYGN 343
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1370483583 655 KCLLRDSRGRTPIH--LSAACG------------HIGVLGALLQSAASMDAnpatADNHGYTAL 704
Cdd:PHA02716  344 DLNEPDNIGNTVLHtyLSMLSVvnildpetdndiRLDVIQCLISLGADITA----VNCLGYTPL 403
PHA02791 PHA02791
ankyrin-like protein; Provisional
41-219 9.43e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 39.25  E-value: 9.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583  41 SADVNARDKNWQTPLHIAAANKAVKC------AEALVPLLSNvnvsdragRTALHHAAFSGHGEMVKLLLSRGANINAFD 114
Cdd:PHA02791   20 SKDAFKADVHGHSALYYAIADNNVRLvctllnAGALKNLLEN--------EFPLHQAATLEDTKIVKILLFSGMDDSQFD 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370483583 115 KKDRRAIHWAAYMGHIEVVKLLVSHGAEVTCKDKKSY-TPLHAAASSGMISVVKYLL-------DLGVDMnepnaygnTP 186
Cdd:PHA02791   92 DKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLseipstfDLAILL--------SC 163
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1370483583 187 LHVACYNGQDVVVNELIDCGAIVNQKNEKGFTP 219
Cdd:PHA02791  164 IHITIKNGHVDMMILLLDYMTSTNTNNSLLFIP 196
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
699-724 9.80e-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: 34.54  E-value: 9.80e-03
                          10        20
                  ....*....|....*....|....*.
gi 1370483583 699 HGYTALHWACYNGHETCVELLLEQEV 724
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGA 26
 
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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