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Conserved domains on  [gi|1785376409|ref|XP_031760399|]
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serine/threonine-protein phosphatase 6 regulatory ankyrin repeat subunit A isoform X1 [Xenopus tropicalis]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
81-370 2.24e-49

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 177.07  E-value: 2.24e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   81 AEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNV 160
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  161 NVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAA 240
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  241 ASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLV 320
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1785376409  321 cNGADVNIKSKDGKTPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPL 370
Cdd:COG0666    241 -AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
693-1023 1.96e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.48  E-value: 1.96e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  693 LRLLIGNADVQAAVDIHDGNGQTPLMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANF 772
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  773 LLRDCRGRTPIHLAAACGHIGVLSALLQTAISVDVVpaiaDNHGYTPLHWACYNGHDACVELLLEQevfqkmegnsfspl 852
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR----DKDGETPLHLAAYNGNLEIVKLLLEA-------------- 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  853 hcavindneGAAemlidtlgtsiVNSVDSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAV 932
Cdd:COG0666    143 ---------GAD-----------VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  933 EVLVsSAKADLTLQDKNKNTALHLACSKGHETSALLILEQITDrnlINATNSALQTPLHVAARNGLTVVVQELLGKGASV 1012
Cdd:COG0666    203 KLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
                          330
                   ....*....|.
gi 1785376409 1013 LAVDENGYTPA 1023
Cdd:COG0666    279 AAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
249-530 7.05e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 7.05e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  249 IKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLVCNGADVNI 328
Cdd:COG0666      3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  329 KSKDGKTPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSRADTSKRGIHGMFPLHLAAL 408
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  409 SGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSG 488
Cdd:COG0666    163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1785376409  489 ASVNDLDERGCSPLHYAATSDTDGKCLEYLLRNDANPGIRDK 530
Cdd:COG0666    243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
PHA03100 super family cl39094
ankyrin repeat protein; Provisional
416-651 1.15e-16

ankyrin repeat protein; Provisional


The actual alignment was detected with superfamily member PHA03100:

Pssm-ID: 476869 [Multi-domain]  Cd Length: 422  Bit Score: 83.95  E-value: 1.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  416 RKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAA-----ANCNYQCLFALVGSGAS 490
Cdd:PHA03100    19 KYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGAN 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  491 VNDLDERGCSPLHYAATSD-TDGKCLEYLLRNDANPGIRDKHGYNAVHYAaayghrlcLELIARETPLDVLMETSGTDMl 569
Cdd:PHA03100    99 VNAPDNNGITPLLYAISKKsNSYSIVEYLLDNGANVNIKNSDGENLLHLY--------LESNKIDLKILKLLIDKGVDI- 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  570 nDAETRapisplhlaayhghhqaLEVLVQSLLDLDVRNSTGRTPLDLAAFKGHVECVDVLINQGASILVKDYVVKrTPIH 649
Cdd:PHA03100   170 -NAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD-TPLH 230

                   ..
gi 1785376409  650 SA 651
Cdd:PHA03100   231 IA 232
PTZ00322 super family cl31426
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
10-124 2.84e-06

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


The actual alignment was detected with superfamily member PTZ00322:

Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 2.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   10 EEGEDDAPHftsKLPQRKILTPP--GIVTPPLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELL 87
Cdd:PTZ00322    58 ENKDATPDH---NLTTEEVIDPVvaHMLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVL 134
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1785376409   88 ILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHS 124
Cdd:PTZ00322   135 LEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHS 171
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
81-370 2.24e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 177.07  E-value: 2.24e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   81 AEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNV 160
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  161 NVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAA 240
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  241 ASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLV 320
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1785376409  321 cNGADVNIKSKDGKTPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPL 370
Cdd:COG0666    241 -AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
49-337 1.19e-40

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 157.11  E-value: 1.19e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   49 DEVRALIFKKEDVNFQDNEKRTPLHAaaYLG-----DAEIIELLILSGARVNAKDSKWLTPLHRAV-ASCSEDAVQVLLK 122
Cdd:PHA03095    28 EEVRRLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLyNATTLDVIKLLIK 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  123 HSADVNARDKNWQTPLHIAAANKAVkcaealvpllsnvnvsdragrtalhhaafsgHVEMVSLLLSRGANINAFDKKDRR 202
Cdd:PHA03095   106 AGADVNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  203 AIHwaAYMGH----IEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMIS--VIKYLLDLGVDMNESNAYGNTPLHVACYN 276
Cdd:PHA03095   155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785376409  277 G--QDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLVCnGADVNIKSKDGKTPL 337
Cdd:PHA03095   233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIAL-GADINAVSSDGNTPL 294
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
693-1023 1.96e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.48  E-value: 1.96e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  693 LRLLIGNADVQAAVDIHDGNGQTPLMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANF 772
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  773 LLRDCRGRTPIHLAAACGHIGVLSALLQTAISVDVVpaiaDNHGYTPLHWACYNGHDACVELLLEQevfqkmegnsfspl 852
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR----DKDGETPLHLAAYNGNLEIVKLLLEA-------------- 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  853 hcavindneGAAemlidtlgtsiVNSVDSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAV 932
Cdd:COG0666    143 ---------GAD-----------VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  933 EVLVsSAKADLTLQDKNKNTALHLACSKGHETSALLILEQITDrnlINATNSALQTPLHVAARNGLTVVVQELLGKGASV 1012
Cdd:COG0666    203 KLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
                          330
                   ....*....|.
gi 1785376409 1013 LAVDENGYTPA 1023
Cdd:COG0666    279 AAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
249-530 7.05e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 7.05e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  249 IKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLVCNGADVNI 328
Cdd:COG0666      3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  329 KSKDGKTPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSRADTSKRGIHGMFPLHLAAL 408
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  409 SGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSG 488
Cdd:COG0666    163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1785376409  489 ASVNDLDERGCSPLHYAATSDTDGKCLEYLLRNDANPGIRDK 530
Cdd:COG0666    243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
PHA03095 PHA03095
ankyrin-like protein; Provisional
246-532 4.41e-31

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 128.60  E-value: 4.41e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  246 ISVIKYLLDLGVDMNESNAYGNTPLHV--ACYNGQDV-VVNELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLVCN 322
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHLylHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  323 GADVNIKSKDGKTPLHmtaihgrfsrsqiiiqngaeIDCEDKNGNTPlhiaaryghelLINTLITSRADTSKRGIHGMFP 402
Cdd:PHA03095   107 GADVNAKDKVGRTPLH--------------------VYLSGFNINPK-----------VIRLLLRKGADVNALDLYGMTP 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  403 LHlaALSGFSDCC----RKLLSSGFDIDTHDDFGRTCLH--AAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAA-- 474
Cdd:PHA03095   156 LA--VLLKSRNANvellRLLIDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATgs 233
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1785376409  475 NCNYQCLFALVGSGASVNDLDERGCSPLHYAATSDTDGKClEYLLRNDANPGIRDKHG 532
Cdd:PHA03095   234 SCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRAC-RRLIALGADINAVSSDG 290
Ank_2 pfam12796
Ankyrin repeats (3 copies);
105-197 4.86e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 4.86e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  105 LHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLsNVNVSDRaGRTALHHAAFSGHVEMVS 184
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1785376409  185 LLLSRGANINAFD 197
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
403-495 2.07e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.01  E-value: 2.07e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  403 LHLAALSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTgADFNKKDKfGRTPLHYAAANCNYQCLF 482
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1785376409  483 ALVGSGASVNDLD 495
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
694-1023 5.97e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 91.24  E-value: 5.97e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  694 RLLIGNADVQaavdiHDGN-GQTPLMLSVLNGH---TECVYSLLNKGANVDAKDKWGRTALH---RGAVTghEECVEALL 766
Cdd:PHA03095    32 RLLAAGADVN-----FRGEyGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHlylYNATT--LDVIKLLI 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  767 QHNANFLLRDCRGRTPIH--LAAACGHIGVLSALLQTAISVDVVpaiaDNHGYTPLHwACYNGHDACVELLleqevfqkm 844
Cdd:PHA03095   105 KAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNAL----DLYGMTPLA-VLLKSRNANVELL--------- 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  845 egnsfsplhcavindnegaaEMLIDTlGTSIVNsVDSKGRTPLH--AAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMM 922
Cdd:PHA03095   171 --------------------RLLIDA-GADVYA-VDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHS 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  923 AAengqtsavevLVSSAKADLTLQdknkntalhlacskghetsalLILEQITdrnlINATNSALQTPLHVAARNGLTVVV 1002
Cdd:PHA03095   229 MA----------TGSSCKRSLVLP---------------------LLIAGIS----INARNRYGQTPLHYAAVFNNPRAC 273
                          330       340
                   ....*....|....*....|.
gi 1785376409 1003 QELLGKGASVLAVDENGYTPA 1023
Cdd:PHA03095   274 RRLIALGADINAVSSDGNTPL 294
Ank_2 pfam12796
Ankyrin repeats (3 copies);
717-807 1.19e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 1.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  717 LMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNAnfLLRDCRGRTPIHLAAACGHIGVLS 796
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 1785376409  797 ALLQTAISVDV 807
Cdd:pfam12796   79 LLLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
416-651 1.15e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.95  E-value: 1.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  416 RKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAA-----ANCNYQCLFALVGSGAS 490
Cdd:PHA03100    19 KYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGAN 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  491 VNDLDERGCSPLHYAATSD-TDGKCLEYLLRNDANPGIRDKHGYNAVHYAaayghrlcLELIARETPLDVLMETSGTDMl 569
Cdd:PHA03100    99 VNAPDNNGITPLLYAISKKsNSYSIVEYLLDNGANVNIKNSDGENLLHLY--------LESNKIDLKILKLLIDKGVDI- 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  570 nDAETRapisplhlaayhghhqaLEVLVQSLLDLDVRNSTGRTPLDLAAFKGHVECVDVLINQGASILVKDYVVKrTPIH 649
Cdd:PHA03100   170 -NAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD-TPLH 230

                   ..
gi 1785376409  650 SA 651
Cdd:PHA03100   231 IA 232
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
101-308 1.50e-13

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: 75.05  E-value: 1.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  101 WLTPLHRAVASCSEDAVQVLLK-HSADVNARDKNWQTPLHIAAANKAVKCAEAL---VPLLSNVNV-SD-RAGRTALHHA 174
Cdd:cd22192     17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLmeaAPELVNEPMtSDlYQGETALHIA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  175 AFSGHVEMVSLLLSRGANIN-------AFDKKDRRAIHW-------AAYMGHIEVVKLLVTHGAEVMCKDkksytplhaa 240
Cdd:cd22192     97 VVNQNLNLVRELIARGADVVspratgtFFRPGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQD---------- 166
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785376409  241 assgmisvikylldlgvdmnesnAYGNTPLHVACYNGQDVVVNELIDC----GANVNQV------NERGFTPLHFAAA 308
Cdd:cd22192    167 -----------------------SLGNTVLHILVLQPNKTFACQMYDLilsyDKEDDLQpldlvpNNQGLTPFKLAAK 221
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
301-470 1.09e-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: 68.89  E-value: 1.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  301 TPLhFAAASTHGALCLE-LLVCNGADVNIKSKDGKTPLHMTAIHGRFSRSQIIIQNGAE-----IDCEDKNGNTPLHIAA 374
Cdd:cd22192     19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  375 RYGHELLINTLITSRADTSKRGIHGMFplhlaalsgFSDCCRKLLSsgfdidthddFGRTCLHAAAAGGNLECLNLLLST 454
Cdd:cd22192     98 VNQNLNLVRELIARGADVVSPRATGTF---------FRPGPKNLIY----------YGEHPLSFAACVGNEEIVRLLIEH 158
                          170
                   ....*....|....*.
gi 1785376409  455 GADFNKKDKFGRTPLH 470
Cdd:cd22192    159 GADIRAQDSLGNTVLH 174
Ank_2 pfam12796
Ankyrin repeats (3 copies);
537-640 2.32e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.90  E-value: 2.32e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  537 HYAAAYGHRLCLELIAREtpldvlmetsGTDMlnDAETRAPISPLHLAAYHGHHQALEVLVQSLlDLDVRNStGRTPLDL 616
Cdd:pfam12796    2 HLAAKNGNLELVKLLLEN----------GADA--NLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHY 67
                           90       100
                   ....*....|....*....|....
gi 1785376409  617 AAFKGHVECVDVLINQGASILVKD 640
Cdd:pfam12796   68 AARSGHLEIVKLLLEKGADINVKD 91
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
405-662 1.47e-08

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 58.74  E-value: 1.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  405 LAALSGFSDCCRKLLSSgfDIDTHDDFGRTCLHAAA---AGGNLECLNLLLSTGADFNKKDKF-----------GRTPLH 470
Cdd:cd21882      1 LEELLGLLECLRWYLTD--SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELvnapctdefyqGQTALH 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  471 YAAANCNYQCLFALVGSGASVN-----DLDER--------GCSPLHYAATSDTDgKCLEYLLRNDANP---GIRDKHGYN 534
Cdd:cd21882     79 IAIENRNLNLVRLLVENGADVSaratgRFFRKspgnlfyfGELPLSLAACTNQE-EIVRLLLENGAQPaalEAQDSLGNT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  535 AVHyaaayghrlCLELIARETPLDVLMETSGTDMLndaetrapispLHLAAYHGHHQALEvlvqslldlDVRNSTGRTPL 614
Cdd:cd21882    158 VLH---------ALVLQADNTPENSAFVCQMYNLL-----------LSYGAHLDPTQQLE---------EIPNHQGLTPL 208
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1785376409  615 DLAAFKGHVECVDVLINQGASILVKDYVVKRT-----PIHSA--EIQMVDS--RNSV 662
Cdd:cd21882    209 KLAAVEGKIVMFQHILQREFSGPYQPLSRKFTewtygPVTSSlyDLSEIDSweKNSV 265
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
772-1008 5.95e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.94  E-value: 5.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  772 FLLRDCRGR-TPIHLAAACGHIGVLSALLQTAiSVDVVPAIAdnHGYTPLHWACYNGHDACVELLLEQE---VFQKMEGN 847
Cdd:cd22192      9 HLLQQKRISeSPLLLAAKENDVQAIKKLLKCP-SCDLFQRGA--LGETALHVAALYDNLEAAVVLMEAApelVNEPMTSD 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  848 SF---SPLHCAVINDNEGAAEMLI----DTL-----GTSIVNSVDSK---GRTPLHAAAFTDHIECLQLLLSHNAQVNAV 912
Cdd:cd22192     86 LYqgeTALHIAVVNQNLNLVRELIargaDVVspratGTFFRPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQ 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  913 DSTGKTPL-MMAAENGQTSAVEVLvssakaDLTL-QDKNKNtalhlacskghetsaLLILEQItdrnlinaTNSALQTPL 990
Cdd:cd22192    166 DSLGNTVLhILVLQPNKTFACQMY------DLILsYDKEDD---------------LQPLDLV--------PNNQGLTPF 216
                          250
                   ....*....|....*...
gi 1785376409  991 HVAARNGLTVVVQELLGK 1008
Cdd:cd22192    217 KLAAKEGNIVMFQHLVQK 234
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
55-307 2.80e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 54.70  E-value: 2.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   55 IFKKEDVNFQDNEKrtplhaaAYLGDAEIIELLILSGARVNAK-------DSKWLTPLHRAVA-SCSEDAVQVLLKHSAD 126
Cdd:TIGR00870    6 IVPAEESPLSDEEK-------AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  127 VNARDknwqTPLHIAAANKAVKCAEALVPLLSN---------VNVSDR----AGRTALHHAAFSGHVEMVSLLLSRGANI 193
Cdd:TIGR00870   79 GAVGD----TLLHAISLEYVDAVEAILLHLLAAfrksgplelANDQYTseftPGITALHLAAHRQNYEIVKLLLERGASV 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  194 NA------FDKKDRRA--------IHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAAAssgmisvikylldlgvdM 259
Cdd:TIGR00870  155 PAracgdfFVKSQGVDsfyhgespLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV-----------------M 217
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409  260 NESNAYGNTPLHVACYNG--------QDVVVNELIdcganvnqVNERGFTPLHFAA 307
Cdd:TIGR00870  218 ENEFKAEYEELSCQMYNFalslldklRDSKELEVI--------LNHQGLTPLKLAA 265
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
10-124 2.84e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 2.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   10 EEGEDDAPHftsKLPQRKILTPP--GIVTPPLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELL 87
Cdd:PTZ00322    58 ENKDATPDH---NLTTEEVIDPVvaHMLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVL 134
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1785376409   88 ILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHS 124
Cdd:PTZ00322   135 LEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHS 171
Ank_4 pfam13637
Ankyrin repeats (many copies);
36-88 4.91e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 4.91e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1785376409   36 TPPLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLI 88
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
167-195 9.73e-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: 43.35  E-value: 9.73e-06
                            10        20
                    ....*....|....*....|....*....
gi 1785376409   167 GRTALHHAAFSGHVEMVSLLLSRGANINA 195
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
418-621 5.04e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.38  E-value: 5.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  418 LLSSGFDIDThddfGRTCLHAAAAG--GNLE-CLNLLL----STGADFNKKDK------FGRTPLHYAAANCNYQCLFAL 484
Cdd:TIGR00870   72 LLNLSCRGAV----GDTLLHAISLEyvDAVEaILLHLLaafrKSGPLELANDQytseftPGITALHLAAHRQNYEIVKLL 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  485 VGSGASVN--------------DLDERGCSPLH-YAATSDTDgkCLEYLLRNDANPGIRDKHGyNAVhyaaayghrlcLE 549
Cdd:TIGR00870  148 LERGASVParacgdffvksqgvDSFYHGESPLNaAACLGSPS--IVALLSEDPADILTADSLG-NTL-----------LH 213
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785376409  550 LIARETPLDVLMETSGTDMLNDAetrapispLHLAAYHGHHQALEVlvqslldldVRNSTGRTPLDLAAFKG 621
Cdd:TIGR00870  214 LLVMENEFKAEYEELSCQMYNFA--------LSLLDKLRDSKELEV---------ILNHQGLTPLKLAAKEG 268
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
713-857 5.30e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.38  E-value: 5.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  713 GQTPLMLSVLNGHTECVYSLLNKGANVDAKDK--------------WGRTALHRGAVTGHEECVEALLQHNANFLLRDCR 778
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  779 GRTPIHLAA------------ACG-HIGVLSALLQTAISVDvVPAIADNHGYTPLHWACYNGHDACVELLLEQEVFQ-KM 844
Cdd:TIGR00870  208 GNTLLHLLVmenefkaeyeelSCQmYNFALSLLDKLRDSKE-LEVILNHQGLTPLKLAAKEGRIVLFRLKLAIKYKQkKF 286
                          170
                   ....*....|...
gi 1785376409  845 EGNSFSPLHCAVI 857
Cdd:TIGR00870  287 VAWPNGQQLLSLY 299
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
432-460 2.90e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 2.90e-04
                            10        20
                    ....*....|....*....|....*....
gi 1785376409   432 GRTCLHAAAAGGNLECLNLLLSTGADFNK 460
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
882-911 3.14e-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: 3.14e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1785376409   882 KGRTPLHAAAFTDHIECLQLLLSHNAQVNA 911
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
610-636 3.49e-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: 3.49e-03
                            10        20
                    ....*....|....*....|....*..
gi 1785376409   610 GRTPLDLAAFKGHVECVDVLINQGASI 636
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
38-106 4.33e-03

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: 41.15  E-value: 4.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   38 PLVQAIFNGDPDEVRALIFKKEDVN--------FQDNEKRT------PLHAAAYLGDAEIIELLILSGARVNAKDSKWLT 103
Cdd:cd22192     92 ALHIAVVNQNLNLVRELIARGADVVspratgtfFRPGPKNLiyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171

                   ...
gi 1785376409  104 PLH 106
Cdd:cd22192    172 VLH 174
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
81-370 2.24e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 177.07  E-value: 2.24e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   81 AEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNV 160
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  161 NVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAA 240
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  241 ASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLV 320
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1785376409  321 cNGADVNIKSKDGKTPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPL 370
Cdd:COG0666    241 -AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
27-303 9.86e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 175.14  E-value: 9.86e-49
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   27 KILTPPGIVTPPLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLH 106
Cdd:COG0666     13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  107 RAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLL 186
Cdd:COG0666     93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  187 LSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMISVIKYLLDLGVDMNESNAYG 266
Cdd:COG0666    173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252
                          250       260       270
                   ....*....|....*....|....*....|....*..
gi 1785376409  267 NTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPL 303
Cdd:COG0666    253 LTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
49-319 1.31e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 172.06  E-value: 1.31e-47
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   49 DEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVN 128
Cdd:COG0666      2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  129 ARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAA 208
Cdd:COG0666     82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  209 YMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDC 288
Cdd:COG0666    162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1785376409  289 GANVNQVNERGFTPLHFAAASTHGALCLELL 319
Cdd:COG0666    242 GADLNAKDKDGLTALLLAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
150-434 1.66e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 165.90  E-value: 1.66e-45
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  150 AEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVTHGAEVMCK 229
Cdd:COG0666      4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  230 DKKSYTPLHAAASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAAS 309
Cdd:COG0666     84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  310 THGALcLELLVCNGADVNIKSKDGKTPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSR 389
Cdd:COG0666    164 GNLEI-VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*
gi 1785376409  390 ADTSKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTHDDFGRT 434
Cdd:COG0666    243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
180-469 2.45e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 156.65  E-value: 2.45e-42
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  180 VEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMISVIKYLLDLGVDM 259
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  260 NESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALcLELLVCNGADVNIKSKDGKTPLHM 339
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI-VKLLLEAGADVNAQDNDGNTPLHL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  340 TAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSRADTSKRGIHGMFPLHLAALSGFSDCCRKLL 419
Cdd:COG0666    160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|
gi 1785376409  420 SSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPL 469
Cdd:COG0666    240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
49-337 1.19e-40

