NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|24581258|ref|NP_608724|]
View 

uncharacterized protein Dmel_CG3104, isoform A [Drosophila melanogaster]

Protein Classification

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

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

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

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
13-277 5.42e-52

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.22  E-value: 5.42e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  13 LHMAAMRGDEVALLRVLDSGKVHVDCKDEDGTTPLILAAAGGHTYCVMELLDQGADPNSRRLTGTTPLFFAAQGGHLDVV 92
Cdd:COG0666  24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  93 KILIKAGASVDTPSADGGTPLFVACQGGHVKIVRELLDCGANVNAHMKDRATPVFISAQNGHRTVLSLLIQAGAEIDIKR 172
Cdd:COG0666 104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258 173 IDGATPLWIAAQMGQDHICKVLLQNGANVDTVRCDGATPLFKAAHKGHAAVITVLLKYRPNL-GQLPNGESALHAAAMFG 251
Cdd:COG0666 184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLnAKDKDGLTALLLAAAAG 263

                       250       260
                ....*....|....*....|....*.
gi 24581258 252 HMTVCKQLVAAGSDVLLKNHDGLTAL 277
Cdd:COG0666 264 AALIVKLLLLALLLLAAALLDLLTLL 289
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
13-277 5.42e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.22  E-value: 5.42e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  13 LHMAAMRGDEVALLRVLDSGKVHVDCKDEDGTTPLILAAAGGHTYCVMELLDQGADPNSRRLTGTTPLFFAAQGGHLDVV 92
Cdd:COG0666  24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  93 KILIKAGASVDTPSADGGTPLFVACQGGHVKIVRELLDCGANVNAHMKDRATPVFISAQNGHRTVLSLLIQAGAEIDIKR 172
Cdd:COG0666 104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258 173 IDGATPLWIAAQMGQDHICKVLLQNGANVDTVRCDGATPLFKAAHKGHAAVITVLLKYRPNL-GQLPNGESALHAAAMFG 251
Cdd:COG0666 184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLnAKDKDGLTALLLAAAAG 263

                       250       260
                ....*....|....*....|....*.
gi 24581258 252 HMTVCKQLVAAGSDVLLKNHDGLTAL 277
Cdd:COG0666 264 AALIVKLLLLALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 62-233 1.17e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.43  E-value: 1.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   62 LLDQGADPNSRRLTGTTPLFFAAQGGH-----LDVVKILIKAGASVDTPSADGGTPLFVACQG--GHVKIVRELLDCGAN 134
Cdd:PHA03100  54 LLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGAN 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  135 VNAHMKDRATPVFISAQNGHRT--VLSLLIQAGAEIDIK-RID---------------GATPLWIAAQMGQDHICKVLLQ 196
Cdd:PHA03100 134 VNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKnRVNyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLD 213

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 24581258  197 NGANVDTVRCDGATPLFKAAHKGHAAVITVLLKYRPN 233
Cdd:PHA03100 214 LGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
47-137 4.53e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 4.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258    47 LILAAAGGHTYCVMELLDQGADPNSRRLTGTTPLFFAAQGGHLDVVKILIKAGASVDTPsaDGGTPLFVACQGGHVKIVR 126
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 24581258   127 ELLDCGANVNA 137
Cdd:pfam12796  79 LLLEKGADINV 89
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 45-231 1.83e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 58.49  E-value: 1.83e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  45 TPLILAAAGGHTYCVMELLDQ-GADPNSRRLTGTTPLFFAAQGGHLDVVKILIKAGAS-VDTP-SAD---GGTPLFVACQ 118
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPmTSDlyqGETALHIAVV 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258 119 GGHVKIVRELLDCGANVNahmKDRATPVFIS-----------------AQNGHRTVLSLLIQAGAeiDIKRID--GATPL 179
Cdd:cd22192  99 NQNLNLVRELIARGADVV---SPRATGTFFRpgpknliyygehplsfaACVGNEEIVRLLIEHGA--DIRAQDslGNTVL 173

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581258 180 WI-AAQMGQDHICKVL--------LQNGANVDTVRC-DGATPLFKAAHKGHAAVITVLLKYR 231
Cdd:cd22192 174 HIlVLQPNKTFACQMYdlilsydkEDDLQPLDLVPNnQGLTPFKLAAKEGNIVMFQHLVQKR 235
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 108-137 1.13e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 1.13e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 24581258    108 DGGTPLFVACQGGHVKIVRELLDCGANVNA 137
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 6-295 1.96e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.06  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258     6 ETPSDVQLHMAAMRGDEVALLRVLD-SGKVHVDCKDEDGTTPLILAAAGGHTYCVMELLdqgadPNSRRL--TGTTPLFF 82
Cdd:TIGR00870  14 LSDEEKAFLPAAERGDLASVYRDLEePKKLNINCPDRLGRSALFVAAIENENLELTELL-----LNLSCRgaVGDTLLHA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258    83 AAQGGHlDVVKILI-----KAGASVDTPSAD---------GGTPLFVACQGGHVKIVRELLDCGANVNAhmkdRATPV-F 147
Cdd:TIGR00870  89 ISLEYV-DAVEAILlhllaAFRKSGPLELANdqytseftpGITALHLAAHRQNYEIVKLLLERGASVPA----RACGDfF 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   148 ISAQngHRTVLSLliqagaeidikridGATPLWIAAQMGQDHICKVLLQNGANVDTVRCDGATPLfkaahkgHAAVITvl 227
Cdd:TIGR00870 164 VKSQ--GVDSFYH--------------GESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLL-------HLLVME-- 218

