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Conserved domains on  [gi|1720355778|ref|XP_030110857|]
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serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit B isoform X9 [Mus musculus]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-271 8.60e-50

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 177.84  E-value: 8.60e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778   1 MWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGH 80
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  81 MEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEI 160
Cdd:COG0666   100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 161 DEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHM 240
Cdd:COG0666   180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLLEAGADLNAKDKDGLTALLL 258
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1720355778 241 TAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 271
Cdd:COG0666   259 AAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
432-706 5.57e-37

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.86  E-value: 5.57e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 432 NKMILGNAHDNSEELERAREVKEKDAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNTGFEESDGG 511
Cdd:COG0666     8 LLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 512 AlkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVING 591
Cdd:COG0666    88 N--TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 592 HTLCLRLLLE-TADnpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLE 670
Cdd:COG0666   165 NLEIVKLLLEaGAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1720355778 671 QEASILCKDSRGRTPLHYAAARGHATWLNELLQIAL 706
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
596-921 1.77e-31

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.07  E-value: 1.77e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 596 LRLLLETADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQEASI 675
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 676 LCKDSRGRTPLHYAAARGHATWLNELLQialSEEDCCLKDNQGYTPLHWACYNGNENCIEVLLEQkcfrkfignpftplh 755
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA--------------- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 756 caiinghescaslllGAiDPSIvscRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVD 835
Cdd:COG0666   143 ---------------GA-DVNA---QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 836 ILVNsAQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIAARNGLKVVVEELLAKGACVL 915
Cdd:COG0666   204 LLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279

                  ....*.
gi 1720355778 916 AVDENA 921
Cdd:COG0666   280 AALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
181-480 7.48e-30

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.44  E-value: 7.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 181 AVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI 260
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 261 DCVDKDGNTPLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSsgqkysivslfsnehvlsA 340
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE------------------A 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 341 GFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVNETDDWGRTA 420
Cdd:COG0666   143 GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTA 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 421 LHYAAASDMDRNKMILGNAHDNSEELERAREVKEKDAALCLEFLLQNDANPSIRDKEGYN 480
Cdd:COG0666   223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-271 8.60e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 177.84  E-value: 8.60e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778   1 MWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGH 80
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  81 MEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEI 160
Cdd:COG0666   100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 161 DEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHM 240
Cdd:COG0666   180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLLEAGADLNAKDKDGLTALLL 258
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1720355778 241 TAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 271
Cdd:COG0666   259 AAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
14-287 4.84e-40

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 154.80  E-value: 4.84e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  14 SEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSS---VNVSDRGGRTALHHAALNGH-MEMVNLLLA 89
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAgadVNAPERCGFTPLHLYLYNATtLDVIKLLIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  90 KGANINAFDKKDRRALHwaAYMG----HLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISV--VKHLLNLGVEIDEI 163
Cdd:PHA03095  106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 164 NVYGNTALHIACYNGQD--AVVNELIDYGANVNQPNNSGFTPLHFAAA-STHGALCLELLVNNGADVNIQSKDGKSPLHM 240
Cdd:PHA03095  184 DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1720355778 241 TAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLI 287
Cdd:PHA03095  264 AAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
432-706 5.57e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.86  E-value: 5.57e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 432 NKMILGNAHDNSEELERAREVKEKDAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNTGFEESDGG 511
Cdd:COG0666     8 LLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 512 AlkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVING 591
Cdd:COG0666    88 N--TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 592 HTLCLRLLLE-TADnpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLE 670
Cdd:COG0666   165 NLEIVKLLLEaGAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1720355778 671 QEASILCKDSRGRTPLHYAAARGHATWLNELLQIAL 706
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
596-921 1.77e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.07  E-value: 1.77e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 596 LRLLLETADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQEASI 675
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 676 LCKDSRGRTPLHYAAARGHATWLNELLQialSEEDCCLKDNQGYTPLHWACYNGNENCIEVLLEQkcfrkfignpftplh 755
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA--------------- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 756 caiinghescaslllGAiDPSIvscRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVD 835
Cdd:COG0666   143 ---------------GA-DVNA---QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 836 ILVNsAQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIAARNGLKVVVEELLAKGACVL 915
Cdd:COG0666   204 LLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279

                  ....*.
gi 1720355778 916 AVDENA 921
Cdd:COG0666   280 AALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
181-480 7.48e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.44  E-value: 7.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 181 AVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI 260
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 261 DCVDKDGNTPLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSsgqkysivslfsnehvlsA 340
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE------------------A 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 341 GFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVNETDDWGRTA 420
Cdd:COG0666   143 GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTA 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 421 LHYAAASDMDRNKMILGNAHDNSEELERAREVKEKDAALCLEFLLQNDANPSIRDKEGYN 480
Cdd:COG0666   223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
PHA03095 PHA03095
ankyrin-like protein; Provisional
140-421 6.67e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 112.43  E-value: 6.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 140 AAASNGQISVVKHLLNLGVEIDEINVYGNTALH--IACYNGQDA-VVNELIDYGANVNQPNNSGFTPLHFAAASTHGALC 216
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 217 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAAR-HGHEL-LINTLITSGAD 292
Cdd:PHA03095  100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKsRNANVeLLRLLIDAGAD 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 293 TAKCGIHSMFPLHLAALNAHSDccrkllssgqkYSIVslfsnEHVLSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQ- 371
Cdd:PHA03095  180 VYAVDDRFRSLLHHHLQSFKPR-----------ARIV-----RELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPl 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720355778 372 -SSGADFHKKDKCGRTPLHYAAA--NCHF--HCIKAlvttGANVNETDDWGRTAL 421
Cdd:PHA03095  244 lIAGISINARNRYGQTPLHYAAVfnNPRAcrRLIAL----GADINAVSSDGNTPL 294
PHA03095 PHA03095
ankyrin-like protein; Provisional
283-610 5.41e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 100.48  E-value: 5.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 283 INTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRkllssgqkysIVSLfsnehVLSAGFEIDTPDTFGRTCLHAAAAGG 362
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKD----------IVRL-----LLEAGADVNAPERCGFTPLHLYLYNA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 363 NVE-CIKLLQSSGADFHKKDKCGRTPLH-YAA-ANCHFHCIKALVTTGANVNETDDWGRTALHyaaasdmdrnkmILGNA 439
Cdd:PHA03095   95 TTLdVIKLLIKAGADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLA------------VLLKS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 440 HDNSEELerarevkekdaalcLEFLLQNDANPSIRDKEGYNSIHYAAAYGH--RQCLELLLERTNTGFEESDGGalKSPL 517
Cdd:PHA03095  163 RNANVEL--------------LRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLG--NTPL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 518 HLAAYNGHHQALEV--LLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLC 595
Cdd:PHA03095  227 HSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNTPLSLMVRNNNGRA 305
                         330
                  ....*....|....*
gi 1720355778 596 LRLLLETADNPEVVD 610
Cdd:PHA03095  306 VRAALAKNPSAETVA 320
PHA03095 PHA03095
ankyrin-like protein; Provisional
597-912 4.47e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 97.79  E-value: 4.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 597 RLLLETADnpevVDVKDAKGQTPLMLAVAYGH---IDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEE-CVQMLLEQE 672
Cdd:PHA03095   32 RLLAAGAD----VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 673 ASILCKDSRGRTPLH-YAA-ARGHATWLNELLQIALseeDCCLKDNQGYTPLHwaCYNGNENC----IEVLLEQKCF--- 743
Cdd:PHA03095  108 ADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGA---DVNALDLYGMTPLA--VLLKSRNAnvelLRLLIDAGADvya 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 744 RKFIGNpfTPLH--CAIINGHESCASLLLGA-IDPsivSCRDDKGRTTLHAAAFGDHAECLQL--LLRHDAQVNAVDNSG 818
Cdd:PHA03095  183 VDDRFR--SLLHhhLQSFKPRARIVRELIRAgCDP---AATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYG 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 819 KTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDESLINAKNSALQTPLHIAARN 898
Cdd:PHA03095  258 QTPLHYAAVFNNPRACRRLIA-LGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTASVAGGDIPSD 336
                         330
                  ....*....|....
gi 1720355778 899 GLKVVVEELLAKGA 912
Cdd:PHA03095  337 ATRLCVAKVVLRGA 350
Ank_2 pfam12796
Ankyrin repeats (3 copies);
105-197 7.14e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 7.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 105 LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLgVEIDEINvYGNTALHIACYNGQDAVVN 184
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1720355778 185 ELIDYGANVNQPN 197
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
550-646 1.45e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 550 LYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLETADnpevVDVKDaKGQTPLMLAVAYGHI 629
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHL 74
                          90
                  ....*....|....*..
gi 1720355778 630 DAVSLLLEKEANVDAVD 646
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
789-885 9.24e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 9.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 789 LHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKdlnTPLHLAISKGHEKCA 868
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77
                          90
                  ....*....|....*..
gi 1720355778 869 LLILDKIQDeslINAKN 885
Cdd:pfam12796  78 KLLLEKGAD---INVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
2-209 2.09e-16

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 83.91  E-value: 2.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778   2 WLTPLHRAVASRSEEAVQVLIK-HSADVNARDKNWQTPLHVAAANKAVKCAEVII---PLLssVNV---SD-RGGRTALH 73
Cdd:cd22192    17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaaPEL--VNEpmtSDlYQGETALH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  74 HAALNGHMEMVNLLLAKGANIN------AFDKKDRRAL-----H---WAAYMGHLDVVALLINHGAEVTCKDKKGYTPLH 139
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355778 140 AAASNGQISVVKH----LLNLGVEIDEINVYgntalHIacyngqdavvnelidyganvnqPNNSGFTPLHFAAA 209
Cdd:cd22192   175 ILVLQPNKTFACQmydlILSYDKEDDLQPLD-----LV----------------------PNNQGLTPFKLAAK 221
Ank_2 pfam12796
Ankyrin repeats (3 copies);
355-428 1.01e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 1.01e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355778 355 LHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTgANVNETDDwGRTALHYAAASD 428
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSG 72
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
548-730 7.76e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 65.80  E-value: 7.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 548 TALYLAAFKGHTECVEAL-VNQGASIFVKDNVTKrTPLHASVINGHTLCLRLLLETAdnPEVVDVKDA----KGQTPLML 622
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLlKCPSCDLFQRGALGE-TALHVAALYDNLEAAVVLMEAA--PELVNEPMTsdlyQGETALHI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 623 AVAYGHIDAVSLLLEKEANVDAVDIVGcTALHRGI---------------MTGHEECVQMLLEQEASILCKDSRGRTPLH 687
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVVSPRATG-TFFRPGPknliyygehplsfaaCVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720355778 688 YAAARGHATWLNELLQIALSEE----DCCL---KDNQGYTPLHWACYNGN 730
Cdd:cd22192   175 ILVLQPNKTFACQMYDLILSYDkeddLQPLdlvPNNQGLTPFKLAAKEGN 224
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
1-208 5.24e-10

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 63.18  E-value: 5.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778   1 MWLTPLHRAVA-SRSEEAVQVLIKHSADVNARDknwqTPLHVAAANKAVKCAEVIIPLLSS---------VNVSDRG--- 67
Cdd:TIGR00870  51 LGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAISLEYVDAVEAILLHLLAAfrksgplelANDQYTSeft 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  68 -GRTALHHAALNGHMEMVNLLLAKGANINA------FDKKDRRA--------LHWAAYMGHLDVVALLINHGAEVTCKDK 132
Cdd:TIGR00870 127 pGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDsfyhgespLNAAACLGSPSIVALLSEDPADILTADS 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 133 KGYTplhaaasngqisvVKHLLNLGVEideiNVYGNTALHIACYngqdavvNELIDYGANVNQ-------PNNSGFTPLH 205
Cdd:TIGR00870 207 LGNT-------------LLHLLVMENE----FKAEYEELSCQMY-------NFALSLLDKLRDskeleviLNHQGLTPLK 262

                  ...
gi 1720355778 206 FAA 208
Cdd:TIGR00870 263 LAA 265
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
268-422 8.17e-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: 59.26  E-value: 8.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 268 NTPLHVAARHGHELLINTLITS-GADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSgqkysiVSLFSNEHVLSAGFEidt 346
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEA------APELVNEPMTSDLYQ--- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 347 pdtfGRTCLHAAAAGGNVECIKLLQSSGAD----------FHKKDKC----GRTPLHYAAANCHFHCIKALVTTGANVNE 412
Cdd:cd22192    89 ----GETALHIAVVNQNLNLVRELIARGADvvspratgtfFRPGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRA 164
                         170
                  ....*....|
gi 1720355778 413 TDDWGRTALH 422
Cdd:cd22192   165 QDSLGNTVLH 174
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
537-759 7.00e-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: 56.63  E-value: 7.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 537 VDLDIRDEKGRTALYLAAFKG-HTECVEALVNQGASIFVKDNVtkrtpLHASVINGH---TLCLRLLL----ETADNPEV 608
Cdd:TIGR00870  43 LNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTL-----LHAISLEYVdavEAILLHLLaafrKSGPLELA 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 609 VDVKDA---KGQTPLMLAVAYGHIDAVSLLLEKEANVDAVdiVGCTALHRGIM----------------TGHEECVQMLL 669
Cdd:TIGR00870 118 NDQYTSeftPGITALHLAAHRQNYEIVKLLLERGASVPAR--ACGDFFVKSQGvdsfyhgesplnaaacLGSPSIVALLS 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 670 EQEASILCKDSRGRTPLHYAAARGHATWLNELL-------------QIALSEEDCCLKDNQGYTPLHWACYNGNENCIEV 736
Cdd:TIGR00870 196 EDPADILTADSLGNTLLHLLVMENEFKAEYEELscqmynfalslldKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRL 275
                         250       260
                  ....*....|....*....|....
gi 1720355778 737 LLEQKCF-RKFIGNPFTPLHCAII 759
Cdd:TIGR00870 276 KLAIKYKqKKFVAWPNGQQLLSLY 299
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
68-96 4.31e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.12  E-value: 4.31e-06
                           10        20
                   ....*....|....*....|....*....
gi 1720355778   68 GRTALHHAALNGHMEMVNLLLAKGANINA 96
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
666-910 4.69e-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: 50.40  E-value: 4.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 666 QMLLEQEasiLCKDSRGR-TPLHYAAARGHATWLNELLQiaLSEEDCCLKDNQGYTPLHWACYNGNENCIEVLLEqkCFR 744
Cdd:cd22192     3 QMLDELH---LLQQKRISeSPLLLAAKENDVQAIKKLLK--CPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 745 KFIGNPFT--------PLHCAIINGHESCASLLL--GAidpSIVSCRDD-----KGRTTLhaAAFGDHAeclqlllrhda 809
Cdd:cd22192    76 ELVNEPMTsdlyqgetALHIAVVNQNLNLVRELIarGA---DVVSPRATgtffrPGPKNL--IYYGEHP----------- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 810 qvnavdnsgktaLMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCA------LLILDKIQDE-SLIN 882
Cdd:cd22192   140 ------------LSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVLHILVLQPNKTFAcqmydlILSYDKEDDLqPLDL 206
                         250       260
                  ....*....|....*....|....*...
gi 1720355778 883 AKNSALQTPLHIAARNGLKVVVEELLAK 910
Cdd:cd22192   207 VPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
260-422 2.02e-04

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: 45.07  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 260 IDCVDKDGNTPLHVAARHG-HELLINTLITSGA-----DTAkcgihsmfpLHLAALNAH---SDCCRKLLSSGQKYSIVS 330
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISLEYVdavEAILLHLLAAFRKSGPLE 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 331 LfsnehvlsaGFEIDTPD-TFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKC--------------GRTPLHYAAANC 395
Cdd:TIGR00870 116 L---------ANDQYTSEfTPGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLG 186
                         170       180
                  ....*....|....*....|....*..
gi 1720355778 396 HFHCIKALVTTGANVNETDDWGRTALH 422
Cdd:TIGR00870 187 SPSIVALLSEDPADILTADSLGNTLLH 213
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
384-412 2.55e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 2.55e-04
                           10        20
                   ....*....|....*....|....*....
gi 1720355778  384 GRTPLHYAAANCHFHCIKALVTTGANVNE 412
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
717-739 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 1720355778  717 QGYTPLHWACYNGNENCIEVLLE 739
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLD 23
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
666-909 2.25e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.99  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 666 QMLLEQEAS-ILCKDSRGRTPLHYAAARGHatwlNELLQIALSEEDCclKDNQGYTPLHWACYNGNENCIEVLLEQKCFR 744
Cdd:TIGR00870  35 RDLEEPKKLnINCPDRLGRSALFVAAIENE----NLELTELLLNLSC--RGAVGDTLLHAISLEYVDAVEAILLHLLAAF 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 745 KFIGNPF--------------TPLHCAIINGHESCASLLL--GAIDPSIVSCRDDK----------GRTTLHAAAFGDHA 798
Cdd:TIGR00870 109 RKSGPLElandqytseftpgiTALHLAAHRQNYEIVKLLLerGASVPARACGDFFVksqgvdsfyhGESPLNAAACLGSP 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 799 ECLQLLLRHDAQVNAVDNSGKTALMMAAEngqagavdilvnsaQADLTVKDKDLNTPLHLAiskghekcALLILDKIQD- 877
Cdd:TIGR00870 189 SIVALLSEDPADILTADSLGNTLLHLLVM--------------ENEFKAEYEELSCQMYNF--------ALSLLDKLRDs 246
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1720355778 878 ESLINAKNSALQTPLHIAARNGLKVVVEELLA 909
Cdd:TIGR00870 247 KELEVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
615-644 2.95e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 2.95e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1720355778  615 KGQTPLMLAVAYGHIDAVSLLLEKEANVDA 644
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-271 8.60e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 177.84  E-value: 8.60e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778   1 MWLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGH 80
Cdd:COG0666    20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  81 MEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEI 160
Cdd:COG0666   100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 161 DEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHM 240
Cdd:COG0666   180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEI-VKLLLEAGADLNAKDKDGLTALLL 258
                         250       260       270
                  ....*....|....*....|....*....|.
gi 1720355778 241 TAVHGRFTRSQTLIQNGGEIDCVDKDGNTPL 271
Cdd:COG0666   259 AAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
21-295 1.73e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 177.07  E-value: 1.73e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  21 LIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKK 100
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 101 DRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQD 180
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 181 AVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI 260
Cdd:COG0666   167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI-VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1720355778 261 DCVDKDGNTPLHVAARHGHELLINTLITSGADTAK 295
Cdd:COG0666   246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
51-325 3.13e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 164.74  E-value: 3.13e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  51 AEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCK 130
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 131 DKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAAS 210
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 211 THGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSG 290
Cdd:COG0666   164 GNLEI-VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1720355778 291 ADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGQK 325
Cdd:COG0666   243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
PHA03095 PHA03095
ankyrin-like protein; Provisional
14-287 4.84e-40