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 157.11  E-value: 1.19e-40
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   49 DEVRALIFKKEDVNFQDNEKRTPLHAaaYLG-----DAEIIELLILSGARVNAKDSKWLTPLHRAV-ASCSEDAVQVLLK 122
Cdd:PHA03095    28 EEVRRLLAAGADVNFRGEYGKTPLHL--YLHyssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLyNATTLDVIKLLIK 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  123 HSADVNARDKNWQTPLHIAAANKAVkcaealvpllsnvnvsdragrtalhhaafsgHVEMVSLLLSRGANINAFDKKDRR 202
Cdd:PHA03095   106 AGADVNAKDKVGRTPLHVYLSGFNI-------------------------------NPKVIRLLLRKGADVNALDLYGMT 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  203 AIHwaAYMGH----IEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMIS--VIKYLLDLGVDMNESNAYGNTPLHVACYN 276
Cdd:PHA03095   155 PLA--VLLKSrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLGNTPLHSMATG 232
                          250       260       270       280       290       300
                   ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785376409  277 G--QDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLVCnGADVNIKSKDGKTPL 337
Cdd:PHA03095   233 SscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIAL-GADINAVSSDGNTPL 294
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
213-498 4.07e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.41  E-value: 4.07e-39
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  213 IEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDCGANV 292
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  293 NQVNERGFTPLHFAAASTHGALcLELLVCNGADVNIKSKDGKTPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHI 372
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEI-VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  373 AARYGHELLINTLITSRADTSKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLL 452
Cdd:COG0666    160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1785376409  453 STGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDERG 498
Cdd:COG0666    240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
693-1023 1.96e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.48  E-value: 1.96e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  693 LRLLIGNADVQAAVDIHDGNGQTPLMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANF 772
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  773 LLRDCRGRTPIHLAAACGHIGVLSALLQTAISVDVVpaiaDNHGYTPLHWACYNGHDACVELLLEQevfqkmegnsfspl 852
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR----DKDGETPLHLAAYNGNLEIVKLLLEA-------------- 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  853 hcavindneGAAemlidtlgtsiVNSVDSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAV 932
Cdd:COG0666    143 ---------GAD-----------VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  933 EVLVsSAKADLTLQDKNKNTALHLACSKGHETSALLILEQITDrnlINATNSALQTPLHVAARNGLTVVVQELLGKGASV 1012
Cdd:COG0666    203 KLLL-EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGAD---LNAKDKDGLTALLLAAAAGAALIVKLLLLALLLL 278
                          330
                   ....*....|.
gi 1785376409 1013 LAVDENGYTPA 1023
Cdd:COG0666    279 AAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
249-530 7.05e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 7.05e-38
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  249 IKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLVCNGADVNI 328
Cdd:COG0666      3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  329 KSKDGKTPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSRADTSKRGIHGMFPLHLAAL 408
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  409 SGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSG 488
Cdd:COG0666    163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1785376409  489 ASVNDLDERGCSPLHYAATSDTDGKCLEYLLRNDANPGIRDK 530
Cdd:COG0666    243 ADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
PHA03100 PHA03100
ankyrin repeat protein; Provisional
50-328 1.77e-37

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 146.35  E-value: 1.77e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   50 EVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLH-----RAVASCSEDAVQVLLKHS 124
Cdd:PHA03100    17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYG 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  125 ADVNARDKNWQTPLHIAAANKavkcaealvpllsnvnvsdragrtalhhaafSGHVEMVSLLLSRGANINAFDKKDRRAI 204
Cdd:PHA03100    97 ANVNAPDNNGITPLLYAISKK-------------------------------SNSYSIVEYLLDNGANVNIKNSDGENLL 145
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  205 HWAAYMGHI--EVVKLLVTHGAEVMCKDKksytplhaaassgmisvIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVV 282
Cdd:PHA03100   146 HLYLESNKIdlKILKLLIDKGVDINAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFV 208
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1785376409  283 NELIDCGANVNQVNERGFTPLHFAAASTHGALcLELLVCNGADVNI 328
Cdd:PHA03100   209 KYLLDLGANPNLVNKYGDTPLHIAILNNNKEI-FKLLLNNGPSIKT 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
290-552 1.82e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.79  E-value: 1.82e-37
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  290 ANVNQVNERGFTPLHFAAASTHGALCLELLVCNGADVNIKSKDGKTPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTP 369
Cdd:COG0666     11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  370 LHIAARYGHELLINTLITSRADTSKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLN 449
Cdd:COG0666     91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  450 LLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDERGCSPLHYAATSDtDGKCLEYLLRNDANPGIRD 529
Cdd:COG0666    171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENG-NLEIVKLLLEAGADLNAKD 249
                          250       260
                   ....*....|....*....|...
gi 1785376409  530 KHGYNAVHYAAAYGHRLCLELIA 552
Cdd:COG0666    250 KDGLTALLLAAAAGAALIVKLLL 272
PHA02876 PHA02876
ankyrin repeat protein; Provisional
49-376 7.74e-35

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 142.89  E-value: 7.74e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   49 DEVR---ALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSA 125
Cdd:PHA02876   156 DELLiaeMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRS 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  126 DVNARDKNwqtpLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHV-EMVSLLLSRGANINAFDKKDRRAI 204
Cdd:PHA02876   236 NINKNDLS----LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPL 311
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  205 HWAAYMGH-IEVVKLLVTHGAEVMCKDKKSYTPLHAAAS-SGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVV 282
Cdd:PHA02876   312 YLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVII 391
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  283 NELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLVCNGADVNIKSKDGKTPLHMTAIHG-RFSRSQIIIQNGAEIDC 361
Cdd:PHA02876   392 NTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNA 471
                          330
                   ....*....|....*
gi 1785376409  362 EDKNGNTPLHIAARY 376
Cdd:PHA02876   472 INIQNQYPLLIALEY 486
PHA02874 PHA02874
ankyrin repeat protein; Provisional
43-391 8.41e-35

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 138.94  E-value: 8.41e-35
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   43 IFNGDPDEVRALIFKKED-VNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLL 121
Cdd:PHA02874     9 IYSGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  122 KHSADVNARDknwqtplhiaaankavkcaealVPLLSNvnvsdragrtalhhaafsghvEMVSLLLSRGANINAFDKKDR 201
Cdd:PHA02874    89 DNGVDTSILP----------------------IPCIEK---------------------DMIKTILDCGIDVNIKDAELK 125
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  202 RAIHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVV 281
Cdd:PHA02874   126 TFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  282 VNELIDCGANVNQVNERGFTPLHfaAASTHGALCLELLVcNGADVNIKSKDGKTPLHMtAIHGRFSRS--QIIIQNGAEI 359
Cdd:PHA02874   206 IKLLIDHGNHIMNKCKNGFTPLH--NAIIHNRSAIELLI-NNASINDQDIDGSTPLHH-AINPPCDIDiiDILLYHKADI 281
                          330       340       350
                   ....*....|....*....|....*....|....*...
gi 1785376409  360 DCEDKNGNTPLHIAARYGH------ELLINTLITSRAD 391
Cdd:PHA02874   282 SIKDNKGENPIDTAFKYINkdpvikDIIANAVLIKEAD 319
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
732-1041 1.24e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.31  E-value: 1.24e-34
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  732 LLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPIHLAAACGHIGVLSALLQTAISVDvvpaI 811
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN----A 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  812 ADNHGYTPLHWACYNGHDACVELLLEQevfqkmegnsfsplhcavindneGAaemlidtlgtsIVNSVDSKGRTPLHAAA 891
Cdd:COG0666     83 KDDGGNTLLHAAARNGDLEIVKLLLEA-----------------------GA-----------DVNARDKDGETPLHLAA 128
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  892 FTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAVEVLVSsAKADLTLQDKNKNTALHLACSKGHETSALLILE 971
Cdd:COG0666    129 YNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLE-AGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207
                          250       260       270       280       290       300       310
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  972 QITDrnlINATNSALQTPLHVAARNGLTVVVQELLGKGASVLAVDENGYTPALACAPNKDVADCLALILA 1041
Cdd:COG0666    208 AGAD---VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
PHA03095 PHA03095
ankyrin-like protein; Provisional
113-393 2.71e-33

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 135.15  E-value: 2.71e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  113 SEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLL---SNVNVSDRAGRTALH-HAAFSGHVEMVSLLLS 188
Cdd:PHA03095    26 TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIVRLLLeagADVNAPERCGFTPLHlYLYNATTLDVIKLLIK 105
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  189 RGANINAFDKKDRRAIHwaAYMG----HIEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMISV--IKYLLDLGVDMNES 262
Cdd:PHA03095   106 AGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV 183
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  263 NAYGNTPLHVACYNGQD--VVVNELIDCGANVNQVNERGFTPLHFAAA-STHGALCLELLVCNGADVNIKSKDGKTPLHM 339
Cdd:PHA03095   184 DDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATgSSCKRSLVLPLLIAGISINARNRYGQTPLHY 263
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1785376409  340 TAIHGR---FSRsqiIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSRADTS 393
Cdd:PHA03095   264 AAVFNNpraCRR---LIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
810-1065 2.74e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 130.46  E-value: 2.74e-33
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  810 AIADNHGYTPLHWACYNGHDACVELLLEQEVFQKMEGNSFSPLHCAVINDNEGAAEMLIDTLGTSIvNSVDSKGRTPLHA 889
Cdd:COG0666     15 LLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI-NAKDDGGNTLLHA 93
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  890 AAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAVEVLVSsAKADLTLQDKNKNTALHLACSKGHETSALLI 969
Cdd:COG0666     94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLE-AGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  970 LEQITDrnlINATNSALQTPLHVAARNGLTVVVQELLGKGASVLAVDENGYTPALACAPNKDVADCLALILATMMPVSSS 1049
Cdd:COG0666    173 LEAGAD---VNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249
                          250
                   ....*....|....*.
gi 1785376409 1050 SSLPSMTLNAINHYNN 1065
Cdd:COG0666    250 KDGLTALLLAAAAGAA 265
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
567-837 2.36e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.76  E-value: 2.36e-32
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  567 DMLNDAETRAPISPLHLAAYHGHHQALEVLVQSLLDLDVRNSTGRTPLDLAAFKGHVECVDVLINQGASILVKDYVvKRT 646
Cdd:COG0666     44 LLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD-GET 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  647 PIHSAeiqmvdsrnsvnknntelcnsaqkkvrakdmpsAINGHSECLRLLIGNAdvqAAVDIHDGNGQTPLMLSVLNGHT 726
Cdd:COG0666    123 PLHLA---------------------------------AYNGNLEIVKLLLEAG---ADVNAQDNDGNTPLHLAAANGNL 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  727 ECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPIHLAAACGHIGVLSALLQTAISVD 806
Cdd:COG0666    167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1785376409  807 vvpaIADNHGYTPLHWACYNGHDACVELLLE 837
Cdd:COG0666    247 ----AKDKDGLTALLLAAAAGAALIVKLLLL 273
PHA03095 PHA03095
ankyrin-like protein; Provisional
246-532 4.41e-31

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 128.60  E-value: 4.41e-31
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  246 ISVIKYLLDLGVDMNESNAYGNTPLHV--ACYNGQDV-VVNELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLVCN 322
Cdd:PHA03095    27 VEEVRRLLAAGADVNFRGEYGKTPLHLylHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLIKA 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  323 GADVNIKSKDGKTPLHmtaihgrfsrsqiiiqngaeIDCEDKNGNTPlhiaaryghelLINTLITSRADTSKRGIHGMFP 402
Cdd:PHA03095   107 GADVNAKDKVGRTPLH--------------------VYLSGFNINPK-----------VIRLLLRKGADVNALDLYGMTP 155
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  403 LHlaALSGFSDCC----RKLLSSGFDIDTHDDFGRTCLH--AAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAA-- 474
Cdd:PHA03095   156 LA--VLLKSRNANvellRLLIDAGADVYAVDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATgs 233
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1785376409  475 NCNYQCLFALVGSGASVNDLDERGCSPLHYAATSDTDGKClEYLLRNDANPGIRDKHG 532
Cdd:PHA03095   234 SCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRAC-RRLIALGADINAVSSDG 290
PHA03100 PHA03100
ankyrin repeat protein; Provisional
213-496 1.57e-29

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 122.85  E-value: 1.57e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  213 IEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMISVIKYLLDLGVDMNESNAYGNTPLH---VACYNGQDVV--VNELID 287
Cdd:PHA03100    15 VKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsNIKYNLTDVKeiVKLLLE 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  288 CGANVNQVNERGFTPLHFAAASTHGALCL-ELLVCNGADVNIKSKDGKTPLHMTA--IHGRFSRSQIIIQNGAEIDCEDK 364
Cdd:PHA03100    95 YGANVNAPDNNGITPLLYAISKKSNSYSIvEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKNR 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  365 ngntplhiaaryghellINTLItsradtskrgihgmfplhlaalsgfsdccrkllSSGFDIDTHDDFGRTCLHAAAAGGN 444
Cdd:PHA03100   175 -----------------VNYLL---------------------------------SYGVPINIKDVYGFTPLHYAVYNNN 204
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1785376409  445 LECLNLLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDE 496
Cdd:PHA03100   205 PEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
685-838 2.36e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 119.29  E-value: 2.36e-29
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  685 AINGHSECLRLLIgnaDVQAAVDIHDGNGQTPLMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEA 764
Cdd:COG0666     95 ARNGDLEIVKLLL---EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKL 171
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785376409  765 LLQHNANFLLRDCRGRTPIHLAAACGHIGVLSALLQTAISVDvvpaIADNHGYTPLHWACYNGHDACVELLLEQ 838
Cdd:COG0666    172 LLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN----AKDNDGKTALDLAAENGNLEIVKLLLEA 241
PHA02874 PHA02874
ankyrin repeat protein; Provisional
243-573 1.30e-28

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 120.45  E-value: 1.30e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  243 SGMISVIKYLL-DLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLhFAAASTHGALCLELLVC 321
Cdd:PHA02874    11 SGDIEAIEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPL-LTAIKIGAHDIIKLLID 89
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  322 NGADVNIkskdgktpLHMTAIHGRFSRSqiIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSRADTSKRGIHGMF 401
Cdd:PHA02874    90 NGVDTSI--------LPIPCIEKDMIKT--ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCY 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  402 PLHLAALSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAanCNYQCL 481
Cdd:PHA02874   160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI--IHNRSA 237
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  482 FALVGSGASVNDLDERGCSPLHYAATSDTDGKCLEYLLRNDANPGIRDKHGYNAVHYAAAYGHRLCL--ELIARETPLDV 559
Cdd:PHA02874   238 IELLINNASINDQDIDGSTPLHHAINPPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVikDIIANAVLIKE 317
                          330
                   ....*....|....
gi 1785376409  560 LMETSGTDMLNDAE 573
Cdd:PHA02874   318 ADKLKDSDFLEHIE 331
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
379-652 4.98e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.44  E-value: 4.98e-28
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  379 ELLINTLITSRADTSKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADF 458
Cdd:COG0666      1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  459 NKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDERGCSPLHYAATSDtDGKCLEYLLRNDANPGIRDKHGYNAVHY 538
Cdd:COG0666     81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG-NLEIVKLLLEAGADVNAQDNDGNTPLHL 159
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  539 AAAYGHRLCLE-LIARetpldvlmetsGTDMlnDAETRAPISPLHLAAYHGHHQALEVLVQSLLDLDVRNSTGRTPLDLA 617
Cdd:COG0666    160 AAANGNLEIVKlLLEA-----------GADV--NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA 226
                          250       260       270
                   ....*....|....*....|....*....|....*
gi 1785376409  618 AFKGHVECVDVLINQGASILVKDYVVKRTPIHSAE 652
Cdd:COG0666    227 AENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261
PHA03095 PHA03095
ankyrin-like protein; Provisional
281-632 7.59e-27