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581258   228 lkyrpNLGQLPNGESALH----AAAMFGHMTVCKQLvaagSDVLlkNHDGLTALQLAHQQKYTSICDYLQER 295
Cdd:TIGR00870 219 -----NEFKAEYEELSCQmynfALSLLDKLRDSKEL----EVIL--NHQGLTPLKLAAKEGRIVLFRLKLAI 279
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
13-277 5.42e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.22  E-value: 5.42e-52
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  13 LHMAAMRGDEVALLRVLDSGKVHVDCKDEDGTTPLILAAAGGHTYCVMELLDQGADPNSRRLTGTTPLFFAAQGGHLDVV 92
Cdd:COG0666  24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  93 KILIKAGASVDTPSADGGTPLFVACQGGHVKIVRELLDCGANVNAHMKDRATPVFISAQNGHRTVLSLLIQAGAEIDIKR 172
Cdd:COG0666 104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258 173 IDGATPLWIAAQMGQDHICKVLLQNGANVDTVRCDGATPLFKAAHKGHAAVITVLLKYRPNL-GQLPNGESALHAAAMFG 251
Cdd:COG0666 184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLnAKDKDGLTALLLAAAAG 263

                       250       260
                ....*....|....*....|....*.
gi 24581258 252 HMTVCKQLVAAGSDVLLKNHDGLTAL 277
Cdd:COG0666 264 AALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
23-295 2.37e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.58  E-value: 2.37e-46
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  23 VALLRVLDSGKVHVDCKDEDGTTPLILAAAGGHTYCVMELLDQGADPNSRRLTGTTPLFFAAQGGHLDVVKILIKAGASV 102
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258 103 DTPSADGGTPLFVACQGGHVKIVRELLDCGANVNAHMKDRATPVFISAQNGHRTVLSLLIQAGAEIDIKRIDGATPLWIA 182
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258 183 AQMGQDHICKVLLQNGANVDTVRCDGATPLFKAAHKGHAAVITVLLKYRPNLG-QLPNGESALHAAAMFGHMTVCKQLVA 261
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNaKDNDGKTALDLAAENGNLEIVKLLLE 240

                       250       260       270
                ....*....|....*....|....*....|....
gi 24581258 262 AGSDVLLKNHDGLTALQLAHQQKYTSICDYLQER 295
Cdd:COG0666 241 AGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 62-233 1.17e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.43  E-value: 1.17e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   62 LLDQGADPNSRRLTGTTPLFFAAQGGH-----LDVVKILIKAGASVDTPSADGGTPLFVACQG--GHVKIVRELLDCGAN 134
Cdd:PHA03100  54 LLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGAN 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  135 VNAHMKDRATPVFISAQNGHRT--VLSLLIQAGAEIDIK-RID---------------GATPLWIAAQMGQDHICKVLLQ 196
Cdd:PHA03100 134 VNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAKnRVNyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLD 213

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 24581258  197 NGANVDTVRCDGATPLFKAAHKGHAAVITVLLKYRPN 233
Cdd:PHA03100 214 LGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA03095 PHA03095
ankyrin-like protein; Provisional
 21-280 2.14e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 97.02  E-value: 2.14e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   21 DEVALLRVLDSGkvhVDCKDEDGTTPLilaAAGGHTYC------VMELLDQGADPNSRRLTGTTPLFFAAQGGH-LDVVK 93
Cdd:PHA03095  28 EEVRRLLAAGAD---VNFRGEYGKTPL---HLYLHYSSekvkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIK 101

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   94 ILIKAGASVDTPSADGGTPLFVACQGG--HVKIVRELLDCGANVNAHMKDRATP--VFISAQNGHRTVLSLLIQAGAEID 169
Cdd:PHA03095 102 LLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPlaVLLKSRNANVELLRLLIDAGADVY 181

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  170 IKRIDGATPLWIAAQMGQDHICKV--LLQNGANVDTVRCDGATPLFKAAHKGHAAVITVL--------LKYRPNLGQLPn 239
Cdd:PHA03095 182 AVDDRFRSLLHHHLQSFKPRARIVreLIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLplliagisINARNRYGQTP- 260

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|.
gi 24581258  240 gesaLHAAAMFGHMTVCKQLVAAGSDVLLKNHDGLTALQLA 280
Cdd:PHA03095 261 ----LHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
Ank_2 pfam12796
Ankyrin repeats (3 copies);
47-137 4.53e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 4.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258    47 LILAAAGGHTYCVMELLDQGADPNSRRLTGTTPLFFAAQGGHLDVVKILIKAGASVDTPsaDGGTPLFVACQGGHVKIVR 126
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKD--NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 24581258   127 ELLDCGANVNA 137
Cdd:pfam12796  79 LLLEKGADINV 89
PHA03095 PHA03095
ankyrin-like protein; Provisional
 4-261 1.23e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 92.01  E-value: 1.23e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258    4 KKETPSDVQLHMAAMRGDEVALLRVLDSGKVHVDCKDEDGTTPLilaaaggHTYC--------VME-LLDQGADPNSRRL 74
Cdd:PHA03095  78 APERCGFTPLHLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPL-------HVYLsgfninpkVIRlLLRKGADVNALDL 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   75 TGTTPL--FFAAQGGHLDVVKILIKAGASVDTPSADGGTPLFVACQGGHV--KIVRELLDCGANVNAHMKDRATPVFISA 150
Cdd:PHA03095 151 YGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMA 230

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  151 QNG--HRTVLSLLIQAGAEIDIKRIDGATPLWIAAQMGQDHICKVLLQNGANVDTVRCDGATPLFKAAHKGHAAVITVLL 228
Cdd:PHA03095 231 TGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 24581258  229 KYRPNLGQLPNgesALHAAAMFGHMTVC---KQLVA 261
Cdd:PHA03095 311 AKNPSAETVAA---TLNTASVAGGDIPSdatRLCVA 343
Ank_2 pfam12796
Ankyrin repeats (3 copies);
80-171 3.01e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 3.01e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258    80 LFFAAQGGHLDVVKILIKAGASVDTPSADGGTPLFVACQGGHVKIVRELLDCgANVNAHMKDRaTPVFISAQNGHRTVLS 159
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 24581258   160 LLIQAGAEIDIK 171
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 12-170 7.79e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 86.20  E-value: 7.79e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   12 QLHMAAMRGDEVALLRVLDSGKVHVDCKDEDGTTPLILAAAGGHTYCVMELLDQGADPNSRRLTGTTPLFFAAQGGHLDV 91
Cdd:PHA02875  71 ELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKG 150