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 154.80  E-value: 4.84e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  14 SEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSS---VNVSDRGGRTALHHAALNGH-MEMVNLLLA 89
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLEAgadVNAPERCGFTPLHLYLYNATtLDVIKLLIK 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  90 KGANINAFDKKDRRALHwaAYMG----HLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISV--VKHLLNLGVEIDEI 163
Cdd:PHA03095  106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 164 NVYGNTALHIACYNGQD--AVVNELIDYGANVNQPNNSGFTPLHFAAA-STHGALCLELLVNNGADVNIQSKDGKSPLHM 240
Cdd:PHA03095  184 DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*..
gi 1720355778 241 TAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLI 287
Cdd:PHA03095  264 AAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
82-421 1.09e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.17  E-value: 1.09e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  82 EMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEID 161
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 162 EINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMT 241
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI-VKLLLEAGADVNAQDNDGNTPLHLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 242 AVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGADtakcgihsmfplhlaalnahsdccrklls 321
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD----------------------------- 211
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 322 sgqkysivslfsnehvlsagfeIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIK 401
Cdd:COG0666   212 ----------------------VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269
                         330       340
                  ....*....|....*....|
gi 1720355778 402 ALVTTGANVNETDDWGRTAL 421
Cdd:COG0666   270 LLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
432-706 5.57e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.86  E-value: 5.57e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 432 NKMILGNAHDNSEELERAREVKEKDAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNTGFEESDGG 511
Cdd:COG0666     8 LLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 512 AlkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVING 591
Cdd:COG0666    88 N--TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANG 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 592 HTLCLRLLLE-TADnpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLE 670
Cdd:COG0666   165 NLEIVKLLLEaGAD----VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1720355778 671 QEASILCKDSRGRTPLHYAAARGHATWLNELLQIAL 706
Cdd:COG0666   241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALL 276
PHA03100 PHA03100
ankyrin repeat protein; Provisional
4-229 6.09e-37

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 144.42  E-value: 6.09e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778   4 TPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAV-----KCAEVIIPLLSSVNVSDRGGRTALHHAALN 78
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISK 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  79 --GHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGH--LDVVALLINHGAEVTCKDKkgytplhaaasngqisvVKHLL 154
Cdd:PHA03100  117 ksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNR-----------------VNYLL 179
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720355778 155 NLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNI 229
Cdd:PHA03100  180 SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI-FKLLLNNGPSIKT 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
461-741 2.05e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 2.05e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 461 LEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNTGFEESDGGALKSPLHLAAYNGHHQALEVLLQSLVDLD 540
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 541 IRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLET-ADnpevVDVKDAKGQTP 619
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAgAD----VNAQDNDGNTP 156
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 620 LMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHATWLN 699
Cdd:COG0666   157 LHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1720355778 700 ELLQIALSEEDcclKDNQGYTPLHWACYNGNENCIEVLLEQK 741
Cdd:COG0666   237 LLLEAGADLNA---KDKDGLTALLLAAAAGAALIVKLLLLAL 275
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
564-888 1.34e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 131.23  E-value: 1.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 564 ALVNQGASIFVKDNVTKRTPLHASVINGHTLCLRLLLETADNpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVD 643
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLA---LALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 644 AVDIVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHATWLNELLQialSEEDCCLKDNQGYTPLH 723
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE---AGADVNAQDNDGNTPLH 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 724 WACYNGNENCIEVLLEqkcfrkfignpftplHCAIINGhescaslllgaidpsivscRDDKGRTTLHAAAFGDHAECLQL 803
Cdd:COG0666   159 LAAANGNLEIVKLLLE---------------AGADVNA-------------------RDNDGETPLHLAAENGHLEIVKL 204
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 804 LLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDESLINA 883
Cdd:COG0666   205 LLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE-AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283

                  ....*
gi 1720355778 884 KNSAL 888
Cdd:COG0666   284 DLLTL 288
PHA03095 PHA03095
ankyrin-like protein; Provisional
4-238 3.44e-32

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 131.30  E-value: 3.44e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778   4 TPLHRAVASRSE---EAVQVLIKHSADVNARDKNWQTPLHVAAANKAVkcaEVIIPLL----SSVNVSDRGGRTALH-HA 75
Cdd:PHA03095   49 TPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATT---LDVIKLLikagADVNAKDKVGRTPLHvYL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  76 A-LNGHMEMVNLLLAKGANINAFDKKDRRALHwaAYMGH----LDVVALLINHGAEVTCKDKKGYTPLHAAASNGQIS-- 148
Cdd:PHA03095  126 SgFNINPKVIRLLLRKGADVNALDLYGMTPLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRar 203
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 149 VVKHLLNLGVEIDEINVYGNTALHIACYNG--QDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLvNNGAD 226
Cdd:PHA03095  204 IVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLI-ALGAD 282
                         250
                  ....*....|..
gi 1720355778 227 VNIQSKDGKSPL 238
Cdd:PHA03095  283 INAVSSDGNTPL 294
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
596-921 1.77e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.07  E-value: 1.77e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 596 LRLLLETADNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQEASI 675
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 676 LCKDSRGRTPLHYAAARGHATWLNELLQialSEEDCCLKDNQGYTPLHWACYNGNENCIEVLLEQkcfrkfignpftplh 755
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA--------------- 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 756 caiinghescaslllGAiDPSIvscRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVD 835
Cdd:COG0666   143 ---------------GA-DVNA---QDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 836 ILVNsAQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIAARNGLKVVVEELLAKGACVL 915
Cdd:COG0666   204 LLLE-AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279

                  ....*.
gi 1720355778 916 AVDENA 921
Cdd:COG0666   280 AALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
217-550 4.47e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.91  E-value: 4.47e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 217 LELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGADTAKC 296
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 297 GIHSMFPLHLAALNAHSDCCRKLLSsgqkysivslfsnehvlsAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGAD 376
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLE------------------AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD 145
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 377 FHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVNETDDWGRTALHYAAASdmdrnkmilgnahdNSEELerarevkekd 456
Cdd:COG0666   146 VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAEN--------------GHLEI---------- 201
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 457 aalcLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNTGFEESDGGalKSPLHLAAYNGHHQALEVLLQSL 536
Cdd:COG0666   202 ----VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG--LTALLLAAAAGAALIVKLLLLAL 275
                         330
                  ....*....|....
gi 1720355778 537 VDLDIRDEKGRTAL 550
Cdd:COG0666   276 LLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
420-686 7.06e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.14  E-value: 7.06e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 420 ALHYAAASDMDRNKMILGNAHDNSEELERAREVKEKDAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLE 499
Cdd:COG0666    29 ALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLE 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 500 R-TNTGFEESDGGalkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNv 578
Cdd:COG0666   109 AgADVNARDKDGE---TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN- 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 579 TKRTPLHASVINGHTLCLRLLLET-ADnpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGI 657
Cdd:COG0666   185 DGETPLHLAAENGHLEIVKLLLEAgAD----VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260
                         250       260
                  ....*....|....*....|....*....
gi 1720355778 658 MTGHEECVQMLLEQEASILCKDSRGRTPL 686
Cdd:COG0666   261 AAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02874 PHA02874
ankyrin repeat protein; Provisional
4-295 1.20e-30

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 126.23  E-value: 1.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778   4 TPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVA---AANKAVKcaeviIPLLSSVNVSdrggrtALHHAALNGh 80
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAikiGAHDIIK-----LLIDNGVDTS------ILPIPCIEK- 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  81 mEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEI 160
Cdd:PHA02874  105 -DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 161 DEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHfaAASTHGALCLELLVNNgADVNIQSKDGKSPLHM 240
Cdd:PHA02874  184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLH--NAIIHNRSAIELLINN-ASINDQDIDGSTPLHH 260
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720355778 241 tAVHGRFTRS--QTLIQNGGEIDCVDKDGNTPLHVAARHGH------ELLINTLITSGADTAK 295
Cdd:PHA02874  261 -AINPPCDIDiiDILLYHKADISIKDNKGENPIDTAFKYINkdpvikDIIANAVLIKEADKLK 322
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
181-480 7.48e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.44  E-value: 7.48e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 181 AVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI 260
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 261 DCVDKDGNTPLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSsgqkysivslfsnehvlsA 340
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE------------------A 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 341 GFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVNETDDWGRTA 420
Cdd:COG0666   143 GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTA 222
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 421 LHYAAASDMDRNKMILGNAHDNSEELERAREVKEKDAALCLEFLLQNDANPSIRDKEGYN 480
Cdd:COG0666   223 LDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
PHA02876 PHA02876
ankyrin repeat protein; Provisional
51-411 1.50e-28

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 122.48  E-value: 1.50e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  51 AEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCK 130
Cdd:PHA02876  161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKN 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 131 DkkgyTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQ-DAVVNELIDYGANVNQPNNSGFTPLHFAAA 209
Cdd:PHA02876  241 D----LSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAK 316
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 210 STHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQ-TLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLIT 288
Cdd:PHA02876  317 NGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIViTLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLD 396
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 289 SGADtakcgihsmfplhLAALNahsdccrkllssgQKYSivslfsnehvlsagfeidtpdtfgrTCLHAAAAGGN-VECI 367
Cdd:PHA02876  397 YGAD-------------IEALS-------------QKIG-------------------------TALHFALCGTNpYMSV 425
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|....*
gi 1720355778 368 KLLQSSGADFHKKDKCGRTPLHYAAA-NCHFHCIKALVTTGANVN 411
Cdd:PHA02876  426 KTLIDRGANVNSKNKDLSTPLHYACKkNCKLDVIEMLLDNGADVN 470
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
338-615 1.88e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.21  E-value: 1.88e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 338 LSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVNETDDWG 417
Cdd:COG0666    74 LAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDG 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 418 RTALHYAAASdmdrnkmilgnahdNSEELerarevkekdaalcLEFLLQNDANPSIRDKEGYnsihyaaayghrqclell 497
Cdd:COG0666   154 NTPLHLAAAN--------------GNLEI--------------VKLLLEAGADVNARDNDGE------------------ 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 498 lertntgfeesdggalkSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDN 577
Cdd:COG0666   188 -----------------TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1720355778 578 VTKRTPLHASVINGHTLCLRLLLETADNPEVVDVKDAK 615
Cdd:COG0666   251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
PHA02876 PHA02876
ankyrin repeat protein; Provisional
3-313 9.02e-28

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 120.17  E-value: 9.02e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778   3 LTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDrggrTALHHAALNGHME 82
Cdd:PHA02876  179 ITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND----LSLLKAIRNEDLE 254
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  83 MVNLLLAKGANINAFDKKDRRALHWAAYMGHLD-VVALLINHGAEVTCKDKKGYTPLHAAASNG-QISVVKHLLNLGVEI 160
Cdd:PHA02876  255 TSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADV 334
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 161 DEINVYGNTALHIACY--NGQDAVVNeLIDYGANVNQPNNSGFTPLHFAAAStHGALCLELLVNNGADVNIQSKDGKSPL 238
Cdd:PHA02876  335 NAADRLYITPLHQASTldRNKDIVIT-LLELGANVNARDYCDKTPIHYAAVR-NNVVIINTLLDYGADIEALSQKIGTAL 412
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355778 239 HMtAVHGR--FTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHEL-LINTLITSGADTAKCGIHSMFPLhLAALNAHS 313
Cdd:PHA02876  413 HF-ALCGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAINIQNQYPL-LIALEYHG 488
PHA02878 PHA02878
ankyrin repeat protein; Provisional
3-274 2.73e-26

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 113.82  E-value: 2.73e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778   3 LTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVA--AANKavkcaEVIIPLLSSVNVSDRG-GRTALHHAALNG 79
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckEPNK-----LGMKEMIRSINKCSVFyTLVAIKDAFNNR 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  80 HMEMVNLLLakganINAFDKK---DRRALHWAAYMGHLD--VVALLINHGAEVTCKDK-KGYTPLHAAASNGQISVVKHL 153
Cdd:PHA02878  113 NVEIFKIIL-----TNRYKNIqtiDLVYIDKKSKDDIIEaeITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELL 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 154 LNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSK- 232
Cdd:PHA02878  188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYi 267
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1720355778 233 DGKSPLHMTAVHGRFTRsqTLIQNGGEIDCVDKDGNTPLHVA 274
Cdd:PHA02878  268 LGLTALHSSIKSERKLK--LLLEYGADINSLNSYKLTPLSSA 307
PHA03095 PHA03095
ankyrin-like protein; Provisional
140-421 6.67e-26

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 112.43  E-value: 6.67e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 140 AAASNGQISVVKHLLNLGVEIDEINVYGNTALH--IACYNGQDA-VVNELIDYGANVNQPNNSGFTPLHFAAASTHGALC 216
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHlyLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDV 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 217 LELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAAR-HGHEL-LINTLITSGAD 292
Cdd:PHA03095  100 IKLLIKAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKsRNANVeLLRLLIDAGAD 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 293 TAKCGIHSMFPLHLAALNAHSDccrkllssgqkYSIVslfsnEHVLSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQ- 371
Cdd:PHA03095  180 VYAVDDRFRSLLHHHLQSFKPR-----------ARIV-----RELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPl 243
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720355778 372 -SSGADFHKKDKCGRTPLHYAAA--NCHF--HCIKAlvttGANVNETDDWGRTAL 421
Cdd:PHA03095  244 lIAGISINARNRYGQTPLHYAAVfnNPRAcrRLIAL----GADINAVSSDGNTPL 294
PHA03100 PHA03100
ankyrin repeat protein; Provisional
120-411 2.25e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 110.14  E-value: 2.25e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 120 LINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIAC---YNGQDAV--VNELIDYGANVN 194
Cdd:PHA03100   21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikYNLTDVKeiVKLLLEYGANVN 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 195 QPNNSGFTPLHFAAASTHGALCL-ELLVNNGADVNIQSKDGKSPLHMtavhgrFTRSqtliqnggeiDCVDKDgntplhv 273
Cdd:PHA03100  101 APDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHL------YLES----------NKIDLK------- 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 274 aarhghelLINTLITSGADtakcgihsmfplhlaaLNAhsdCCRkllssgqkysiVSLFsnehvLSAGFEIDTPDTFGRT 353
Cdd:PHA03100  158 --------ILKLLIDKGVD----------------INA---KNR-----------VNYL-----LSYGVPINIKDVYGFT 194
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355778 354 CLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVN 411
Cdd:PHA03100  195 PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02876 PHA02876
ankyrin repeat protein; Provisional
3-292 3.02e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 109.00  E-value: 3.02e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778   3 LTPLHRAVASRSEEAVQVLIKHSADVNARDKNwqtpLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHM- 81
Cdd:PHA02876  212 LSVLECAVDSKNIDTIKAIIDNRSNINKNDLS----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLs 287
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  82 EMVNLLLAKGANINAFDKKDRRALHWAAYMGH-LDVVALLINHGAEVTCKDKKGYTPLHAAAS-NGQISVVKHLLNLGVE 159
Cdd:PHA02876  288 RLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGAN 367
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 160 IDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELLVNNGADVNIQSKDGKSPLH 239
Cdd:PHA02876  368 VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLH 447
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720355778 240 MTAVHG-RFTRSQTLIQNGGEIDCVDKDGNTPLHVAArhGHELLINTLITSGAD 292
Cdd:PHA02876  448 YACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAE 499
PHA02874 PHA02874
ankyrin repeat protein; Provisional
61-292 4.01e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 100.42  E-value: 4.01e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  61 VNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAE-------------- 126
Cdd:PHA02874   28 INISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDtsilpipciekdmi 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 127 ---------VTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPN 197
Cdd:PHA02874  108 ktildcgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 198 NSGFTPLHFAAASTHGAlCLELLVNNGADVNIQSKDGKSPLHMTAVHGRftRSQTLIQNGGEIDCVDKDGNTPLHVAARH 277
Cdd:PHA02874  188 NNGESPLHNAAEYGDYA-CIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR--SAIELLINNASINDQDIDGSTPLHHAINP 264
                         250
                  ....*....|....*.
gi 1720355778 278 GHEL-LINTLITSGAD 292
Cdd:PHA02874  265 PCDIdIIDILLYHKAD 280
PHA03095 PHA03095
ankyrin-like protein; Provisional
283-610 5.41e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 100.48  E-value: 5.41e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 283 INTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRkllssgqkysIVSLfsnehVLSAGFEIDTPDTFGRTCLHAAAAGG 362
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKD----------IVRL-----LLEAGADVNAPERCGFTPLHLYLYNA 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 363 NVE-CIKLLQSSGADFHKKDKCGRTPLH-YAA-ANCHFHCIKALVTTGANVNETDDWGRTALHyaaasdmdrnkmILGNA 439
Cdd:PHA03095   95 TTLdVIKLLIKAGADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLA------------VLLKS 162
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 440 HDNSEELerarevkekdaalcLEFLLQNDANPSIRDKEGYNSIHYAAAYGH--RQCLELLLERTNTGFEESDGGalKSPL 517
Cdd:PHA03095  163 RNANVEL--------------LRLLIDAGADVYAVDDRFRSLLHHHLQSFKprARIVRELIRAGCDPAATDMLG--NTPL 226
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 518 HLAAYNGHHQALEV--LLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLC 595
Cdd:PHA03095  227 HSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSS-DGNTPLSLMVRNNNGRA 305
                         330
                  ....*....|....*
gi 1720355778 596 LRLLLETADNPEVVD 610
Cdd:PHA03095  306 VRAALAKNPSAETVA 320
PHA02874 PHA02874
ankyrin repeat protein; Provisional
251-553 2.02e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 98.11  E-value: 2.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 251 QTLIQNGGE-IDCVDKDGNTPLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGQKYSIV 329
Cdd:PHA02874   18 EKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 330 SL--FSNEHV---LSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALV 404
Cdd:PHA02874   98 PIpcIEKDMIktiLDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 405 TTGANVNETDDWGRTALHYAaasdmdrnkmilgnahdnseelerareVKEKDAAlCLEFLLQNDANPSIRDKEGYNSIHY 484
Cdd:PHA02874  178 EKGAYANVKDNNGESPLHNA---------------------------AEYGDYA-CIKLLIDHGNHIMNKCKNGFTPLHN 229
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 485 AAAYgHRQCLELLLERTNTGFEESDGgalKSPLHLA-AYNGHHQALEVLLQSLVDLDIRDEKGRTALYLA 553
Cdd:PHA02874  230 AIIH-NRSAIELLINNASINDQDIDG---STPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
PHA03095 PHA03095
ankyrin-like protein; Provisional
597-912 4.47e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 97.79  E-value: 4.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 597 RLLLETADnpevVDVKDAKGQTPLMLAVAYGH---IDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEE-CVQMLLEQE 672
Cdd:PHA03095   32 RLLAAGAD----VNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 673 ASILCKDSRGRTPLH-YAA-ARGHATWLNELLQIALseeDCCLKDNQGYTPLHwaCYNGNENC----IEVLLEQKCF--- 743
Cdd:PHA03095  108 ADVNAKDKVGRTPLHvYLSgFNINPKVIRLLLRKGA---DVNALDLYGMTPLA--VLLKSRNAnvelLRLLIDAGADvya 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 744 RKFIGNpfTPLH--CAIINGHESCASLLLGA-IDPsivSCRDDKGRTTLHAAAFGDHAECLQL--LLRHDAQVNAVDNSG 818
Cdd:PHA03095  183 VDDRFR--SLLHhhLQSFKPRARIVRELIRAgCDP---AATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYG 257
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 819 KTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDESLINAKNSALQTPLHIAARN 898
Cdd:PHA03095  258 QTPLHYAAVFNNPRACRRLIA-LGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTASVAGGDIPSD 336
                         330
                  ....*....|....
gi 1720355778 899 GLKVVVEELLAKGA 912
Cdd:PHA03095  337 ATRLCVAKVVLRGA 350
Ank_2 pfam12796
Ankyrin repeats (3 copies);
105-197 7.14e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 7.14e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 105 LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLgVEIDEINvYGNTALHIACYNGQDAVVN 184
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1720355778 185 ELIDYGANVNQPN 197
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
72-164 2.38e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 2.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  72 LHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHgAEVTCKDkKGYTPLHAAASNGQISVVK 151
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1720355778 152 HLLNLGVEIDEIN 164
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
325-610 3.99e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 93.96  E-value: 3.99e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 325 KYSIVSLFSNEHVLSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCH-----FHC 399
Cdd:PHA03100    9 KSRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEI 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 400 IKALVTTGANVNETDDWGRTALHYAAASDMDRNKMIlgnahdnseelerarevkekdaalclEFLLQNDANPSIRDKEGY 479
Cdd:PHA03100   89 VKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIV--------------------------EYLLDNGANVNIKNSDGE 142
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 480 NSIHYAAAYGHR--QCLELLLERTNtgfeesdggalksplHLAAYNghhqALEVLLQSLVDLDIRDEKGRTALYLAAFKG 557
Cdd:PHA03100  143 NLLHLYLESNKIdlKILKLLIDKGV---------------DINAKN----RVNYLLSYGVPINIKDVYGFTPLHYAVYNN 203
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720355778 558 HTECVEALVNQGASIFVKDNVTKrTPLHASVINGHTLCLRLLLETADNPEVVD 610
Cdd:PHA03100  204 NPEFVKYLLDLGANPNLVNKYGD-TPLHIAILNNNKEIFKLLLNNGPSIKTII 255
PHA02875 PHA02875
ankyrin repeat protein; Provisional
3-194 4.88e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 93.90  E-value: 4.88e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778   3 LTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVN-VSDRGGRTALHHAALNGHM 81
Cdd:PHA02875   36 ISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  82 EMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEID 161
Cdd:PHA02875  116 DIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1720355778 162 EINVYGN-TALHIACYNGQDAVVNELIDYGANVN 194
Cdd:PHA02875  196 YFGKNGCvAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02876 PHA02876
ankyrin repeat protein; Provisional
110-642 7.49e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 95.13  E-value: 7.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 110 YMGHLDVVALLIN-----HGAEvTCKDKK-GYTPLHAAASNGQISVVKHLLNLGVEIDEINVYG-NTALHIACY--NGQD 180
Cdd:PHA02876   12 RGNCIDILSAIDNydlhkHGAN-QCENESiPFTAIHQALQLRQIDIVEEIIQQNPELIYITDHKcHSTLHTICIipNVMD 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 181 AVVNELIDYGANVNQPNNSGFTPLHfaaasTHGALCLELLVN--NGADVNIqSKDGKSPLHMTAVHGRFTR-----SQTL 253
Cdd:PHA02876   91 IVISLTLDCDIILDIKYASIILNKH-----KLDEACIHILKEaiSGNDIHY-DKINESIEYMKLIKERIQQdelliAEML 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 254 IQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLS-----SGQKYSI 328
Cdd:PHA02876  165 LEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDnrsniNKNDLSL 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 329 VSLFSNEH------VLSAGFEIDTPDTFGRTCLHAAAAGGNVECI--KLLQsSGADFHKKDKCGRTPLHYAAANCH-FHC 399
Cdd:PHA02876  245 LKAIRNEDletsllLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvpKLLE-RGADVNAKNIKGETPLYLMAKNGYdTEN 323
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 400 IKALVTTGANVNETDDWGRTALHyaAASDMDRNKMILGNahdnseelerarevkekdaalclefLLQNDANPSIRDKEGY 479
Cdd:PHA02876  324 IRTLIMLGADVNAADRLYITPLH--QASTLDRNKDIVIT-------------------------LLELGANVNARDYCDK 376
                         410       420       430       440       450       460       470       480
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 480 NSIHYAAAYGHRQCLELLLertntgfeesDGGAlksplhlaaynghhqalevllqslvDLDIRDEKGRTALYLAAFKGHT 559
Cdd:PHA02876  377 TPIHYAAVRNNVVIINTLL----------DYGA-------------------------DIEALSQKIGTALHFALCGTNP 421
                         490       500       510       520       530       540       550       560
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 560 -ECVEALVNQGASIFVKdNVTKRTPLHASVINGHTL-CLRLLLetaDNPEVVDVKDAKGQTPLMLAVAYGHIdaVSLLLE 637
Cdd:PHA02876  422 yMSVKTLIDRGANVNSK-NKDLSTPLHYACKKNCKLdVIEMLL---DNGADVNAINIQNQYPLLIALEYHGI--VNILLH 495