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 115.51  E-value: 7.59e-27
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  281 VVNELIDCGANVNQVNERGFTPLHFAAASTHGAL--CLELLVCNGADVNIKSKDGKTPLHMTAIHGrfSRSQII---IQN 355
Cdd:PHA03095    29 EVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdIVRLLLEAGADVNAPERCGFTPLHLYLYNA--TTLDVIkllIKA 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  356 GAEIDCEDKNGNTPLHIAAR--YGHELLINTLITSRADTSKRGIHGMFPLHlaALSGFSDCcrkllssgfdidthddfgr 433
Cdd:PHA03095   107 GADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLA--VLLKSRNA------------------- 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  434 tclhaaaaggNLECLNLLLSTGADFNKKDKFGRTPLHYAAANC--NYQCLFALVGSGASVNDLDERGCSPLHYAATSdtd 511
Cdd:PHA03095   166 ----------NVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFkpRARIVRELIRAGCDPAATDMLGNTPLHSMATG--- 232
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  512 GKCLEYLLRNdanpgirdkhgynavhyaaayghrlcleLIARetpldvlmetsGTDMlnDAETRAPISPLHLAAYHGHHQ 591
Cdd:PHA03095   233 SSCKRSLVLP----------------------------LLIA-----------GISI--NARNRYGQTPLHYAAVFNNPR 271
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|.
gi 1785376409  592 ALEVLVQSLLDLDVRNSTGRTPLDLAAFKGHVECVDVLINQ 632
Cdd:PHA03095   272 ACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
418-783 8.21e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.89  E-value: 8.21e-26
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  418 LLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDER 497
Cdd:COG0666      7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  498 GCSPLHYAATSDtDGKCLEYLLRNDANPGIRDKHGYnavhyaaayghrlcleliaretpldvlmetsgtdmlndaetrap 577
Cdd:COG0666     87 GNTLLHAAARNG-DLEIVKLLLEAGADVNARDKDGE-------------------------------------------- 121
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  578 iSPLHLAAYHGHHQALEVLVQSLLDLDVRNSTGRTPLDLAAFKGHVECVDVLINQGASILVKDYVvKRTPIHSAeiqmvd 657
Cdd:COG0666    122 -TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLA------ 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  658 srnsvnknntelcnsaqkkvrakdmpsAINGHSECLRLLIGNAdvqAAVDIHDGNGQTPLMLSVLNGHTECVYSLLNKGA 737
Cdd:COG0666    194 ---------------------------AENGHLEIVKLLLEAG---ADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGA 243
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*.
gi 1785376409  738 NVDAKDKWGRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPI 783
Cdd:COG0666    244 DLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02878 PHA02878
ankyrin repeat protein; Provisional
102-373 7.21e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 109.58  E-value: 7.21e-25
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  102 LTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIA--AANKavkcaEALVPLLSNVNVSD-----RAGRTALHHA 174
Cdd:PHA02878    38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIIckEPNK-----LGMKEMIRSINKCSvfytlVAIKDAFNNR 112
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  175 afsgHVEMV-SLLLSRGANINAFDKKDRRAIHWAAYMgHIEVVKLLVTHGAEVMCKDK-KSYTPLHAAASSGMISVIKYL 252
Cdd:PHA02878   113 ----NVEIFkIILTNRYKNIQTIDLVYIDKKSKDDII-EAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELL 187
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  253 LDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLVCNGADVNIKSK- 331
Cdd:PHA02878   188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILKLLLEHGVDVNAKSYi 267
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|..
gi 1785376409  332 DGKTPLHMtAIHGRfSRSQIIIQNGAEIDCEDKNGNTPLHIA 373
Cdd:PHA02878   268 LGLTALHS-SIKSE-RKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02878 PHA02878
ankyrin repeat protein; Provisional
57-344 3.65e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 101.50  E-value: 3.65e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   57 KKEDVNFQDNEKRT---------PLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLK----- 122
Cdd:PHA02878    17 LKYIEYIDHTENYStsaslipfiPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkc 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  123 -------------HSADVNA-------RDKNWQTP--LHIAAANKAVKCAEALVPLL----SNVNVSDR-AGRTALHHAA 175
Cdd:PHA02878    97 svfytlvaikdafNNRNVEIfkiiltnRYKNIQTIdlVYIDKKSKDDIIEAEITKLLlsygADINMKDRhKGNTALHYAT 176
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  176 FSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGM-ISVIKYLLD 254
Cdd:PHA02878   177 ENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKdYDILKLLLE 256
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  255 LGVDMN-ESNAYGNTPLHVACYNGQdvVVNELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLVCNGADVNIKSKDG 333
Cdd:PHA02878   257 HGVDVNaKSYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRILISNICLLKRIKPDI 334
                          330
                   ....*....|....*
gi 1785376409  334 KTPL----HMTAIHG 344
Cdd:PHA02878   335 KNSEgfidNMDCITS 349
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
834-1039 6.11e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.33  E-value: 6.11e-22
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  834 LLLEQEVFQKMEGNSFSPLHCAVINDNEGAAEMLIDTLGTSIVNSVDSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVD 913
Cdd:COG0666      5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  914 STGKTPLMMAAENGQTSAVEVLVSsAKADLTLQDKNKNTALHLACSKGHETSALLILEQITDrnlINATNSALQTPLHVA 993
Cdd:COG0666     85 DGGNTLLHAAARNGDLEIVKLLLE-AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAD---VNAQDNDGNTPLHLA 160
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1785376409  994 ARNGLTVVVQELLGKGASVLAVDENGYTPALACAPNKDVADCLALI 1039
Cdd:COG0666    161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206
Ank_2 pfam12796
Ankyrin repeats (3 copies);
105-197 4.86e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 4.86e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  105 LHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLsNVNVSDRaGRTALHHAAFSGHVEMVS 184
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1785376409  185 LLLSRGANINAFD 197
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
138-230 4.86e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 4.86e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  138 LHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRgANINAFDkKDRRAIHWAAYMGHIEVVK 217
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1785376409  218 LLVTHGAEVMCKD 230
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
204-296 9.60e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.78  E-value: 9.60e-20
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  204 IHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMISVIKYLLDlGVDMNESNaYGNTPLHVACYNGQDVVVN 283
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1785376409  284 ELIDCGANVNQVN 296
Cdd:pfam12796   79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
171-260 1.40e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 1.40e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  171 LHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVTHgAEVMCKDKKsYTPLHAAASSGMISVIK 250
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78
                           90
                   ....*....|
gi 1785376409  251 YLLDLGVDMN 260
Cdd:pfam12796   79 LLLEKGADIN 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
403-495 2.07e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.01  E-value: 2.07e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  403 LHLAALSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTgADFNKKDKfGRTPLHYAAANCNYQCLF 482
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1785376409  483 ALVGSGASVNDLD 495
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
219-636 2.59e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 93.59  E-value: 2.59e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  219 LVTHGAEvMCKDKK-SYTPLHAAASSGMISVIKYLLDLGVDMNESNAYG-NTPLHVACY--NGQDVVVNELIDCGANVNq 294
Cdd:PHA02876    27 LHKHGAN-QCENESiPFTAIHQALQLRQIDIVEEIIQQNPELIYITDHKcHSTLHTICIipNVMDIVISLTLDCDIILD- 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  295 vnergftpLHFAAASTH----GALCLELL--VCNGADVNIkSKDGKTPLHMTAIHGRFSRSQIII-----QNGAEIDCED 363
Cdd:PHA02876   105 --------IKYASIILNkhklDEACIHILkeAISGNDIHY-DKINESIEYMKLIKERIQQDELLIaemllEGGADVNAKD 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  364 KNGNTPLHIAARYGHELLINTLITSRADTSKRGIHGMFPLHLAALSGFSDCCRK-------------------------- 417
Cdd:PHA02876   176 IYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAiidnrsninkndlsllkairnedlet 255
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  418 ---LLSSGFDIDTHDDFGRTCLHAAAAGGNLECL-NLLLSTGADFNKKDKFGRTPLHYAAAN-CNYQCLFALVGSGASVN 492
Cdd:PHA02876   256 sllLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNgYDTENIRTLIMLGADVN 335
                          330       340       350       360       370       380       390       400
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  493 DLDERGCSPLHYAATSDTDGKCLEYLLRNDANPGIRDKHGYNAVHYAAAYGHRLCLE-LIARETPLDVLMETSGTdmlnd 571
Cdd:PHA02876   336 AADRLYITPLHQASTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINtLLDYGADIEALSQKIGT----- 410
                          410       420       430       440       450       460
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1785376409  572 aetrapisPLHLAAYHGH-HQALEVLVQSLLDLDVRNSTGRTPLDLAAFKG-HVECVDVLINQGASI 636
Cdd:PHA02876   411 --------ALHFALCGTNpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADV 469
PHA03095 PHA03095
ankyrin-like protein; Provisional
694-1023 5.97e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 91.24  E-value: 5.97e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  694 RLLIGNADVQaavdiHDGN-GQTPLMLSVLNGH---TECVYSLLNKGANVDAKDKWGRTALH---RGAVTghEECVEALL 766
Cdd:PHA03095    32 RLLAAGADVN-----FRGEyGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHlylYNATT--LDVIKLLI 104
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  767 QHNANFLLRDCRGRTPIH--LAAACGHIGVLSALLQTAISVDVVpaiaDNHGYTPLHwACYNGHDACVELLleqevfqkm 844
Cdd:PHA03095   105 KAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNAL----DLYGMTPLA-VLLKSRNANVELL--------- 170
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  845 egnsfsplhcavindnegaaEMLIDTlGTSIVNsVDSKGRTPLH--AAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMM 922
Cdd:PHA03095   171 --------------------RLLIDA-GADVYA-VDDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHS 228
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  923 AAengqtsavevLVSSAKADLTLQdknkntalhlacskghetsalLILEQITdrnlINATNSALQTPLHVAARNGLTVVV 1002
Cdd:PHA03095   229 MA----------TGSSCKRSLVLP---------------------LLIAGIS----INARNRYGQTPLHYAAVFNNPRAC 273
                          330       340
                   ....*....|....*....|.
gi 1785376409 1003 QELLGKGASVLAVDENGYTPA 1023
Cdd:PHA03095   274 RRLIALGADINAVSSDGNTPL 294
Ank_2 pfam12796
Ankyrin repeats (3 copies);
39-131 5.98e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 5.98e-19
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   39 LVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLiLSGARVNAKDSKWlTPLHRAVASCSEDAVQ 118
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDNGR-TALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1785376409  119 VLLKHSADVNARD 131
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
69-295 8.13e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 87.35  E-value: 8.13e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   69 RTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVK 148
Cdd:PHA02875     3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  149 CAEALvpLLSNVNVSD---RAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVTHGAE 225
Cdd:PHA02875    83 AVEEL--LDLGKFADDvfyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785376409  226 VMCKDKKSYTPLHAAASSGMISVIKYLLDLGVDMNESNAYGN-TPLHVACYNGQDVVVNELIDCGANVNQV 295
Cdd:PHA02875   161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIM 231
PHA02876 PHA02876
ankyrin repeat protein; Provisional
594-925 9.18e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 88.58  E-value: 9.18e-18
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  594 EVLVQSLLDLDVRNSTGRTPLDLAAFKGHVECVDVLINQGAS---ILVKDYVVKRTPIHSAEIQ----MVDSRNSVNKNN 666
Cdd:PHA02876   162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADvniIALDDLSVLECAVDSKNIDtikaIIDNRSNINKND 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  667 TELCNSaqkkVRAKDMPSA---------INGHSECLRLLIGNAD------------VQAAVDIHDGN--GQTPLMLSVLN 723
Cdd:PHA02876   242 LSLLKA----IRNEDLETSlllydagfsVNSIDDCKNTPLHHASqapslsrlvpklLERGADVNAKNikGETPLYLMAKN 317
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  724 GH-TECVYSLLNKGANVDAKDKWGRTALHRGAVTG-HEECVEALLQHNANFLLRDCRGRTPIHLAAACGHIGVLSALLQT 801
Cdd:PHA02876   318 GYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDY 397
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  802 AISVDvvpAIADNHGyTPLHWACYNGhdacvellleqevfqkmegNSFSplhcavindnegAAEMLIDTLGTsiVNSVDS 881
Cdd:PHA02876   398 GADIE---ALSQKIG-TALHFALCGT-------------------NPYM------------SVKTLIDRGAN--VNSKNK 440
                          330       340       350       360
                   ....*....|....*....|....*....|....*....|....*
gi 1785376409  882 KGRTPLHAAAFTD-HIECLQLLLSHNAQVNAVDSTGKTPLMMAAE 925
Cdd:PHA02876   441 DLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALE 485
PHA03095 PHA03095
ankyrin-like protein; Provisional
416-808 1.07e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 87.39  E-value: 1.07e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  416 RKLLSSGFDIDTHDDFGRTCLHAAAAGGN---LECLNLLLSTGADFNKKDKFGRTPLH-YAAANCNYQCLFALVGSGASV 491
Cdd:PHA03095    31 RRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADV 110
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  492 NDLDERGCSPLH-YAATSDTDGKCLEYLLRNDANPGIRDKHGYnavhyaaayghrlcleliareTPLDVLMETSGTDmln 570
Cdd:PHA03095   111 NAKDKVGRTPLHvYLSGFNINPKVIRLLLRKGADVNALDLYGM---------------------TPLAVLLKSRNAN--- 166
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  571 daetrapisplhlaayhghhqalevlvqslldldvrnstgrtpldlaafkghVECVDVLINQGASILVKDyVVKRTPIHS 650
Cdd:PHA03095   167 ----------------------------------------------------VELLRLLIDAGADVYAVD-DRFRSLLHH 193
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  651 aEIQMVDSRNSVNKNNTEL-CNSAQKKVRAKDMPSAINGHSECLRLLIGNadvqaavdihdgngqtplmlsvlnghtecv 729
Cdd:PHA03095   194 -HLQSFKPRARIVRELIRAgCDPAATDMLGNTPLHSMATGSSCKRSLVLP------------------------------ 242
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785376409  730 ysLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPIHLAAACGHIGVLSALLQTAISVDVV 808
Cdd:PHA03095   243 --LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV 319
Ank_2 pfam12796
Ankyrin repeats (3 copies);
717-807 1.19e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 1.19e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  717 LMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNAnfLLRDCRGRTPIHLAAACGHIGVLS 796
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|.
gi 1785376409  797 ALLQTAISVDV 807
Cdd:pfam12796   79 LLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
370-462 2.41e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 2.41e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  370 LHIAARYGHELLINTLITSRADTSKRGIHGMFPLHLAALSGFSDCCRKLLSSgFDIDtHDDFGRTCLHAAAAGGNLECLN 449
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78
                           90
                   ....*....|...
gi 1785376409  450 LLLSTGADFNKKD 462
Cdd:pfam12796   79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
193-472 5.75e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 85.32  E-value: 5.75e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  193 INAFDKKDRRA----------IHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMISVIKYLLDLGVDMNES 262
Cdd:PHA02878    20 IEYIDHTENYStsaslipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVF 99
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  263 NAYgnTPLHVACYNgQDVVVNE--LIDCGANVNQVNERGFTPLHFAAASThgALCLELLVCNGADVNIKSKD-GKTPLHM 339
Cdd:PHA02878   100 YTL--VAIKDAFNN-RNVEIFKiiLTNRYKNIQTIDLVYIDKKSKDDIIE--AEITKLLLSYGADINMKDRHkGNTALHY 174
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  340 TAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSRADTSKRGIHGMFPLHLAALSGFS-DCCRKL 418
Cdd:PHA02878   175 ATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDyDILKLL 254
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1785376409  419 LSSGFDIDTHDDF-GRTCLHAAAAggNLECLNLLLSTGADFNKKDKFGRTPLHYA 472
Cdd:PHA02878   255 LEHGVDVNAKSYIlGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02874 PHA02874
ankyrin repeat protein; Provisional
39-220 9.56e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 84.24  E-value: 9.56e-17
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   39 LVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQ 118
Cdd:PHA02874   128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  119 VLLKHSADVNARDKNWQTPLHIAAA-NKAVkcaealVPLLSN---VNVSDRAGRTALHHA-AFSGHVEMVSLLLSRGANI 193
Cdd:PHA02874   208 LLIDHGNHIMNKCKNGFTPLHNAIIhNRSA------IELLINnasINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADI 281
                          170       180
                   ....*....|....*....|....*...
gi 1785376409  194 NAFDKKDRRAIHWA-AYMGHIEVVKLLV 220
Cdd:PHA02874   282 SIKDNKGENPIDTAfKYINKDPVIKDII 309
Ank_2 pfam12796
Ankyrin repeats (3 copies);
685-776 1.06e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 1.06e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  685 AINGHSECLRLLIGNadvQAAVDIHDGNGQTPLMLSVLNGHTECVYSLLNKgANVDAKDKwGRTALHRGAVTGHEECVEA 764
Cdd:pfam12796    5 AKNGNLELVKLLLEN---GADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKL 79
                           90
                   ....*....|..
gi 1785376409  765 LLQHNANFLLRD 776
Cdd:pfam12796   80 LLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
416-651 1.15e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.95  E-value: 1.15e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  416 RKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAA-----ANCNYQCLFALVGSGAS 490
Cdd:PHA03100    19 KYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGAN 98
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  491 VNDLDERGCSPLHYAATSD-TDGKCLEYLLRNDANPGIRDKHGYNAVHYAaayghrlcLELIARETPLDVLMETSGTDMl 569
Cdd:PHA03100    99 VNAPDNNGITPLLYAISKKsNSYSIVEYLLDNGANVNIKNSDGENLLHLY--------LESNKIDLKILKLLIDKGVDI- 169
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  570 nDAETRapisplhlaayhghhqaLEVLVQSLLDLDVRNSTGRTPLDLAAFKGHVECVDVLINQGASILVKDYVVKrTPIH 649
Cdd:PHA03100   170 -NAKNR-----------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGD-TPLH 230

                   ..
gi 1785376409  650 SA 651
Cdd:PHA03100   231 IA 232
Ank_2 pfam12796
Ankyrin repeats (3 copies);
750-840 1.58e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 1.58e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  750 LHRGAVTGHEECVEALLQHNANFLLRDCRGRTPIHLAAACGHIGVLSALLQTAISVDvvpaiaDNHGYTPLHWACYNGHD 829
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL------KDNGRTALHYAARSGHL 74
                           90
                   ....*....|.
gi 1785376409  830 ACVELLLEQEV 840
Cdd:pfam12796   75 EIVKLLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
887-980 3.65e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.77  E-value: 3.65e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  887 LHAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAVEVLVSSAKADLTLqdkNKNTALHLACSKGHETSA 966
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD---NGRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 1785376409  967 LLILEQITDRNLIN 980
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
60-225 4.17e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 81.96  E-value: 4.17e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   60 DVNFQDneKRTPLHAAAYLGDAEIIELLILSGARVN-AKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPL 138
Cdd:PHA02875    62 DVKYPD--IESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPL 139
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  139 HIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKK-DRRAIHWAAYMGHIEVVK 217
Cdd:PHA02875   140 HLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVR 219

                   ....*...
gi 1785376409  218 LLVTHGAE 225
Cdd:PHA02875   220 LFIKRGAD 227
PHA02798 PHA02798
ankyrin-like protein; Provisional
82-345 5.87e-16

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 82.19  E-value: 5.87e-16
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   82 EIIELLILSGARVNAKDSKWLTPLHRAVASCSE-----DAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPL 156
Cdd:PHA02798    52 DIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFM 131
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  157 LSN---VNVSDRAGRTALHHAAFSGH---VEMVSLLLSRGANINAFDkkdrraiHWAAYmghievvkllvthgAEVMCKD 230
Cdd:PHA02798   132 IENgadTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHN-------NKEKY--------------DTLHCYF 190
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  231 KKSYTPLHAaassgmiSVIKYLLDLGVDMNESNAYGNTP----LHVACYNGQDVVVN--ELIDCGANVNQVNERGFTPLH 304
Cdd:PHA02798   191 KYNIDRIDA-------DILKLFVDNGFIINKENKSHKKKfmeyLNSLLYDNKRFKKNilDFIFSYIDINQVDELGFNPLY 263
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|.
gi 1785376409  305 FAAASTHGALClELLVCNGADVNIKSKDGKTPLhMTAIHGR 345
Cdd:PHA02798   264 YSVSHNNRKIF-EYLLQLGGDINIITELGNTCL-FTAFENE 302
PHA03100 PHA03100
ankyrin repeat protein; Provisional
706-915 1.20e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.48  E-value: 1.20e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  706 VDIHDGNGQTPLMLSVLNGHT-----ECVYSLLNKGANVDAKDKWGRTALHRGAVT--GHEECVEALLQHNANFLLRDCR 778
Cdd:PHA03100    61 INSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSD 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  779 GRTPIHLAAACGHI--GVLSALLQTAISVDV-----------VPA-IADNHGYTPLHWACYNGHDACVELLLEqevfqkm 844
Cdd:PHA03100   141 GENLLHLYLESNKIdlKILKLLIDKGVDINAknrvnyllsygVPInIKDVYGFTPLHYAVYNNNPEFVKYLLD------- 213
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785376409  845 egnsfsplhcavindnegaaemlidtLGTSIvNSVDSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDST 915
Cdd:PHA03100   214 --------------------------LGANP-NLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
57-228 1.83e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 81.45  E-value: 1.83e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   57 KKEDVNFQDNEKRTPLHAAAYL------GDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNAR 130
Cdd:PLN03192   508 NVGDLLGDNGGEHDDPNMASNLltvastGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIR 587
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  131 DKNWQTPLHIAAANKAVKCAEALVPLLSnvnVSD-RAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAY 209
Cdd:PLN03192   588 DANGNTALWNAISAKHHKIFRILYHFAS---ISDpHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMA 664
                          170
                   ....*....|....*....
gi 1785376409  210 MGHIEVVKLLVTHGAEVMC 228
Cdd:PLN03192   665 EDHVDMVRLLIMNGADVDK 683
PHA02878 PHA02878
ankyrin repeat protein; Provisional
51-222 1.99e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 80.31  E-value: 1.99e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   51 VRALIFKKEDVNFQDNEK-RTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNA 129
Cdd:PHA02878   150 TKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  130 RDKNWQTPLHIAAAnkAVKCAEALVPLL---SNVNV-SDRAGRTALHHAAFSGHVemVSLLLSRGANINAFDKKDRRAIH 205
Cdd:PHA02878   230 RDKCGNTPLHISVG--YCKDYDILKLLLehgVDVNAkSYILGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLS 305
                          170
                   ....*....|....*....
gi 1785376409  206 WAA--YMGhIEVVKLLVTH 222
Cdd:PHA02878   306 SAVkqYLC-INIGRILISN 323
PHA02878 PHA02878
ankyrin repeat protein; Provisional
260-529 2.94e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 79.92  E-value: 2.94e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  260 NESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLvcngadvNIKSKDgKTPLHM 339
Cdd:PHA02878    31 TSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI-------RSINKC-SVFYTL 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  340 TAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSR-----ADTSKRGIH-GMFPLHLAALSGFSD 413
Cdd:PHA02878   103 VAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLllsygADINMKDRHkGNTALHYATENKDQR 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  414 CCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAANC-NYQCLFALVGSGASVN 492
Cdd:PHA02878   183 LTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCkDYDILKLLLEHGVDVN 262
                          250       260       270
                   ....*....|....*....|....*....|....*...
gi 1785376409  493 DLDE-RGCSPLHYAATSDtdgKCLEYLLRNDANPGIRD 529
Cdd:PHA02878   263 AKSYiLGLTALHSSIKSE---RKLKLLLEYGADINSLN 297
PHA02876 PHA02876
ankyrin repeat protein; Provisional
36-247 3.58e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 80.49  E-value: 3.58e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   36 TPPLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLG-DAEIIELLILSGARVNAKDSKWLTPLHRAVASCSE 114
Cdd:PHA02876   309 TPLYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNV 388
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  115 DAVQVLLKHSADVNARDKNWQTPLHIA-AANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSG-HVEMVSLLLSRGAN 192
Cdd:PHA02876   389 VIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGAD 468
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1785376409  193 INAFDKKDRRAIHWAayMGHIEVVKLLVTHGAEVmcKDKKSytpLHAAASSGMIS 247
Cdd:PHA02876   469 VNAINIQNQYPLLIA--LEYHGIVNILLHYGAEL--RDSRV---LHKSLNDNMFS 516
Ank_2 pfam12796
Ankyrin repeats (3 copies);
820-913 4.68e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.69  E-value: 4.68e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  820 LHWACYNGHDACVELLLEQEV-FQKMEGNSFSPLHCAVINDNEGAAEMLIDTLGTSIVNsvdsKGRTPLHAAAFTDHIEC 898
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD----NGRTALHYAARSGHLEI 76
                           90
                   ....*....|....*
gi 1785376409  899 LQLLLSHNAQVNAVD 913
Cdd:pfam12796   77 VKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
240-459 4.80e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 78.88  E-value: 4.80e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  240 AASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDCGA--NVNQVNERgfTPLHFAAASTHGALCLE 317
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIE--SELHDAVEEGDVKAVEE 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  318 LLVCNGADVNIKSKDGKTPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSRADTSKRGI 397
Cdd:PHA02875    87 LLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166
                          170       180       190       200       210       220
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409  398 HGMFPLHLAALSGFSDCCRKLLSSGFDIDThddFGR----TCLHAAAAGGNLECLNLLLSTGADFN 459
Cdd:PHA02875   167 CGCTPLIIAMAKGDIAICKMLLDSGANIDY---FGKngcvAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02876 PHA02876
ankyrin repeat protein; Provisional
763-1017 5.75e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 79.72  E-value: 5.75e-15
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  763 EALLQHNANFLLRDCRGRTPIHLAAACGHIGVLSALLQTAISVDVVPAiadnHGYTPLHWACYNGHDACVELLLEQEvfQ 842
Cdd:PHA02876   162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIAL----DDLSVLECAVDSKNIDTIKAIIDNR--S 235
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  843 KMEGNSFSPLHcAVINDNEGAAEMLIDTlGTSiVNSVDSKGRTPLHAAAFTDHIECL-QLLLSHNAQVNAVDSTGKTPLM 921
Cdd:PHA02876   236 NINKNDLSLLK-AIRNEDLETSLLLYDA-GFS-VNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLY 312
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  922 MAAENG-QTSAVEVLVSSAkADLTLQDKNKNTALHLACSKGHETSALLILEQITDRnlINATNSALQTPLHVAARNGLTV 1000
Cdd:PHA02876   313 LMAKNGyDTENIRTLIMLG-ADVNAADRLYITPLHQASTLDRNKDIVITLLELGAN--VNARDYCDKTPIHYAAVRNNVV 389
                          250
                   ....*....|....*..
gi 1785376409 1001 VVQELLGKGASVLAVDE 1017
Cdd:PHA02876   390 IINTLLDYGADIEALSQ 406
PHA02798 PHA02798
ankyrin-like protein; Provisional
213-459 1.59e-14