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   92 VKILIKAGASVDTPSADGGTPLFVACQGGHVKIVRELLDCGANVNAHMKDRATPVFISA-QNGHRTVLSLLIQAGAEIDI 170
Cdd:PHA02875 151 IELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAiENNKIDIVRLFIKRGADCNI 230
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 18-280 2.42e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 85.50  E-value: 2.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   18 MRGDEVALLRVLDSGKVHVDCKDEDGTTPLILAAAGGHTYCVMELLDQGADPNSRRLTGTTPLFFAAQGGHLDVVKILI- 96
Cdd:PHA02876 153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIId 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   97 ----------------------------KAGASVDTPSADGGTPLFVACQGGHV-KIVRELLDCGANVNAHMKDRATPVF 147
Cdd:PHA02876 233 nrsninkndlsllkairnedletslllyDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLY 312

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  148 ISAQNGHRTV-LSLLIQAGAEIDIKRIDGATPLWIAAQMGQDH-ICKVLLQNGANVDTVRCDGATPLFKAAHKGHAAVIT 225
Cdd:PHA02876 313 LMAKNGYDTEnIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIIN 392

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 24581258  226 VLLKYRPNLGQLPNG-ESALHaAAMFG---HMTVcKQLVAAGSDVLLKNHDGLTALQLA 280
Cdd:PHA02876 393 TLLDYGADIEALSQKiGTALH-FALCGtnpYMSV-KTLIDRGANVNSKNKDLSTPLHYA 449
Ank_2 pfam12796
Ankyrin repeats (3 copies);
179-270 6.74e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.08  E-value: 6.74e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   179 LWIAAQMGQDHICKVLLQNGANVDTVRCDGATPLFKAAHKGHAAVITVLLKYrPNLGQLPNGESALHAAAMFGHMTVCKQ 258
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 24581258   259 LVAAGSDVLLKN 270
Cdd:pfam12796  80 LLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 14-207 2.74e-17

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 82.61  E-value: 2.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   14 HMAAMRGDEVALLRVlDSGKVHVDCKDEdgtTPLILAAAGGHTYCVMELLDQGADPNSRRLTGTTPLFFAAQGGHLDVVK 93
Cdd:PLN03192 500 HHKELHDLNVGDLLG-DNGGEHDDPNMA---SNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVL 575

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   94 ILIKAGASVDTPSADGGTPLFVACQGGHVKIVRELLDCGANVNAHMKdrATPVFISAQNGHRTVLSLLIQAGAEIDIKRI 173
Cdd:PLN03192 576 VLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAA--GDLLCTAAKRNDLTAMKELLKQGLNVDSEDH 653

                        170       180       190
                 ....*....|....*....|....*....|....
gi 24581258  174 DGATPLWIAAQMGQDHICKVLLQNGANVDTVRCD 207
Cdd:PLN03192 654 QGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
Ank_2 pfam12796
Ankyrin repeats (3 copies);
13-104 2.90e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 2.90e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258    13 LHMAAMRGDeVALLRVLDSGKVHVDCKDEDGTTPLILAAAGGHTYCVMELLDQgADPNSrRLTGTTPLFFAAQGGHLDVV 92
Cdd:pfam12796   1 LHLAAKNGN-LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNL-KDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|..
gi 24581258    93 KILIKAGASVDT 104
Cdd:pfam12796  78 KLLLEKGADINV 89
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 11-229 5.04e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 81.19  E-value: 5.04e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   11 VQLHMAAMRGDEVALLRVLDSGkVHVDCKDEDGTTPLILAAAGGHTYCVMELLDQGADPNSRRLTGTTPLFFAAQGGHLD 90
Cdd:PHA02875   4 VALCDAILFGELDIARRLLDIG-INPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   91 VVKILIKAGASV-DTPSADGGTPLFVACQGGHVKIVRELLDCGANVNAHMKDRATPVFISAQNGHRTVLSLLIQAGAEID 169
Cdd:PHA02875  83 AVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24581258  170 IKRIDGATPLWIAAQMGQDHICKVLLQNGANVDTVRCDG-ATPLFKAAHKGHAAVITVLLK 229
Cdd:PHA02875 163 IEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIK 223
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 11-300 1.46e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.62  E-value: 1.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   11 VQLHMAAMRGDEVALLRVLDSGKVHVDCKDEDGTTPLILAAAGGHTYCVMELLDQGADPNSRRLTGTTPLFFAAQGGHLD 90
Cdd:PHA02874   3 QDLRMCIYSGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHD 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   91 VVKILI-----------------------KAGASVDTPSADGGTPLFVACQGGHVKIVRELLDCGANVNAHMKDRATPVF 147
Cdd:PHA02874  83 IIKLLIdngvdtsilpipciekdmiktilDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIH 162

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  148 ISAQNGHRTVLSLLIQAGAEIDIKRIDGATPLWIAAQMGQDHICKVLLQNGANVdTVRCD-GATPLFKAAHKGHaAVITV 226
Cdd:PHA02874 163 IAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHI-MNKCKnGFTPLHNAIIHNR-SAIEL 240

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581258  227 LLKYRPNLGQLPNGESALHAAAMFG-HMTVCKQLVAAGSDVLLKNHDGLTALQLAHqqKYTSICDYLQERIRTMV 300
Cdd:PHA02874 241 LINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAF--KYINKDPVIKDIIANAV 313
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 2-205 3.46e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 79.34  E-value: 3.46e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258    2 SLKKETPsdvqLHMAAMRGDEVALLRVLDSGKVHVDCKDEDGTTPLILAAA-GGHTYCVMELLDQGADPNSRRLTGTTPL 80
Cdd:PHA02876 304 NIKGETP----LYLMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPI 379

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   81 FFAAQGGHLDVVKILIKAGASVDTPSADGGTPL-FVACQGGHVKIVRELLDCGANVNAHMKDRATPVFISAQNGHR-TVL 158
Cdd:PHA02876 380 HYAAVRNNVVIINTLLDYGADIEALSQKIGTALhFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVI 459