                  ....*
gi 1720355778 638 KEANV 642
Cdd:PHA02876  496 YGAEL 500
PHA03100 PHA03100
ankyrin repeat protein; Provisional
3-166 9.09e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 93.19  E-value: 9.09e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778   3 LTPLH-----RAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKavKCAEVIIPLLSS----VNVSDRGGRTALH 73
Cdd:PHA03100   69 STPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKK--SNSYSIVEYLLDnganVNIKNSDGENLLH 146
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  74 HAALNGH--MEMVNLLLAKGANINAFDK-------------KDRR---ALHWAAYMGHLDVVALLINHGAEVTCKDKKGY 135
Cdd:PHA03100  147 LYLESNKidLKILKLLIDKGVDINAKNRvnyllsygvpiniKDVYgftPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD 226
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1720355778 136 TPLHAAASNGQISVVKHLLNLGVEIDEINVY 166
Cdd:PHA03100  227 TPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
Ank_2 pfam12796
Ankyrin repeats (3 copies);
39-131 4.68e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 4.68e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  39 LHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKgANINAFDkKDRRALHWAAYMGHLDVVA 118
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1720355778 119 LLINHGAEVTCKD 131
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
6-98 7.40e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.09  E-value: 7.40e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778   6 LHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEViipLLSSVNVSDRG-GRTALHHAALNGHMEMV 84
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKL---LLEHADVNLKDnGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 1720355778  85 NLLLAKGANINAFD 98
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
550-646 1.45e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.45e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 550 LYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLCLRLLLETADnpevVDVKDaKGQTPLMLAVAYGHI 629
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEHAD----VNLKD-NGRTALHYAARSGHL 74
                          90
                  ....*....|....*..
gi 1720355778 630 DAVSLLLEKEANVDAVD 646
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
138-230 1.74e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 1.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 138 LHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYgANVNQPNNsGFTPLHFAAASTHGAlCL 217
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE-IV 77
                          90
                  ....*....|...
gi 1720355778 218 ELLVNNGADVNIQ 230
Cdd:pfam12796  78 KLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
517-610 5.60e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 5.60e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 517 LHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQgasIFVKDNVTKRTPLHASVINGHTLCL 596
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 1720355778 597 RLLLETADNPEVVD 610
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
517-792 1.48e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 86.56  E-value: 1.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 517 LHLAAYNGHHQALEVLLQSLVD-LDIRDEKGRTALYLAAFKGHTECVEALVNQGASIfvkDNVTKRTP---LHASVINGH 592
Cdd:PHA02874    5 LRMCIYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADI---NHINTKIPhplLTAIKIGAH 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 593 TLCLRLLLETADN-----PEV--------------VDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTAL 653
Cdd:PHA02874   82 DIIKLLIDNGVDTsilpiPCIekdmiktildcgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPI 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 654 HRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHATWLNELLQialSEEDCCLKDNQGYTPLHWACYNgNENC 733
Cdd:PHA02874  162 HIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLID---HGNHIMNKCKNGFTPLHNAIIH-NRSA 237
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355778 734 IEVLLEQKCFRKFIGNPFTPLHCAIingHESCA-----SLLLGAIDPSIvscRDDKGRTTLHAA 792
Cdd:PHA02874  238 IELLINNASINDQDIDGSTPLHHAI---NPPCDidiidILLYHKADISI---KDNKGENPIDTA 295
PHA02874 PHA02874
ankyrin repeat protein; Provisional
144-491 4.37e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 85.02  E-value: 4.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 144 NGQISVVKHLLN-----LGVEIDEINvygnTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLhFAAASTHGALCLE 218
Cdd:PHA02874   11 SGDIEAIEKIIKnkgncINISVDETT----TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPL-LTAIKIGAHDIIK 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 219 LLVNNGADVNIqskdgkspLHMTAVHGRFTRsqTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGADTAKCGI 298
Cdd:PHA02874   86 LLIDNGVDTSI--------LPIPCIEKDMIK--TILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDD 155
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 299 HSMFPLHLAalnahsdccrkllSSGQKYSIVSLfsnehVLSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFH 378
Cdd:PHA02874  156 NGCYPIHIA-------------IKHNFFDIIKL-----LLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIM 217
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 379 KKDKCGRTPLHYAAanCHFHCIKALVTTGANVNETDDWGRTALHYAAASDMDRNkmilgnahdnseelerarevkekdaa 458
Cdd:PHA02874  218 NKCKNGFTPLHNAI--IHNRSAIELLINNASINDQDIDGSTPLHHAINPPCDID-------------------------- 269
                         330       340       350
                  ....*....|....*....|....*....|...
gi 1720355778 459 lCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHR 491
Cdd:PHA02874  270 -IIDILLYHKADISIKDNKGENPIDTAFKYINK 301
PHA02875 PHA02875
ankyrin repeat protein; Provisional
461-673 8.83e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 83.89  E-value: 8.83e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 461 LEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLerTNTGFEESDGGALKSPLHLAAYNGHHQALEVLLQS--LVD 538
Cdd:PHA02875   18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLM--KHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLgkFAD 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 539 lDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKdNVTKRTPLHASVINGHTLCLRLLLetaDNPEVVDVKDAKGQT 618
Cdd:PHA02875   96 -DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP-NTDKFSPLHLAVMMGDIKGIELLI---DHKACLDIEDCCGCT 170
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355778 619 PLMLAVAYGHIDAVSLLLEKEANVDAVDIVGC-TALHRGIMTGHEECVQMLLEQEA 673
Cdd:PHA02875  171 PLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGA 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
789-885 9.24e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 9.24e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 789 LHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKdlnTPLHLAISKGHEKCA 868
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR---TALHYAARSGHLEIV 77
                          90
                  ....*....|....*..
gi 1720355778 869 LLILDKIQDeslINAKN 885
Cdd:pfam12796  78 KLLLEKGAD---INVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
2-209 2.09e-16

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 83.91  E-value: 2.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778   2 WLTPLHRAVASRSEEAVQVLIK-HSADVNARDKNWQTPLHVAAANKAVKCAEVII---PLLssVNV---SD-RGGRTALH 73
Cdd:cd22192    17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMeaaPEL--VNEpmtSDlYQGETALH 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  74 HAALNGHMEMVNLLLAKGANIN------AFDKKDRRAL-----H---WAAYMGHLDVVALLINHGAEVTCKDKKGYTPLH 139
Cdd:cd22192    95 IAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLiyygeHplsFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355778 140 AAASNGQISVVKH----LLNLGVEIDEINVYgntalHIacyngqdavvnelidyganvnqPNNSGFTPLHFAAA 209
Cdd:cd22192   175 ILVLQPNKTFACQmydlILSYDKEDDLQPLD-----LV----------------------PNNQGLTPFKLAAK 221
PHA02875 PHA02875
ankyrin repeat protein; Provisional
69-301 2.37e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 82.35  E-value: 2.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  69 RTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQIS 148
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 149 VVKHLLNLGVEIDEInVY--GNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGAD 226
Cdd:PHA02875   83 AVEELLDLGKFADDV-FYkdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG-IELLIDHKAC 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355778 227 VNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHEL-LINTLITSGADtakCGIHSM 301
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIdIVRLFIKRGAD---CNIMFM 233
PHA02798 PHA02798
ankyrin-like protein; Provisional
6-292 5.21e-16

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 81.80  E-value: 5.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778   6 LHRAvaSRSEEAVQVLIKHSADVNARDKNWQTPLhvaaankavkCAeviipLLSsvNVSDrggrtalhhaaLNGHMEMVN 85
Cdd:PHA02798   44 LQRD--SPSTDIVKLFINLGANVNGLDNEYSTPL----------CT-----ILS--NIKD-----------YKHMLDIVK 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  86 LLLAKGANINAFDKKDRRALHWA---AYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNG---QISVVKHLLNLGVE 159
Cdd:PHA02798   94 ILIENGADINKKNSDGETPLYCLlsnGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVD 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 160 IDEI-NVYGNTALHiaCY-----NGQDA-VVNELIDYGANVNQPNNSgftplhfaAASTHGALCLELLVNNG-------- 224
Cdd:PHA02798  174 INTHnNKEKYDTLH--CYfkyniDRIDAdILKLFVDNGFIINKENKS--------HKKKFMEYLNSLLYDNKrfkknild 243
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720355778 225 ---ADVNIQSKD--GKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGAD 292
Cdd:PHA02798  244 fifSYIDINQVDelGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPN 316
PHA02876 PHA02876
ankyrin repeat protein; Provisional
335-689 6.35e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 82.42  E-value: 6.35e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 335 EHVLSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVNetd 414
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN--- 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 415 dwgrtalhyaaasdmdRNKMILGNAHDNsEELERArevkekdaalclefLLQNDANPSIRDKEGYNSihyaaayghrqcl 494
Cdd:PHA02876  239 ----------------KNDLSLLKAIRN-EDLETS--------------LLLYDAGFSVNSIDDCKN------------- 274
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 495 elllertntgfeesdggalkSPLHLAAYNGHHQAL-EVLLQSLVDLDIRDEKGRTALYLAAFKGH-TECVEALVNQGASI 572
Cdd:PHA02876  275 --------------------TPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADV 334
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 573 FVKDNVTKrTPLH-ASVINGHTLCLRLLLETADNpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCT 651
Cdd:PHA02876  335 NAADRLYI-TPLHqASTLDRNKDIVITLLELGAN---VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGT 410
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1720355778 652 ALHRGIM-TGHEECVQMLLEQEASILCKDSRGRTPLHYA 689
Cdd:PHA02876  411 ALHFALCgTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449
Ank_2 pfam12796
Ankyrin repeats (3 copies);
653-742 7.50e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.61  E-value: 7.50e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 653 LHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHAtwlnELLQIALSEEDCCLKDNqGYTPLHWACYNGNEN 732
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHL----EIVKLLLEHADVNLKDN-GRTALHYAARSGHLE 75
                          90
                  ....*....|
gi 1720355778 733 CIEVLLEQKC 742
Cdd:pfam12796  76 IVKLLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
482-576 8.51e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.61  E-value: 8.51e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 482 IHYAAAYGHRQCLELLLE-RTNTGFEESDGgalKSPLHLAAYNGHHQALEVLLQSlVDLDIRDEkGRTALYLAAFKGHTE 560
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEnGADANLQDKNG---RTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLE 75
                          90
                  ....*....|....*.
gi 1720355778 561 CVEALVNQGASIFVKD 576
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
355-428 1.01e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.23  E-value: 1.01e-15
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355778 355 LHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTgANVNETDDwGRTALHYAAASD 428
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSG 72
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
495-677 1.30e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 81.45  E-value: 1.30e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 495 ELLLERTntgfEESDGGALKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFV 574
Cdd:PLN03192  511 DLLGDNG----GEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI 586
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 575 KDnVTKRTPLHASVINGHTLCLRLL--LETADNPEVvdvkdakGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTA 652
Cdd:PLN03192  587 RD-ANGNTALWNAISAKHHKIFRILyhFASISDPHA-------AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
                         170       180
                  ....*....|....*....|....*
gi 1720355778 653 LHRGIMTGHEECVQMLLEQEASILC 677
Cdd:PLN03192  659 LQVAMAEDHVDMVRLLIMNGADVDK 683
Ank_2 pfam12796
Ankyrin repeats (3 copies);
722-815 1.48e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.84  E-value: 1.48e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 722 LHWACYNGNENCIEVLLEQKC-FRKFIGNPFTPLHCAIINGHESCASLLLGAIDPSIvscrDDKGRTTLHAAAFGDHAEC 800
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL----KDNGRTALHYAARSGHLEI 76
                          90
                  ....*....|....*
gi 1720355778 801 LQLLLRHDAQVNAVD 815
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
443-854 3.87e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 79.72  E-value: 3.87e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 443 SEELERAREVKEK---DAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLER-TNTGFEESDGgalkspLH 518
Cdd:PHA02876  140 NESIEYMKLIKERiqqDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYgADVNIIALDD------LS 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 519 LAAYNGHHQALEVLlQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDnVTKRTPLHASVINGH--TLCL 596
Cdd:PHA02876  214 VLECAVDSKNIDTI-KAIIDNRSNINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSID-DCKNTPLHHASQAPSlsRLVP 291
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 597 RLLLETADnpevVDVKDAKGQTPLMLAVAYGH-IDAVSLLLEKEANVDAVDIVGCTALHRG-IMTGHEECVQMLLEQEAS 674
Cdd:PHA02876  292 KLLERGAD----VNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGAN 367
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 675 ILCKDSRGRTPLHYAAARGHATWLNELLQIALSEEdcCLKDNQGyTPLHWACYNgnencievlleqkcfrkfiGNPFTPL 754
Cdd:PHA02876  368 VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIE--ALSQKIG-TALHFALCG-------------------TNPYMSV 425
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 755 HCAIINGHEscaslllgaidpsiVSCRDDKGRTTLHAAAFGD-HAECLQLLLRHDAQVNAVDNSGKTALMMAAenGQAGA 833
Cdd:PHA02876  426 KTLIDRGAN--------------VNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGI 489
                         410       420
                  ....*....|....*....|...
gi 1720355778 834 VDILVNSAQA--DLTVKDKDLNT 854
Cdd:PHA02876  490 VNILLHYGAElrDSRVLHKSLND 512
PHA02874 PHA02874
ankyrin repeat protein; Provisional
513-689 1.29e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 77.31  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 513 LKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNVTKrTPLHASVINGH 592
Cdd:PHA02874  124 LKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGE-SPLHNAAEYGD 202
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 593 TLCLRLLLETADNpevVDVKDAKGQTPLMLAVAYGHiDAVSLLLeKEANVDAVDIVGCTALHRGIMTG-HEECVQMLLEQ 671
Cdd:PHA02874  203 YACIKLLIDHGNH---IMNKCKNGFTPLHNAIIHNR-SAIELLI-NNASINDQDIDGSTPLHHAINPPcDIDIIDILLYH 277
                         170
                  ....*....|....*...
gi 1720355778 672 EASILCKDSRGRTPLHYA 689
Cdd:PHA02874  278 KADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
304-414 1.30e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 304 LHLAALNAHSDCCRKLLSSGqkysivslfsnehvlsagFEIDTPDTFGRTCLHAAAAGGNVECIKLLqSSGADFHKKDKc 383
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG------------------ADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDN- 60
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1720355778 384 GRTPLHYAAANCHFHCIKALVTTGANVNETD 414
Cdd:pfam12796  61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
620-694 1.51e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.76  E-value: 1.51e-14
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720355778 620 LMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQEAsiLCKDSRGRTPLHYAAARGH 694
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGH 73
PHA02876 PHA02876
ankyrin repeat protein; Provisional
563-918 2.92e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.03  E-value: 2.92e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 563 EALVNQGASIFVKDnVTKRTPLHASVINGHTLCLRLLLETADNPEVVDVKDAkgqTPLMLAVAYGHIDAVSLLLEKEANV 642
Cdd:PHA02876  162 EMLLEGGADVNAKD-IYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDL---SVLECAVDSKNIDTIKAIIDNRSNI 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 643 DAVDIvgctALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAargHATWLNELLQIALSE-EDCCLKDNQGYTP 721
Cdd:PHA02876  238 NKNDL----SLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHAS---QAPSLSRLVPKLLERgADVNAKNIKGETP 310
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 722 LHWACYNGNENcievlleqkcfrkfignpftplhcaiinghESCASLLLGAIDpsiVSCRDDKGRTTLHAAAFGD-HAEC 800
Cdd:PHA02876  311 LYLMAKNGYDT------------------------------ENIRTLIMLGAD---VNAADRLYITPLHQASTLDrNKDI 357
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 801 LQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCALLILdkIQDESL 880
Cdd:PHA02876  358 VITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG-ADIEALSQKIGTALHFALCGTNPYMSVKTL--IDRGAN 434
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1720355778 881 INAKNSALQTPLHIAARNGLKV-VVEELLAKGACVLAVD 918
Cdd:PHA02876  435 VNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAIN 473
Ank_2 pfam12796
Ankyrin repeats (3 copies);
686-770 3.22e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.99  E-value: 3.22e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 686 LHYAAARGHATWLNELLQialSEEDCCLKDNQGYTPLHWACYNGNENCIEVLLEQKCFRKFiGNPFTPLHCAIINGHESC 765
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLE---NGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK-DNGRTALHYAARSGHLEI 76