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 77.57  E-value: 1.59e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  213 IEVVKLLVTHGAEVMCKDKKSYTPLHAAASS-----GMISVIKYLLDLGVDMNESNAYGNTPLHVACYNG---QDVVVNE 284
Cdd:PHA02798    51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLF 130
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  285 LIDCGANVNQVNERGFTPLHFAAASTHGAL--CLELLVCNGADVNIKS-KDGKTPLHmTAIHGRFSR-----SQIIIQNG 356
Cdd:PHA02798   131 MIENGADTTLLDKDGFTMLQVYLQSNHHIDieIIKLLLEKGVDINTHNnKEKYDTLH-CYFKYNIDRidadiLKLFVDNG 209
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  357 AEIDCEDKNGNTPLhiaARYGHELLINT---------LITSRADTSKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDT 427
Cdd:PHA02798   210 FIINKENKSHKKKF---MEYLNSLLYDNkrfkknildFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINI 286
                          250       260       270
                   ....*....|....*....|....*....|..
gi 1785376409  428 HDDFGRTCLHAAAAGGNLECLNLLLSTGADFN 459
Cdd:PHA02798   287 ITELGNTCLFTAFENESKFIFNSILNKKPNKN 318
PHA02876 PHA02876
ankyrin repeat protein; Provisional
418-800 2.96e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.41  E-value: 2.96e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  418 LLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDer 497
Cdd:PHA02876   164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKND-- 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  498 gCSPLHYAATSDTDGKCLEYllrnDANPGIR--DKHGYNAVHYA--AAYGHRLCLELIARetpldvlmetsGTDMlnDAE 573
Cdd:PHA02876   242 -LSLLKAIRNEDLETSLLLY----DAGFSVNsiDDCKNTPLHHAsqAPSLSRLVPKLLER-----------GADV--NAK 303
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  574 TRAPISPLHLAAYHGHH-QALEVLVQSLLDLDVRNSTGRTPLDLAA-FKGHVECVDVLINQGASILVKDYvVKRTPIHSA 651
Cdd:PHA02876   304 NIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDY-CDKTPIHYA 382
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  652 EIqmvdsRNSVNKNNTELCNSAQKKVRAKDMPSAINgHSEClrllignadvqaavdihdgnGQTPLMlsvlnghteCVYS 731
Cdd:PHA02876   383 AV-----RNNVVIINTLLDYGADIEALSQKIGTALH-FALC--------------------GTNPYM---------SVKT 427
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  732 LLNKGANVDAKDKWGRTALHRGAVTGHE-ECVEALLQHNANFLLRDCRGRTPihLAAACGHIGVLSALLQ 800
Cdd:PHA02876   428 LIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYP--LLIALEYHGIVNILLH 495
PHA02876 PHA02876
ankyrin repeat protein; Provisional
732-1024 3.28e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.41  E-value: 3.28e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  732 LLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPIHLAAACGHIGVLSALLQTAISVD----- 806
Cdd:PHA02876   164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINkndls 243
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  807 VVPAIA--------------------DNHGYTPLHWACYNGH-DACVELLLEQEV---FQKMEGNSfsPLHCAVINDNEG 862
Cdd:PHA02876   244 LLKAIRnedletslllydagfsvnsiDDCKNTPLHHASQAPSlSRLVPKLLERGAdvnAKNIKGET--PLYLMAKNGYDT 321
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  863 AAEMLIDTLGTSiVNSVDSKGRTPLHAAAFTD-HIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAVEVLVSSAkA 941
Cdd:PHA02876   322 ENIRTLIMLGAD-VNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG-A 399
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  942 DLTLQDKNKNTALHLACskgHETSALLILEQITDRNL-INATNSALQTPLHVAARNGLTV-VVQELLGKGASVLAVDENG 1019
Cdd:PHA02876   400 DIEALSQKIGTALHFAL---CGTNPYMSVKTLIDRGAnVNSKNKDLSTPLHYACKKNCKLdVIEMLLDNGADVNAINIQN 476

                   ....*
gi 1785376409 1020 YTPAL 1024
Cdd:PHA02876   477 QYPLL 481
PHA03095 PHA03095
ankyrin-like protein; Provisional
44-195 4.72e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.83  E-value: 4.72e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   44 FNGDPDEVRALIFKKEDVNFQDNEKRTPLHaaAYLG----DAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDA--V 117
Cdd:PHA03095   128 FNINPKVIRLLLRKGADVNALDLYGMTPLA--VLLKsrnaNVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRAriV 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  118 QVLLKHSADVNARDKNWQTPLHIAAANKAVKcAEALVPLLSN---VNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANIN 194
Cdd:PHA03095   206 RELIRAGCDPAATDMLGNTPLHSMATGSSCK-RSLVLPLLIAgisINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284

                   .
gi 1785376409  195 A 195
Cdd:PHA03095   285 A 285
Ank_2 pfam12796
Ankyrin repeats (3 copies);
337-429 7.90e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.22  E-value: 7.90e-14
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  337 LHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHIAARYGH----ELLINTLITSRADtskrgiHGMFPLHLAALSGFS 412
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHleivKLLLEHADVNLKD------NGRTALHYAARSGHL 74
                           90
                   ....*....|....*..
gi 1785376409  413 DCCRKLLSSGFDIDTHD 429
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
920-1016 1.34e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 1.34e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  920 LMMAAENGQTSAVEVLVSSaKADLTLQDKNKNTALHLACSKGHETSALLILEQItDRNLINATNsalqTPLHVAARNGLT 999
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLEN-GADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDNGR----TALHYAARSGHL 74
                           90
                   ....*....|....*..
gi 1785376409 1000 VVVQELLGKGASVLAVD 1016
Cdd:pfam12796   75 EIVKLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
101-308 1.50e-13

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: 75.05  E-value: 1.50e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  101 WLTPLHRAVASCSEDAVQVLLK-HSADVNARDKNWQTPLHIAAANKAVKCAEAL---VPLLSNVNV-SD-RAGRTALHHA 174
Cdd:cd22192     17 SESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLmeaAPELVNEPMtSDlYQGETALHIA 96
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  175 AFSGHVEMVSLLLSRGANIN-------AFDKKDRRAIHW-------AAYMGHIEVVKLLVTHGAEVMCKDkksytplhaa 240
Cdd:cd22192     97 VVNQNLNLVRELIARGADVVspratgtFFRPGPKNLIYYgehplsfAACVGNEEIVRLLIEHGADIRAQD---------- 166
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785376409  241 assgmisvikylldlgvdmnesnAYGNTPLHVACYNGQDVVVNELIDC----GANVNQV------NERGFTPLHFAAA 308
Cdd:cd22192    167 -----------------------SLGNTVLHILVLQPNKTFACQMYDLilsyDKEDDLQpldlvpNNQGLTPFKLAAK 221
Ank_2 pfam12796
Ankyrin repeats (3 copies);
270-363 4.52e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.91  E-value: 4.52e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  270 LHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLvcNGADVNIKSkDGKTPLHMTAIHGRFSRS 349
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL--EHADVNLKD-NGRTALHYAARSGHLEIV 77
                           90
                   ....*....|....
gi 1785376409  350 QIIIQNGAEIDCED 363
Cdd:pfam12796   78 KLLLEKGADINVKD 91
PHA02798 PHA02798
ankyrin-like protein; Provisional
281-527 5.72e-13

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 72.56  E-value: 5.72e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  281 VVNELIDCGANVNQVNERGFTPLHFAAAS----THGALCLELLVCNGADVNIKSKDGKTPLHMTAIHGRFSRSQII---I 353
Cdd:PHA02798    53 IVKLFINLGANVNGLDNEYSTPLCTILSNikdyKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILlfmI 132
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  354 QNGAEIDCEDKNGNTPLHIAARYGHELLINTLitsradtskrgihgmfplhlaalsgfsdccRKLLSSGFDIDTHDD-FG 432
Cdd:PHA02798   133 ENGADTTLLDKDGFTMLQVYLQSNHHIDIEII------------------------------KLLLEKGVDINTHNNkEK 182
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  433 RTCLHAAAAgGNLECLN-----LLLSTGADFNKKDKFGRT-------PLHYAAANCNYQcLFALVGSGASVNDLDERGCS 500
Cdd:PHA02798   183 YDTLHCYFK-YNIDRIDadilkLFVDNGFIINKENKSHKKkfmeylnSLLYDNKRFKKN-ILDFIFSYIDINQVDELGFN 260
                          250       260
                   ....*....|....*....|....*..
gi 1785376409  501 PLHYAATSDTDgKCLEYLLRNDANPGI 527
Cdd:PHA02798   261 PLYYSVSHNNR-KIFEYLLQLGGDINI 286
PHA03100 PHA03100
ankyrin repeat protein; Provisional
832-1018 7.97e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.01  E-value: 7.97e-13
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  832 VELLLEQ--EVFQKMEGNSfSPLH-----CAVINDNEGAAEMLIDtLGTSIvNSVDSKGRTPLHAAAFT--DHIECLQLL 902
Cdd:PHA03100    51 VKILLDNgaDINSSTKNNS-TPLHylsniKYNLTDVKEIVKLLLE-YGANV-NAPDNNGITPLLYAISKksNSYSIVEYL 127
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  903 LSHNAQVNAVDSTGKTPLMMAAENGQ--TSAVEVLVSS-----AK----------ADLTLQDKNKNTALHLACSKGHETS 965
Cdd:PHA03100   128 LDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKgvdinAKnrvnyllsygVPINIKDVYGFTPLHYAVYNNNPEF 207
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1785376409  966 ALLILEQITDRNLINATNSalqTPLHVAARNGLTVVVQELLGKGASVLAVDEN 1018
Cdd:PHA03100   208 VKYLLDLGANPNLVNKYGD---TPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
Ank_2 pfam12796
Ankyrin repeats (3 copies);
614-743 1.37e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.37  E-value: 1.37e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  614 LDLAAFKGHVECVDVLINQGASILVKDyVVKRTPIHSAeiqmvdsrnsvnknntelcnsaqkkvrakdmpsAINGHSECL 693
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQD-KNGRTALHLA---------------------------------AKNGHLEIV 46
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1785376409  694 RLLIGNADVQAavdihDGNGQTPLMLSVLNGHTECVYSLLNKGANVDAKD 743
Cdd:pfam12796   47 KLLLEHADVNL-----KDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
167-220 2.84e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 62.29  E-value: 2.84e-12
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1785376409  167 GRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLV 220
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
306-460 7.49e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 69.90  E-value: 7.49e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  306 AAASTHGALCLELLVCNGADVNIKSKDGKTPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTL 385
Cdd:PLN03192   531 TVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785376409  386 ITSrADTSKRGIHGMFpLHLAALSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNK 460
Cdd:PLN03192   611 YHF-ASISDPHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
PHA02876 PHA02876
ankyrin repeat protein; Provisional
450-837 7.64e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 69.71  E-value: 7.64e-12
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  450 LLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDERGCSPLHYAATSDtDGKCLEYLLRNDANPGIRD 529
Cdd:PHA02876   163 MLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSK-NIDTIKAIIDNRSNINKND 241
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  530 KHGYNAVhyaaayghrlcleliaRETPLD--VLMETSG--TDMLNDAETrapiSPLHLAAyhgHHQALEVLVQSLL---- 601
Cdd:PHA02876   242 LSLLKAI----------------RNEDLEtsLLLYDAGfsVNSIDDCKN----TPLHHAS---QAPSLSRLVPKLLerga 298
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  602 DLDVRNSTGRTPLDLAAFKGH-VECVDVLINQGASILVKDYVVKrTPIHSAeiqmvdsrnsvnknntelcnsaqkkvrak 680
Cdd:PHA02876   299 DVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYI-TPLHQA----------------------------- 348
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  681 dmpsainghseclrllignadvqaavdihdgngqtplmlSVLNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEE 760
Cdd:PHA02876   349 ---------------------------------------STLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVV 389
                          330       340       350       360       370       380       390
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785376409  761 CVEALLQHNANFLLRDCRGRTPIHLaAACGHIGVLSalLQTAISVDVVPAIADNHGYTPLHWACYNG-HDACVELLLE 837
Cdd:PHA02876   390 IINTLLDYGADIEALSQKIGTALHF-ALCGTNPYMS--VKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLD 464
Ank_4 pfam13637
Ankyrin repeats (many copies);
432-485 1.07e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.75  E-value: 1.07e-11
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1785376409  432 GRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFALV 485
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
301-470 1.09e-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: 68.89  E-value: 1.09e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  301 TPLhFAAASTHGALCLE-LLVCNGADVNIKSKDGKTPLHMTAIHGRFSRSQIIIQNGAE-----IDCEDKNGNTPLHIAA 374
Cdd:cd22192     19 SPL-LLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIAV 97
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  375 RYGHELLINTLITSRADTSKRGIHGMFplhlaalsgFSDCCRKLLSsgfdidthddFGRTCLHAAAAGGNLECLNLLLST 454
Cdd:cd22192     98 VNQNLNLVRELIARGADVVSPRATGTF---------FRPGPKNLIY----------YGEHPLSFAACVGNEEIVRLLIEH 158
                          170
                   ....*....|....*.
gi 1785376409  455 GADFNKKDKFGRTPLH 470
Cdd:cd22192    159 GADIRAQDSLGNTVLH 174
PHA02874 PHA02874
ankyrin repeat protein; Provisional
581-823 1.99e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 67.68  E-value: 1.99e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  581 LHLAAYHGHHQALEVLVQS---LLDLDVRNSTgrTPLDLAAFKGHVECVDVLINQGASIlvkDYVVKRTP--------IH 649
Cdd:PHA02874     5 LRMCIYSGDIEAIEKIIKNkgnCINISVDETT--TPLIDAIRSGDAKIVELFIKHGADI---NHINTKIPhplltaikIG 79
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  650 SAEIQMVDSRNSVNKN-------NTELCNSAQK---KVRAKDMPSAI-------NGHSECLRLLIgnaDVQAAVDIHDGN 712
Cdd:PHA02874    80 AHDIIKLLIDNGVDTSilpipciEKDMIKTILDcgiDVNIKDAELKTflhyaikKGDLESIKMLF---EYGADVNIEDDN 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  713 GQTPLMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPIHLAAAcgHI 792
Cdd:PHA02874   157 GCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HN 234
                          250       260       270
                   ....*....|....*....|....*....|.
gi 1785376409  793 GVLSALLQTAISVDVvpaiADNHGYTPLHWA 823
Cdd:PHA02874   235 RSAIELLINNASIND----QDIDGSTPLHHA 261
Ank_2 pfam12796
Ankyrin repeats (3 copies);
537-640 2.32e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.90  E-value: 2.32e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  537 HYAAAYGHRLCLELIAREtpldvlmetsGTDMlnDAETRAPISPLHLAAYHGHHQALEVLVQSLlDLDVRNStGRTPLDL 616
Cdd:pfam12796    2 HLAAKNGNLELVKLLLEN----------GADA--NLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKDN-GRTALHY 67
                           90       100
                   ....*....|....*....|....
gi 1785376409  617 AAFKGHVECVDVLINQGASILVKD 640
Cdd:pfam12796   68 AARSGHLEIVKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
281-527 2.61e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.94  E-value: 2.61e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  281 VVNELIDCGANVNQVNERGFTPLHFAAaSTHGALCLELLVCNGADVNIKSKDGKTPLHMTAIHGRFSRSQIIIQNGAEI- 359
Cdd:PHA02875    17 IARRLLDIGINPNFEIYDGISPIKLAM-KFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAd 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  360 DCEDKNGNTPLHiaaryghellintlitsradtskrgihgmfplhLAALSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAA 439
Cdd:PHA02875    96 DVFYKDGMTPLH---------------------------------LATILKKLDIMKLLIARGADPDIPNTDKFSPLHLA 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  440 AAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDERGCSPLHYAATSDTDGKCLEYLL 519
Cdd:PHA02875   143 VMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFI 222

                   ....*...
gi 1785376409  520 RNDANPGI 527
Cdd:PHA02875   223 KRGADCNI 230
PHA03100 PHA03100
ankyrin repeat protein; Provisional
825-1029 2.91e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.00  E-value: 2.91e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  825 YNGHDACVELLLEQEVFQKMEGNSFS------PLHCAVINDNEGAAEMLIDTlGTSIvNSVDSKGRTPLH-----AAAFT 893
Cdd:PHA03100     6 VLTKSRIIKVKNIKYIIMEDDLNDYSykkpvlPLYLAKEARNIDVVKILLDN-GADI-NSSTKNNSTPLHylsniKYNLT 83
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  894 DHIECLQLLLSHNAQVNAVDSTGKTPLMMAAEN--GQTSAVEVLVSSAkADLTLQDKNKNTALHLACSKGHETSAL--LI 969
Cdd:PHA03100    84 DVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYLESNKIDLKIlkLL 162
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785376409  970 LEQITDRNLINATNSALQ-------------TPLHVAARNGLTVVVQELLGKGASVLAVDENGYTPA-LACAPN 1029
Cdd:PHA03100   163 IDKGVDINAKNRVNYLLSygvpinikdvygfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLhIAILNN 236
PHA02874 PHA02874
ankyrin repeat protein; Provisional
756-1036 3.98e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.53  E-value: 3.98e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  756 TGHEECVEALLQHNANFL-LRDCRGRTPIHLAAACGHIGVLSALLQTAISVDVVPAIADNhgytPLHWACYNGHDACVEL 834
Cdd:PHA02874    11 SGDIEAIEKIIKNKGNCInISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPH----PLLTAIKIGAHDIIKL 86
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  835 LLEQEVfqkmeGNSFSPLHCavINDnegaaEMLIDTLGTSI-VNSVDSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVD 913
Cdd:PHA02874    87 LIDNGV-----DTSILPIPC--IEK-----DMIKTILDCGIdVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIED 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  914 STGKTPLMMAAENGQTSAVEVLVSSAkADLTLQDKNKNTALHLACSKGHETSALLILEQITdrNLINATNSALqTPLHVA 993
Cdd:PHA02874   155 DNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN--HIMNKCKNGF-TPLHNA 230
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*.
gi 1785376409  994 ARNGLTVVvqELLGKGASVLAVDENGYTP---ALACAPNKDVADCL 1036
Cdd:PHA02874   231 IIHNRSAI--ELLINNASINDQDIDGSTPlhhAINPPCDIDIIDIL 274
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
227-372 7.87e-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: 66.19  E-value: 7.87e-11
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  227 MCKDKK-SYTPLHAAASSGMISVIKYLLDL-GVDMNESNAYGNTPLHVACYNGQDVVVNELIDCGANVnqVNE------- 297
Cdd:cd22192     10 LLQQKRiSESPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPEL--VNEpmtsdly 87
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  298 RGFTPLHFAAASTHGALcLELLVCNGADVN---------IKSKD-----GKTPLHMTAIHGRFSRSQIIIQNGAEIDCED 363
Cdd:cd22192     88 QGETALHIAVVNQNLNL-VRELIARGADVVspratgtffRPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166

                   ....*....
gi 1785376409  364 KNGNTPLHI 372
Cdd:cd22192    167 SLGNTVLHI 175
Ank_2 pfam12796
Ankyrin repeats (3 copies);
502-607 1.65e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.59  E-value: 1.65e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  502 LHYAATSDtDGKCLEYLLRNDANPGIRDKHGYNAVHYAAAYGHRLCLELiaretpldvLMETSGTDMLNDAETrapisPL 581
Cdd:pfam12796    1 LHLAAKNG-NLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKL---------LLEHADVNLKDNGRT-----AL 65
                           90       100
                   ....*....|....*....|....*.
gi 1785376409  582 HLAAYHGHHQALEVLVQSLLDLDVRN 607
Cdd:pfam12796   66 HYAARSGHLEIVKLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
689-898 2.13e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.89  E-value: 2.13e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  689 HSECLRLLIGNADVQAAVDIHDGNGQTPLMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQH 768
Cdd:PLN03192   501 HKELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKH 580
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  769 NANFLLRDCRGRTPIHLAAACGH-------------------------------IGVLSALLQTAISVDVvpaiADNHGY 817
Cdd:PLN03192   581 ACNVHIRDANGNTALWNAISAKHhkifrilyhfasisdphaagdllctaakrndLTAMKELLKQGLNVDS----EDHQGA 656
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  818 TPLHWACYNGHDACVELLLEQ--EVFQKMEGNSFSPLHC-AVINDNE-GAAEMLIDTLGTSIVNSVDSKGRTPLHAAAFT 893
Cdd:PLN03192   657 TALQVAMAEDHVDMVRLLIMNgaDVDKANTDDDFSPTELrELLQKRElGHSITIVDSVPADEPDLGRDGGSRPGRLQGTS 736

                   ....*
gi 1785376409  894 DHIEC 898
Cdd:PLN03192   737 SDNQC 741
PHA02878 PHA02878
ankyrin repeat protein; Provisional
782-1012 2.58e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.13  E-value: 2.58e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  782 PIHLAAACGHIGVLSALLQTAISVDVvpaiADNHGYTPLHWACYNGHDACVELLLeQEVFQKMEGNSFSPLHCAVINDNE 861
Cdd:PHA02878    40 PLHQAVEARNLDVVKSLLTRGHNVNQ----PDHRDLTPLHIICKEPNKLGMKEMI-RSINKCSVFYTLVAIKDAFNNRNV 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  862 GAAEMLIDTLGTSIVNSVDSKGRTplhaAAFTDHIEC--LQLLLSHNAQVNAVD-STGKTPLMMAAENGQTSAVEVLVSS 938
Cdd:PHA02878   115 EIFKIILTNRYKNIQTIDLVYIDK----KSKDDIIEAeiTKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSY 190
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785376409  939 AkADLTLQDKNKNTALHLACSKGHETSALLILEQITDrnlINATNSALQTPLHVAARNGLTV-VVQELLGKGASV 1012
Cdd:PHA02878   191 G-ANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS---TDARDKCGNTPLHISVGYCKDYdILKLLLEHGVDV 261
Ank_2 pfam12796
Ankyrin repeats (3 copies);
469-551 2.95e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.82  E-value: 2.95e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  469 LHYAAANCNYQCLFALVGSGASVNDLDERGCSPLHYAATSDTDgKCLEYLLRNdANPGIRDkHGYNAVHYAAAYGHRLCL 548
Cdd:pfam12796    1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHL-EIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIV 77

                   ...
gi 1785376409  549 ELI 551
Cdd:pfam12796   78 KLL 80
PHA02876 PHA02876
ankyrin repeat protein; Provisional
730-1029 2.98e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 64.31  E-value: 2.98e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  730 YSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANFL-LRDCRGRTPIHlaAACGHIGVLSALLQTAISVDVV 808
Cdd:PHA02876    25 YDLHKHGANQCENESIPFTAIHQALQLRQIDIVEEIIQQNPELIyITDHKCHSTLH--TICIIPNVMDIVISLTLDCDII 102
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  809 PAIAdnhgYTPLHWACYNGHDACVELLleqevfqkMEGNSFSPLHCAVIN---------------DNEGAAEMLIDtlGT 873
Cdd:PHA02876   103 LDIK----YASIILNKHKLDEACIHIL--------KEAISGNDIHYDKINesieymklikeriqqDELLIAEMLLE--GG 168
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  874 SIVNSVDSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAVEVLVSSA----KADLTLQDKN 949
Cdd:PHA02876   169 ADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRsninKNDLSLLKAI 248
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  950 KNTALhlacskghETSALLILEQITdrnlINATNSALQTPLHVAARN-GLTVVVQELLGKGASVLAVDENGYTPALACAP 1028
Cdd:PHA02876   249 RNEDL--------ETSLLLYDAGFS----VNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAK 316