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 24581258  159 SLLIQAGAEIDIKRIDGATPLWIAaqMGQDHICKVLLQNGANVDTVR 205
Cdd:PHA02876 460 EMLLDNGADVNAINIQNQYPLLIA--LEYHGIVNILLHYGAELRDSR 504
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 59-274 1.08e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 77.31  E-value: 1.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   59 VMELLDQGADPNSRRLTGTTPLFFAAQGGHLDVVKILIKAGASVDTPSADGGTPLFVACQGGHVKIVRELLDCGANVNAH 138
Cdd:PHA02874 107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  139 MKDRATPVFISAQNGHRTVLSLLIQAGAEIDIKRIDGATPLWIAAQMGQDHIckVLLQNGANVDTVRCDGATPLFKA-AH 217
Cdd:PHA02874 187 DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAiNP 264

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 24581258  218 KGHAAVITVLLKYRPNLG-QLPNGESALHAAAMF-GHMTVCKQLVAagSDVLLKNHDGL 274
Cdd:PHA02874 265 PCDIDIIDILLYHKADISiKDNKGENPIDTAFKYiNKDPVIKDIIA--NAVLIKEADKL 321
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 21-172 4.11e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.47  E-value: 4.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   21 DEVALLRVLDSGKVHVDCKDEDGTTPLILAAAG--GHTYCVMELLDQGADPNSRRLTGTTPLFFAAQGGHLDV------- 91
Cdd:PHA03100  84 DVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLkilklli 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   92 -----------VKILIKAGASVDTPSADGGTPLFVACQGGHVKIVRELLDCGANVNAHMKDRATPVFISAQNGHRTVLSL 160
Cdd:PHA03100 164 dkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKL 243

                        170
                 ....*....|..
gi 24581258  161 LIQAGAEIDIKR 172
Cdd:PHA03100 244 LLNNGPSIKTII 255
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 9-228 6.70e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 75.10  E-value: 6.70e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258    9 SDVQLHMAAMRGDEVALLRVLDSGkVHVDCKDEDGTTPLILAA-AGGHTYCVMELLDQGADPNSRRLTGTTPLFFAAQGG 87
Cdd:PHA02876 240 NDLSLLKAIRNEDLETSLLLYDAG-FSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNG 318

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   88 H-LDVVKILIKAGASVDTPSADGGTPLFVACQGGHVK-IVRELLDCGANVNAHMKDRATPVFISAQNGHRTVLSLLIQAG 165
Cdd:PHA02876 319 YdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYG 398

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24581258  166 AEIDIKRIDGATPLWIAAQMGQDHI-CKVLLQNGANVDTVRCDGATPLFKAAHKG-HAAVITVLL 228
Cdd:PHA02876 399 ADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLL 463
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 5-234 1.19e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 74.71  E-value: 1.19e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258    5 KETPsdvqLHMAAMRGDEVALLRVLDSGKVHVDCKDEDGTTPLILAAAGGH-TYCVMELLDQGADPNSRRLTGTTPLFFA 83
Cdd:PHA02876 273 KNTP----LHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQA 348

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   84 AQ-GGHLDVVKILIKAGASVDTPSADGGTPLFVACQGGHVKIVRELLDCGANVNAHMKDRATPV-FISAQNGHRTVLSLL 161
Cdd:PHA02876 349 STlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALhFALCGTNPYMSVKTL 428

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24581258  162 IQAGAEIDIKRIDGATPLWIAAQMG-QDHICKVLLQNGANVDTVRCDGATPLFKAAhkGHAAVITVLLKYRPNL 234
Cdd:PHA02876 429 IDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 22-197 1.34e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 74.15  E-value: 1.34e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   22 EVALLRVLDSGKVHVDCKDED-GTTPLILAAAGGHTYCVMELLDQGADPNSRRLTGTTPLFFAAQGGHLDVVKILIKAGA 100
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  101 SVDTPSADGGTPLFVACqgGHVK---IVRELLDCGANVNAHMKDRA-TPVFISAQNghRTVLSLLIQAGAEIDIKRIDGA 176
Cdd:PHA02878 226 STDARDKCGNTPLHISV--GYCKdydILKLLLEHGVDVNAKSYILGlTALHSSIKS--ERKLKLLLEYGADINSLNSYKL 301

                        170       180
                 ....*....|....*....|..
gi 24581258  177 TPLWIAAQMGQD-HICKVLLQN 197
Cdd:PHA02878 302 TPLSSAVKQYLCiNIGRILISN 323
Ank_2 pfam12796
Ankyrin repeats (3 copies);
147-234 1.35e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.22  E-value: 1.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   147 FISAQNGHRTVLSLLIQAGAEIDIKRIDGATPLWIAAQMGQDHICKVLLQNgANVDtVRCDGATPLFKAAHKGHAAVITV 226
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVKL 79


                  ....*...
gi 24581258   227 LLKYRPNL 234
Cdd:pfam12796  80 LLEKGADI 87
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 57-280 2.71e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.78  E-value: 2.71e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   57 YCVMEllDQGADPNSRRLTgtTPLFFAAQGGHLDVVKILIKAGASVDTPSADGGTPLFVACQGGHV-----KIVRELLDC 131
Cdd:PHA03100  20 YIIME--DDLNDYSYKKPV--LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEY 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  132 GANVNAHMKDRATPVFISAQN--GHRTVLSLLIQAGAEIDIKRIDGATPLWIAAQMGQD--HICKVLLQNGANVDTvrCD 207
Cdd:PHA03100  96 GANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINA--KN 173

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24581258  208 gatplfkaahkghaaVITVLLKYR-----PNLgqlpNGESALHAAAMFGHMTVCKQLVAAGSDVLLKNHDGLTALQLA 280
Cdd:PHA03100 174 ---------------RVNYLLSYGvpiniKDV----YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 132-292 4.94e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 72.59  E-value: 4.94e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  132 GANVNAHMkdrATPVFISAQNGHRTVLSLLIQAGAEIDIKRIDGATPLWIAAQMGQDHICKVLLQNGANVDTVRCDGATP 211
Cdd:PLN03192 518 GEHDDPNM---ASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTA 594

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  212 LFKAAHKGHAAVITVLLKYrPNLGQLPNGESALHAAAMFGHMTVCKQLVAAGSDVLLKNHDGLTALQLAHQQKYTSICDY 291
Cdd:PLN03192 595 LWNAISAKHHKIFRILYHF-ASISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRL 673