                  ....*
gi 1720355778 766 ASLLL 770
Cdd:pfam12796  77 VKLLL 81
PHA02875 PHA02875
ankyrin repeat protein; Provisional
101-336 3.57e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 75.80  E-value: 3.57e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 101 DRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVeIDEINVYG-NTALHIACYNGQ 179
Cdd:PHA02875    2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDiESELHDAVEEGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 180 DAVVNELIDYGANVNQP-NNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGG 258
Cdd:PHA02875   81 VKAVEELLDLGKFADDVfYKDGMTPLHLATILKKLDI-MKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKA 159
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355778 259 EIDCVDKDGNTPLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAAL-NAHSDCCRKLLSSGQKYSIVSLFSNEH 336
Cdd:PHA02875  160 CLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIeNNKIDIVRLFIKRGADCNIMFMIEGEE 238
PHA02876 PHA02876
ankyrin repeat protein; Provisional
530-912 5.76e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.26  E-value: 5.76e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 530 EVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGA--SIFVKDNVTKrtpLHASVINGHTLCLRLLLETADNPE 607
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGAdvNIIALDDLSV---LECAVDSKNIDTIKAIIDNRSNIN 238
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 608 vvdvkdaKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGH-EECVQMLLEQEASILCKDSRGRTPL 686
Cdd:PHA02876  239 -------KNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPL 311
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 687 HYAAARGHATwlNELLQIALSEEDCCLKDNQGYTPLHWA-CYNGNENCIEVLLEqkcfrkfignpftplhcaiinghesc 765
Cdd:PHA02876  312 YLMAKNGYDT--ENIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLE-------------------------- 363
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 766 asllLGAidpsIVSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMA-AENGQAGAVDILVNSAqAD 844
Cdd:PHA02876  364 ----LGA----NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRG-AN 434
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355778 845 LTVKDKDLNTPLHLAISKgheKCALLILDKIQDESL-INAKNSALQTPLHIAArnGLKVVVEELLAKGA 912
Cdd:PHA02876  435 VNSKNKDLSTPLHYACKK---NCKLDVIEMLLDNGAdVNAINIQNQYPLLIAL--EYHGIVNILLHYGA 498
PHA02876 PHA02876
ankyrin repeat protein; Provisional
666-919 9.24e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 75.49  E-value: 9.24e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 666 QMLLEQEASILCKDSRGRTPLHYAAARGHATWLNELLQIAlseEDCCLKDNQGYTPLHWACYNGNENCIEVLLEQkcfRK 745
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYG---ADVNIIALDDLSVLECAVDSKNIDTIKAIIDN---RS 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 746 FIGNPFTPLHCAIINgHESCASLLLGAIDPSIVSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMA 825
Cdd:PHA02876  236 NINKNDLSLLKAIRN-EDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLM 314
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 826 AENGQAGAVDILVNSAQADLTVKDKDLNTPLHLAISKGHEKCALLILdkIQDESLINAKNSALQTPLHIAARNGLKVVVE 905
Cdd:PHA02876  315 AKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKDIVITL--LELGANVNARDYCDKTPIHYAAVRNNVVIIN 392
                         250
                  ....*....|....
gi 1720355778 906 ELLAKGACVLAVDE 919
Cdd:PHA02876  393 TLLDYGADIEALSQ 406
PHA02878 PHA02878
ankyrin repeat protein; Provisional
161-496 1.17e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 74.53  E-value: 1.17e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 161 DEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALCLELL-VNNGADVNIQSKDGKSPLH 239
Cdd:PHA02878   31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIrSINKCSVFYTLVAIKDAFN 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 240 MTAVH-------GRFTRSQTLiqNGGEIDCVDKDGNTPLHVaarhghellINTLITSGADTAKCGIHSM-FPLHLAALNA 311
Cdd:PHA02878  111 NRNVEifkiiltNRYKNIQTI--DLVYIDKKSKDDIIEAEI---------TKLLLSYGADINMKDRHKGnTALHYATENK 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 312 HSDCCRKLLSSGQkysivslfsnehvlsagfEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYA 391
Cdd:PHA02878  180 DQRLTELLLSYGA------------------NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 392 AANC-HFHCIKALVTTGANVN-ETDDWGRTALHYAAASDmDRNKMILG-----NAHDNSEELERAREVKEKDAALCLEFL 464
Cdd:PHA02878  242 VGYCkDYDILKLLLEHGVDVNaKSYILGLTALHSSIKSE-RKLKLLLEygadiNSLNSYKLTPLSSAVKQYLCINIGRIL 320
                         330       340       350
                  ....*....|....*....|....*....|....*..
gi 1720355778 465 -----LQNDANPSIRDKEGYnSIHYAAAYGHRQCLEL 496
Cdd:PHA02878  321 isnicLLKRIKPDIKNSEGF-IDNMDCITSNKRLNQI 356
PHA02875 PHA02875
ankyrin repeat protein; Provisional
182-411 2.67e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 73.10  E-value: 2.67e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 182 VVNELIDYGANVNQPNNSGFTPLHFAAaSTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEI- 260
Cdd:PHA02875   17 IARRLLDIGINPNFEIYDGISPIKLAM-KFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAd 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 261 DCVDKDGNTPLHVAARHGHELLINTLITSGADTakcgihsmfplhlaalnahsdccrkllssgqkysivslfsnehvlsa 340
Cdd:PHA02875   96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADP----------------------------------------------- 128
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720355778 341 gfeiDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVN 411
Cdd:PHA02875  129 ----DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
Ank_2 pfam12796
Ankyrin repeats (3 copies);
822-918 2.85e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.29  E-value: 2.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 822 LMMAAENGQAGAVDILVNSaQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQdeslINAKNSAlQTPLHIAARNGLK 901
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD----VNLKDNG-RTALHYAARSGHL 74
                          90
                  ....*....|....*..
gi 1720355778 902 VVVEELLAKGACVLAVD 918
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
538-770 6.13e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.01  E-value: 6.13e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 538 DLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLclrllletADNPEVVDvkdakgq 617
Cdd:PHA03100   27 LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTK-NNSTPLHYLSNIKYNL--------TDVKEIVK------- 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 618 tplmlavayghidavsLLLEKEANVDAVDIVGCTALHRGIMT--GHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHA 695
Cdd:PHA03100   91 ----------------LLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKI 154
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 696 TwlNELLQIALS---------EEDCCL--------KDNQGYTPLHWACYNGNENCIEVLLEQKCF---RKFIGNpfTPLH 755
Cdd:PHA03100  155 D--LKILKLLIDkgvdinaknRVNYLLsygvpiniKDVYGFTPLHYAVYNNNPEFVKYLLDLGANpnlVNKYGD--TPLH 230
                         250
                  ....*....|....*
gi 1720355778 756 CAIINGHESCASLLL 770
Cdd:PHA03100  231 IAILNNNKEIFKLLL 245
PHA02878 PHA02878
ankyrin repeat protein; Provisional
94-391 9.85e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.45  E-value: 9.85e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  94 INAFDKKDRRA----------LHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEI 163
Cdd:PHA02878   20 IEYIDHTENYStsaslipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVF 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 164 NVYgnTALHIACYNGQDAVVNE-LIDYGANVNQPNNSGFTPLHFAAASThgALCLELLVNNGADVNIQSKD-GKSPLHMT 241
Cdd:PHA02878  100 YTL--VAIKDAFNNRNVEIFKIiLTNRYKNIQTIDLVYIDKKSKDDIIE--AEITKLLLSYGADINMKDRHkGNTALHYA 175
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 242 AVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGADT---AKCGihsMFPLHLAAlnahsdccrk 318
Cdd:PHA02878  176 TENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTdarDKCG---NTPLHISV---------- 242
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355778 319 llSSGQKYSIVSLfsnehVLSAGFEIDTPDTF-GRTCLHAAAAGGNVecIKLLQSSGADFHKKDKCGRTPLHYA 391
Cdd:PHA02878  243 --GYCKDYDILKL-----LLEHGVDVNAKSYIlGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
21-166 1.42e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.82  E-value: 1.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  21 LIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKK 100
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG 623
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355778 101 DrrALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVY 166
Cdd:PLN03192  624 D--LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
PHA02878 PHA02878
ankyrin repeat protein; Provisional
387-624 1.88e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 70.68  E-value: 1.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 387 PLHYAAANCHFHCIKALVTTGANVNETDDWGRTALH--------------------------YAAASDM--DRN----KM 434
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHiickepnklgmkemirsinkcsvfytLVAIKDAfnNRNveifKI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 435 ILGNAHDNSEELErAREVKEKDAALCLE-----FLLQNDANPSIRDKEGYNS-IHYAAAYGHRQCLELLL---------E 499
Cdd:PHA02878  120 ILTNRYKNIQTID-LVYIDKKSKDDIIEaeitkLLLSYGADINMKDRHKGNTaLHYATENKDQRLTELLLsyganvnipD 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 500 RTNtgfeesdggalKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLA-AFKGHTECVEALVNQGASIFVKDNV 578
Cdd:PHA02878  199 KTN-----------NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYI 267
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*.
gi 1720355778 579 TKRTPLHASVINGHTlcLRLLLETADNPEVVdvkDAKGQTPLMLAV 624
Cdd:PHA02878  268 LGLTALHSSIKSERK--LKLLLEYGADINSL---NSYKLTPLSSAV 308
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
689-858 2.27e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 71.05  E-value: 2.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 689 AAARGHATWLNELLQIALSEEdccLKDNQGYTPLHWACYNGNENCIEVLLEQKC---FRKFIGNpfTPLHCAIINGHESC 765
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPD---IGDSKGRTPLHIAASKGYEDCVLVLLKHACnvhIRDANGN--TALWNAISAKHHKI 606
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 766 ASLLL---GAIDPSIvscrddkGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILV-NSA 841
Cdd:PLN03192  607 FRILYhfaSISDPHA-------AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLImNGA 679
                         170
                  ....*....|....*..
gi 1720355778 842 QADLTVKDKDLnTPLHL 858
Cdd:PLN03192  680 DVDKANTDDDF-SPTEL 695
Ank_2 pfam12796
Ankyrin repeats (3 copies);
460-543 2.82e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.60  E-value: 2.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 460 CLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLLERTNTGFEESDggalKSPLHLAAYNGHHQALEVLLQSLVDL 539
Cdd:pfam12796  12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNG----RTALHYAARSGHLEIVKLLLEKGADI 87

                  ....
gi 1720355778 540 DIRD 543
Cdd:pfam12796  88 NVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
529-741 3.46e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 69.69  E-value: 3.46e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 529 LEVLLQSLVDLDIRDEKGRTALYLAAFKGHT-----ECVEALVNQGASIFVKDNVTKrTPLHASVIN--GHTLCLRLLLE 601
Cdd:PHA03100   51 VKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGI-TPLLYAISKksNSYSIVEYLLD 129
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 602 TADNpevVDVKDAKGQTPLMLAVAYGHIDA--VSLLLEKEANVDAVDIVgctalhrgimtgheecvQMLLEQEASILCKD 679
Cdd:PHA03100  130 NGAN---VNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAKNRV-----------------NYLLSYGVPINIKD 189
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720355778 680 SRGRTPLHYAAARGHATWLNELLQIALSEEDCclkDNQGYTPLHWACYNGNENCIEVLLEQK 741
Cdd:PHA03100  190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLV---NKYGDTPLHIAILNNNKEIFKLLLNNG 248
Ank_2 pfam12796
Ankyrin repeats (3 copies);
271-381 6.27e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 6.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 271 LHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGQKYSivslfsnehvlsagfeidtpDTF 350
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--------------------KDN 60
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1720355778 351 GRTCLHAAAAGGNVECIKLLQSSGADFHKKD 381
Cdd:pfam12796  61 GRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
237-556 6.27e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.14  E-value: 6.27e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 237 PLHMtAVHGR-FTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSgadTAKCGIHSmfplhlaALNAHSDC 315
Cdd:PHA02878   40 PLHQ-AVEARnLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS---INKCSVFY-------TLVAIKDA 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 316 CRKLLSSGQKYSIVSLFSNEHVLSAgFEIDTPDTFGRTclhaaaaggNVECIKLLQSSGADFHKKDK-CGRTPLHYAAAN 394
Cdd:PHA02878  109 FNNRNVEIFKIILTNRYKNIQTIDL-VYIDKKSKDDII---------EAEITKLLLSYGADINMKDRhKGNTALHYATEN 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 395 CHFHCIKALVTTGANVNETDDWGRTALHYAAASdmdRNKMIlgnahdnseelerarevkekdaalcLEFLLQNDANPSIR 474
Cdd:PHA02878  179 KDQRLTELLLSYGANVNIPDKTNNSPLHHAVKH---YNKPI-------------------------VHILLENGASTDAR 230
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 475 DKEGYNSIHYAAAY-GHRQCLELLLERTNTGFEESDGGALkSPLHLAAYNghHQALEVLLQSLVDLDIRDEKGRTALYLA 553
Cdd:PHA02878  231 DKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGL-TALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307

                  ...
gi 1720355778 554 AFK 556
Cdd:PHA02878  308 VKQ 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
68-121 7.23e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.14  E-value: 7.23e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720355778  68 GRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLI 121
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
35-287 1.07e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 68.50  E-value: 1.07e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  35 WQTPLHVAAANKAVKCaevIIPLL--SSVNVSDRG--GRTALHHAALNGHMEMVNLLLakganinafdkkdrralhwaay 110
Cdd:cd22192    17 SESPLLLAAKENDVQA---IKKLLkcPSCDLFQRGalGETALHVAALYDNLEAAVVLM---------------------- 71
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 111 mghlDVVALLINHgaEVTCkdkkgytplhaaasngqisvvkhllnlgveideiNVY-GNTALHIACYNGQDAVVNELIDY 189
Cdd:cd22192    72 ----EAAPELVNE--PMTS----------------------------------DLYqGETALHIAVVNQNLNLVRELIAR 111
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 190 GANVNQPNNSG--FT------------PLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI- 254
Cdd:cd22192   112 GADVVSPRATGtfFRpgpknliyygehPLSFAACVGNEEI-VRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYd 190
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|..
gi 1720355778 255 --------QNGGEIDCV-DKDGNTPLHVAARHGHELLINTLI 287
Cdd:cd22192   191 lilsydkeDDLQPLDLVpNNQGLTPFKLAAKEGNIVMFQHLV 232
PHA02946 PHA02946
ankyin-like protein; Provisional
60-240 1.08e-11