                   .
gi 1785376409 1029 N 1029
Cdd:PHA02876   317 N 317
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
584-771 3.90e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 64.12  E-value: 3.90e-10
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  584 AAYHGHHQALEVLVQSLLDLDVRNSTGRTPLDLAAFKGHVECVDVLINQGASILVKDYvvkrtpihsaeiqmvdsrnsvn 663
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDA---------------------- 589
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  664 KNNTELCNSAqkkvrakdmpsaINGHSECLRLLIGNA---DVQAAVDIhdgngqtpLMLSVLNGHTECVYSLLNKGANVD 740
Cdd:PLN03192   590 NGNTALWNAI------------SAKHHKIFRILYHFAsisDPHAAGDL--------LCTAAKRNDLTAMKELLKQGLNVD 649
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1785376409  741 AKDKWGRTALHRGAVTGHEECVEALLQHNAN 771
Cdd:PLN03192   650 SEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
Ank_4 pfam13637
Ankyrin repeats (many copies);
579-630 5.01e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 5.01e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1785376409  579 SPLHLAAYHGHHQALEVLVQSLLDLDVRNSTGRTPLDLAAFKGHVECVDVLI 630
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
234-278 5.01e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.13  E-value: 5.01e-10
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1785376409  234 YTPLHAAASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQ 278
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
Ank_4 pfam13637
Ankyrin repeats (many copies);
101-154 9.75e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 9.75e-10
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1785376409  101 WLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALV 154
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
201-253 1.09e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 1.09e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1785376409  201 RRAIHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMISVIKYLL 253
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
747-938 1.19e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.93  E-value: 1.19e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  747 RTALHRGAVTGHEECVEALLQ--HNANFLLRDcrGRTPIHLAAACGHIGVLSALLqtaiSVDVVPAIADNHGYTPLHWAC 824
Cdd:PHA02875     3 QVALCDAILFGELDIARRLLDigINPNFEIYD--GISPIKLAMKFRDSEAIKLLM----KHGAIPDVKYPDIESELHDAV 76
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  825 YNGHDACVELLLE-----QEVFQKmEGNSfsPLHCAVINDNEGAAEMLIDTLGTSIVNSVDSKgrTPLHAAAFTDHIECL 899
Cdd:PHA02875    77 EEGDVKAVEELLDlgkfaDDVFYK-DGMT--PLHLATILKKLDIMKLLIARGADPDIPNTDKF--SPLHLAVMMGDIKGI 151
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1785376409  900 QLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAVEVLVSS 938
Cdd:PHA02875   152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDS 190
PHA03100 PHA03100
ankyrin repeat protein; Provisional
567-808 1.84e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.22  E-value: 1.84e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  567 DMLNDAETRAPISPLHLAAYHGHHQALEVLVQSLLDLDVRNSTGRTPLDLAAFKGHV-----ECVDVLINQGASILVKDy 641
Cdd:PHA03100    25 DDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPD- 103
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  642 vvkrtpihsaeiqmvdsrnsvNKNNTELCNSAQKKVrakdmpsainGHSECLRLLIGNAdvqAAVDIHDGNGQTPLMLSV 721
Cdd:PHA03100   104 ---------------------NNGITPLLYAISKKS----------NSYSIVEYLLDNG---ANVNIKNSDGENLLHLYL 149
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  722 LNGHTEC------------------VYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPI 783
Cdd:PHA03100   150 ESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPL 229
                          250       260
                   ....*....|....*....|....*
gi 1785376409  784 HLAAACGHIGVLSALLQTAISVDVV 808
Cdd:PHA03100   230 HIAILNNNKEIFKLLLNNGPSIKTI 254
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
281-470 3.44e-09

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 61.08  E-value: 3.44e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  281 VVNELIDCG-ANVNQV-NERGFTPLHFAAASTHGAL-CLELLVCNGADVNIKSKDGKTPLHMTAIHGRFSRSQI--IIQN 355
Cdd:PHA02716   157 LIKYMVDVGiVNLNYVcKKTGYGILHAYLGNMYVDIdILEWLCNNGVNVNLQNNHLITPLHTYLITGNVCASVIkkIIEL 236
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  356 GAEIDCEDKNGNTPLH---IAARYGHELLINTLITSRADTSKRGIHGMFPLHLAALSGFS-DCCRKLLSSGFDIDTHDDF 431
Cdd:PHA02716   237 GGDMDMKCVNGMSPIMtyiINIDNINPEITNIYIESLDGNKVKNIPMILHSYITLARNIDiSVVYSFLQPGVKLHYKDSA 316
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|.
gi 1785376409  432 GRTCLHAAAAGGNL--ECLNLLLSTGADFNKKDKFGRTPLH 470
Cdd:PHA02716   317 GRTCLHQYILRHNIstDIIKLLHEYGNDLNEPDNIGNTVLH 357
Ank_4 pfam13637
Ankyrin repeats (many copies);
883-936 4.15e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 4.15e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1785376409  883 GRTPLHAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAVEVLV 936
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02989 PHA02989
ankyrin repeat protein; Provisional
82-344 5.09e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 60.14  E-value: 5.09e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   82 EIIELLILSGARVNAKdSKWLTPL-----HRAVASCS-EDAVQVLLKHSADVNARDKNWQTPlhiaaankavkcaeaLVP 155
Cdd:PHA02989    51 KIVKLLIDNGADVNYK-GYIETPLcavlrNREITSNKiKKIVKLLLKFGADINLKTFNGVSP---------------IVC 114
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  156 LLSNVNVSDragrtalhhaafsghVEMVSLLLSRGANINafDKKDRRA-----IHWAAYMGHIEVVKLLVTHGAEVMckD 230
Cdd:PHA02989   115 FIYNSNINN---------------CDMLRFLLSKGINVN--DVKNSRGynllhMYLESFSVKKDVIKILLSFGVNLF--E 175
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  231 KKSY---TPLHAAASSGM----ISVIKYLLDLGVDMNESNAYGNTPL------HVACYNGQDVVVNeLIDCGANVNQVNE 297
Cdd:PHA02989   176 KTSLyglTPMNIYLRNDIdvisIKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLN-FILKYIKINKKDK 254
                          250       260       270       280
                   ....*....|....*....|....*....|....*....|....*..
gi 1785376409  298 RGFTPLHFAAASTHGALCLELLVCnGADVNIKSKDGKTPLHMTAIHG 344
Cdd:PHA02989   255 KGFNPLLISAKVDNYEAFNYLLKL-GDDIYNVSKDGDTVLTYAIKHG 300
Ank_4 pfam13637
Ankyrin repeats (many copies);
136-187 7.04e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 7.04e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1785376409  136 TPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLL 187
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
402-452 7.46e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 7.46e-09
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1785376409  402 PLHLAALSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLL 452
Cdd:pfam13637    4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02859 PHA02859
ankyrin repeat protein; Provisional
99-277 7.97e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 57.14  E-value: 7.97e-09
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   99 SKWLTPLHRAVASCSEDAVQvllKHSADVNARDKNWQTPLHIAAANKAV--KCAEALVPLLSNVNVSDRA-GRTALHH-A 174
Cdd:PHA02859    19 YRYCNPLFYYVEKDDIEGVK---KWIKFVNDCNDLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTRDnNLSALHHyL 95
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  175 AFSGHV--EMVSLLLSRGANINAFDKKDRRAIHwaAYMGH----IEVVKLLVTHGAEVMCKDKK------SYTPLHAAAS 242
Cdd:PHA02859    96 SFNKNVepEILKILIDSGSSITEEDEDGKNLLH--MYMCNfnvrINVIKLLIDSGVSFLNKDFDnnnilySYILFHSDKK 173
                          170       180       190
                   ....*....|....*....|....*....|....*
gi 1785376409  243 sgmisVIKYLLDLGVDMNESNAYGNTPLHVACYNG 277
Cdd:PHA02859   174 -----IFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
PHA02875 PHA02875
ankyrin repeat protein; Provisional
786-1041 1.11e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.85  E-value: 1.11e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  786 AAACGHIGVLSALLQTAISvdvvPAIADNHGYTPLHWACYNGHDACVELLLEQEVFQKMEGNSF-SPLHCAVINDNEGAA 864
Cdd:PHA02875     9 AILFGELDIARRLLDIGIN----PNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIeSELHDAVEEGDVKAV 84
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  865 EMLIDtLGTSIVNSVDSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAVEVLVSsakadlt 944
Cdd:PHA02875    85 EELLD-LGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLID------- 156
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  945 lqdknkntalHLACskghetsallileqitdrnlINATNSALQTPLHVAARNGLTVVVQELLGKGASVLAVDENGYTPAL 1024
Cdd:PHA02875   157 ----------HKAC--------------------LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAAL 206
                          250
                   ....*....|....*..
gi 1785376409 1025 ACAPNKDVADCLALILA 1041
Cdd:PHA02875   207 CYAIENNKIDIVRLFIK 223
PHA02946 PHA02946
ankyin-like protein; Provisional
76-303 1.17e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 58.91  E-value: 1.17e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   76 AYLG----DAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLH-IAAANKAVkca 150
Cdd:PHA02946    43 AYCGikglDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYyLSGTDDEV--- 119
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  151 ealvpllsnvnvsdragrtalhhaafsghVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVTHGAEVMCKD 230
Cdd:PHA02946   120 -----------------------------IERINLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVD 170
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409  231 K--KSYTPLHAAASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNG-QDVVVNELIDCGANVNQVNERGFTPL 303
Cdd:PHA02946   171 KfgKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTvKNVDIINLLLPSTDVNKQNKFGDSPL 246
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
405-662 1.47e-08

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 58.74  E-value: 1.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  405 LAALSGFSDCCRKLLSSgfDIDTHDDFGRTCLHAAA---AGGNLECLNLLLSTGADFNKKDKF-----------GRTPLH 470
Cdd:cd21882      1 LEELLGLLECLRWYLTD--SAYQRGATGKTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELvnapctdefyqGQTALH 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  471 YAAANCNYQCLFALVGSGASVN-----DLDER--------GCSPLHYAATSDTDgKCLEYLLRNDANP---GIRDKHGYN 534
Cdd:cd21882     79 IAIENRNLNLVRLLVENGADVSaratgRFFRKspgnlfyfGELPLSLAACTNQE-EIVRLLLENGAQPaalEAQDSLGNT 157
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  535 AVHyaaayghrlCLELIARETPLDVLMETSGTDMLndaetrapispLHLAAYHGHHQALEvlvqslldlDVRNSTGRTPL 614
Cdd:cd21882    158 VLH---------ALVLQADNTPENSAFVCQMYNLL-----------LSYGAHLDPTQQLE---------EIPNHQGLTPL 208
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1785376409  615 DLAAFKGHVECVDVLINQGASILVKDYVVKRT-----PIHSA--EIQMVDS--RNSV 662
Cdd:cd21882    209 KLAAVEGKIVMFQHILQREFSGPYQPLSRKFTewtygPVTSSlyDLSEIDSweKNSV 265
PHA02878 PHA02878
ankyrin repeat protein; Provisional
590-821 1.47e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.74  E-value: 1.47e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  590 HQALEV----LVQSLLDLDVR-NSTGR---TPLDLAAFKGHVECVDVLInqgaSILVKD-----YVVKRTPIHSAEIQMV 656
Cdd:PHA02878    42 HQAVEArnldVVKSLLTRGHNvNQPDHrdlTPLHIICKEPNKLGMKEMI----RSINKCsvfytLVAIKDAFNNRNVEIF 117
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  657 DS--RNSVNKNNTelcnSAQKKVRAKDMPSAINghSECLRLLIG-NADVQAaVDIHDGNgqTPLMLSVLNGHTECVYSLL 733
Cdd:PHA02878   118 KIilTNRYKNIQT----IDLVYIDKKSKDDIIE--AEITKLLLSyGADINM-KDRHKGN--TALHYATENKDQRLTELLL 188
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  734 NKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPIHLAAA-CGHIGVLSALLQTAISVDVVPAIA 812
Cdd:PHA02878   189 SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGyCKDYDILKLLLEHGVDVNAKSYIL 268

                   ....*....
gi 1785376409  813 dnhGYTPLH 821
Cdd:PHA02878   269 ---GLTALH 274
PHA02878 PHA02878
ankyrin repeat protein; Provisional
336-651 1.51e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.35  E-value: 1.51e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  336 PLHMtAIHGR-FSRSQIIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSRADTS----KRGIHGMFplHLAALSG 410
Cdd:PHA02878    40 PLHQ-AVEARnLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSvfytLVAIKDAF--NNRNVEI 116
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  411 FsdccRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDK-FGRTPLHYAAANCNYQCLFALVGSGA 489
Cdd:PHA02878   117 F----KIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGA 192
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  490 SVNDLDERGCSPLHYAaTSDTDGKCLEYLLRNDANpgirdkhgynavhyaaayghrlcleliaretpldvlmetsgtdml 569
Cdd:PHA02878   193 NVNIPDKTNNSPLHHA-VKHYNKPIVHILLENGAS--------------------------------------------- 226
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  570 ndaetrapisplhlaayhghhqalevlvqslldLDVRNSTGRTPLDLAAfkGHVECVDV---LINQGASILVKDYVVKRT 646
Cdd:PHA02878   227 ---------------------------------TDARDKCGNTPLHISV--GYCKDYDIlklLLEHGVDVNAKSYILGLT 271

                   ....*
gi 1785376409  647 PIHSA 651
Cdd:PHA02878   272 ALHSS 276
PHA02859 PHA02859
ankyrin repeat protein; Provisional
180-302 2.19e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 55.60  E-value: 2.19e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  180 VEMVSLLLSRGANINAFDKKDRRAI--HWAAYMGHI--EVVKLLVTHGAEVMCKDKKSYTPLHAAAS--SGMISVIKYLL 253
Cdd:PHA02859    66 VEILKFLIENGADVNFKTRDNNLSAlhHYLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHMYMCnfNVRINVIKLLI 145
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|
gi 1785376409  254 DLGVDMNESNAYGNTPLHV-ACYNGQDVVVNELIDCGANVNQVNERGFTP 302
Cdd:PHA02859   146 DSGVSFLNKDFDNNNILYSyILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
PHA03100 PHA03100
ankyrin repeat protein; Provisional
49-133 2.31e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.75  E-value: 2.31e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   49 DEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVN 128
Cdd:PHA03100   173 NRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252

                   ....*
gi 1785376409  129 ARDKN 133
Cdd:PHA03100   253 TIIET 257
Ank_4 pfam13637
Ankyrin repeats (many copies);
746-799 3.03e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.12  E-value: 3.03e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1785376409  746 GRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPIHLAAACGHIGVLSALL 799
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
69-121 4.27e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 4.27e-08
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1785376409   69 RTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLL 121
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
712-912 4.48e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.92  E-value: 4.48e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  712 NGQTPLMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNA---NFLLRDcrGRTPIHLAAA 788
Cdd:PHA02875    34 DGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATI 111
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  789 CGHIGVLSALLQTAISVDvvpaIADNHGYTPLHWACYNGHDACVELLLEQEVFQKME-GNSFSPLHCAVINDNEGAAEML 867
Cdd:PHA02875   112 LKKLDIMKLLIARGADPD----IPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEdCCGCTPLIIAMAKGDIAICKML 187
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|....*.
gi 1785376409  868 IDTlGTSIvNSVDSKGRTPLHAAAFTDH-IECLQLLLSHNAQVNAV 912
Cdd:PHA02875   188 LDS-GANI-DYFGKNGCVAALCYAIENNkIDIVRLFIKRGADCNIM 231
PHA02946 PHA02946
ankyin-like protein; Provisional
417-537 4.76e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 56.99  E-value: 4.76e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  417 KLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAANCN--YQCLFALVGSGASVND- 493
Cdd:PHA02946    57 ELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNs 136
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1785376409  494 LDERGCSPLhyAATSDTDGKCLEYLLRNDANPGIRDKHGYNAVH 537
Cdd:PHA02946   137 VDEEGCGPL--LACTDPSERVFKKIMSIGFEARIVDKFGKNHIH 178
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
60-303 5.39e-08

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 57.23  E-value: 5.39e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   60 DVNFQDNEKRTP-LHAaaYLG----DAEIIELLILSGARVNAKDSKWLTPLHRAV--ASCSEDAVQVLLKHSADVNARDK 132
Cdd:PHA02716   168 NLNYVCKKTGYGiLHA--YLGnmyvDIDILEWLCNNGVNVNLQNNHLITPLHTYLitGNVCASVIKKIIELGGDMDMKCV 245
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  133 NWQTPLHIAAANkavkcAEALVPLLSNVNVSDRAGRTALHHAafsghvEMVSLLLSRGANINafdkkdrraihwaaymgh 212
Cdd:PHA02716   246 NGMSPIMTYIIN-----IDNINPEITNIYIESLDGNKVKNIP------MILHSYITLARNID------------------ 296
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  213 IEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMIS--VIKYLLDLGVDMNESNAYGNTPLH--------VACYNGQ---D 279
Cdd:PHA02716   297 ISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNIStdIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvVNILDPEtdnD 376
                          250       260
                   ....*....|....*....|....*..
gi 1785376409  280 V---VVNELIDCGANVNQVNERGFTPL 303
Cdd:PHA02716   377 IrldVIQCLISLGADITAVNCLGYTPL 403
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
772-1008 5.95e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.94  E-value: 5.95e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  772 FLLRDCRGR-TPIHLAAACGHIGVLSALLQTAiSVDVVPAIAdnHGYTPLHWACYNGHDACVELLLEQE---VFQKMEGN 847
Cdd:cd22192      9 HLLQQKRISeSPLLLAAKENDVQAIKKLLKCP-SCDLFQRGA--LGETALHVAALYDNLEAAVVLMEAApelVNEPMTSD 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  848 SF---SPLHCAVINDNEGAAEMLI----DTL-----GTSIVNSVDSK---GRTPLHAAAFTDHIECLQLLLSHNAQVNAV 912
Cdd:cd22192     86 LYqgeTALHIAVVNQNLNLVRELIargaDVVspratGTFFRPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQ 165
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  913 DSTGKTPL-MMAAENGQTSAVEVLvssakaDLTL-QDKNKNtalhlacskghetsaLLILEQItdrnlinaTNSALQTPL 990
Cdd:cd22192    166 DSLGNTVLhILVLQPNKTFACQMY------DLILsYDKEDD---------------LQPLDLV--------PNNQGLTPF 216
                          250
                   ....*....|....*...
gi 1785376409  991 HVAARNGLTVVVQELLGK 1008
Cdd:cd22192    217 KLAAKEGNIVMFQHLVQK 234
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
869-942 5.99e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 5.99e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  869 DTLGTSIV-------NSVDSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAVEVLVSSAKA 941
Cdd:PTZ00322    94 DAVGARILltggadpNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173

                   .
gi 1785376409  942 D 942
Cdd:PTZ00322   174 H 174
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
210-401 6.40e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.80  E-value: 6.40e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  210 MGHIEVVKLLVTHGAEVmcKDKKSYTPLHAAASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDCG 289
Cdd:PLN03192   504 LHDLNVGDLLGDNGGEH--DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  290 ANVNQVNERGFTPLHFAAASTHGALCLELLVCNGADVNIKSKDgktPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTP 369
Cdd:PLN03192   582 CNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGD---LLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATA 658
                          170       180       190
                   ....*....|....*....|....*....|..
gi 1785376409  370 LHIAARYGHELLINTLITSRADTSKRGIHGMF 401
Cdd:PLN03192   659 LQVAMAEDHVDMVRLLIMNGADVDKANTDDDF 690
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
713-823 6.65e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 56.56  E-value: 6.65e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  713 GQTPLMLSVLNGHTECVYSLLNKGANV--------------DAKDKWGRTALHRGAVTGHEECVEALLQHNANFLLRDCR 778
Cdd:cd22192     89 GETALHIAVVNQNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1785376409  779 GRTPIHLAA-------ACGHIGVLSAL--LQTAISVDVVPaiaDNHGYTPLHWA 823
Cdd:cd22192    169 GNTVLHILVlqpnktfACQMYDLILSYdkEDDLQPLDLVP---NNQGLTPFKLA 219
PHA02875 PHA02875
ankyrin repeat protein; Provisional
38-194 6.80e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 6.80e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   38 PLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLIlsgarvnakdskwltplhravascsedav 117
Cdd:PHA02875   105 PLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLI----------------------------- 155
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1785376409  118 qvllKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVN-VSDRAGRTALHHAAFSGHVEMVSLLLSRGANIN 194
Cdd:PHA02875   156 ----DHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGADCN 229
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
420-636 9.30e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.41  E-value: 9.30e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  420 SSGFDIDTHDDFGrtcLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNdldergc 499
Cdd:PLN03192   516 NGGEHDDPNMASN---LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVH------- 585
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  500 splhyaatsdtdgkcleyllrndanpgIRDKHGYNAVHYAAAYGHrlcleliarETPLDVLMETSGtdmLNDAETRAPIs 579
Cdd:PLN03192   586 ---------------------------IRDANGNTALWNAISAKH---------HKIFRILYHFAS---ISDPHAAGDL- 625
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1785376409  580 pLHLAAYHGHHQALEVLVQSLLDLDVRNSTGRTPLDLAAFKGHVECVDVLINQGASI 636
Cdd:PLN03192   626 -LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
174-332 9.62e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.41  E-value: 9.62e-08
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  174 AAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMISVIKYLL 253
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  254 DLGvdmNESNAY-GNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALcLELLVCNGADVNIKSKD 332
Cdd:PLN03192   612 HFA---SISDPHaAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDM-VRLLIMNGADVDKANTD 687
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
880-1008 1.11e-07

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 55.92  E-value: 1.11e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  880 DSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDST--------------GKTPLMMAAENGQTSAVEVLVSSAKADLTL 945
Cdd:cd22194    138 AYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKESTDITS 217
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785376409  946 QDKNKNTALHLAC-----SKGHETSALLILEQI----TDRNLINATNSALQTPLHVAARNGLTVVVQELLGK 1008
Cdd:cd22194    218 QDSRGNTVLHALVtvaedSKTQNDFVKRMYDMIllksENKNLETIRNNEGLTPLQLAAKMGKAEILKYILSR 289
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
216-288 1.13e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 1.13e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785376409  216 VKLLVTHGAEVMCKDKKSYTPLHAAASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDC 288
Cdd:PTZ00322    98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02946 PHA02946
ankyin-like protein; Provisional
161-339 1.19e-07