                 .
gi 24581258  292 L 292
Cdd:PLN03192 674 L 674
PHA03095 PHA03095
ankyrin-like protein; Provisional
 89-292 5.45e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.36  E-value: 5.45e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   89 LDVVKILIKAGASVDTPSADGGTPL--FVACQGGHVK-IVRELLDCGANVNAHMKDRATPVFISAQNGHR-TVLSLLIQA 164
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLhlYLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  165 GAEIDIKRIDGATPLwiaaqmgqdHIC-----------KVLLQNGANVDTVRCDGATPL--FKAAHKGHAAVITVLLK-- 229
Cdd:PHA03095 107 GADVNAKDKVGRTPL---------HVYlsgfninpkviRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDag 177

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  230 --------------------YRPN---------LGQLPN-----GESALHAAAMFGHmtvCK-----QLVAAGSDVLLKN 270
Cdd:PHA03095 178 advyavddrfrsllhhhlqsFKPRarivrelirAGCDPAatdmlGNTPLHSMATGSS---CKrslvlPLLIAGISINARN 254

                        250       260
                 ....*....|....*....|..
gi 24581258  271 HDGLTALQLAHQQKYTSICDYL 292
Cdd:PHA03095 255 RYGQTPLHYAAVFNNPRACRRL 276
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 62-315 2.12e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.78  E-value: 2.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   62 LLDQGADPNSRRLTGTTPLFFAAQGGHLDVVKILIKAGASVDTPSADGGTPLFVACQGGHVKIVRELLDCGANVNAH--- 138
Cdd:PHA02876 164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNdls 243

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  139 ---------------MKD-----------RATPVFISAQNGHRTVL-SLLIQAGAEIDIKRIDGATPLWIAAQMGQD-HI 190
Cdd:PHA02876 244 llkairnedletsllLYDagfsvnsiddcKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYDtEN 323

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  191 CKVLLQNGANVDTVRCDGATPLFKAA--HKGHAAVITVLlkyrpNLGQLPNG-----ESALHAAAMFGHMTVCKQLVAAG 263
Cdd:PHA02876 324 IRTLIMLGADVNAADRLYITPLHQAStlDRNKDIVITLL-----ELGANVNArdycdKTPIHYAAVRNNVVIINTLLDYG 398

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 24581258  264 SDVLLKNHDGLTALQLA--HQQKYTSicdylqerIRTMVARSAKAMATSGVSST 315
Cdd:PHA02876 399 ADIEALSQKIGTALHFAlcGTNPYMS--------VKTLIDRGANVNSKNKDLST 444
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 62-266 4.35e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.17  E-value: 4.35e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   62 LLDQGADPNSRRLTGTTPLFFAAQGGHLDVVKILIKAGASVDTPSADGGTPLFVACQGGHVKIVRELLDCGANVNahmkd 141
Cdd:PHA02875  21 LLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD----- 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  142 ratpvfisaqnghrtvlslliqagaeiDIKRIDGATPLWIAAQMGQDHICKVLLQNGANVDTVRCDGATPLFKAAHKGHA 221
Cdd:PHA02875  96 ---------------------------DVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 24581258  222 AVITVLLKYRPNLG-QLPNGESALHAAAMFGHMTVCKQLVAAGSDV 266
Cdd:PHA02875 149 KGIELLIDHKACLDiEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 4-131 9.36e-12

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 65.69  E-value: 9.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258    4 KKETPSDVQLHMAAMRGDEVAL----LRVLDSGKVHVDCKDEDGTT-----PLILA---------AAGGHTYCVMELLDQ 65
Cdd:PTZ00322  25 RKRRAKPISFERMAAIQEEIARidthLEALEATENKDATPDHNLTTeevidPVVAHmltvelcqlAASGDAVGARILLTG 104

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24581258   66 GADPNSRRLTGTTPLFFAAQGGHLDVVKILIKAGASVDTPSADGGTPLFVACQGGHVKIVRELLDC 131
Cdd:PTZ00322 105 GADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 123-303 3.96e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.66  E-value: 3.96e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  123 KIVRELLDCGANVNahMKDR---ATPVFISAQNGHRTVLSLLIQAGAEIDIKRIDGATPLWIAAQMGQDHICKVLLQNGA 199
Cdd:PHA02878 148 EITKLLLSYGADIN--MKDRhkgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  200 NVDTVRCDGATPL-FKAAHKGHAAVITVLLKYRP--NLGQLPNGESALHAAamFGHMTVCKQLVAAGSDVLLKNHDGLTA 276
Cdd:PHA02878 226 STDARDKCGNTPLhISVGYCKDYDILKLLLEHGVdvNAKSYILGLTALHSS--IKSERKLKLLLEYGADINSLNSYKLTP 303

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 24581258  277 LQLAHQQKY---------TSICdyLQERIRTMVARS 303
Cdd:PHA02878 304 LSSAVKQYLcinigriliSNIC--LLKRIKPDIKNS 337
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 92-161 4.41e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.68  E-value: 4.41e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   92 VKILIKAGASVDTPSADGGTPLFVACQGGHVKIVRELLDCGANVNAHMKDRATPVFISAQNGHRTVLSLL 161
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank_4 pfam13637
Ankyrin repeats (many copies);
76-129 4.93e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 4.93e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 24581258    76 GTTPLFFAAQGGHLDVVKILIKAGASVDTPSADGGTPLFVACQGGHVKIVRELL 129
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
43-96 1.70e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 1.70e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 24581258    43 GTTPLILAAAGGHTYCVMELLDQGADPNSRRLTGTTPLFFAAQGGHLDVVKILI 96
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 45-231 1.83e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 58.49  E-value: 1.83e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  45 TPLILAAAGGHTYCVMELLDQ-GADPNSRRLTGTTPLFFAAQGGHLDVVKILIKAGAS-VDTP-SAD---GGTPLFVACQ 118
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCpSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPmTSDlyqGETALHIAVV 98