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 68.16  E-value: 1.08e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  60 SVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGH--LDVVALLINHGAEVTCK-DKKGYT 136
Cdd:PHA02946   64 SPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNSvDEEGCG 143
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 137 PLHAAASNGQiSVVKHLLNLGVEIDEINVYGNTAL--HIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGA 214
Cdd:PHA02946  144 PLLACTDPSE-RVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKN 222
                         170       180
                  ....*....|....*....|....*.
gi 1720355778 215 LCLELLVNNGADVNIQSKDGKSPLHM 240
Cdd:PHA02946  223 VDIINLLLPSTDVNKQNKFGDSPLTL 248
Ank_4 pfam13637
Ankyrin repeats (many copies);
102-154 1.16e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 1.16e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720355778 102 RRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLL 154
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
204-292 1.73e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 1.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 204 LHFAAASTHgALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNgGEIDCVDkDGNTPLHVAARHGHELLI 283
Cdd:pfam12796   1 LHLAAKNGN-LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                  ....*....
gi 1720355778 284 NTLITSGAD 292
Cdd:pfam12796  78 KLLLEKGAD 86
Ank_4 pfam13637
Ankyrin repeats (many copies);
351-404 2.16e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.60  E-value: 2.16e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720355778 351 GRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALV 404
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
111-302 3.18e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.20  E-value: 3.18e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 111 MGHLDVVALLINHGAEVTckDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYG 190
Cdd:PLN03192  504 LHDLNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 191 ANVNQPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSkdGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTP 270
Cdd:PLN03192  582 CNVHIRDANGNTALWNAISAKHHKI-FRILYHFASISDPHA--AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1720355778 271 LHVAARHGHELLINTLITSGADTAKCGIHSMF 302
Cdd:PLN03192  659 LQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
4-129 4.63e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.82  E-value: 4.63e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778   4 TPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGgrTALHHAALNGHMEM 83
Cdd:PLN03192  560 TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG--DLLCTAAKRNDLTA 637
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720355778  84 VNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTC 129
Cdd:PLN03192  638 MKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
PHA03100 PHA03100
ankyrin repeat protein; Provisional
668-920 4.70e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.84  E-value: 4.70e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 668 LLEQEASILCKDSRGRTPLHYAAARGHATWLNELLqialsEEDCCL--KDNQGYTPLH---WACYNGNEN--CIEVLLEQ 740
Cdd:PHA03100   21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILL-----DNGADInsSTKNNSTPLHylsNIKYNLTDVkeIVKLLLEY 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 741 -KCFRKFIGNPFTPLHCAIIN--GHESCASLLLG-AIDPSIVSCRddkGRTTLHAAAFGDHA--ECLQLLLRHDAQVNAV 814
Cdd:PHA03100   96 gANVNAPDNNGITPLLYAISKksNSYSIVEYLLDnGANVNIKNSD---GENLLHLYLESNKIdlKILKLLIDKGVDINAK 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 815 DNsgktalmmaaengqagaVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHI 894
Cdd:PHA03100  173 NR-----------------VNYLLSYG-VPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGAN---PNLVNKYGDTPLHI 231
                         250       260
                  ....*....|....*....|....*.
gi 1720355778 895 AARNGLKVVVEELLAKGACVLAVDEN 920
Cdd:PHA03100  232 AILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02878 PHA02878
ankyrin repeat protein; Provisional
715-914 6.54e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 65.67  E-value: 6.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 715 DNQGYTPLHWACYNGNENCIEVLLEQKCFRKfIGNPFTPLHCAIINGHESCASLLLGAIDPSIVSCRDDKGRTTLHAAAF 794
Cdd:PHA02878   67 DHRDLTPLHIICKEPNKLGMKEMIRSINKCS-VFYTLVAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDII 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 795 gdHAECLQLLLRHDAQVNAVD-NSGKTALMMAAENGQAGAVDILVnSAQADLTVKDKDLNTPLHLAISKGHEKcALLILd 873
Cdd:PHA02878  146 --EAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLL-SYGANVNIPDKTNNSPLHHAVKHYNKP-IVHIL- 220
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1720355778 874 kIQDESLINAKNSALQTPLHIAARNGLKV-VVEELLAKGACV 914
Cdd:PHA02878  221 -LENGASTDARDKCGNTPLHISVGYCKDYdILKLLLEHGVDV 261
PHA02859 PHA02859
ankyrin repeat protein; Provisional
78-203 7.55e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 62.53  E-value: 7.55e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  78 NGHMEMVNLLLAKGANINAFDKKDRRAL--HWAAYMGHL--DVVALLINHGAEVTCKDKKGYTPLHAAASNG--QISVVK 151
Cdd:PHA02859   63 KVNVEILKFLIENGADVNFKTRDNNLSAlhHYLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHMYMCNFnvRINVIK 142
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720355778 152 HLLNLGVEIDEINVYGNTALH-IACYNGQDAVVNELIDYGANVNQPNNSGFTP 203
Cdd:PHA02859  143 LLIDSGVSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
548-730 7.76e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 65.80  E-value: 7.76e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 548 TALYLAAFKGHTECVEAL-VNQGASIFVKDNVTKrTPLHASVINGHTLCLRLLLETAdnPEVVDVKDA----KGQTPLML 622
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLlKCPSCDLFQRGALGE-TALHVAALYDNLEAAVVLMEAA--PELVNEPMTsdlyQGETALHI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 623 AVAYGHIDAVSLLLEKEANVDAVDIVGcTALHRGI---------------MTGHEECVQMLLEQEASILCKDSRGRTPLH 687
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVVSPRATG-TFFRPGPknliyygehplsfaaCVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1720355778 688 YAAARGHATWLNELLQIALSEE----DCCL---KDNQGYTPLHWACYNGN 730
Cdd:cd22192   175 ILVLQPNKTFACQMYDLILSYDkeddLQPLdlvPNNQGLTPFKLAAKEGN 224
PHA03095 PHA03095
ankyrin-like protein; Provisional
3-163 8.01e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.43  E-value: 8.01e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778   3 LTPLHRAVASR--SEEAVQVLIKHSADVNARDKNWQTPLHVAAAN--KAVKCAEVIIPLLSSVNVSDRGGRTALHHAALN 78
Cdd:PHA03095  153 MTPLAVLLKSRnaNVELLRLLIDAGADVYAVDDRFRSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMATG 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  79 GHMEMVNL--LLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNL 156
Cdd:PHA03095  233 SSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312

                  ....*..
gi 1720355778 157 GVEIDEI 163
Cdd:PHA03095  313 NPSAETV 319
PHA02875 PHA02875
ankyrin repeat protein; Provisional
502-685 1.91e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.86  E-value: 1.91e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 502 NTGFEESDGgalKSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGAsiFVKDNVTKR 581
Cdd:PHA02875   27 NPNFEIYDG---ISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK--FADDVFYKD 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 582 --TPLHASVINGHTLCLRLLLETADNPevvDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMT 659
Cdd:PHA02875  102 gmTPLHLATILKKLDIMKLLIARGADP---DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAK 178
                         170       180
                  ....*....|....*....|....*.
gi 1720355778 660 GHEECVQMLLEQEASIlckDSRGRTP 685
Cdd:PHA02875  179 GDIAICKMLLDSGANI---DYFGKNG 201
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
75-204 2.47e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.50  E-value: 2.47e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  75 AALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPL---------------- 138
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakhhkifrily 611
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 139 --------HA-------AASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPN-NSGFT 202
Cdd:PLN03192  612 hfasisdpHAagdllctAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDDDFS 691

                  ..
gi 1720355778 203 PL 204
Cdd:PLN03192  692 PT 693
Ank_2 pfam12796
Ankyrin repeats (3 copies);
238-328 2.98e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.82  E-value: 2.98e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 238 LHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGAdtAKCGIHSMFPLHLAALNAHSDCCR 317
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|.
gi 1720355778 318 KLLSSGQKYSI 328
Cdd:pfam12796  79 LLLEKGADINV 89
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
484-703 3.50e-10

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 63.88  E-value: 3.50e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 484 YAAAYGHRQCLELLLERTNTGFEESdgGAL-KSPLHLAAYNGHHQALEVLLQS---LVDLDIRDE--KGRTALYLAAFKG 557
Cdd:cd22192    23 LAAKENDVQAIKKLLKCPSCDLFQR--GALgETALHVAALYDNLEAAVVLMEAapeLVNEPMTSDlyQGETALHIAVVNQ 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 558 HTECVEALVNQGAsifvkDNVTKRTPLHASVINGHTLCLRllletadnpevvdvkdakGQTPLMLAVAYGHIDAVSLLLE 637
Cdd:cd22192   101 NLNLVRELIARGA-----DVVSPRATGTFFRPGPKNLIYY------------------GEHPLSFAACVGNEEIVRLLIE 157
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355778 638 KEANVDAVDIVGCTALHRGIMTGHEECV-QM---LLEQEASI------LCKDSRGRTPLHYAAARGHATWLNELLQ 703
Cdd:cd22192   158 HGADIRAQDSLGNTVLHILVLQPNKTFAcQMydlILSYDKEDdlqpldLVPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
1-208 5.24e-10

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 63.18  E-value: 5.24e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778   1 MWLTPLHRAVA-SRSEEAVQVLIKHSADVNARDknwqTPLHVAAANKAVKCAEVIIPLLSS---------VNVSDRG--- 67
Cdd:TIGR00870  51 LGRSALFVAAIeNENLELTELLLNLSCRGAVGD----TLLHAISLEYVDAVEAILLHLLAAfrksgplelANDQYTSeft 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  68 -GRTALHHAALNGHMEMVNLLLAKGANINA------FDKKDRRA--------LHWAAYMGHLDVVALLINHGAEVTCKDK 132
Cdd:TIGR00870 127 pGITALHLAAHRQNYEIVKLLLERGASVPAracgdfFVKSQGVDsfyhgespLNAAACLGSPSIVALLSEDPADILTADS 206
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 133 KGYTplhaaasngqisvVKHLLNLGVEideiNVYGNTALHIACYngqdavvNELIDYGANVNQ-------PNNSGFTPLH 205
Cdd:TIGR00870 207 LGNT-------------LLHLLVMENE----FKAEYEELSCQMY-------NFALSLLDKLRDskeleviLNHQGLTPLK 262

                  ...
gi 1720355778 206 FAA 208
Cdd:TIGR00870 263 LAA 265
PHA02874 PHA02874
ankyrin repeat protein; Provisional
618-919 5.39e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.67  E-value: 5.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 618 TPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQ--EASIL------------------- 676
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNgvDTSILpipciekdmiktildcgid 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 677 --CKDSRGRTPLHYAAARGHATWLNELLQIAlseEDCCLKDNQGYTPLHWACYNGNENCIEVLLEQKCFrkfignpftpl 754
Cdd:PHA02874  117 vnIKDAELKTFLHYAIKKGDLESIKMLFEYG---ADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY----------- 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 755 hcaiinghescaslllgaidpsiVSCRDDKGRTTLH-AAAFGDHAeCLQLLLRHDAQVNAVDNSGKTALMMAAENGQAgA 833
Cdd:PHA02874  183 -----------------------ANVKDNNGESPLHnAAEYGDYA-CIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-A 237
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 834 VDILVNSAQadLTVKDKDLNTPLHLAIskgHEKCALLILDK-IQDESLINAKNSALQTPLHIAARNGLKV-VVEELLAKG 911
Cdd:PHA02874  238 IELLINNAS--INDQDIDGSTPLHHAI---NPPCDIDIIDIlLYHKADISIKDNKGENPIDTAFKYINKDpVIKDIIANA 312

                  ....*...
gi 1720355778 912 ACVLAVDE 919
Cdd:PHA02874  313 VLIKEADK 320
PHA02875 PHA02875
ankyrin repeat protein; Provisional
581-693 6.57e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.32  E-value: 6.57e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 581 RTPLHASVINGHTLCLRLLLETadNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTG 660
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDL--GKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146
                          90       100       110
                  ....*....|....*....|....*....|...
gi 1720355778 661 HEECVQMLLEQEASILCKDSRGRTPLHYAAARG 693
Cdd:PHA02875  147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKG 179
Ank_4 pfam13637
Ankyrin repeats (many copies);
618-669 7.37e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 7.37e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720355778 618 TPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLL 669
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
36-210 8.95e-10

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 62.59  E-value: 8.95e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  36 QTPLHVAAANKAVKCAEVIIPLLSSVNVSDRG--------------GRTALHHAALNGHMEMVNLLLAKGANINA----- 96
Cdd:cd21882    27 KTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAratgr 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  97 FDKKDRR--------ALHWAAYMGHLDVVALLINHGAE---VTCKDKKGYTPLHAAasngqisvvkhllnlgVEIDEiNV 165
Cdd:cd21882   107 FFRKSPGnlfyfgelPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHAL----------------VLQAD-NT 169
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720355778 166 YGNTALHIACYNGqdavvneLIDYGANVNQ-------PNNSGFTPLHFAAAS 210
Cdd:cd21882   170 PENSAFVCQMYNL-------LLSYGAHLDPtqqleeiPNHQGLTPLKLAAVE 214
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
72-154 1.86e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.45  E-value: 1.86e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  72 LHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAAASNGQISVVK 151
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                  ...
gi 1720355778 152 HLL 154
Cdd:PTZ00322  166 LLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
515-566 2.46e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 2.46e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720355778 515 SPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALV 566
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
18-201 6.06e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 59.46  E-value: 6.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  18 VQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLL---SSVNVSDRGGRTALHHAALNGH---MEMVNLLLAKG 91
Cdd:PHA02798   92 VKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFMIengADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKG 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  92 ANINAFDKKDR-RALHwaAYMGH------LDVVALLINHG---------------------------------------A 125
Cdd:PHA02798  172 VDINTHNNKEKyDTLH--CYFKYnidridADILKLFVDNGfiinkenkshkkkfmeylnsllydnkrfkknildfifsyI 249
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355778 126 EVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGF 201
Cdd:PHA02798  250 DINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKNTISYTYY 325
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
268-422 8.17e-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: 59.26  E-value: 8.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 268 NTPLHVAARHGHELLINTLITS-GADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSgqkysiVSLFSNEHVLSAGFEidt 346
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEA------APELVNEPMTSDLYQ--- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 347 pdtfGRTCLHAAAAGGNVECIKLLQSSGAD----------FHKKDKC----GRTPLHYAAANCHFHCIKALVTTGANVNE 412
Cdd:cd22192    89 ----GETALHIAVVNQNLNLVRELIARGADvvspratgtfFRPGPKNliyyGEHPLSFAACVGNEEIVRLLIEHGADIRA 164
                         170
                  ....*....|
gi 1720355778 413 TDDWGRTALH 422
Cdd:cd22192   165 QDSLGNTVLH 174
PHA02878 PHA02878
ankyrin repeat protein; Provisional
638-918 9.31e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.74  E-value: 9.31e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 638 KEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHATWLNELLQIALseedcclKDNQ 717
Cdd:PHA02878   26 TENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSIN-------KCSV 98
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 718 GYT--PLHWACYNGNENCIEVLLeqkcFRKFIGNpftplhcAIINGHESCASLLLGAIDPSIVSC-----------RDDK 784
Cdd:PHA02878   99 FYTlvAIKDAFNNRNVEIFKIIL----TNRYKNI-------QTIDLVYIDKKSKDDIIEAEITKLllsygadinmkDRHK 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 785 GRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGH 864
Cdd:PHA02878  168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENG-ASTDARDKCGNTPLHISVGYCK 246
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720355778 865 EKCALLILdkIQDESLINAKNSALQ-TPLHIAARNGLKVVVeeLLAKGACVLAVD 918
Cdd:PHA02878  247 DYDILKLL--LEHGVDVNAKSYILGlTALHSSIKSERKLKL--LLEYGADINSLN 297
Ank_4 pfam13637
Ankyrin repeats (many copies);
384-426 1.30e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 1.30e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1720355778 384 GRTPLHYAAANCHFHCIKALVTTGANVNETDDWGRTALHYAAA 426
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAAS 43
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
202-389 1.52e-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: 58.49  E-value: 1.52e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 202 TPLhFAAASTHGALCLE-LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGE-----IDCVDKDGNTPLHVAA 275
Cdd:cd22192    19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 276 RHGHELLINTLITSGADTAK---CGihSMFPLHLAALnahsdccrkllssgqkysivsLFSNEHVLSagfeidtpdtFgr 352
Cdd:cd22192    98 VNQNLNLVRELIARGADVVSpraTG--TFFRPGPKNL---------------------IYYGEHPLS----------F-- 142
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1720355778 353 tclhaAAAGGNVECIKLLQSSGADFHKKDKCGRTPLH 389
Cdd:cd22192   143 -----AACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
Ank_4 pfam13637
Ankyrin repeats (many copies);
134-187 1.69e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 1.69e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720355778 134 GYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELI 187
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
720-922 1.77e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.05  E-value: 1.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 720 TPLHWACYNGNENCIEVLLEQKCFRKFIG-NPFTPLHCAI-INGHESCASLLLGAIDPSI-------------------- 777
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINtKIPHPLLTAIkIGAHDIIKLLIDNGVDTSIlpipciekdmiktildcgid 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 778 VSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLH 857
Cdd:PHA02874  117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLH 195
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720355778 858 LAISKGHEKCALLILDkiqDESLINAKNSALQTPLHIAARNGLKVVveELLAKGACVLAVDENAS 922
Cdd:PHA02874  196 NAAEYGDYACIKLLID---HGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGS 255
PHA02859 PHA02859
ankyrin repeat protein; Provisional
5-178 2.92e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 55.21  E-value: 2.92e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778   5 PLHRAVASRSEEAVQVLIKHSADVNardKNWQTPLHVAAANKAV--KCAEVIIPLLSSVNVSDRGGRTALHHAAL----N 78
Cdd:PHA02859   24 PLFYYVEKDDIEGVKKWIKFVNDCN---DLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRDNNLSALHHYLsfnkN 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  79 GHMEMVNLLLAKGANINAFDKKDRRALHwaAYMGH----LDVVALLINHGAEVTCKDKKGYTPLHA-AASNGQISVVKHL 153
Cdd:PHA02859  101 VEPEILKILIDSGSSITEEDEDGKNLLH--MYMCNfnvrINVIKLLIDSGVSFLNKDFDNNNILYSyILFHSDKKIFDFL 178
                         170       180
                  ....*....|....*....|....*
gi 1720355778 154 LNLGVEIDEINVYGNTALHIACYNG 178
Cdd:PHA02859  179 TSLGIDINETNKSGYNCYDLIKFRN 203
PHA02946 PHA02946
ankyin-like protein; Provisional
251-499 3.14e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 56.99  E-value: 3.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 251 QTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHL-------------------AALNA 311
Cdd:PHA02946   56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsgtddevierinllvqygAKINN 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 312 HSD--CCRKLLSSGQKYSIVSlfsnEHVLSAGFEIDTPDTFGRTCLHAAAAGGN--VECIKLLQSSGADFHKKDKCGRTP 387
Cdd:PHA02946  136 SVDeeGCGPLLACTDPSERVF----KKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHDGNTP 211
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 388 LHYAAANCHFHC-IKALVTTGANVNETDDWGRTALHYAAASdmdrnkmiLGNAHDNSEELERAREVKEKDAALCLeFLLQ 466
Cdd:PHA02946  212 LHIVCSKTVKNVdIINLLLPSTDVNKQNKFGDSPLTLLIKT--------LSPAHLINKLLSTSNVITDQTVNICI-FYDR 282
                         250       260       270
                  ....*....|....*....|....*....|....*.
gi 1720355778 467 NDANPSIRDK-EGYNSIHY--AAAYGHRQCLELLLE 499
Cdd:PHA02946  283 DDVLEIINDKgKQYDSTDFkmAVEVGSIRCVKYLLD 318
Ank_4 pfam13637
Ankyrin repeats (many copies);
2-55 5.27e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 5.27e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720355778   2 WLTPLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVII 55
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
537-759 7.00e-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: 56.63  E-value: 7.00e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 537 VDLDIRDEKGRTALYLAAFKG-HTECVEALVNQGASIFVKDNVtkrtpLHASVINGH---TLCLRLLL----ETADNPEV 608
Cdd:TIGR00870  43 LNINCPDRLGRSALFVAAIENeNLELTELLLNLSCRGAVGDTL-----LHAISLEYVdavEAILLHLLaafrKSGPLELA 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 609 VDVKDA---KGQTPLMLAVAYGHIDAVSLLLEKEANVDAVdiVGCTALHRGIM----------------TGHEECVQMLL 669
Cdd:TIGR00870 118 NDQYTSeftPGITALHLAAHRQNYEIVKLLLERGASVPAR--ACGDFFVKSQGvdsfyhgesplnaaacLGSPSIVALLS 195
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 670 EQEASILCKDSRGRTPLHYAAARGHATWLNELL-------------QIALSEEDCCLKDNQGYTPLHWACYNGNENCIEV 736
Cdd:TIGR00870 196 EDPADILTADSLGNTLLHLLVMENEFKAEYEELscqmynfalslldKLRDSKELEVILNHQGLTPLKLAAKEGRIVLFRL 275
                         250       260
                  ....*....|....*....|....
gi 1720355778 737 LLEQKCF-RKFIGNPFTPLHCAII 759
Cdd:TIGR00870 276 KLAIKYKqKKFVAWPNGQQLLSLY 299
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
357-572 7.55e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.41  E-value: 7.55e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 357 AAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVNETDDWGRTALHYAAASDMDRNKMIL 436
Cdd:PLN03192  531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 437 gnahdnseelerarevkekdaalclefllqndanpsirdkegynsIHYAAAyghrqclelllertntgfeeSDGGALKSP 516
Cdd:PLN03192  611 ---------------------------------------------YHFASI--------------------SDPHAAGDL 625
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355778 517 LHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASI 572
Cdd:PLN03192  626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
209-278 8.12e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 8.12e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 209 ASTHGALCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHG 278
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
PHA02989 PHA02989
ankyrin repeat protein; Provisional
16-284 1.00e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 55.52  E-value: 1.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  16 EAVQVLIKHSADVNARDKnWQTPLhvaaankavkCAeviipLLSSVNVSDrggrtalhhaalNGHMEMVNLLLAKGANIN 95
Cdd:PHA02989   51 KIVKLLIDNGADVNYKGY-IETPL----------CA-----VLRNREITS------------NKIKKIVKLLLKFGADIN 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  96 AFDKKDRRALHWAAYMGH---LDVVALLINHGAEV-TCKDKKGYTPLHAAASNGQIS--VVKHLLNLGVEIDEI-NVYGN 168
Cdd:PHA02989  103 LKTFNGVSPIVCFIYNSNinnCDMLRFLLSKGINVnDVKNSRGYNLLHMYLESFSVKkdVIKILLSFGVNLFEKtSLYGL 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 169 TALHIACYNGQDAVVNELIDY----GANVNQPNNSGFTPLHfAAASTHGAL---CLELL--VNNGADVNIQSKDGKSPLH 239
Cdd:PHA02989  183 TPMNIYLRNDIDVISIKVIKYlikkGVNIETNNNGSESVLE-SFLDNNKILskkEFKVLnfILKYIKINKKDKKGFNPLL 261
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1720355778 240 MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLIN 284
Cdd:PHA02989  262 ISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLN 306
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
253-421 1.05e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 1.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 253 LIQNGGEIDCVDKDGNtpLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLLSSGQKYSIVSLF 332
Cdd:PLN03192  513 LGDNGGEHDDPNMASN--LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDAN 590
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 333 SNE---HVLSAG----FEI-------DTPDTFGrTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFH 398
Cdd:PLN03192  591 GNTalwNAISAKhhkiFRIlyhfasiSDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVD 669
                         170       180
                  ....*....|....*....|....*.
gi 1720355778 399 CIKALVTTGANV---NETDDWGRTAL 421
Cdd:PLN03192  670 MVRLLIMNGADVdkaNTDDDFSPTEL 695
Ank_4 pfam13637
Ankyrin repeats (many copies);
37-88 1.15e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 1.15e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720355778  37 TPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLL 88
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
581-838 1.18e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.00  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 581 RTPLHASVINGHTLCLRLLLETADNP--EVVDvkdakGQTPLMLAVAYGHIDAVSLLLEKEA--NVDAVDIVgcTALHRG 656
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPnfEIYD-----GISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIE--SELHDA 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 657 IMTGHEECVQMLLEQEA---SILCKDsrGRTPLHYAAARGHATWLNELLQialSEEDCCLKDNQGYTPLHWACYNGNENC 733
Cdd:PHA02875   76 VEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIA---RGADPDIPNTDKFSPLHLAVMMGDIKG 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 734 IEVLLEQK-CFRKFIGNPFTPLHCAIINGH-ESCASLLLGAIDPSIVSCRDDKgrTTLHAAAFGDHAECLQLLLRHDAQV 811
Cdd:PHA02875  151 IELLIDHKaCLDIEDCCGCTPLIIAMAKGDiAICKMLLDSGANIDYFGKNGCV--AALCYAIENNKIDIVRLFIKRGADC 228
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1720355778 812 N---AVDNSGKTALMMAAE---NGQAGAVDILV 838
Cdd:PHA02875  229 NimfMIEGEECTILDMICNmctNLESEAIDALI 261
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
217-421 1.91e-07