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 55.45  E-value: 1.19e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  161 NVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGH--IEVVKLLVTHGAEVMCK-DKKSYTPL 237
Cdd:PHA02946    66 NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNSvDEEGCGPL 145
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  238 HAAASSGMiSVIKYLLDLGVDMNESNAYGNTPLH--VACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALC 315
Cdd:PHA02946   146 LACTDPSE-RVFKKIMSIGFEARIVDKFGKNHIHrhLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKNVD 224
                          170       180
                   ....*....|....*....|....
gi 1785376409  316 LELLVCNGADVNIKSKDGKTPLHM 339
Cdd:PHA02946   225 IINLLLPSTDVNKQNKFGDSPLTL 248
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
404-498 1.34e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 1.34e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  404 HLAAlSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFA 483
Cdd:PTZ00322    88 QLAA-SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166
                           90
                   ....*....|....*
gi 1785376409  484 LVGSGASVNDLDERG 498
Cdd:PTZ00322   167 LSRHSQCHFELGANA 181
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
171-253 1.47e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 1.47e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  171 LHHAAFSGHVEMVSLLLSRGANINAFDKKDRRAIHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAAASSGMISVIK 250
Cdd:PTZ00322    86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                   ...
gi 1785376409  251 YLL 253
Cdd:PTZ00322   166 LLS 168
PHA02874 PHA02874
ankyrin repeat protein; Provisional
38-182 1.56e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.97  E-value: 1.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   38 PLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRAV-------- 109
Cdd:PHA02874   160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIihnrsaie 239
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  110 ------------------------ASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAanKAVKCAEALVPLLSNVNVSDR 165
Cdd:PHA02874   240 llinnasindqdidgstplhhainPPCDIDIIDILLYHKADISIKDNKGENPIDTAF--KYINKDPVIKDIIANAVLIKE 317
                          170
                   ....*....|....*..
gi 1785376409  166 AGRtaLHHAAFSGHVEM 182
Cdd:PHA02874   318 ADK--LKDSDFLEHIEI 332
PHA02859 PHA02859
ankyrin repeat protein; Provisional
260-371 1.63e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 53.28  E-value: 1.63e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  260 NESNAYGNTPLHvACYNGQDVVVNE---LIDCGANVN-QVNERGFTPLHFAAASTHGAL--CLELLVCNGADVNIKSKDG 333
Cdd:PHA02859    45 NDCNDLYETPIF-SCLEKDKVNVEIlkfLIENGADVNfKTRDNNLSALHHYLSFNKNVEpeILKILIDSGSSITEEDEDG 123
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|
gi 1785376409  334 KTPLH--MTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLH 371
Cdd:PHA02859   124 KNLLHmyMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILY 163
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
918-1012 2.08e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 55.02  E-value: 2.08e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  918 TPLMMAAENGQTSAVEVLVSSAKADLTLQDKNKNTALHLACSKGHETSALLILEQitDRNLIN-ATNSAL---QTPLHVA 993
Cdd:cd22192     19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEA--APELVNePMTSDLyqgETALHIA 96
                           90
                   ....*....|....*....
gi 1785376409  994 ARNGLTVVVQELLGKGASV 1012
Cdd:cd22192     97 VVNQNLNLVRELIARGADV 115
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
880-1022 2.56e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.87  E-value: 2.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  880 DSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAVEVLVSSAKAdltlqdKNKNTALHLACS 959
Cdd:PLN03192   555 DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASI------SDPHAAGDLLCT 628
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785376409  960 KGHETSaLLILEQITDRNL-INATNSALQTPLHVAARNGLTVVVQELLGKGASVLAVD-ENGYTP 1022
Cdd:PLN03192   629 AAKRND-LTAMKELLKQGLnVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDDDFSP 692
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
55-307 2.80e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 54.70  E-value: 2.80e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   55 IFKKEDVNFQDNEKrtplhaaAYLGDAEIIELLILSGARVNAK-------DSKWLTPLHRAVA-SCSEDAVQVLLKHSAD 126
Cdd:TIGR00870    6 IVPAEESPLSDEEK-------AFLPAAERGDLASVYRDLEEPKklnincpDRLGRSALFVAAIeNENLELTELLLNLSCR 78
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  127 VNARDknwqTPLHIAAANKAVKCAEALVPLLSN---------VNVSDR----AGRTALHHAAFSGHVEMVSLLLSRGANI 193
Cdd:TIGR00870   79 GAVGD----TLLHAISLEYVDAVEAILLHLLAAfrksgplelANDQYTseftPGITALHLAAHRQNYEIVKLLLERGASV 154
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  194 NA------FDKKDRRA--------IHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAAAssgmisvikylldlgvdM 259
Cdd:TIGR00870  155 PAracgdfFVKSQGVDsfyhgespLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV-----------------M 217
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409  260 NESNAYGNTPLHVACYNG--------QDVVVNELIdcganvnqVNERGFTPLHFAA 307
Cdd:TIGR00870  218 ENEFKAEYEELSCQMYNFalslldklRDSKELEVI--------LNHQGLTPLKLAA 265
PHA02875 PHA02875
ankyrin repeat protein; Provisional
515-771 3.02e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.23  E-value: 3.02e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  515 LEYLLRNDANPGIRDKHGYNAVHYAAAYGHRLCLELiaretpldvLMETSGTDMLNDAETRapiSPLHLAAYHGHHQALE 594
Cdd:PHA02875    18 ARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKL---------LMKHGAIPDVKYPDIE---SELHDAVEEGDVKAVE 85
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  595 VLVQS--LLDlDVRNSTGRTPLDLAAFKGHVECVDVLINQGASILVKDyVVKRTPIHSAeiqmvdsrnsvnknntelcns 672
Cdd:PHA02875    86 ELLDLgkFAD-DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPN-TDKFSPLHLA--------------------- 142
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  673 aqkkVRAKDmpsaINGhsecLRLLIgnaDVQAAVDIHDGNGQTPLMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALHR 752
Cdd:PHA02875   143 ----VMMGD----IKG----IELLI---DHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALC 207
                          250       260
                   ....*....|....*....|
gi 1785376409  753 GAVTGHE-ECVEALLQHNAN 771
Cdd:PHA02875   208 YAIENNKiDIVRLFIKRGAD 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
433-786 3.12e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.20  E-value: 3.12e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  433 RTCLHAaaagGNLECLNLLLSTGADF-NKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDERGCSPLhYAATSDTD 511
Cdd:PHA02874     6 RMCIYS----GDIEAIEKIIKNKGNCiNISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPL-LTAIKIGA 80
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  512 GKCLEYLLRNDANPGIrdkhgynavhyaaayghrLCLELIARETPLDVLmeTSGTDM-LNDAETRapiSPLHLAAYHGHH 590
Cdd:PHA02874    81 HDIIKLLIDNGVDTSI------------------LPIPCIEKDMIKTIL--DCGIDVnIKDAELK---TFLHYAIKKGDL 137
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  591 QALEVLVQSLLDLDVRNSTGRTPLDLAAFKGHVECVDVLINQGASILVKDYVVKrTPIHSAeiqmvdsrnsvnknntelc 670
Cdd:PHA02874   138 ESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGE-SPLHNA------------------- 197
                          250       260       270       280       290       300       310       320
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  671 nsaqkkvrakdmpsAINGHSECLRLLIGNADvqaAVDIHDGNGQTPLMLSVLngHTECVYSLLNKGANVDAKDKWGRTAL 750
Cdd:PHA02874   198 --------------AEYGDYACIKLLIDHGN---HIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPL 258
                          330       340       350
                   ....*....|....*....|....*....|....*..
gi 1785376409  751 HRG-AVTGHEECVEALLQHNANFLLRDCRGRTPIHLA 786
Cdd:PHA02874   259 HHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTA 295
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
111-188 3.17e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 3.17e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  111 SCSEDAV--QVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLS 188
Cdd:PTZ00322    90 AASGDAVgaRILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PHA02875 PHA02875
ankyrin repeat protein; Provisional
406-645 3.62e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.84  E-value: 3.62e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  406 AALSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFALV 485
Cdd:PHA02875     9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  486 GSGASVND-LDERGCSPLHYAATSdtdgKCLEYLlrndanpgirdkhgynavhyaaayghRLcleLIARETPLDVlmetS 564
Cdd:PHA02875    89 DLGKFADDvFYKDGMTPLHLATIL----KKLDIM--------------------------KL---LIARGADPDI----P 131
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  565 GTDMLndaetrapiSPLHLAAYHGHHQALEVLVQSLLDLDVRNSTGRTPLDLAAFKGHVECVDVLINQGASIlvkDYVVK 644
Cdd:PHA02875   132 NTDKF---------SPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI---DYFGK 199

                   .
gi 1785376409  645 R 645
Cdd:PHA02875   200 N 200
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
308-377 4.27e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 4.27e-07
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  308 ASTHGALCLELLVCNGADVNIKSKDGKTPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHIAARYG 377
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
PHA02874 PHA02874
ankyrin repeat protein; Provisional
852-1022 4.82e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.43  E-value: 4.82e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  852 LHCAVINDNEGAAEMLIDTlgTSIVNSVDSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSA 931
Cdd:PHA02874   128 LHYAIKKGDLESIKMLFEY--GADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  932 VEVLVSSAkADLTLQDKNKNTALHLACSkgHETSALLILeqITDRNlINATNSALQTPLHVAARNGLTV-VVQELLGKGA 1010
Cdd:PHA02874   206 IKLLIDHG-NHIMNKCKNGFTPLHNAII--HNRSAIELL--INNAS-INDQDIDGSTPLHHAINPPCDIdIIDILLYHKA 279
                          170
                   ....*....|..
gi 1785376409 1011 SVLAVDENGYTP 1022
Cdd:PHA02874   280 DISIKDNKGENP 291
Ank_4 pfam13637
Ankyrin repeats (many copies);
335-386 5.14e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 5.14e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1785376409  335 TPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLI 386
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
404-520 5.56e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 5.56e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  404 HLAALSGFSDccrKLLSSGFDIDTHDDFGRTCLHAA-------AAGGNLECLNLLLSTGADFNKKDKFGRTPLHYAAANC 476
Cdd:PTZ00322    50 HLEALEATEN---KDATPDHNLTTEEVIDPVVAHMLtvelcqlAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANG 126
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....
gi 1785376409  477 NYQCLFALVGSGASVNDLDERGCSPLHYAATSDTdGKCLEYLLR 520
Cdd:PTZ00322   127 HVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF-REVVQLLSR 169
PHA03095 PHA03095
ankyrin-like protein; Provisional
47-170 6.60e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.10  E-value: 6.60e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   47 DPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGD--AEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHS 124
Cdd:PHA03095   201 RARIVRELIRAGCDPAATDMLGNTPLHSMATGSSckRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALG 280
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|....*.
gi 1785376409  125 ADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTA 170
Cdd:PHA03095   281 ADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTA 326
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
869-1040 7.22e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 7.22e-07
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  869 DTLGTSIVNSVDSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAVEVLVSSAkADLTLQDK 948
Cdd:PLN03192   511 DLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDA 589
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  949 NKNTALHLACSKGHETsALLILEQITDRNLINATNSALQTplhvAARNGLTVVVQELLGKGASVLAVDENGYTpALACAP 1028
Cdd:PLN03192   590 NGNTALWNAISAKHHK-IFRILYHFASISDPHAAGDLLCT----AAKRNDLTAMKELLKQGLNVDSEDHQGAT-ALQVAM 663
                          170
                   ....*....|..
gi 1785376409 1029 NKDVADCLALIL 1040
Cdd:PLN03192   664 AEDHVDMVRLLI 675
Ank_4 pfam13637
Ankyrin repeats (many copies);
715-766 8.40e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 8.40e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1785376409  715 TPLMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALL 766
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
465-519 8.65e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 8.65e-07
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1785376409  465 GRTPLHYAAANCNYQCLFALVGSGASVNDLDERGCSPLHYAATSDtDGKCLEYLL 519
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG-NVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
726-923 1.05e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.57  E-value: 1.05e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  726 TECVYSLLNKGANVDAKDK-WGRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPIHLAAACGHIGVLSALLQTAIS 804
Cdd:PHA02878   147 AEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  805 VDvvpaIADNHGYTPLHWAcynghdacVELLLEQEVFQkmegnsfsplhcavindnegaaeMLIDTlGTSIVNSVDSKGR 884
Cdd:PHA02878   227 TD----ARDKCGNTPLHIS--------VGYCKDYDILK-----------------------LLLEH-GVDVNAKSYILGL 270
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1785376409  885 TPLHAAAFTDHIecLQLLLSHNAQVNAVDSTGKTPLMMA 923
Cdd:PHA02878   271 TALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
PHA02859 PHA02859
ankyrin repeat protein; Provisional
434-537 1.08e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 50.59  E-value: 1.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  434 TCLHAAAAggNLECLNLLLSTGADFNKKDK-FGRTPLHYAAA---NCNYQCLFALVGSGASVNDLDERGCSPLH-YAATS 508
Cdd:PHA02859    57 SCLEKDKV--NVEILKFLIENGADVNFKTRdNNLSALHHYLSfnkNVEPEILKILIDSGSSITEEDEDGKNLLHmYMCNF 134
                           90       100
                   ....*....|....*....|....*....
gi 1785376409  509 DTDGKCLEYLLRNDANPGIRDKHGYNAVH 537
Cdd:PHA02859   135 NVRINVIKLLIDSGVSFLNKDFDNNNILY 163
PHA02875 PHA02875
ankyrin repeat protein; Provisional
707-838 1.23e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.30  E-value: 1.23e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  707 DIHDGNGQTPLMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPIHLA 786
Cdd:PHA02875    96 DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1785376409  787 AACGHIGVLSALLQTAISVDVVpaiADNHGYTPLHWACYNGHDACVELLLEQ 838
Cdd:PHA02875   176 MAKGDIAICKMLLDSGANIDYF---GKNGCVAALCYAIENNKIDIVRLFIKR 224
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
406-544 1.33e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 1.33e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  406 AALSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLhYAAANCNYQCLFALV 485
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL-WNAISAKHHKIFRIL 610
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*....
gi 1785376409  486 GSGASVNDLDERGcsPLHYAATSDTDGKCLEYLLRNDANPGIRDKHGYNAVHYAAAYGH 544
Cdd:PLN03192   611 YHFASISDPHAAG--DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDH 667
Ank_4 pfam13637
Ankyrin repeats (many copies);
779-836 1.51e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 1.51e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1785376409  779 GRTPIHLAAACGHIGVLSALLQTAISVDVVpaiaDNHGYTPLHWACYNGHDACVELLL 836
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAV----DGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
786-936 1.61e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.56  E-value: 1.61e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  786 AAACGHIGVLSALLQTAISVDvvpaIADNHGYTPLHWACYNGHDACVELLLEQEV---FQKMEGNS-------------F 849
Cdd:PLN03192   532 VASTGNAALLEELLKAKLDPD----IGDSKGRTPLHIAASKGYEDCVLVLLKHACnvhIRDANGNTalwnaisakhhkiF 607
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  850 SPL-HCAVINDNEGAAEMLIdtlgtsivnsvdskgrtplhAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQ 928
Cdd:PLN03192   608 RILyHFASISDPHAAGDLLC--------------------TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDH 667

                   ....*...
gi 1785376409  929 TSAVEVLV 936
Cdd:PLN03192   668 VDMVRLLI 675
PHA02989 PHA02989
ankyrin repeat protein; Provisional
213-452 2.08e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 51.67  E-value: 2.08e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  213 IEVVKLLVTHGAEVmckDKKSY--TPLHAA------ASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNE 284
Cdd:PHA02989    50 IKIVKLLIDNGADV---NYKGYieTPLCAVlrnreiTSNKIKKIVKLLLKFGADINLKTFNGVSPIVCFIYNSNINNCDM 126
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  285 L---IDCGANVNQV-NERGFTPLH--FAAASTHGALCLELLvcnGADVNIKSKD---GKTPLHmtaIHGRFSRSQI---- 351
Cdd:PHA02989   127 LrflLSKGINVNDVkNSRGYNLLHmyLESFSVKKDVIKILL---SFGVNLFEKTslyGLTPMN---IYLRNDIDVIsikv 200
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  352 ---IIQNGAEIDCEDKNGNTPLHIAAR-----YGHELLINTLITSRADTSKRGIHGMFPLHLAALSGFSDCCRKLLSSGF 423
Cdd:PHA02989   201 ikyLIKKGVNIETNNNGSESVLESFLDnnkilSKKEFKVLNFILKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGD 280
                          250       260
                   ....*....|....*....|....*....
gi 1785376409  424 DIDTHDDFGRTCLHAAAAGGNLECLNLLL 452
Cdd:PHA02989   281 DIYNVSKDGDTVLTYAIKHGNIDMLNRIL 309
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
241-347 2.77e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 2.77e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  241 ASSGMISVIKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGALCLELLV 320
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1785376409  321 CNGADVNI------KSKDGKTPLH----MTAIHGRFS 347
Cdd:PTZ00322   170 HSQCHFELganakpDSFTGKPPSLedspISSHHPDFS 206
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
10-124 2.84e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 2.84e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   10 EEGEDDAPHftsKLPQRKILTPP--GIVTPPLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELL 87
Cdd:PTZ00322    58 ENKDATPDH---NLTTEEVIDPVvaHMLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVL 134
                           90       100       110
                   ....*....|....*....|....*....|....*..
gi 1785376409   88 ILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHS 124
Cdd:PTZ00322   135 LEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHS 171
Ank_4 pfam13637
Ankyrin repeats (many copies);
36-88 4.91e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 4.91e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1785376409   36 TPPLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLI 88
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
266-320 4.91e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 4.91e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1785376409  266 GNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAASTHGAlCLELLV 320
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVE-VLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
167-198 5.74e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.82  E-value: 5.74e-06
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1785376409  167 GRTALHHAAFS-GHVEMVSLLLSRGANINAFDK 198
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02989 PHA02989
ankyrin repeat protein; Provisional
246-505 5.78e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 50.12  E-value: 5.78e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  246 ISVIKYLLDLGVDMNESnaYGNTPLHVACYNGQDV---VVNELIDCGANVNQvneRGF--TPL-----HFAAASTHGALC 315
Cdd:PHA02989    16 KNALEFLLRTGFDVNEE--YRGNSILLLYLKRKDVkikIVKLLIDNGADVNY---KGYieTPLcavlrNREITSNKIKKI 90
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  316 LELLVCNGADVNIKSKDGKTPLhMTAIHG---------RFsrsqiIIQNGAEI-DCEDKNGNTPLHIaarYGHELLINT- 384
Cdd:PHA02989    91 VKLLLKFGADINLKTFNGVSPI-VCFIYNsninncdmlRF-----LLSKGINVnDVKNSRGYNLLHM---YLESFSVKKd 161
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  385 ----LITSRADT-SKRGIHGMFPLHLAALSGFS----DCCRKLLSSGFDIDTHDDFGRTCL------HAAAAGGNLECLN 449
Cdd:PHA02989   162 vikiLLSFGVNLfEKTSLYGLTPMNIYLRNDIDvisiKVIKYLIKKGVNIETNNNGSESVLesfldnNKILSKKEFKVLN 241
                          250       260       270       280       290
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409  450 LLLSTgADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDERGCSPLHYA 505
Cdd:PHA02989   242 FILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYA 296
Ank_5 pfam13857
Ankyrin repeats (many copies);
218-273 5.81e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 5.81e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409  218 LLVTHGAEVMCKDKKSYTPLHAAASSGMISVIKYLLDLGVDMNESNAYGNTPLHVA 273
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
924-1019 6.17e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.28  E-value: 6.17e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  924 AENGQTSAVEVLVSSAkADLTLQDKNKNTALHLACSKGHETSALLILEQITDRNLINATNsalQTPLHVAARNGLTVVVQ 1003
Cdd:PTZ00322    90 AASGDAVGARILLTGG-ADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDG---KTPLELAEENGFREVVQ 165
                           90
                   ....*....|....*.
gi 1785376409 1004 ELLGKGASVLAVDENG 1019
Cdd:PTZ00322   166 LLSRHSQCHFELGANA 181
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
338-491 6.82e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.25  E-value: 6.82e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  338 HMTAIHGrFSRSQIIIQNGAEIDceDKNGNTPLHIAARYGHELLINTLITSRADTSKRGIHGMFPLHLAALSGFSDCCRK 417
Cdd:PLN03192   500 HHKELHD-LNVGDLLGDNGGEHD--DPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLV 576
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  418 LLSSGFDIDTHDDFGRTCL------------------------HA-------AAAGGNLECLNLLLSTGADFNKKDKFGR 466
Cdd:PLN03192   577 LLKHACNVHIRDANGNTALwnaisakhhkifrilyhfasisdpHAagdllctAAKRNDLTAMKELLKQGLNVDSEDHQGA 656
                          170       180
                   ....*....|....*....|....*
gi 1785376409  467 TPLHYAAANCNYQCLFALVGSGASV 491
Cdd:PLN03192   657 TALQVAMAEDHVDMVRLLIMNGADV 681
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
70-207 8.87e-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: 49.63  E-value: 8.87e-06
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   70 TPLHAAAYLGDAEIIELLILSGARVNA---------KDSKWLT-----PLHRAVASCSEDAVQVLLKHSADVNARDKNWQ 135
Cdd:cd22192     91 TALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKNLIyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  136 TPLHIAA--ANKAVKCAE-----ALVPLLSNVNVS---DRAGRTALHHAAFSGHVEMVSLLLSRganinafdkkdRRAIH 205
Cdd:cd22192    171 TVLHILVlqPNKTFACQMydlilSYDKEDDLQPLDlvpNNQGLTPFKLAAKEGNIVMFQHLVQK-----------RRHIQ 239