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258 119 GGHVKIVRELLDCGANVNahmKDRATPVFIS-----------------AQNGHRTVLSLLIQAGAeiDIKRID--GATPL 179
Cdd:cd22192  99 NQNLNLVRELIARGADVV---SPRATGTFFRpgpknliyygehplsfaACVGNEEIVRLLIEHGA--DIRAQDslGNTVL 173

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581258 180 WI-AAQMGQDHICKVL--------LQNGANVDTVRC-DGATPLFKAAHKGHAAVITVLLKYR 231
Cdd:cd22192 174 HIlVLQPNKTFACQMYdlilsydkEDDLQPLDLVPNnQGLTPFKLAAKEGNIVMFQHLVQKR 235
Ank_2 pfam12796
Ankyrin repeats (3 copies);
212-292 2.06e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.97  E-value: 2.06e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   212 LFKAAHKGHAAVITVLLKYRPNLG-QLPNGESALHAAAMFGHMTVCKQLVAAGSdvLLKNHDGLTALQLAHQQKYTSICD 290
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANlQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78


                  ..
gi 24581258   291 YL 292
Cdd:pfam12796  79 LL 80
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 78-299 3.40e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 57.72  E-value: 3.40e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  78 TPLFFAAQGGHLDVVKILIKAgASVD--TPSADGGTPLFVACQGGHVKIVRELLDCGAN-VNAHMKDR----ATPVFISA 150
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKC-PSCDlfQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSDlyqgETALHIAV 97

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258 151 QNGHRTVLSLLIQAGAEIDIKRIDGAT--------------PLWIAAQMGQDHICKVLLQNGANVDTVRCDGATPLfkaa 216
Cdd:cd22192  98 VNQNLNLVRELIARGADVVSPRATGTFfrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL---- 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258 217 HkghaavITVLlkyrpnlgqLPNGESALHAAAMFghMTVCKQLVAAGSDvLLKNHDGLTALQLAHQQKYTSICDYLQERI 296
Cdd:cd22192 174 H------ILVL---------QPNKTFACQMYDLI--LSYDKEDDLQPLD-LVPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235


                ...
gi 24581258 297 RTM 299
Cdd:cd22192 236 RHI 238
PHA02798 PHA02798
ankyrin-like protein; Provisional
 36-233 5.80e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 56.77  E-value: 5.80e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   36 VDCKDEDGTTPLILAAAGGHTY-----CVMELLDQGADPNSRRLTGTTPLFFAAQGGHLDVVKIL---IKAGASVDTPSA 107
Cdd:PHA02798  64 VNGLDNEYSTPLCTILSNIKDYkhmldIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILlfmIENGADTTLLDK 143

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  108 DGGTPLFVACQGGH---VKIVRELLDCGANVNAH------------------------MKDRATPVFI--SAQNGHRT-- 156
Cdd:PHA02798 144 DGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHnnkekydtlhcyfkynidridadiLKLFVDNGFIinKENKSHKKkf 223

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  157 ---VLSLLIQAG-----------AEIDIKRID--GATPLWIAAQMGQDHICKVLLQNGANVDTVRCDGATPLFKAAHKGH 220
Cdd:PHA02798 224 meyLNSLLYDNKrfkknildfifSYIDINQVDelGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENES 303

                        250
                 ....*....|...
gi 24581258  221 AAVITVLLKYRPN 233
Cdd:PHA02798 304 KFIFNSILNKKPN 316
PHA02798 PHA02798
ankyrin-like protein; Provisional
 89-203 8.09e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 56.38  E-value: 8.09e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   89 LDVVKILIKAGASVDTPSADGGTPLFVACQG-----GHVKIVRELLDCGANVNAHMKDRATPVFISAQNGH---RTVLSL 160
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLF 130

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 24581258  161 LIQAGAEIDIKRIDGATPLWIAAQMG---QDHICKVLLQNGANVDT 203
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDINT 176
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 120-292 1.28e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.77  E-value: 1.28e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  120 GHVKIVRELLDCGANVNAHMKDRATPVFISAQNGHRTVLSLLIQAGAEIDIKRIDGATPLWIAAQMGQDHICKVLLQNGA 199
Cdd:PHA02875  13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  200 NVDTV-RCDGATPLFKAAHKGHAAVITVLLKYRPNlGQLPNGE--SALHAAAMFGHMTVCKQLVAAGSDVLLKNHDGLTA 276
Cdd:PHA02875  93 FADDVfYKDGMTPLHLATILKKLDIMKLLIARGAD-PDIPNTDkfSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTP 171

                        170
                 ....*....|....*.
gi 24581258  277 LQLAHQQKYTSICDYL 292
Cdd:PHA02875 172 LIIAMAKGDIAICKML 187
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 118-315 1.32e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.76  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  118 QGGHVKIVRELLDCGANVNAHMKDRATPVFISAQNGHRTVLSLLIQAGAEIDIKRIDGATPLWIAAQMGQDHICKVLLQN 197
Cdd:PHA02876 154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  198 GANVDTvrcdGATPLFKAAHkgHAAVITVLLKYrpNLGQLPNG-----ESALHAAAMFGHMT-VCKQLVAAGSDVLLKNH 271
Cdd:PHA02876 234 RSNINK----NDLSLLKAIR--NEDLETSLLLY--DAGFSVNSiddckNTPLHHASQAPSLSrLVPKLLERGADVNAKNI 305

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 24581258  272 DGLTALQLAHQQKYTSicdylqERIRTMVARSAKAMATSGVSST 315
Cdd:PHA02876 306 KGETPLYLMAKNGYDT------ENIRTLIMLGADVNAADRLYIT 343
Ank_4 pfam13637
Ankyrin repeats (many copies);
177-228 2.68e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 2.68e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 24581258   177 TPLWIAAQMGQDHICKVLLQNGANVDTVRCDGATPLFKAAHKGHAAVITVLL 228
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 13-186 3.70e-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: 51.55  E-value: 3.70e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  13 LHMAAMRG-DEVALLrVLDS--GKVHVDCKDE--DGTTPLILAAAGGHTYCVMELLDQGADPNSRRLTGTT--------- 78
Cdd:cd22192  55 LHVAALYDnLEAAVV-LMEAapELVNEPMTSDlyQGETALHIAVVNQNLNLVRELIARGADVVSPRATGTFfrpgpknli 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  79 -----PLFFAAQGGHLDVVKILIKAGASVDTPSADGGTPLfvacqggHVKIvrelLDCGANVNAHMKDratpvFISAQNG 153
Cdd:cd22192 134 yygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL-------HILV----LQPNKTFACQMYD-----LILSYDK 197