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 54.92  E-value: 1.91e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 217 LELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRS--QTLIQNGGEIDCVDKDGNTPLH---VAARHGHELLINTLITSGA 291
Cdd:PHA02716  195 LEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASviKKIIELGGDMDMKCVNGMSPIMtyiINIDNINPEITNIYIESLD 274
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 292 DTAKCGIHSMFPLHLAalnahsdccrklLSSGQKYSIVslfsnEHVLSAGFEIDTPDTFGRTCLHAAAAGGNV--ECIKL 369
Cdd:PHA02716  275 GNKVKNIPMILHSYIT------------LARNIDISVV-----YSFLQPGVKLHYKDSAGRTCLHQYILRHNIstDIIKL 337
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355778 370 LQSSGADFHKKDKCGRTPLH-YAAANCHFH-------------CIKALVTTGANVNETDDWGRTAL 421
Cdd:PHA02716  338 LHEYGNDLNEPDNIGNTVLHtYLSMLSVVNildpetdndirldVIQCLISLGADITAVNCLGYTPL 403
Ank_4 pfam13637
Ankyrin repeats (many copies);
651-694 1.92e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.92e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1720355778 651 TALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGH 694
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
422-647 1.93e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.26  E-value: 1.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 422 HYAAASDMDRNKMILGNA--HDNSEELERAREVKEKDAALCLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQClellle 499
Cdd:PLN03192  500 HHKELHDLNVGDLLGDNGgeHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDC------ 573
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 500 rtntgfeesdggalksplhlaaynghhqaLEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEALvNQGASIfvKDNVT 579
Cdd:PLN03192  574 -----------------------------VLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL-YHFASI--SDPHA 621
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355778 580 KRTPLHASVINGHTLCLRLLLETADNpevVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDI 647
Cdd:PLN03192  622 AGDLLCTAAKRNDLTAMKELLKQGLN---VDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANT 686
PHA02859 PHA02859
ankyrin repeat protein; Provisional
137-296 2.73e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 52.13  E-value: 2.73e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 137 PLHAAASNGQISVVKHLLNLgveIDEINVYGNTALHiACYNGQDAVVNE---LIDYGANVN-QPNNSGFTPLHFAAASTH 212
Cdd:PHA02859   24 PLFYYVEKDDIEGVKKWIKF---VNDCNDLYETPIF-SCLEKDKVNVEIlkfLIENGADVNfKTRDNNLSALHHYLSFNK 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 213 GAL--CLELLVNNGADVNIQSKDGKSPLH--MTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHV-AARHGHELLINTLI 287
Cdd:PHA02859  100 NVEpeILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSyILFHSDKKIFDFLT 179

                  ....*....
gi 1720355778 288 TSGADTAKC 296
Cdd:PHA02859  180 SLGIDINET 188
Ank_5 pfam13857
Ankyrin repeats (many copies);
120-174 2.79e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.11  E-value: 2.79e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355778 120 LINHG-AEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIA 174
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
167-221 4.46e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 4.46e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720355778 167 GNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGAlCLELLV 221
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
515-741 5.11e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.35  E-value: 5.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 515 SPLHLAAYNGHHQALEVLLQSLVDLDIRDE--KGRTALY---LAAFKghtecvEALVNQGASIFVKDNVTKRTPLHASVI 589
Cdd:PHA02878   72 TPLHIICKEPNKLGMKEMIRSINKCSVFYTlvAIKDAFNnrnVEIFK------IILTNRYKNIQTIDLVYIDKKSKDDII 145
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 590 NghTLCLRLLLETADNPEVVDvkDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLL 669
Cdd:PHA02878  146 E--AEITKLLLSYGADINMKD--RHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILL 221
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1720355778 670 EQEASILCKDSRGRTPLHYAAARGHATwlnELLQIALsEEDCCLKDNQ---GYTPLHWACYngNENCIEVLLEQK 741
Cdd:PHA02878  222 ENGASTDARDKCGNTPLHISVGYCKDY---DILKLLL-EHGVDVNAKSyilGLTALHSSIK--SERKLKLLLEYG 290
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
335-441 5.40e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 5.40e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 335 EHVLSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPL-------HYAAANCHFHC-------- 399
Cdd:PLN03192  542 EELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALwnaisakHHKIFRILYHFasisdpha 621
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355778 400 ----------------IKALVTTGANVNETDDWGRTALHYAAASD-MDRNKMILGNAHD 441
Cdd:PLN03192  622 agdllctaakrndltaMKELLKQGLNVDSEDHQGATALQVAMAEDhVDMVRLLIMNGAD 680
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
117-189 6.55e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 6.55e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720355778 117 VALLINHGAEVTCKDKKGYTPLHAAASNGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDY 189
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
236-287 9.04e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 9.04e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720355778 236 SPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLI 287
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
11-88 9.53e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 9.53e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355778  11 ASRSEEAVQVLIKHSADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLL 88
Cdd:PTZ00322   91 ASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
40-126 1.25e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 1.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  40 HVAAANKAVKcAEVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVAL 119
Cdd:PTZ00322   88 QLAASGDAVG-ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                  ....*..
gi 1720355778 120 LINHGAE 126
Cdd:PTZ00322  167 LSRHSQC 173
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
768-918 1.29e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 1.29e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 768 LLLGAIDPSIvscRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTV 847
Cdd:PLN03192  544 LLKAKLDPDI---GDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPH 620
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720355778 848 KDKDLntpLHLAISKGHekcaLLILDKIQDESL-INAKNSALQTPLHIAARNGLKVVVEELLAKGACVLAVD 918
Cdd:PLN03192  621 AAGDL---LCTAAKRND----LTAMKELLKQGLnVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
Ank_4 pfam13637
Ankyrin repeats (many copies);
785-838 2.17e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 2.17e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720355778 785 GRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILV 838
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
682-738 2.17e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 2.17e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355778 682 GRTPLHYAAARGHatwlNELLQIAL-SEEDCCLKDNQGYTPLHWACYNGNENCIEVLL 738
Cdd:pfam13637   1 ELTALHAAAASGH----LELLRLLLeKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
359-428 2.34e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 2.34e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 359 AAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVNETDDWGRTALHYAAASD 428
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
768-844 3.00e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 3.00e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720355778 768 LLLGAIDPSivsCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQAD 844
Cdd:PTZ00322  101 LLTGGADPN---CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCH 174
Ank_4 pfam13637
Ankyrin repeats (many copies);
718-770 3.75e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 3.75e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720355778 718 GYTPLHWACYNGNENCIEVLLEQKC-FRKFIGNPFTPLHCAIINGHESCASLLL 770
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGAdINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
68-96 4.31e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.12  E-value: 4.31e-06
                           10        20
                   ....*....|....*....|....*....
gi 1720355778   68 GRTALHHAALNGHMEMVNLLLAKGANINA 96
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
666-910 4.69e-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: 50.40  E-value: 4.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 666 QMLLEQEasiLCKDSRGR-TPLHYAAARGHATWLNELLQiaLSEEDCCLKDNQGYTPLHWACYNGNENCIEVLLEqkCFR 744
Cdd:cd22192     3 QMLDELH---LLQQKRISeSPLLLAAKENDVQAIKKLLK--CPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAP 75
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 745 KFIGNPFT--------PLHCAIINGHESCASLLL--GAidpSIVSCRDD-----KGRTTLhaAAFGDHAeclqlllrhda 809
Cdd:cd22192    76 ELVNEPMTsdlyqgetALHIAVVNQNLNLVRELIarGA---DVVSPRATgtffrPGPKNL--IYYGEHP----------- 139
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 810 qvnavdnsgktaLMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCA------LLILDKIQDE-SLIN 882
Cdd:cd22192   140 ------------LSFAACVGNEEIVRLLIEHG-ADIRAQDSLGNTVLHILVLQPNKTFAcqmydlILSYDKEDDLqPLDL 206
                         250       260
                  ....*....|....*....|....*...
gi 1720355778 883 AKNSALQTPLHIAARNGLKVVVEELLAK 910
Cdd:cd22192   207 VPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
Ank_5 pfam13857
Ankyrin repeats (many copies);
86-141 5.96e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 5.96e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355778  86 LLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGYTPLHAA 141
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
489-728 6.37e-06

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 49.88  E-value: 6.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 489 GHRQCLELLLertnTGFEESDGGALKSPLHLAAYNGHHQALE---VLLQS---------LVDLDIRDE--KGRTALYLAA 554
Cdd:cd21882     6 GLLECLRWYL----TDSAYQRGATGKTCLHKAALNLNDGVNEaimLLLEAapdsgnpkeLVNAPCTDEfyQGQTALHIAI 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 555 FKGHTECVEALVNQGASIFVKDNVT--KRTPlhasvingHTLCLRllletadnpevvdvkdakGQTPLMLAVAYGHIDAV 632
Cdd:cd21882    82 ENRNLNLVRLLVENGADVSARATGRffRKSP--------GNLFYF------------------GELPLSLAACTNQEEIV 135
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 633 SLLLE---KEANVDAVDIVGCTALHRGIMTGHEE------CVQM---LLEQEASI-------LCKDSRGRTPLHYAAARG 693
Cdd:cd21882   136 RLLLEngaQPAALEAQDSLGNTVLHALVLQADNTpensafVCQMynlLLSYGAHLdptqqleEIPNHQGLTPLKLAAVEG 215
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1720355778 694 HATWLNELLQIALSEEDCCL--KDNQ-GYTPLHWACYN 728
Cdd:cd21882   216 KIVMFQHILQREFSGPYQPLsrKFTEwTYGPVTSSLYD 253
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
68-210 7.97e-06

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 49.80  E-value: 7.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  68 GRTALHHAALN---GHMEMVNLLL---AKGANINAF------DK--KDRRALHWAAYMGHLDVVALLINHGAEVTC---- 129
Cdd:cd22196    47 GKTCLLKAMLNlhnGQNDTISLLLdiaEKTGNLKEFvnaaytDSyyKGQTALHIAIERRNMHLVELLVQNGADVHArasg 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 130 ------KDKKGY----TPLHAAASNGQISVVKHLLN---LGVEIDEINVYGNTALH----IAcYNGQD------AVVNEL 186
Cdd:cd22196   127 effkkkKGGPGFyfgeLPLSLAACTNQLDIVKFLLEnphSPADISARDSMGNTVLHalveVA-DNTPEntkfvtKMYNEI 205
                         170       180       190
                  ....*....|....*....|....*....|.
gi 1720355778 187 IDYGANVNQ-------PNNSGFTPLHFAAAS 210
Cdd:cd22196   206 LILGAKIRPllkleeiTNKKGLTPLKLAAKT 236
Ank_4 pfam13637
Ankyrin repeats (many copies);
752-805 8.07e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 8.07e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720355778 752 TPLHCAIINGHESCASLLLGAidPSIVSCRDDKGRTTLHAAAFGDHAECLQLLL 805
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEK--GADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
590-669 1.10e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 1.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 590 NGHTLCLRLLLETADNPevvDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLL 669
Cdd:PTZ00322   92 SGDAVGARILLTGGADP---NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
826-921 1.44e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 1.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 826 AENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDESLINAKNsalQTPLHIAARNGLKVVVE 905
Cdd:PTZ00322   90 AASGDAVGARILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDG---KTPLELAEENGFREVVQ 165
                          90
                  ....*....|....*.
gi 1720355778 906 ELLAKGACVLAVDENA 921
Cdd:PTZ00322  166 LLSRHSQCHFELGANA 181
PHA02791 PHA02791
ankyrin-like protein; Provisional
696-891 1.50e-05