                   ..
gi 1785376409  206 WA 207
Cdd:cd22192    240 WT 241
Ank_4 pfam13637
Ankyrin repeats (many copies);
816-868 9.58e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 9.58e-06
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1785376409  816 GYTPLHWACYNGHDACVELLLEQEV-FQKMEGNSFSPLHCAVINDNEGAAEMLI 868
Cdd:pfam13637    1 ELTALHAAAASGHLELLRLLLEKGAdINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
167-195 9.73e-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: 43.35  E-value: 9.73e-06
                            10        20
                    ....*....|....*....|....*....
gi 1785376409   167 GRTALHHAAFSGHVEMVSLLLSRGANINA 195
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
79-153 9.79e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 9.79e-06
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785376409   79 GDAEIIELLILSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIAAANKAVKCAEAL 153
Cdd:PTZ00322    93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PHA02946 PHA02946
ankyin-like protein; Provisional
282-469 1.19e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 49.28  E-value: 1.19e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  282 VNELIDCGANVNQVNERGFTPLHFAAASTHGALcLELLVCNGADVNIKSKDGKTPLHMTAIHGR--FSRSQIIIQNGAEI 359
Cdd:PHA02946    55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRI-VAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKI 133
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  360 DCE-DKNGNTPLhIAARYGHELLINTLITSRADT------SKRGIHgmfpLHLAALSGFSDCCRKLLSSGFDIDTHDDFG 432
Cdd:PHA02946   134 NNSvDEEGCGPL-LACTDPSERVFKKIMSIGFEArivdkfGKNHIH----RHLMSDNPKASTISWMMKLGISPSKPDHDG 208
                          170       180       190
                   ....*....|....*....|....*....|....*....
gi 1785376409  433 RTCLHAAAAG--GNLECLNLLLSTgADFNKKDKFGRTPL 469
Cdd:PHA02946   209 NTPLHIVCSKtvKNVDIINLLLPS-TDVNKQNKFGDSPL 246
Ank_5 pfam13857
Ankyrin repeats (many copies);
424-472 1.24e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.24e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1785376409  424 DIDTHDDFGRTCLHAAAAGGNLECLNLLLSTGADFNKKDKFGRTPLHYA 472
Cdd:pfam13857    8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
120-174 1.30e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 1.30e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409  120 LLKH-SADVNARDKNWQTPLHIAAANKAVKCAEALVPLLSNVNVSDRAGRTALHHA 174
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
135-309 1.75e-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: 48.72  E-value: 1.75e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  135 QTPLHIAAANKAVKCAEALVPLLSNVNVSDRA--------------GRTALHHAAFSGHVEMVSLLLSRGANINA----- 195
Cdd:cd21882     27 KTCLHKAALNLNDGVNEAIMLLLEAAPDSGNPkelvnapctdefyqGQTALHIAIENRNLNLVRLLVENGADVSAratgr 106
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  196 -FDKKDRRAIHW-------AAYMGHIEVVKLLVTHGAE---VMCKDKKSYTPLHAAAssgmisvikylldlgvdMNESNA 264
Cdd:cd21882    107 fFRKSPGNLFYFgelplslAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHALV-----------------LQADNT 169
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1785376409  265 YGNTPLHVACYNGqdvvvneLIDCGANVNQV-------NERGFTPLHFAAAS 309
Cdd:cd21882    170 PENSAFVCQMYNL-------LLSYGAHLDPTqqleeipNHQGLTPLKLAAVE 214
Ank_4 pfam13637
Ankyrin repeats (many copies);
850-903 1.76e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 1.76e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....
gi 1785376409  850 SPLHCAVINDNEGAAEMLIDTlgTSIVNSVDSKGRTPLHAAAFTDHIECLQLLL 903
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEK--GADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
285-339 1.96e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 1.96e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1785376409  285 LIDCG-ANVNQVNERGFTPLHFAAasTHGAL-CLELLVCNGADVNIKSKDGKTPLHM 339
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAA--KYGALeIVRVLLAYGVDLNLKDEEGLTALDL 55
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
695-768 2.46e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 2.46e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785376409  695 LLIGNADVqaavDIHDGNGQTPLMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQH 768
Cdd:PTZ00322   101 LLTGGADP----NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
350-420 2.84e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 2.84e-05
                           10        20        30        40        50        60        70
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1785376409  350 QIIIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSRADTSKRGIHGMFPLHLAALSGFSDCCRKLLS 420
Cdd:PTZ00322    99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
754-836 3.02e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 3.02e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  754 AVTGHEECVEALLQHNANFLLRDCRGRTPIHLAAACGHIGVLSALLQTAISvdvvPAIADNHGYTPLHWACYNGHDACVE 833
Cdd:PTZ00322    90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGAD----PTLLDKDGKTPLELAEENGFREVVQ 165

                   ...
gi 1785376409  834 LLL 836
Cdd:PTZ00322   166 LLS 168
PHA02798 PHA02798
ankyrin-like protein; Provisional
732-926 3.76e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.52  E-value: 3.76e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  732 LLNKGANVDAKDKWGRTA----LHRGAVTgHEECVEALLQHNANFLLRDCRGRTPIHLAAACGH---IGVLSALLQTAIS 804
Cdd:PHA02798    95 LIENGADINKKNSDGETPlyclLSNGYIN-NLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVD 173
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  805 VDVvpaIADNHGYTPLHwaCY-----NGHDA-CVELLLEQEVFQKMEGNS----FSPLHCAVINDNEGAAEMLIDTLGTS 874
Cdd:PHA02798   174 INT---HNNKEKYDTLH--CYfkyniDRIDAdILKLFVDNGFIINKENKShkkkFMEYLNSLLYDNKRFKKNILDFIFSY 248
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|...
gi 1785376409  875 I-VNSVDSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAEN 926
Cdd:PHA02798   249 IdINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFEN 301
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
261-377 3.78e-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: 47.83  E-value: 3.78e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  261 ESNAYGNTPLHVACYNGQDVVVNELIDCGANVN----------QVNERGF----TPLHFAAASTHGALcLELLVCNGADv 326
Cdd:cd22194    136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpKYKHEGFyfgeTPLALAACTNQPEI-VQLLMEKEST- 213
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785376409  327 NIKSKD--GKTPLHMTAIHGRFSRSQI--IIQNGAEI--DCEDKN--------GNTPLHIAARYG 377
Cdd:cd22194    214 DITSQDsrGNTVLHALVTVAEDSKTQNdfVKRMYDMIllKSENKNletirnneGLTPLQLAAKMG 278
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
167-195 4.59e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 41.47  E-value: 4.59e-05
                           10        20
                   ....*....|....*....|....*....
gi 1785376409  167 GRTALHHAAFSGHVEMVSLLLSRGANINA 195
Cdd:pfam13606    2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
252-306 4.71e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 4.71e-05
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409  252 LLDLG-VDMNESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFA 306
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
418-621 5.04e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.38  E-value: 5.04e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  418 LLSSGFDIDThddfGRTCLHAAAAG--GNLE-CLNLLL----STGADFNKKDK------FGRTPLHYAAANCNYQCLFAL 484
Cdd:TIGR00870   72 LLNLSCRGAV----GDTLLHAISLEyvDAVEaILLHLLaafrKSGPLELANDQytseftPGITALHLAAHRQNYEIVKLL 147
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  485 VGSGASVN--------------DLDERGCSPLH-YAATSDTDgkCLEYLLRNDANPGIRDKHGyNAVhyaaayghrlcLE 549
Cdd:TIGR00870  148 LERGASVParacgdffvksqgvDSFYHGESPLNaAACLGSPS--IVALLSEDPADILTADSLG-NTL-----------LH 213
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1785376409  550 LIARETPLDVLMETSGTDMLNDAetrapispLHLAAYHGHHQALEVlvqslldldVRNSTGRTPLDLAAFKG 621
Cdd:TIGR00870  214 LLVMENEFKAEYEELSCQMYNFA--------LSLLDKLRDSKELEV---------ILNHQGLTPLKLAAKEG 268
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
713-857 5.30e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.38  E-value: 5.30e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  713 GQTPLMLSVLNGHTECVYSLLNKGANVDAKDK--------------WGRTALHRGAVTGHEECVEALLQHNANFLLRDCR 778
Cdd:TIGR00870  128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  779 GRTPIHLAA------------ACG-HIGVLSALLQTAISVDvVPAIADNHGYTPLHWACYNGHDACVELLLEQEVFQ-KM 844
Cdd:TIGR00870  208 GNTLLHLLVmenefkaeyeelSCQmYNFALSLLDKLRDSKE-LEVILNHQGLTPLKLAAKEGRIVLFRLKLAIKYKQkKF 286
                          170
                   ....*....|...
gi 1785376409  845 EGNSFSPLHCAVI 857
Cdd:TIGR00870  287 VAWPNGQQLLSLY 299
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
402-599 6.44e-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: 46.93  E-value: 6.44e-05
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  402 PLHLAALSGFSDCCRKLL-SSGFDIDTHDDFGRTCLHAAAAGGNLECLNLLLS----------TGADFNkkdkfGRTPLH 470
Cdd:cd22192     20 PLLLAAKENDVQAIKKLLkCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEaapelvnepmTSDLYQ-----GETALH 94
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  471 YAAANCNYQCLFALVGSGASVN--------------DLDERGCSPLHYAATSDTDgKCLEYLLRNDANPGIRDKHGYNAV 536
Cdd:cd22192     95 IAVVNQNLNLVRELIARGADVVspratgtffrpgpkNLIYYGEHPLSFAACVGNE-EIVRLLIEHGADIRAQDSLGNTVL 173
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  537 HYaaayghrlcLELIARETP----LDVLM--ETSGTDM-LNDAETRAPISPLHLAAYHGHHQALEVLVQS 599
Cdd:cd22192    174 HI---------LVLQPNKTFacqmYDLILsyDKEDDLQpLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQK 234
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
265-293 8.34e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.65  E-value: 8.34e-05
                            10        20
                    ....*....|....*....|....*....
gi 1785376409   265 YGNTPLHVACYNGQDVVVNELIDCGANVN 293
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
882-913 1.01e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 1.01e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1785376409  882 KGRTPLHAAA-FTDHIECLQLLLSHNAQVNAVD 913
Cdd:pfam00023    1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
500-649 1.05e-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: 46.16  E-value: 1.05e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  500 SPLHYAAtSDTDGKCLEYLLR-NDANPGIRDKHGYNAVHYAAAYGHRLCLELIARETPLDVLMETsgTDMLNDAETrapi 578
Cdd:cd22192     19 SPLLLAA-KENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPM--TSDLYQGET---- 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  579 sPLHLAAYHGHhqalEVLVQSLLD--LDVRNST----------------GRTPLDLAAFKGHVECVDVLINQGASILVKD 640
Cdd:cd22192     92 -ALHIAVVNQN----LNLVRELIArgADVVSPRatgtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166

                   ....*....
gi 1785376409  641 YvVKRTPIH 649
Cdd:cd22192    167 S-LGNTVLH 174
Ank_4 pfam13637
Ankyrin repeats (many copies);
301-347 1.13e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 1.13e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*..
gi 1785376409  301 TPLHFAAASTHGAlCLELLVCNGADVNIKSKDGKTPLHMTAIHGRFS 347
Cdd:pfam13637    3 TALHAAAASGHLE-LLRLLLEKGADINAVDGNGETALHFAASNGNVE 48
PHA02859 PHA02859
ankyrin repeat protein; Provisional
292-372 1.17e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.42  E-value: 1.17e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  292 VNQVNERGFTPLHFAAASTHGAL-CLELLVCNGADVNIKSKD-GKTPLH-MTAIHGRFSRS--QIIIQNGAEIDCEDKNG 366
Cdd:PHA02859    44 VNDCNDLYETPIFSCLEKDKVNVeILKFLIENGADVNFKTRDnNLSALHhYLSFNKNVEPEilKILIDSGSSITEEDEDG 123

                   ....*.
gi 1785376409  367 NTPLHI 372
Cdd:PHA02859   124 KNLLHM 129
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
265-297 1.28e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 1.28e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1785376409  265 YGNTPLHVACY-NGQDVVVNELIDCGANVNQVNE 297
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
703-751 1.85e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 1.85e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*....
gi 1785376409  703 QAAVDIHDGNGQTPLMLSVLNGHTECVYSLLNKGANVDAKDKWGRTALH 751
Cdd:pfam13857    6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
186-240 2.06e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 2.06e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409  186 LLSRG-ANINAFDKKDRRAIHWAAYMGHIEVVKLLVTHGAEVMCKDKKSYTPLHAA 240
Cdd:pfam13857    1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
432-460 2.90e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 2.90e-04
                            10        20
                    ....*....|....*....|....*....
gi 1785376409   432 GRTCLHAAAAGGNLECLNLLLSTGADFNK 460
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
882-911 3.14e-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: 3.14e-04
                            10        20        30
                    ....*....|....*....|....*....|
gi 1785376409   882 KGRTPLHAAAFTDHIECLQLLLSHNAQVNA 911
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
249-405 3.40e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 44.66  E-value: 3.40e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  249 IKYLLDLGVDMNESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQVNERGFTPLHFAAAS------------THGAL-- 314
Cdd:PHA02946    55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTddevierinllvQYGAKin 134
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  315 -------CLELLVCN-------------GADVNIKSKDGKTPLHMTAIHGRFSRSQI--IIQNGAEIDCEDKNGNTPLHI 372
Cdd:PHA02946   135 nsvdeegCGPLLACTdpservfkkimsiGFEARIVDKFGKNHIHRHLMSDNPKASTIswMMKLGISPSKPDHDGNTPLHI 214
                          170       180       190
                   ....*....|....*....|....*....|....
gi 1785376409  373 A-ARYGHELLINTLITSRADTSKRGIHGMFPLHL 405
Cdd:PHA02946   215 VcSKTVKNVDIINLLLPSTDVNKQNKFGDSPLTL 248
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
432-463 3.55e-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: 3.55e-04
                           10        20        30
                   ....*....|....*....|....*....|...
gi 1785376409  432 GRTCLHAAAA-GGNLECLNLLLSTGADFNKKDK 463
Cdd:pfam00023    2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
872-923 3.79e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 3.79e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1785376409  872 GTSIVNSVDSKGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMA 923
Cdd:pfam13857    5 GPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
59-108 3.86e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 3.86e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1785376409   59 EDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWLTPLHRA 108
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
918-963 3.90e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 3.90e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1785376409  918 TPLMMAAENGQTSAVEVLVSSaKADLTLQDKNKNTALHLACSKGHE 963
Cdd:pfam13637    3 TALHAAAASGHLELLRLLLEK-GADINAVDGNGETALHFAASNGNV 47
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
712-744 3.99e-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: 3.99e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1785376409  712 NGQTPLMLSVL-NGHTECVYSLLNKGANVDAKDK 744
Cdd:pfam00023    1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
977-1022 4.43e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 4.43e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*.
gi 1785376409  977 NLINATNSALQTPLHVAARNGLTVVVQELLGKGASVLAVDENGYTP 1022
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTA 52
Ank_5 pfam13857
Ankyrin repeats (many copies);
318-373 4.52e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 4.52e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409  318 LLVCNGADVNIKSKDGKTPLHMTAIHGRFSRSQIIIQNGAEIDCEDKNGNTPLHIA 373
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
92-141 4.84e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 4.84e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|
gi 1785376409   92 ARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQTPLHIA 141
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
718-803 4.94e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 4.94e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  718 MLSV------LNGHTECVYSLLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPIHLAAACGH 791
Cdd:PTZ00322    81 MLTVelcqlaASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF 160
                           90
                   ....*....|..
gi 1785376409  792 IGVLSALLQTAI 803
Cdd:PTZ00322   161 REVVQLLSRHSQ 172
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
298-331 5.15e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.42  E-value: 5.15e-04
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1785376409  298 RGFTPLHFAAASTHGALCLELLVCNGADVNIKSK 331
Cdd:pfam00023    1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
412-601 6.62e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.98  E-value: 6.62e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  412 SDCCRKLLSSGFdidTHDDF-GRTCLHAAAAGGNLECLNLLLSTGAD---------FNKKDK-----FGRTPLHYAAanC 476
Cdd:cd22194    123 NGILDRFINAEY---TEEAYeGQTALNIAIERRQGDIVKLLIAKGADvnahakgvfFNPKYKhegfyFGETPLALAA--C 197
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  477 NYQ---CLFALVGSGASVNDLDERGCSPLHYAATSDTDGK--------CLEYLLRNDAN---PGIRDKHGYNAVHYAAAY 542
Cdd:cd22194    198 TNQpeiVQLLMEKESTDITSQDSRGNTVLHALVTVAEDSKtqndfvkrMYDMILLKSENknlETIRNNEGLTPLQLAAKM 277
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1785376409  543 GHRLCLELI-ARETPLDVLMETSG--TDM-----------LNDAETRAPISPLHLAAY---HGHHQ---ALEVLvQSLL 601
Cdd:cd22194    278 GKAEILKYIlSREIKEKPNRSLSRkfTDWaygpvssslydLTNVDTTTDNSVLEIIVYntnIDNRHemlTLEPL-HTLL 355
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
234-261 7.30e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 7.30e-04
                            10        20
                    ....*....|....*....|....*...
gi 1785376409   234 YTPLHAAASSGMISVIKYLLDLGVDMNE 261
Cdd:smart00248    3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
755-1011 7.72e-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: 43.33  E-value: 7.72e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  755 VTGHEECVEALLqhNANFLLRDCRGRTPIHLAAACGHIGVLSA---LLQTAISVDVVPAIADN-------HGYTPLHWAC 824
Cdd:cd21882      4 LLGLLECLRWYL--TDSAYQRGATGKTCLHKAALNLNDGVNEAimlLLEAAPDSGNPKELVNApctdefyQGQTALHIAI 81
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  825 YNGHDACVELLLEQ--EVFQKMEGNSFSPLHCAVIndnegaaemlidtlgtsivnsvdSKGRTPLHAAAFTDHIECLQLL 902
Cdd:cd21882     82 ENRNLNLVRLLVENgaDVSARATGRFFRKSPGNLF-----------------------YFGELPLSLAACTNQEEIVRLL 138
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  903 LSHNAQVNAV---DSTGKTPLMMaaengqtsavevlvssakadLTLQDKNKNTALHLAC-------SKGHETSALLILEQ 972
Cdd:cd21882    139 LENGAQPAALeaqDSLGNTVLHA--------------------LVLQADNTPENSAFVCqmynlllSYGAHLDPTQQLEE 198
                          250       260       270
                   ....*....|....*....|....*....|....*....
gi 1785376409  973 ITDRNLInatnsalqTPLHVAARNGLTVVVQELLGKGAS 1011
Cdd:cd21882    199 IPNHQGL--------TPLKLAAVEGKIVMFQHILQREFS 229
Ank_5 pfam13857
Ankyrin repeats (many copies);
732-786 9.01e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 9.01e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*
gi 1785376409  732 LLNKGANVDAKDKWGRTALHRGAVTGHEECVEALLQHNANFLLRDCRGRTPIHLA 786
Cdd:pfam13857    2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02884 PHA02884
ankyrin repeat protein; Provisional
82-222 9.16e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 42.66  E-value: 9.16e-04
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   82 EIIELLILSGARVNAK----DSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKNWQ-TPLHIAAANKAVKCAEALVPL 156
Cdd:PHA02884    47 DIIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSY 126
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409  157 LSNVNVSDRAGRTALHHAAFSGHVEMVSLLlsRGANINAFDKKDRRaihwaaYMGHIEVVKLLVTH 222
Cdd:PHA02884   127 GADINIQTNDMVTPIELALMICNNFLAFMI--CDNEISNFYKHPKK------ILINFDILKILVSH 184
PHA02795 PHA02795
ankyrin-like protein; Provisional
154-195 9.18e-04

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 43.06  E-value: 9.18e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1785376409  154 VPLLSNVNVSDRAGRTALHHAAFSGHVEMVSLLLSRGANINA 195
Cdd:PHA02795   208 IPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNA 249
Ank_5 pfam13857
Ankyrin repeats (many copies);
489-539 9.94e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 9.94e-04
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1785376409  489 ASVNDLDERGCSPLHYAAtSDTDGKCLEYLLRNDANPGIRDKHGYNAVHYA 539
Cdd:pfam13857    7 IDLNRLDGEGYTPLHVAA-KYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
450-505 1.02e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 1.02e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409  450 LLLSTGADFNKKDKFGRTPLHYAAANCNYQCLFALVGSGASVNDLDERGCSPLHYA 505
Cdd:pfam13857    1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
816-1006 1.08e-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: 43.15  E-value: 1.08e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  816 GYTPLHWACYNGHDACVELLLEQEVFQKMEGNSFsplhcavindnegaaeMLIDTLGTSIvnsvdSKGRTPLHAAAFTDH 895
Cdd:TIGR00870   82 GDTLLHAISLEYVDAVEAILLHLLAAFRKSGPLE----------------LANDQYTSEF-----TPGITALHLAAHRQN 140
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  896 IECLQLLLSHNAQVNA------------VDST--GKTPLMMAAENGQTSAVEvLVSSAKADLTLQDKNKNTALHL----- 956
Cdd:TIGR00870  141 YEIVKLLLERGASVPAracgdffvksqgVDSFyhGESPLNAAACLGSPSIVA-LLSEDPADILTADSLGNTLLHLlvmen 219
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1785376409  957 -------ACSKGHETSALLILEQITD-RNLINATNSALQTPLHVAARNGLTVVVQELL 1006
Cdd:TIGR00870  220 efkaeyeELSCQMYNFALSLLDKLRDsKELEVILNHQGLTPLKLAAKEGRIVLFRLKL 277
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
815-837 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 1785376409   815 HGYTPLHWACYNGHDACVELLLE 837
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLD 23
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
265-293 1.24e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 1.24e-03
                           10        20
                   ....*....|....*....|....*....
gi 1785376409  265 YGNTPLHVACYNGQDVVVNELIDCGANVN 293
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02884 PHA02884
ankyrin repeat protein; Provisional
248-340 1.30e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 42.28  E-value: 1.30e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  248 VIKYLLDLGVDMN----ESNAYGNTPLHVACYNGQDVVVNELIDCGANVNQ-VNERGFTPLHFAAasTHGAL-CLELLVC 321
Cdd:PHA02884    48 IIDAILKLGADPEapfpLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKITPLYISV--LHGCLkCLEILLS 125
                           90
                   ....*....|....*....
gi 1785376409  322 NGADVNIKSKDGKTPLHMT 340
Cdd:PHA02884   126 YGADINIQTNDMVTPIELA 144
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
371-453 1.37e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 1.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  371 HIAARyGHELLINTLITSRADTSKRGIHGMFPLHLAALSGFSDCCRKLLSSGFDIDTHDDFGRTCLHAAAAGGNLECLNL 450
Cdd:PTZ00322    88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166