                       170       180       190
                ....*....|....*....|....*....|....
gi 24581258 154 HRTVLSL-LIQAGaeidikriDGATPLWIAAQMG 186
Cdd:cd22192 198 EDDLQPLdLVPNN--------QGLTPFKLAAKEG 223
PHA02798 PHA02798
ankyrin-like protein; Provisional
 59-170 1.47e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 49.45  E-value: 1.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   59 VMELLDQGADPNSRRLTGTTPLF-----FAAQGGHLDVVKILIKAGASVDTPSADGGTPLFVACQGGHV---KIVRELLD 130
Cdd:PHA02798  54 VKLFINLGANVNGLDNEYSTPLCtilsnIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYInnlEILLFMIE 133

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 24581258  131 CGANVNAHMKDRATPVFISAQNGHRT---VLSLLIQAGAEIDI 170
Cdd:PHA02798 134 NGADTTLLDKDGFTMLQVYLQSNHHIdieIIKLLLEKGVDINT 176
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 150-230 2.24e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 2.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  150 AQNGHRTVLSLLIQAGAEIDIKRIDGATPLWIAAQMGQDHICKVLLQNGANVDTVRCDGATPLFKAAHKGHAAVITVLLK 229
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169


                 .
gi 24581258  230 Y 230
Cdd:PTZ00322 170 H 170
Ank_5 pfam13857
Ankyrin repeats (many copies);
62-113 6.77e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 6.77e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 24581258    62 LLDQG-ADPNSRRLTGTTPLFFAAQGGHLDVVKILIKAGASVDTPSADGGTPL 113
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 55-149 7.72e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 46.90  E-value: 7.72e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   55 HTYCVMEL-LDQGADPNSR----RLTGTTPLFFAAQGGHLDVVKILIKAGASVDTPSADGG-TPLFVACQGGHVKIVREL 128
Cdd:PHA02884  44 HYTDIIDAiLKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEIL 123

                         90       100
                 ....*....|....*....|.
gi 24581258  129 LDCGANVNAHMKDRATPVFIS 149
Cdd:PHA02884 124 LSYGADINIQTNDMVTPIELA 144
Ank_2 pfam12796
Ankyrin repeats (3 copies);
13-72 9.34e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.57  E-value: 9.34e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258    13 LHMAAMRGDEVALLRVLDsgKVHVDCKDeDGTTPLILAAAGGHTYCVMELLDQGADPNSR 72
Cdd:pfam12796  34 LHLAAKNGHLEIVKLLLE--HADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 125-237 1.06e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 1.06e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  125 VRELLDCGANVNAHMKDRATPVFISAQNGHRTVLSLLIQAGAEIDIKRIDGATPLWIAAQMGQDHICKVLLQN------- 197
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHsqchfel 177

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 24581258  198 GANVDTVRCDGATPLFK-----AAHKGHAAVItvllkyRPNLGQL 237
Cdd:PTZ00322 178 GANAKPDSFTGKPPSLEdspisSHHPDFSAVP------QPMMGSL 216
PHA02946 PHA02946
ankyin-like protein; Provisional
 40-181 1.24e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.59  E-value: 1.24e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   40 DEDGTTPLILAAAGGHTYCVMELLDQGADPNSRRLTGTTPLFFAAQGGH--LDVVKILIKAGASVDTPSADGGTPLFVAC 117
Cdd:PHA02946  69 DDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINNSVDEEGCGPLLAC 148

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24581258  118 QGGHVKIVRELLDCG--ANVNAHMKDRATPVFISAQNGHRTVLSLLIQAGAEIDIKRIDGATPLWI 181
Cdd:PHA02946 149 TDPSERVFKKIMSIGfeARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHI 214
Ank_4 pfam13637
Ankyrin repeats (many copies);
109-162 1.85e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 1.85e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 24581258   109 GGTPLFVACQGGHVKIVRELLDCGANVNAHMKDRATPVFISAQNGHRTVLSLLI 162
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
210-260 3.15e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 3.15e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 24581258   210 TPLFKAAHKGHAAVITVLLKYRPNLGQLP-NGESALHAAAMFGHMTVCKQLV 260
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDgNGETALHFAASNGNVEVLKLLL 54
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 166-295 4.90e-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: 44.75  E-value: 4.90e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258 166 AEIDIKRIDGATPLWIAAQMGQDHICKVLLQNGANVDTVRCD--------------GATPLFKAAHKGHAAVITVLLKYR 231
Cdd:cd22194 132 AEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGvffnpkykhegfyfGETPLALAACTNQPEIVQLLMEKE 211

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24581258 232 PNLG--QLPNGESALHAAAMFG-----HMTVCKQ-----LVAAGSDVL--LKNHDGLTALQLAHQQKYTSICDYLQER 295
Cdd:cd22194 212 STDItsQDSRGNTVLHALVTVAedsktQNDFVKRmydmiLLKSENKNLetIRNNEGLTPLQLAAKMGKAEILKYILSR 289
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 90-205 4.97e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 44.73  E-value: 4.97e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   90 DVVKILIKAGASVDTpSADGGTPLFVACQGGHVK--IVRELLDCGANVN----------AHMKDRATpvfisAQNGHRTV 157
Cdd:PHA02989  17 NALEFLLRTGFDVNE-EYRGNSILLLYLKRKDVKikIVKLLIDNGADVNykgyietplcAVLRNREI-----TSNKIKKI 90