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 47.73  E-value: 1.50e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 696 TWLNELLQIALSEEDCCLKDNQGYTPLHWACYNGNENCIEVLLEQKCFRKFIGNPFtPLH-CAIINGHESCASLLLGAID 774
Cdd:PHA02791    8 TWKSKQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF-PLHqAATLEDTKIVKILLFSGMD 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 775 PSIVscrDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSG-KTALMMAAENGQAGAVDILVNSAQA--DLTVkdkd 851
Cdd:PHA02791   87 DSQF---DDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPStfDLAI---- 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1720355778 852 LNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTP 891
Cdd:PHA02791  160 LLSCIHITIKNGHVDMMILLLDYMTS---TNTNNSLLFIP 196
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
68-99 1.53e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 1.53e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1720355778  68 GRTALHHAAL-NGHMEMVNLLLAKGANINAFDK 99
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA02875 PHA02875
ankyrin repeat protein; Provisional
617-840 1.67e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.45  E-value: 1.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 617 QTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHAT 696
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 697 WLNELLQIALSEEDCCLKDnqGYTPLHWACYNGNENCIEVLLEQKCfrkfignpftplhcaiinghescaslllgaiDPS 776
Cdd:PHA02875   83 AVEELLDLGKFADDVFYKD--GMTPLHLATILKKLDIMKLLIARGA-------------------------------DPD 129
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355778 777 IVSCrdDKgRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNS 840
Cdd:PHA02875  130 IPNT--DK-FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDS 190
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
139-242 2.10e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 2.10e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 139 HAAASnGQISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFAAASTHGALcLE 218
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV-VQ 165
                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1720355778 219 LLV-------NNGADVNIQSKDGK------SPLHMTA 242
Cdd:PTZ00322  166 LLSrhsqchfELGANAKPDSFTGKppsledSPISSHH 202
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
68-96 2.72e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.86  E-value: 2.72e-05
                          10        20
                  ....*....|....*....|....*....
gi 1720355778  68 GRTALHHAALNGHMEMVNLLLAKGANINA 96
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
21-75 2.84e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 2.84e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355778  21 LIKH-SADVNARDKNWQTPLHVAAANKAVKCAEVIIPLLSSVNVSDRGGRTALHHA 75
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
164-207 2.90e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 2.90e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1720355778 164 NVYGNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTPLHFA 207
Cdd:pfam13857  13 DGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
820-914 3.03e-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: 47.70  E-value: 3.03e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 820 TALMMAAENGQAGAVDILVNSAQADLTVKDKDLNTPLHLAISKGHEKCALLILDkiQDESLIN-AKNSAL---QTPLHIA 895
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNePMTSDLyqgETALHIA 96
                          90
                  ....*....|....*....
gi 1720355778 896 ARNGLKVVVEELLAKGACV 914
Cdd:cd22192    97 VVNQNLNLVRELIARGADV 115
Ank_4 pfam13637
Ankyrin repeats (many copies);
303-370 3.16e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 3.16e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355778 303 PLHLAALNAHSDCCRKLLSSGqkysivslfsnehvlsagFEIDTPDTFGRTCLHAAAAGGNVECIKLL 370
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKG------------------ADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
186-240 3.16e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.16e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720355778 186 LIDYG-ANVNQPNNSGFTPLHFAAasTHGAL-CLELLVNNGADVNIQSKDGKSPLHM 240
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAA--KYGALeIVRVLLAYGVDLNLKDEEGLTALDL 55
Ank_5 pfam13857
Ankyrin repeats (many copies);
369-424 3.42e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 3.42e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355778 369 LLQSSGADFHKKDKCGRTPLHYAAANCHFHCIKALVTTGANVNETDDWGRTALHYA 424
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
790-883 3.67e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 3.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 790 HAAAFGDhAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAqADLTVKDKDLNTPLHLAISKGHEKCAL 869
Cdd:PTZ00322   88 QLAASGD-AVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG-ADPTLLDKDGKTPLELAEENGFREVVQ 165
                          90
                  ....*....|....
gi 1720355778 870 LILDKIQDESLINA 883
Cdd:PTZ00322  166 LLSRHSQCHFELGA 179
Ank_4 pfam13637
Ankyrin repeats (many copies);
546-600 3.81e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 3.81e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720355778 546 GRTALYLAAFKGHTECVEALVNQGASIFVKDNvTKRTPLHASVINGHTLCLRLLL 600
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
803-859 3.89e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 3.89e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720355778 803 LLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNsAQADLTVKDKDLNTPLHLA 859
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLA-YGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
620-705 3.95e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.56  E-value: 3.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 620 LMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGHATWLN 699
Cdd:PLN03192  529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608

                  ....*.
gi 1720355778 700 ELLQIA 705
Cdd:PLN03192  609 ILYHFA 614
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
597-729 4.01e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 47.45  E-value: 4.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 597 RLLLETADNPEVVDV--------KDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVD--------------IVGCTALH 654
Cdd:cd22194   114 RILLAFAEENGILDRfinaeyteEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykhegfYFGETPLA 193
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 655 RGIMTGHEECVQMLLEQEAS-ILCKDSRGRTPLHYAA-----ARGHATWLNELL-QIALSEEDCCL---KDNQGYTPLHW 724
Cdd:cd22194   194 LAACTNQPEIVQLLMEKESTdITSQDSRGNTVLHALVtvaedSKTQNDFVKRMYdMILLKSENKNLetiRNNEGLTPLQL 273

                  ....*
gi 1720355778 725 ACYNG 729
Cdd:cd22194   274 AAKMG 278
Ank_4 pfam13637
Ankyrin repeats (many copies);
581-636 4.16e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 4.16e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355778 581 RTPLHASVINGHTLCLRLLLEtadNPEVVDVKDAKGQTPLMLAVAYGHIDAVSLLL 636
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLE---KGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
166-194 4.31e-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: 41.03  E-value: 4.31e-05
                           10        20
                   ....*....|....*....|....*....
gi 1720355778  166 YGNTALHIACYNGQDAVVNELIDYGANVN 194
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02884 PHA02884
ankyrin repeat protein; Provisional
164-241 4.85e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 46.51  E-value: 4.85e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 164 NVYGNTALHIACYNGQDAVVNeLIDYGANVNQ-PNNSGFTPLHFAAasTHGAL-CLELLVNNGADVNIQSKDGKSPLHMT 241
Cdd:PHA02884   68 NSKTNPLIYAIDCDNDDAAKL-LIRYGADVNRyAEEAKITPLYISV--LHGCLkCLEILLSYGADINIQTNDMVTPIELA 144
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
141-278 5.17e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 47.06  E-value: 5.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 141 AASNGqisVVKHLLNlgVEIDEINVYGNTALHIACYNGQDAVVNELIDYGANVN--------QP--NNSGF----TPLHF 206
Cdd:cd22194   120 AEENG---ILDRFIN--AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffNPkyKHEGFyfgeTPLAL 194
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 207 AAASTHGALcLELLVNNGADvNIQSKD--GKSPLHMTAVHGRFTRSQT-----------LIQNGGEIDCV-DKDGNTPLH 272
Cdd:cd22194   195 AACTNQPEI-VQLLMEKEST-DITSQDsrGNTVLHALVTVAEDSKTQNdfvkrmydmilLKSENKNLETIrNNEGLTPLQ 272

                  ....*.
gi 1720355778 273 VAARHG 278
Cdd:cd22194   273 LAAKMG 278
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
665-738 5.62e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 5.62e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355778 665 VQMLLEQEASILCKDSRGRTPLHYAAARGHATWLNELLQIAlseEDCCLKDNQGYTPLHWACYNGNENCIEVLL 738
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFG---ADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
238-327 5.91e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 5.91e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 238 LHMTAVH-------GRFTRSQTLIQNGGEIDCVDKDGNTPLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAALN 310
Cdd:PTZ00322   79 AHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
                          90
                  ....*....|....*..
gi 1720355778 311 AHSDCCRKLLSSGQKYS 327
Cdd:PTZ00322  159 GFREVVQLLSRHSQCHF 175
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
304-422 6.05e-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: 46.80  E-value: 6.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 304 LHLAALNAHS---DCCRKLLSSGQKYSIVSLFSNEHVLSAGFEidtpdtfGRTCLHAAAAGGNVECIKLLQSSGADFH-- 378
Cdd:cd21882    30 LHKAALNLNDgvnEAIMLLLEAAPDSGNPKELVNAPCTDEFYQ-------GQTALHIAIENRNLNLVRLLVENGADVSar 102
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355778 379 ------KKDKC-----GRTPLHYAAANCHFHCIKALVTTG---ANVNETDDWGRTALH 422
Cdd:cd21882   103 atgrffRKSPGnlfyfGELPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLH 160
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
68-208 7.34e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 46.68  E-value: 7.34e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  68 GRTALHHAALNGHMEMVNLLLAKGANINA------FDKKDRralHWAAYMGHldvvallinhgaevtckdkkgyTPLHAA 141
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNAhakgvfFNPKYK---HEGFYFGE----------------------TPLALA 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 142 ASNGQISVVKHLL-NLGVEIDEINVYGNTALH---IACYN--GQDAVVNELIDY------GANVNQ-PNNSGFTPLHFAA 208
Cdd:cd22194   196 ACTNQPEIVQLLMeKESTDITSQDSRGNTVLHalvTVAEDskTQNDFVKRMYDMillkseNKNLETiRNNEGLTPLQLAA 275
Ank_4 pfam13637
Ankyrin repeats (many copies);
267-320 7.36e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 7.36e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720355778 267 GNTPLHVAARHGHELLINTLITSGADTAKCGIHSMFPLHLAALNAHSDCCRKLL 320
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
68-210 8.06e-05

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 46.33  E-value: 8.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  68 GRTALHHAALNGHMEMVNLLLAKGANINA------FDKKDRRA--------LHWAAYMGHLDVVALLINHG---AEVTCK 130
Cdd:cd22193    76 GQTALHIAIERRQGDIVALLVENGADVHAhakgrfFQPKYQGEgfyfgelpLSLAACTNQPDIVQYLLENEhqpADIEAQ 155
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 131 DKKGYTPLHAAasngqisvvkhllnlgVEIDEiNVYGNTALHIACYNGqdavvneLIDYGANVNQP-------NNSGFTP 203
Cdd:cd22193   156 DSRGNTVLHAL----------------VTVAD-NTKENTKFVTRMYDM-------ILIRGAKLCPTveleeirNNDGLTP 211

                  ....*..
gi 1720355778 204 LHFAAAS 210
Cdd:cd22193   212 LQLAAKM 218
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
351-504 9.61e-05

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 46.39  E-value: 9.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 351 GRTCLHAAAAGGNVECIKLLQSSGADFH----------KKDKC---GRTPLHYAAANCHFHCIKALVTTG---ANVNETD 414
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVENGADVHaracgrffqkKQGTCfyfGELPLSLAACTKQWDVVNYLLENPhqpASLQAQD 173
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 415 DWGRTALHYAAasdmdrnkMILGNAHDNSEELERA-REVKEKDAALCLEFLLQndanpSIRDKEGYNSIHYAAAYGHRQC 493
Cdd:cd22197   174 SLGNTVLHALV--------MIADNSPENSALVIKMyDGLLQAGARLCPTVQLE-----EISNHEGLTPLKLAAKEGKIEI 240
                         170
                  ....*....|.
gi 1720355778 494 LELLLERTNTG 504
Cdd:cd22197   241 FRHILQREFSG 251
Ank_5 pfam13857
Ankyrin repeats (many copies);
60-108 9.80e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 9.80e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1720355778  60 SVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWA 108
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
142-271 9.89e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 46.06  E-value: 9.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 142 ASNGQISVVKHLLNLGVEIDEINVYGNTALH--IACYNGQDAVVNELIDYGANVNQPNNSGFTPLHfaaaSTHGALCLEL 219
Cdd:PHA02716  292 ARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLH----TYLSMLSVVN 367
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720355778 220 LVNNGADVNIqskdgksplhmtavhgRFTRSQTLIQNGGEIDCVDKDGNTPL 271
Cdd:PHA02716  368 ILDPETDNDI----------------RLDVIQCLISLGADITAVNCLGYTPL 403
PHA02989 PHA02989
ankyrin repeat protein; Provisional
72-213 1.01e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 45.89  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  72 LHHAALNGHMEMVNLLLAKGANINAFDKKDRRAL------HWAAYMGHLDVVALLINHgAEVTCKDKKGYTPLHAAASNG 145
Cdd:PHA02989  189 LRNDIDVISIKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVD 267
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355778 146 QISVVKHLLNLGVEIDEINVYGNTALHIACYNGQDAVVNELIDYganvnQPNNSgFTPLHFAAASTHG 213
Cdd:PHA02989  268 NYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQL-----KPGKY-LIKKTFEYFSEHG 329
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
166-198 1.05e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 1.05e-04
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1720355778 166 YGNTALHIACY-NGQDAVVNELIDYGANVNQPNN 198
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
657-863 1.46e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 45.64  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 657 IMTGHEECVQMLLEQeaSILCKDSRGRTPLHYAAARGHATWLNE---LLQIA--------LSEEDCCLKDNQGYTPLHWA 725
Cdd:cd21882     3 ELLGLLECLRWYLTD--SAYQRGATGKTCLHKAALNLNDGVNEAimlLLEAApdsgnpkeLVNAPCTDEFYQGQTALHIA 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 726 CYNGNENCIEVLLEQKC----------FRKFIGNPF----TPLHCAIINGHESCASLLL-GAIDPSIVSCRDDKGRTTLH 790
Cdd:cd21882    81 IENRNLNLVRLLVENGAdvsaratgrfFRKSPGNLFyfgeLPLSLAACTNQEEIVRLLLeNGAQPAALEAQDSLGNTVLH 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1720355778 791 AaafgdhaeclqLLLRHDaqvNAVDNSgKTALMMAAENGQAGAVdiLVNSAQADLTVKDKDLnTPLHLAISKG 863
Cdd:cd21882   161 A-----------LVLQAD---NTPENS-AFVCQMYNLLLSYGAH--LDPTQQLEEIPNHQGL-TPLKLAAVEG 215
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
260-422 2.02e-04

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: 45.07  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 260 IDCVDKDGNTPLHVAARHG-HELLINTLITSGA-----DTAkcgihsmfpLHLAALNAH---SDCCRKLLSSGQKYSIVS 330
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENeNLELTELLLNLSCrgavgDTL---------LHAISLEYVdavEAILLHLLAAFRKSGPLE 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 331 LfsnehvlsaGFEIDTPD-TFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKC--------------GRTPLHYAAANC 395
Cdd:TIGR00870 116 L---------ANDQYTSEfTPGITALHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLG 186
                         170       180
                  ....*....|....*....|....*..
gi 1720355778 396 HFHCIKALVTTGANVNETDDWGRTALH 422
Cdd:TIGR00870 187 SPSIVALLSEDPADILTADSLGNTLLH 213
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
65-254 2.02e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 45.29  E-value: 2.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  65 DRGGRTALHHAAL--NGHMEMVNLLLAKGANINAFDKKDRRALHwaAYMG----------------HLDVVALLINHGAE 126
Cdd:PHA02716  314 DSAGRTCLHQYILrhNISTDIIKLLHEYGNDLNEPDNIGNTVLH--TYLSmlsvvnildpetdndiRLDVIQCLISLGAD 391
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 127 VTCKDKKGYTPLHAAASNGQ----------------ISVVKH--LLNLGVEIDE---------------INVYGNTALHI 173
Cdd:PHA02716  392 ITAVNCLGYTPLTSYICTAQnymyydiidclisdkvLNMVKHriLQDLLIRVDDtpciihhiiakynipTDLYTDEYEPY 471
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 174 ACYNGQDAVVNELIDYGANVNQPnNSGFTPLHFAAASTHGAL----CLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTR 249
Cdd:PHA02716  472 DSTKIHDVYHCAIIERYNNAVCE-TSGMTPLHVSIISHTNANivmdSFVYLLSIQYNINIPTKNGVTPLMLTMRNNRLSG 550

                  ....*
gi 1720355778 250 SQTLI 254
Cdd:PHA02716  551 HQWYI 555
Ank_4 pfam13637
Ankyrin repeats (many copies);
460-498 2.28e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 2.28e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1720355778 460 CLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELLL 498
Cdd:pfam13637  16 LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
384-412 2.55e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 2.55e-04
                           10        20
                   ....*....|....*....|....*....
gi 1720355778  384 GRTPLHYAAANCHFHCIKALVTTGANVNE 412
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
200-232 2.74e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.19  E-value: 2.74e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1720355778 200 GFTPLHFAAASTHGALCLELLVNNGADVNIQSK 232
Cdd:pfam00023   2 GNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
552-636 2.80e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 2.80e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 552 LAAfKGHTECVEALVNQGASIFVKDnVTKRTPLHASVINGHTLCLRLLLETADNPEVVDvKDakGQTPLMLAVAYGHIDA 631
Cdd:PTZ00322   89 LAA-SGDAVGARILLTGGADPNCRD-YDGRTPLHIACANGHVQVVRVLLEFGADPTLLD-KD--GKTPLELAEENGFREV 163

                  ....*
gi 1720355778 632 VSLLL 636
Cdd:PTZ00322  164 VQLLS 168
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
4-155 2.88e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 44.75  E-value: 2.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778   4 TPLHRAVASRSEEAVQVLIKHSADVNARDKN-WQTPLHvaaankavkcaeviipllssvnvSDRG---GRTALHHAALNG 79
Cdd:cd22194   143 TALNIAIERRQGDIVKLLIAKGADVNAHAKGvFFNPKY-----------------------KHEGfyfGETPLALAACTN 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  80 HMEMVNLLLAKGANINAF-DKKDRRALHwAAYM------GHLDVV-----ALLINHGAEV--TCKDKKGYTPLHAAASNG 145
Cdd:cd22194   200 QPEIVQLLMEKESTDITSqDSRGNTVLH-ALVTvaedskTQNDFVkrmydMILLKSENKNleTIRNNEGLTPLQLAAKMG 278
                         170
                  ....*....|
gi 1720355778 146 QISVVKHLLN 155
Cdd:cd22194   279 KAEILKYILS 288
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
129-275 3.01e-04

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: 44.69  E-value: 3.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 129 CKDKKGYTPL-HAAASNGQISVVKHLLNLGVEIDEinvyGNTALHIACYNGQDAVvNELI----------DYGANVNQPN 197
Cdd:TIGR00870  47 CPDRLGRSALfVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLEYVDAV-EAILlhllaafrksGPLELANDQY 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 198 NSGF----TPLHFAAaSTHGALCLELLVNNGADVNIQSKDG---KSPLHMTAVHGRFTRS-----------QTLIQNGGE 259
Cdd:TIGR00870 122 TSEFtpgiTALHLAA-HRQNYEIVKLLLERGASVPARACGDffvKSQGVDSFYHGESPLNaaaclgspsivALLSEDPAD 200
                         170
                  ....*....|....*.
gi 1720355778 260 IDCVDKDGNTPLHVAA 275
Cdd:TIGR00870 201 ILTADSLGNTLLHLLV 216
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
5-108 3.13e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 44.62  E-value: 3.13e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778   5 PLHRAVASRSEEAVQVLIKHSADVNARDKNWQTPLH--VAAANKAVKCaEVIIPLLSSV---------NVSDRGGRTALH 73
Cdd:cd22192   139 PLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHilVLQPNKTFAC-QMYDLILSYDkeddlqpldLVPNNQGLTPFK 217
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1720355778  74 HAALNGHMEMVNLLLAKganinafdkkdRRALHWA 108
Cdd:cd22192   218 LAAKEGNIVMFQHLVQK-----------RRHIQWT 241
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
784-899 3.30e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 44.36  E-value: 3.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 784 KGRTTLHAAAFGDHAECLQLLLRHDAQVNA---------VDNS-----GKTALMMAAENGQAGAVDILVNSAQADLTVKD 849
Cdd:cd22194   140 EGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHegfyfGETPLALAACTNQPEIVQLLMEKESTDITSQD 219
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355778 850 KDLNTPLHLAI-----SKGHEKCALLILDKI----QDESLINAKNSALQTPLHIAARNG 899
Cdd:cd22194   220 SRGNTVLHALVtvaedSKTQNDFVKRMYDMIllksENKNLETIRNNEGLTPLQLAAKMG 278
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
615-646 3.47e-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: 3.47e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1720355778 615 KGQTPLMLAVA-YGHIDAVSLLLEKEANVDAVD 646
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
384-415 3.47e-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: 3.47e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1720355778 384 GRTPLHYAAANC-HFHCIKALVTTGANVNETDD 415
Cdd:pfam00023   2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
133-162 4.08e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 4.08e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1720355778  133 KGYTPLHAAASNGQISVVKHLLNLGVEIDE 162
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
772-825 4.82e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 4.82e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720355778 772 AIDPSIVSCRDDKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMA 825
Cdd:pfam13857   3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
68-208 4.96e-04