                   ...
gi 1785376409  451 LLS 453
Cdd:PTZ00322   167 LSR 169
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
276-410 1.42e-03

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 42.87  E-value: 1.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  276 NGQDVVVNELIDCGANVNQVNE-----------RGFTPLHFAAASTHGALcLELLVCNGADVN----------IKSKD-- 332
Cdd:cd22196     60 NGQNDTISLLLDIAEKTGNLKEfvnaaytdsyyKGQTALHIAIERRNMHL-VELLVQNGADVHarasgeffkkKKGGPgf 138
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  333 --GKTPLHMTAIHGRFSRSQIIIQN---GAEIDCEDKNGNTPLH---------------IAARYGHELL----INTLITS 388
Cdd:cd22196    139 yfGELPLSLAACTNQLDIVKFLLENphsPADISARDSMGNTVLHalvevadntpentkfVTKMYNEILIlgakIRPLLKL 218
                          170       180
                   ....*....|....*....|..
gi 1785376409  389 RADTSKRgihGMFPLHLAALSG 410
Cdd:cd22196    219 EEITNKK---GLTPLKLAAKTG 237
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
882-1008 1.63e-03

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 42.49  E-value: 1.63e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  882 KGRTPLHAAAFTDHIECLQLLLSHNAQVNAVDST--------------GKTPLMMAAENGQTSAVEVLVSS--AKADLTL 945
Cdd:cd22196     93 KGQTALHIAIERRNMHLVELLVQNGADVHARASGeffkkkkggpgfyfGELPLSLAACTNQLDIVKFLLENphSPADISA 172
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  946 QDKNKNTALHLACS---------------------KGHETSALLILEQITDRNLInatnsalqTPLHVAARNGLTVVVQE 1004
Cdd:cd22196    173 RDSMGNTVLHALVEvadntpentkfvtkmyneiliLGAKIRPLLKLEEITNKKGL--------TPLKLAAKTGKIGIFAY 244

                   ....
gi 1785376409 1005 LLGK 1008
Cdd:cd22196    245 ILGR 248
Ank_5 pfam13857
Ankyrin repeats (many copies);
567-617 2.08e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 2.08e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1785376409  567 DMLNDAETRAPISPLHLAAYHGHHQALEVLVQSLLDLDVRNSTGRTPLDLA 617
Cdd:pfam13857    6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
69-98 2.37e-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: 2.37e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1785376409   69 RTPLHAAAY-LGDAEIIELLILSGARVNAKD 98
Cdd:pfam00023    3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02875 PHA02875
ankyrin repeat protein; Provisional
36-128 2.62e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.52  E-value: 2.62e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   36 TPPLVQAIFNGDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVN-AKDSKWLTPLHRAVASCSE 114
Cdd:PHA02875   136 FSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKI 215
                           90
                   ....*....|....
gi 1785376409  115 DAVQVLLKHSADVN 128
Cdd:PHA02875   216 DIVRLFIKRGADCN 229
PHA02946 PHA02946
ankyin-like protein; Provisional
352-502 2.75e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.58  E-value: 2.75e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  352 IIQNGAEIDCEDKNGNTPLHIAARYGHELLINTLITSRADTSKRGIHGMFPLHLaaLSGFSD------------------ 413
Cdd:PHA02946    58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYY--LSGTDDevierinllvqygakinn 135
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  414 -----------CC--------RKLLSSGFDIDTHDDFGRTCLHAAAAGGN--LECLNLLLSTGADFNKKDKFGRTPLHYA 472
Cdd:PHA02946   136 svdeegcgpllACtdpservfKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHDGNTPLHIV 215
                          170       180       190
                   ....*....|....*....|....*....|.
gi 1785376409  473 AANCNYQC-LFALVGSGASVNDLDERGCSPL 502
Cdd:PHA02946   216 CSKTVKNVdIINLLLPSTDVNKQNKFGDSPL 246
PHA02946 PHA02946
ankyin-like protein; Provisional
785-990 2.85e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.58  E-value: 2.85e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  785 LAAACGHIGVLSALLQTAISVDVVPAIADNHGYTPLHWACYNGHDACVELLLEQEVF-QKMEGNSFSPLHCAVINDNEGA 863
Cdd:PHA02946    41 LHAYCGIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADpNACDKQHKTPLYYLSGTDDEVI 120
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  864 AEM-LIDTLGTSIVNSVDSKGRTPLHAAafTDHIE-CLQLLLSHNAQVNAVDSTGKTPL--MMAAENGQTSAVEVLVSSA 939
Cdd:PHA02946   121 ERInLLVQYGAKINNSVDEEGCGPLLAC--TDPSErVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLG 198
                          170       180       190       200       210
                   ....*....|....*....|....*....|....*....|....*....|.
gi 1785376409  940 KADlTLQDKNKNTALHLACSKghETSALLILEQITDRNLINATNSALQTPL 990
Cdd:PHA02946   199 ISP-SKPDHDGNTPLHIVCSK--TVKNVDIINLLLPSTDVNKQNKFGDSPL 246
PHA02791 PHA02791
ankyrin-like protein; Provisional
812-981 2.87e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 41.18  E-value: 2.87e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  812 ADNHGYTPLHWACYNGHDACVELLLEQEVFQKMEGNSFsPLH-CAVINDNEGAAEMLIDTLGTSivnSVDSKGRTPLHAA 890
Cdd:PHA02791    26 ADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF-PLHqAATLEDTKIVKILLFSGMDDS---QFDDKGNTALYYA 101
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  891 AFTDHIECLQLLLSHNAQVNAVDSTG-KTPLMMAAENGQTSAVEVLVSSAKADLTLQDknKNTALHLACSKGHETSALLI 969
Cdd:PHA02791   102 VDSGNMQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPSTFDLAI--LLSCIHITIKNGHVDMMILL 179
                          170
                   ....*....|..
gi 1785376409  970 LEQITDRNLINA 981
Cdd:PHA02791   180 LDYMTSTNTNNS 191
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
497-530 3.15e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 3.15e-03
                           10        20        30
                   ....*....|....*....|....*....|....
gi 1785376409  497 RGCSPLHYAATSDTDGKCLEYLLRNDANPGIRDK 530
Cdd:pfam00023    1 DGNTPLHLAAGRRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
610-640 3.21e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 3.21e-03
                           10        20        30
                   ....*....|....*....|....*....|..
gi 1785376409  610 GRTPLDLAAFK-GHVECVDVLINQGASILVKD 640
Cdd:pfam00023    2 GNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
902-957 3.47e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 3.47e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1785376409  902 LLSH-NAQVNAVDSTGKTPLMMAAENGQTSAVEVLVsSAKADLTLQDKNKNTALHLA 957
Cdd:pfam13857    1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLL-AYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
610-636 3.49e-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: 3.49e-03
                            10        20
                    ....*....|....*....|....*..
gi 1785376409   610 GRTPLDLAAFKGHVECVDVLINQGASI 636
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02792 PHA02792
ankyrin-like protein; Provisional
248-335 3.51e-03

ankyrin-like protein; Provisional


Pssm-ID: 165155 [Multi-domain]  Cd Length: 631  Bit Score: 41.47  E-value: 3.51e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  248 VIKYLLDLGVDM--NESNAYGNTPLHVACYNGQDVVVNELIDCGA---NVNQVNERGFTPLHFAAAStHGALCLELLVCN 322
Cdd:PHA02792   354 VVEYILKNGNVVveDDDNIINIMPLFPTLSIHESDVLSILKLCKPyidDINKIDKHGRSILYYCIES-HSVSLVEWLIDN 432
                           90
                   ....*....|...
gi 1785376409  323 GADVNIKSKDGKT 335
Cdd:PHA02792   433 GADINITTKYGST 445
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
103-132 4.11e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 4.11e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 1785376409  103 TPLHRAVASC-SEDAVQVLLKHSADVNARDK 132
Cdd:pfam00023    4 TPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
PHA02736 PHA02736
Viral ankyrin protein; Provisional
432-479 4.21e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.09  E-value: 4.21e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|..
gi 1785376409  432 GRTCLHAAAAGGNL---ECLNLLLSTGADFNKKD-KFGRTPLHYAAANCNYQ 479
Cdd:PHA02736    55 GKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKErVFGNTPLHIAVYTQNYE 106
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
58-276 4.33e-03

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 40.94  E-value: 4.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   58 KEDVN--FQDNEKR--TPLHAAAYLGDAEIIELLILSGARVNA------------KDSKWLTPLHRAVASCSE--DAVQV 119
Cdd:cd22196     80 KEFVNaaYTDSYYKgqTALHIAIERRNMHLVELLVQNGADVHArasgeffkkkkgGPGFYFGELPLSLAACTNqlDIVKF 159
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  120 LLKHS---ADVNARDKNWQTPLHiaaankavkcaeALVPLLSNvnvsdragrtALHHAAFSghVEMVSLLLSRGANINAF 196
Cdd:cd22196    160 LLENPhspADISARDSMGNTVLH------------ALVEVADN----------TPENTKFV--TKMYNEILILGAKIRPL 215
                          170       180       190       200       210       220       230       240
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  197 DKkdrraihwaaymghIEVVkllvthgaevmcKDKKSYTPLHAAASSGMISVIKYLLDLGVDMNESN---------AYGn 267
Cdd:cd22196    216 LK--------------LEEI------------TNKKGLTPLKLAAKTGKIGIFAYILGREIKEPECRhlsrkftewAYG- 268

                   ....*....
gi 1785376409  268 tPLHVACYN 276
Cdd:cd22196    269 -PVHSSLYD 276
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
38-106 4.33e-03

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: 41.15  E-value: 4.33e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   38 PLVQAIFNGDPDEVRALIFKKEDVN--------FQDNEKRT------PLHAAAYLGDAEIIELLILSGARVNAKDSKWLT 103
Cdd:cd22192     92 ALHIAVVNQNLNLVRELIARGADVVspratgtfFRPGPKNLiyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNT 171

                   ...
gi 1785376409  104 PLH 106
Cdd:cd22192    172 VLH 174
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
82-276 4.35e-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: 41.28  E-value: 4.35e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   82 EIIELLI-----------LSGARVNAKDSKWLTPLHRAVASCSEDAVQVLLKHSADVNARDKN------WQ--------T 136
Cdd:cd22194    111 EIVRILLafaeengildrFINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkYKhegfyfgeT 190
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  137 PLHIAAANKAVKCAEALVPLLS-NVNVSDRAGRTALH-----------HAAFSGHVEMVSLLLSRGANINAF-DKKDRRA 203
Cdd:cd22194    191 PLALAACTNQPEIVQLLMEKEStDITSQDSRGNTVLHalvtvaedsktQNDFVKRMYDMILLKSENKNLETIrNNEGLTP 270
                          170       180       190       200       210       220       230
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785376409  204 IHWAAYMGHIEVVKLLVthGAEVMCKDKKSYTPLHAAASSGMISviKYLLDL-GVDMNESNAYgntpLHVACYN 276
Cdd:cd22194    271 LQLAAKMGKAEILKYIL--SREIKEKPNRSLSRKFTDWAYGPVS--SSLYDLtNVDTTTDNSV----LEIIVYN 336
PHA02736 PHA02736
Viral ankyrin protein; Provisional
164-274 4.42e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.09  E-value: 4.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  164 DRAGRTALHHAAFSGHVemVSLLLSRGANINA-------FDKKDRRAIHWAAYMGHI---EVVKLLVTHGAEVMCKDKK- 232
Cdd:PHA02736    14 DIEGENILHYLCRNGGV--TDLLAFKNAISDEnrylvleYNRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKERVf 91
                           90       100       110       120
                   ....*....|....*....|....*....|....*....|...
gi 1785376409  233 SYTPLHAAASSGMISVIKYLLDL-GVDMNESNAYGNTPLHVAC 274
Cdd:PHA02736    92 GNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVAC 134
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
712-741 5.37e-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: 35.64  E-value: 5.37e-03
                            10        20        30
                    ....*....|....*....|....*....|
gi 1785376409   712 NGQTPLMLSVLNGHTECVYSLLNKGANVDA 741
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
266-374 5.86e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.83  E-value: 5.86e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  266 GNTPLHVACYNGQDVVvNELI-------DCGANVNQVNE-------RGFTPLHFAAaSTHGALCLELLVCNGADVNIKSK 331
Cdd:TIGR00870   82 GDTLLHAISLEYVDAV-EAILlhllaafRKSGPLELANDqytseftPGITALHLAA-HRQNYEIVKLLLERGASVPARAC 159
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*..
gi 1785376409  332 DG---KTPLHMTAIHGR--------FSRSQII---IQNGAEIDCEDKNGNTPLHIAA 374
Cdd:TIGR00870  160 GDffvKSQGVDSFYHGEsplnaaacLGSPSIVallSEDPADILTADSLGNTLLHLLV 216
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
264-372 5.99e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 40.63  E-value: 5.99e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  264 AYGNTPLHVACYNGQDVVvNELI--------DCGANVNQVNE-------RGFTPLHFAAAStHGALCLELLVCNGADVNI 328
Cdd:cd21882     24 ATGKTCLHKAALNLNDGV-NEAImllleaapDSGNPKELVNApctdefyQGQTALHIAIEN-RNLNLVRLLVENGADVSA 101
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  329 KSKD-------------GKTPLHMTAIHGRFSRSQIIIQNGAEI---DCEDKNGNTPLHI 372
Cdd:cd21882    102 RATGrffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNTVLHA 161
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
815-840 6.18e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 6.18e-03
                           10        20
                   ....*....|....*....|....*.
gi 1785376409  815 HGYTPLHWACYNGHDACVELLLEQEV 840
Cdd:pfam13606    1 DGNTPLHLAARNGRLEIVKLLLENGA 26
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
203-226 6.87e-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: 6.87e-03
                            10        20
                    ....*....|....*....|....
gi 1785376409   203 AIHWAAYMGHIEVVKLLVTHGAEV 226
Cdd:smart00248    5 PLHLAAENGNLEVVKLLLDKGADI 28
PHA02798 PHA02798
ankyrin-like protein; Provisional
876-980 6.96e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.20  E-value: 6.96e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  876 VNSVDSKGRTPL-----HAAAFTDHIECLQLLLSHNAQVNAVDSTGKTPLMMAAENGQTSAVEVLVSSAK--ADLTLQDK 948
Cdd:PHA02798    64 VNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLFMIEngADTTLLDK 143
                           90       100       110
                   ....*....|....*....|....*....|....*
gi 1785376409  949 NKNTALHLACSKGHETSALLI---LEQITDRNLIN 980
Cdd:PHA02798   144 DGFTMLQVYLQSNHHIDIEIIkllLEKGVDINTHN 178
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
876-1012 7.37e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.45  E-value: 7.37e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  876 VNSVDSKGRTPL-HAAAFTDHIECLQLLLSHNAQVnavdSTGKTPLMMAAENGQtSAVEVLvssakadltlqdknkntAL 954
Cdd:TIGR00870   45 INCPDRLGRSALfVAAIENENLELTELLLNLSCRG----AVGDTLLHAISLEYV-DAVEAI-----------------LL 102
                           90       100       110       120       130
                   ....*....|....*....|....*....|....*....|....*....|....*...
gi 1785376409  955 HLACSKGHETSALLILEQITDrnlinaTNSALQTPLHVAARNGLTVVVQELLGKGASV 1012
Cdd:TIGR00870  103 HLLAAFRKSGPLELANDQYTS------EFTPGITALHLAAHRQNYEIVKLLLERGASV 154
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
465-493 7.44e-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: 7.44e-03
                            10        20
                    ....*....|....*....|....*....
gi 1785376409   465 GRTPLHYAAANCNYQCLFALVGSGASVND 493
Cdd:smart00248    2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
203-231 7.56e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 7.56e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 1785376409  203 AIHWAAYM-GHIEVVKLLVTHGAEVMCKDK 231
Cdd:pfam00023    5 PLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
691-804 7.69e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.16  E-value: 7.69e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  691 ECLRLLIGN-ADVQAAV-----DIHDGN-----GQTPLMLSVLNGHTECVYSLL---NKGANVDAKDKWGRTALHrGAVT 756
Cdd:cd22193     90 DIVALLVENgADVHAHAkgrffQPKYQGegfyfGELPLSLAACTNQPDIVQYLLeneHQPADIEAQDSRGNTVLH-ALVT 168
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1785376409  757 GHEECVE--ALLQHNANFLLRDC---------------RGRTPIHLAAACGHIGVLSALLQTAIS 804
Cdd:cd22193    169 VADNTKEntKFVTRMYDMILIRGaklcptveleeirnnDGLTPLQLAAKMGKIEILKYILQREIK 233
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
38-207 8.01e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 40.25  E-value: 8.01e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409   38 PLVQAifngDPDEVRALIFKKEDVNFQDNEKRTPLHAAAYLGDAEIIELLILSGARVNAKDSKWL-------------TP 104
Cdd:cd21882     47 LLLEA----APDSGNPKELVNAPCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARATGRFfrkspgnlfyfgeLP 122
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  105 LHRAVASCSEDAVQVLLKHSAD---VNARDKNWQTPLH--IAAANKAVKCA--------------EALVPLLSNVNVSDR 165
Cdd:cd21882    123 LSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHalVLQADNTPENSafvcqmynlllsygAHLDPTQQLEEIPNH 202
                          170       180       190       200
                   ....*....|....*....|....*....|....*....|..
gi 1785376409  166 AGRTALHHAAFSGHVEMVSLLLSRGANiNAFDKKDRRAIHWA 207
Cdd:cd21882    203 QGLTPLKLAAVEGKIVMFQHILQREFS-GPYQPLSRKFTEWT 243
PHA02791 PHA02791
ankyrin-like protein; Provisional
124-302 8.20e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 39.64  E-value: 8.20e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  124 SADVNARDKNWQTPLHIAAANKAVKC------AEALVPLLSNvnvsdragRTALHHAAFSGHVEMVSLLLSRGANINAFD 197
Cdd:PHA02791    20 SKDAFKADVHGHSALYYAIADNNVRLvctllnAGALKNLLEN--------EFPLHQAATLEDTKIVKILLFSGMDDSQFD 91
                           90       100       110       120       130       140       150       160
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  198 KKDRRAIHWAAYMGHIEVVKLLVTHGAEVMCKDKKSY-TPLHAAASSGMISVIKYLL-------DLGVDMnesnaygnTP 269
Cdd:PHA02791    92 DKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGWkTSFYHAVMLNDVSIVSYFLseipstfDLAILL--------SC 163
                          170       180       190
                   ....*....|....*....|....*....|...
gi 1785376409  270 LHVACYNGQDVVVNELIDCGANVNQVNERGFTP 302
Cdd:PHA02791   164 IHITIKNGHVDMMILLLDYMTSTNTNNSLLFIP 196
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
199-309 8.42e-03

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 40.17  E-value: 8.42e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  199 KDRRAIHWAAYMGHIEVVKLLVTHGAEVMC-------KDKKSYT-------PLHAAASSGMISVIKYLLD---LGVDMNE 261
Cdd:cd22196     93 KGQTALHIAIERRNMHLVELLVQNGADVHArasgeffKKKKGGPgfyfgelPLSLAACTNQLDIVKFLLEnphSPADISA 172
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1785376409  262 SNAYGNTPLHVACYNGQDVVVN---------ELIDCGANVNQV-------NERGFTPLHFAAAS 309
Cdd:cd22196    173 RDSMGNTVLHALVEVADNTPENtkfvtkmynEILILGAKIRPLlkleeitNKKGLTPLKLAAKT 236
Ank_4 pfam13637
Ankyrin repeats (many copies);
951-1006 8.42e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 8.42e-03
                           10        20        30        40        50
                   ....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409  951 NTALHLACSKGHETSALLILEQITDrnlINATNSALQTPLHVAARNGLTVVVQELL 1006
Cdd:pfam13637    2 LTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
365-391 8.88e-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: 34.87  E-value: 8.88e-03
                            10        20
                    ....*....|....*....|....*..
gi 1785376409   365 NGNTPLHIAARYGHELLINTLITSRAD 391
Cdd:smart00248    1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
357-477 9.02e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 39.86  E-value: 9.02e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  357 AEIDCEDKNGNTPLHIAARYGHELLINTLITSRADTSKR------------GIH-GMFPLHLAALSGFSDCCRKLLSSGF 423
Cdd:cd21882     64 APCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARatgrffrkspgnLFYfGELPLSLAACTNQEEIVRLLLENGA 143
                           90       100       110       120       130       140       150
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1785376409  424 DI---DTHDDFGRTCLHA-------AAAGGNLEC--LNLLLSTGADFNKKDKF-------GRTPLHYAAANCN 477
Cdd:cd21882    144 QPaalEAQDSLGNTVLHAlvlqadnTPENSAFVCqmYNLLLSYGAHLDPTQQLeeipnhqGLTPLKLAAVEGK 216
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
298-410 9.60e-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: 9.60e-03
                           10        20        30        40        50        60        70        80
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1785376409  298 RGFTPLHFAAASTHGAlCLELLVCNGADVNIKSKD--------------GKTPLHMTAIHGRFSRSQIIIQNG---AEID 360
Cdd:cd22193     75 EGQTALHIAIERRQGD-IVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEhqpADIE 153
                           90       100       110       120       130       140
                   ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1785376409  361 CEDKNGNTPLHIAARYGHELLINT-LITSRAD-----------TSK----RGIHGMFPLHLAALSG 410
Cdd:cd22193    154 AQDSRGNTVLHALVTVADNTKENTkFVTRMYDmilirgaklcpTVEleeiRNNDGLTPLQLAAKMG 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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