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 44.08  E-value: 4.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  68 GRTALHHAALNGHMEMVNLLLAKGANINA------FDKKDRRALhwaaYMGHLdvvallinhgaevtckdkkgytPLHAA 141
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVENGADVHAracgrfFQKKQGTCF----YFGEL----------------------PLSLA 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 142 ASNGQISVVKHLLNLGVE---IDEINVYGNTALHIACYNGQDAVVN---------ELIDYGANVNQ-------PNNSGFT 202
Cdd:cd22197   148 ACTKQWDVVNYLLENPHQpasLQAQDSLGNTVLHALVMIADNSPENsalvikmydGLLQAGARLCPtvqleeiSNHEGLT 227

                  ....*.
gi 1720355778 203 PLHFAA 208
Cdd:cd22197   228 PLKLAA 233
PHA02791 PHA02791
ankyrin-like protein; Provisional
72-203 5.15e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 43.11  E-value: 5.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  72 LHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVVALLINHGAEVTCKDKKGY-TPLHAAASNGQISVV 150
Cdd:PHA02791   65 LHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIV 144
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720355778 151 KHLLNLGVEIDEINVYgNTALHIACYNGQDAVVNELIDYGANVNQPNNSGFTP 203
Cdd:PHA02791  145 SYFLSEIPSTFDLAIL-LSCIHITIKNGHVDMMILLLDYMTSTNTNNSLLFIP 196
PHA02743 PHA02743
Viral ankyrin protein; Provisional
81-200 5.54e-04

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 41.73  E-value: 5.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  81 MEMVNLLLAKGANINAFDKKDRRALHWAAYMGHLDVV---ALLINHGAEVTCKDKK-GYTPLHAAASNGQISVVKHLL-N 155
Cdd:PHA02743   37 MEVAPFISGDGHLLHRYDHHGRQCTHMVAWYDRANAVmkiELLVNMGADINARELGtGNTLLHIAASTKNYELAEWLCrQ 116
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1720355778 156 LGVEIDEINVYGNTALHIAcYNGQDAVVNE-LIDYGANVNQPNNSG 200
Cdd:PHA02743  117 LGVNLGAINYQHETAYHIA-YKMRDRRMMEiLRANGAVCDDPLSIG 161
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
166-194 6.75e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 6.75e-04
                          10        20
                  ....*....|....*....|....*....
gi 1720355778 166 YGNTALHIACYNGQDAVVNELIDYGANVN 194
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
Ank_4 pfam13637
Ankyrin repeats (many copies);
202-254 6.93e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 6.93e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720355778 202 TPLHFAAASTHGAlCLELLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLI 254
Cdd:pfam13637   3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
364-657 6.96e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.28  E-value: 6.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 364 VECIKLLQSSGADFHKKDKCGRTPL-----HYAAANCHFHCIKALVTTGANVNETDDWGRTALHyaaasdmdrnkMILGN 438
Cdd:PHA02798   51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLY-----------CLLSN 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 439 AHDNSEELerarevkekdaalcLEFLLQNDANPSIRDKEGYNSIHYAAAYGHRQCLELllertntgfeesdggalksplh 518
Cdd:PHA02798  120 GYINNLEI--------------LLFMIENGADTTLLDKDGFTMLQVYLQSNHHIDIEI---------------------- 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 519 laaynghhqaLEVLLQSLVDLD-IRDEKGRTALYlAAFKGHTECVEA-----LVNQGASIFVKDNVTKRTPLhasvingH 592
Cdd:PHA02798  164 ----------IKLLLEKGVDINtHNNKEKYDTLH-CYFKYNIDRIDAdilklFVDNGFIINKENKSHKKKFM-------E 225
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355778 593 TLCLRLLLETADNPEVVDV---------KDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALHRGI 657
Cdd:PHA02798  226 YLNSLLYDNKRFKKNILDFifsyidinqVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAF 299
Ank_4 pfam13637
Ankyrin repeats (many copies);
853-899 7.07e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 7.07e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1720355778 853 NTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIAARNG 899
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNG 45
Ank_5 pfam13857
Ankyrin repeats (many copies);
673-725 7.15e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 7.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720355778 673 ASILCKDSRGRTPLHYAAARGHATWLNELLqiaLSEEDCCLKDNQGYTPLHWA 725
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLL---AYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
663-829 7.18e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.46  E-value: 7.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 663 ECVQMLLEQEASILC-KDSRGRTPLHYAAarghatwLNELLQIA--LSEEDCCLKDN-------QGYTPLHWACYNGNEN 732
Cdd:cd22192    31 QAIKKLLKCPSCDLFqRGALGETALHVAA-------LYDNLEAAvvLMEAAPELVNEpmtsdlyQGETALHIAVVNQNLN 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 733 CIEVLLEQ-----------KCFRKFIGNPFT----PLHCAIINGHESCASLLL--GAidpSIVScRDDKGRTTLHAAAFG 795
Cdd:cd22192   104 LVRELIARgadvvspratgTFFRPGPKNLIYygehPLSFAACVGNEEIVRLLIehGA---DIRA-QDSLGNTVLHILVLQ 179
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1720355778 796 DHA----ECLQLLLRHDAQVNAV------DNSGKTALMMAAENG 829
Cdd:cd22192   180 PNKtfacQMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEG 223
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
589-711 8.20e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 8.20e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 589 INGHTLCLRLLLETADNP-------EVVDVKDAKgqtplMLAVAYGHIDA------VSLLLEKEANVDAVDIVGCTALHR 655
Cdd:PTZ00322   47 IDTHLEALEATENKDATPdhnltteEVIDPVVAH-----MLTVELCQLAAsgdavgARILLTGGADPNCRDYDGRTPLHI 121
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355778 656 GIMTGHEECVQMLLEQEASILCKDSRGRTPLHYAAARGhatwLNELLQIALSEEDC 711
Cdd:PTZ00322  122 ACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG----FREVVQLLSRHSQC 173
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
337-394 8.93e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.96  E-value: 8.93e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720355778 337 VLSAGFEIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYAAAN 394
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158
Ank_5 pfam13857
Ankyrin repeats (many copies);
634-689 9.14e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 9.14e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355778 634 LLLEKEANVDAVDIVGCTALHRGIMTGHEECVQMLLEQEASILCKDSRGRTPLHYA 689
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02791 PHA02791
ankyrin-like protein; Provisional
463-637 9.16e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 42.34  E-value: 9.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 463 FLLQNDANPSirDKEGYNSIHYAAAYGHRQCLELLLertntgfeesDGGALKS------PLHLAAYNGHHQALEVLLQSL 536
Cdd:PHA02791   17 FLSSKDAFKA--DVHGHSALYYAIADNNVRLVCTLL----------NAGALKNllenefPLHQAATLEDTKIVKILLFSG 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 537 VDLDIRDEKGRTALYLAAFKGHTECVEALVNQGASIFVKDNVTKRTPL-HASVINGHTLCLRLLLETadnPEVVDVkdAK 615
Cdd:PHA02791   85 MDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWKTSFyHAVMLNDVSIVSYFLSEI---PSTFDL--AI 159
                         170       180
                  ....*....|....*....|..
gi 1720355778 616 GQTPLMLAVAYGHIDAVSLLLE 637
Cdd:PHA02791  160 LLSCIHITIKNGHVDMMILLLD 181
Ank_4 pfam13637
Ankyrin repeats (many copies);
478-533 1.06e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 1.06e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355778 478 GYNSIHYAAAYGHRQCLELLLERTNTGFEESDGGAlkSPLHLAAYNGHHQALEVLL 533
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE--TALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
343-391 1.10e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1720355778 343 EIDTPDTFGRTCLHAAAAGGNVECIKLLQSSGADFHKKDKCGRTPLHYA 391
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
266-292 1.23e-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: 1.23e-03
                           10        20
                   ....*....|....*....|....*..
gi 1720355778  266 DGNTPLHVAARHGHELLINTLITSGAD 292
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
133-162 1.28e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.85  E-value: 1.28e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1720355778 133 KGYTPLHAAASNGQISVVKHLLNLGVEIDE 162
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
117-246 1.69e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 1.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 117 VALLINHGAEVTCKDKKGYTPLHAAASNGQIS-VVKHLLNlgVEIDEINVYGntalhiacyngqDAV-VNELIDYGANVN 194
Cdd:PTZ00322   44 IARIDTHLEALEATENKDATPDHNLTTEEVIDpVVAHMLT--VELCQLAASG------------DAVgARILLTGGADPN 109
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720355778 195 QPNNSGFTPLHFAAASTHGALcLELLVNNGADVNIQSKDGKSPLHMTAVHGR 246
Cdd:PTZ00322  110 CRDYDGRTPLHIACANGHVQV-VRVLLEFGADPTLLDKDGKTPLELAEENGF 160
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
717-739 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 1720355778  717 QGYTPLHWACYNGNENCIEVLLE 739
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLD 23
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
615-644 1.79e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 1.79e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1720355778 615 KGQTPLMLAVAYGHIDAVSLLLEKEANVDA 644
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
383-412 1.99e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 1.99e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1720355778 383 CGRTPLHYAAANCHFHCIKALVTTGANVNE 412
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02795 PHA02795
ankyrin-like protein; Provisional
52-129 1.99e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 41.52  E-value: 1.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778  52 EVIIPLLSSVNVSDRGGRTALHHAALNGHMEMVNLLLAKGANINAFDKKDRRALHWAAYMG--------HLDVVALLINH 123
Cdd:PHA02795  205 KLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHLKILEILLRE 284

                  ....*.
gi 1720355778 124 GAEVTC 129
Cdd:PHA02795  285 PLSIDC 290
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
545-577 2.00e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 2.00e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1720355778 545 KGRTALYLAAFK-GHTECVEALVNQGASIFVKDN 577
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
606-654 2.01e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 2.01e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1720355778 606 PEVVDVKDAKGQTPLMLAVAYGHIDAVSLLLEKEANVDAVDIVGCTALH 654
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
104-132 2.23e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 2.23e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1720355778 104 ALHWAAYM-GHLDVVALLINHGAEVTCKDK 132
Cdd:pfam00023   5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
666-909 2.25e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.99  E-value: 2.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 666 QMLLEQEAS-ILCKDSRGRTPLHYAAARGHatwlNELLQIALSEEDCclKDNQGYTPLHWACYNGNENCIEVLLEQKCFR 744
Cdd:TIGR00870  35 RDLEEPKKLnINCPDRLGRSALFVAAIENE----NLELTELLLNLSC--RGAVGDTLLHAISLEYVDAVEAILLHLLAAF 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 745 KFIGNPF--------------TPLHCAIINGHESCASLLL--GAIDPSIVSCRDDK----------GRTTLHAAAFGDHA 798
Cdd:TIGR00870 109 RKSGPLElandqytseftpgiTALHLAAHRQNYEIVKLLLerGASVPARACGDFFVksqgvdsfyhGESPLNAAACLGSP 188
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 799 ECLQLLLRHDAQVNAVDNSGKTALMMAAEngqagavdilvnsaQADLTVKDKDLNTPLHLAiskghekcALLILDKIQD- 877
Cdd:TIGR00870 189 SIVALLSEDPADILTADSLGNTLLHLLVM--------------ENEFKAEYEELSCQMYNF--------ALSLLDKLRDs 246
                         250       260       270
                  ....*....|....*....|....*....|..
gi 1720355778 878 ESLINAKNSALQTPLHIAARNGLKVVVEELLA 909
Cdd:TIGR00870 247 KELEVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
351-379 2.37e-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: 2.37e-03
                           10        20
                   ....*....|....*....|....*....
gi 1720355778  351 GRTCLHAAAAGGNVECIKLLQSSGADFHK 379
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
615-644 2.95e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 2.95e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1720355778  615 KGQTPLMLAVAYGHIDAVSLLLEKEANVDA 644
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
798-914 2.96e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.13  E-value: 2.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 798 AECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNSAQADLTVKDKDLNTPLHLA-ISKGHEKCALLILDKIQ 876
Cdd:PHA02875   48 SEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLAtILKKLDIMKLLIARGAD 127
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1720355778 877 DEslinAKNSALQTPLHIAARNGLKVVVEELLAKGACV 914
Cdd:PHA02875  128 PD----IPNTDKFSPLHLAVMMGDIKGIELLIDHKACL 161
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
575-687 3.05e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 41.32  E-value: 3.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 575 KDNVTKRTPLHASVIN---GHTLCLRLLLETAD---------NPEVVDVKdAKGQTPLMLAVAYGHIDAVSLLLEKEANV 642
Cdd:cd22193    24 TESSTGKTCLMKALLNlnpGTNDTIRILLDIAEktdnlkrfiNAEYTDEY-YEGQTALHIAIERRQGDIVALLVENGADV 102
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720355778 643 DAVD--------------IVGCTALHRGIMTGHEECVQMLLE---QEASILCKDSRGRTPLH 687
Cdd:cd22193   103 HAHAkgrffqpkyqgegfYFGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNTVLH 164
Ank_2 pfam12796
Ankyrin repeats (3 copies);
4-32 3.99e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.40  E-value: 3.99e-03
                          10        20
                  ....*....|....*....|....*....
gi 1720355778   4 TPLHRAVASRSEEAVQVLIKHSADVNARD 32
Cdd:pfam12796  63 TALHYAARSGHLEIVKLLLEKGADINVKD 91
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
104-129 4.03e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 4.03e-03
                           10        20
                   ....*....|....*....|....*.
gi 1720355778  104 ALHWAAYMGHLDVVALLINHGAEVTC 129
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
219-274 5.03e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 5.03e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720355778 219 LLVNNGADVNIQSKDGKSPLHMTAVHGRFTRSQTLIQNGGEIDCVDKDGNTPLHVA 274
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
545-574 5.31e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 5.31e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1720355778  545 KGRTALYLAAFKGHTECVEALVNQGASIFV 574
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
514-565 5.74e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 5.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1720355778 514 KSPLHLAAYNGHHQALEVLLQSLVDLDIRDEKGRTALYLAAFKGHTECVEAL 565
Cdd:PTZ00322  116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_5 pfam13857
Ankyrin repeats (many copies);
837-895 5.89e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 5.89e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1720355778 837 LVNSAQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIA 895
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVD---LNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
784-816 6.51e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 6.51e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1720355778 784 KGRTTLHAAA-FGDHAECLQLLLRHDAQVNAVDN 816
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
351-500 6.81e-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: 40.13  E-value: 6.81e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 351 GRTCLHAAAAGGNVECIKLLQSSGAD---------FHKKDK-----CGRTPLHYAAANCHFHCIKALVTTGA-NVNETDD 415
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADvnahakgvfFNPKYKhegfyFGETPLALAACTNQPEIVQLLMEKEStDITSQDS 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 416 WGRTALH--YAAASDMDRNKMILGNAHDnseELERAREVKEkdaalcLEfllqndanpSIRDKEGYNSIHYAAAYGHRQC 493
Cdd:cd22194   221 RGNTVLHalVTVAEDSKTQNDFVKRMYD---MILLKSENKN------LE---------TIRNNEGLTPLQLAAKMGKAEI 282

                  ....*..
gi 1720355778 494 LELLLER 500
Cdd:cd22194   283 LKYILSR 289
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
351-382 7.62e-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: 7.62e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1720355778 351 GRTCLHAAAA-GGNVECIKLLQSSGADFHKKDK 382
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
4-33 7.93e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 7.93e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1720355778   4 TPLHRAVASR-SEEAVQVLIKHSADVNARDK 33
Cdd:pfam00023   4 TPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
PHA02859 PHA02859
ankyrin repeat protein; Provisional
353-422 8.38e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 38.65  E-value: 8.38e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355778 353 TCLHAAAAggNVECIKLLQSSGADF-HKKDKCGRTPLHYAAA---NCHFHCIKALVTTGANVNETDDWGRTALH 422
Cdd:PHA02859   57 SCLEKDKV--NVEILKFLIENGADVnFKTRDNNLSALHHYLSfnkNVEPEILKILIDSGSSITEEDEDGKNLLH 128
PHA02874 PHA02874
ankyrin repeat protein; Provisional
783-912 8.42e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.56  E-value: 8.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 783 DKGRTTLHAAAFGDHAECLQLLLRHDAQVNAVDNSGKTALMMAAENGQAGAVDILVNS---------------------- 840
Cdd:PHA02874   33 DETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNgvdtsilpipciekdmiktild 112
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720355778 841 AQADLTVKDKDLNTPLHLAISKGHEKCALLILDKIQDeslINAKNSALQTPLHIAARNGLKVVVEELLAKGA 912
Cdd:PHA02874  113 CGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGAD---VNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA 181
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
167-278 8.51e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 39.78  E-value: 8.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720355778 167 GNTALHIACYNGQDAVVNELIDYGANVN--------QPNNS------GFTPLHFAAASTHGALCLELLVNNGADVNIQSK 232
Cdd:cd22193    76 GQTALHIAIERRQGDIVALLVENGADVHahakgrffQPKYQgegfyfGELPLSLAACTNQPDIVQYLLENEHQPADIEAQ 155
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720355778 233 D--GKSPLHMTAVHGRFTRSQT---------LIQNGGEI-------DCVDKDGNTPLHVAARHG 278
Cdd:cd22193   156 DsrGNTVLHALVTVADNTKENTkfvtrmydmILIRGAKLcptveleEIRNNDGLTPLQLAAKMG 219
 
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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