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 24581258  158 LSLLIQAGAEIDIKRIDGATPlwIAAQMGQDHI-----CKVLLQNGANVDTVR 205
Cdd:PHA02989  91 VKLLLKFGADINLKTFNGVSP--IVCFIYNSNInncdmLRFLLSKGINVNDVK 141
Ank_4 pfam13637
Ankyrin repeats (many copies);
242-292 5.25e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.34  E-value: 5.25e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 24581258   242 SALHAAAMFGHMTVCKQLVAAGSDVLLKNHDGLTALQLAHQQKYTSICDYL 292
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 108-137 1.13e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.72  E-value: 1.13e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 24581258    108 DGGTPLFVACQGGHVKIVRELLDCGANVNA 137
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 108-137 1.23e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.78  E-value: 1.23e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 24581258   108 DGGTPLFVACQGGHVKIVRELLDCGANVNA 137
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 108-137 1.39e-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: 1.39e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 24581258   108 DGGTPLFVAC-QGGHVKIVRELLDCGANVNA 137
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
Ank_4 pfam13637
Ankyrin repeats (many copies);
142-195 2.36e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 2.36e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 24581258   142 RATPVFISAQNGHRTVLSLLIQAGAEIDIKRIDGATPLWIAAQMGQDHICKVLL 195
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 76-103 3.34e-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: 37.18  E-value: 3.34e-04
                           10        20
                   ....*....|....*....|....*...
gi 24581258     76 GTTPLFFAAQGGHLDVVKILIKAGASVD 103
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
227-280 3.63e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 3.63e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 24581258   227 LLKYRPNLGQLPN--GESALHAAAMFGHMTVCKQLVAAGSDVLLKNHDGLTALQLA 280
Cdd:pfam13857   1 LLEHGPIDLNRLDgeGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 42-72 5.14e-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: 36.88  E-value: 5.14e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 24581258    42 DGTTPLILAAA-GGHTYCVMELLDQGADPNSR 72
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
Ank_4 pfam13637
Ankyrin repeats (many copies);
13-55 6.20e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 6.20e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 24581258    13 LHMAAMRGDEVALLRVLDSGkVHVDCKDEDGTTPLILAAAGGH 55
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKG-ADINAVDGNGETALHFAASNGN 46
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 182-318 6.32e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.13  E-value: 6.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  182 AAQMGQDHICKVLLQNGANVDTVRCDGATPLFKAAHKGHAAVITVLLKYR--PNLgQLPNGESALHAAAMFGHMTVCKQL 259
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGaiPDV-KYPDIESELHDAVEEGDVKAVEEL 87

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581258  260 VAAGS---DVLLKnhDGLTALQLAHQQKYTSIcdylqerIRTMVARSAKamatSGVSSTVKT 318
Cdd:PHA02875  88 LDLGKfadDVFYK--DGMTPLHLATILKKLDI-------MKLLIARGAD----PDIPNTDKF 136
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 174-202 7.92e-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: 36.50  E-value: 7.92e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 24581258   174 DGATPLWIAA-QMGQDHICKVLLQNGANVD 202
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 174-202 1.22e-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: 1.22e-03
                           10        20
                   ....*....|....*....|....*....
gi 24581258    174 DGATPLWIAAQMGQDHICKVLLQNGANVD 202
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 76-103 1.71e-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: 1.71e-03
                          10        20
                  ....*....|....*....|....*....
gi 24581258    76 GTTPLFFAA-QGGHLDVVKILIKAGASVD 103
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 6-295 1.96e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.06  E-value: 1.96e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258     6 ETPSDVQLHMAAMRGDEVALLRVLD-SGKVHVDCKDEDGTTPLILAAAGGHTYCVMELLdqgadPNSRRL--TGTTPLFF 82
Cdd:TIGR00870  14 LSDEEKAFLPAAERGDLASVYRDLEePKKLNINCPDRLGRSALFVAAIENENLELTELL-----LNLSCRgaVGDTLLHA 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258    83 AAQGGHlDVVKILI-----KAGASVDTPSAD---------GGTPLFVACQGGHVKIVRELLDCGANVNAhmkdRATPV-F 147
Cdd:TIGR00870  89 ISLEYV-DAVEAILlhllaAFRKSGPLELANdqytseftpGITALHLAAHRQNYEIVKLLLERGASVPA----RACGDfF 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   148 ISAQngHRTVLSLliqagaeidikridGATPLWIAAQMGQDHICKVLLQNGANVDTVRCDGATPLfkaahkgHAAVITvl 227
Cdd:TIGR00870 164 VKSQ--GVDSFYH--------------GESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLL-------HLLVME-- 218

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24581258   228 lkyrpNLGQLPNGESALH----AAAMFGHMTVCKQLvaagSDVLlkNHDGLTALQLAHQQKYTSICDYLQER 295
Cdd:TIGR00870 219 -----NEFKAEYEELSCQmynfALSLLDKLRDSKEL----EVIL--NHQGLTPLKLAAKEGRIVLFRLKLAI 279
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 42-70 2.50e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 2.50e-03
                           10        20
                   ....*....|....*....|....*....
gi 24581258     42 DGTTPLILAAAGGHTYCVMELLDQGADPN 70
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 169-266 3.58e-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: 38.84  E-value: 3.58e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258 169 DIKRIDgATPLWIAAQMGQ-DHICKVLLQNGANVDTVRCDGATPLFKAAHKGHAAVITVLLKYRPNL------GQLPNGE 241
Cdd:cd22192  12 QQKRIS-ESPLLLAAKENDvQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELvnepmtSDLYQGE 90

                        90       100
                ....*....|....*....|....*
gi 24581258 242 SALHAAAMFGHMTVCKQLVAAGSDV 266
Cdd:cd22192  91 TALHIAVVNQNLNLVRELIARGADV 115
Ank_5 pfam13857
Ankyrin repeats (many copies);
29-83 3.68e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 3.68e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 24581258    29 LDSGKVHVDCKDEDGTTPLILAAAGGHTYCVMELLDQGADPNSRRLTGTTPLFFA 83
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 239-271 4.57e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.19  E-value: 4.57e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 24581258   239 NGESALHAAA-MFGHMTVCKQLVAAGSDVLLKNH 271
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02946 PHA02946
ankyin-like protein; Provisional
 92-169 5.13e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.50  E-value: 5.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   92 VKILIKAGASVDTPSADGGTPLFVACQGGHVKIVRELLDCGANVNAHMKDRATPVFISAQNGHRTV--LSLLIQAGAEID 169
Cdd:PHA02946  55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAKIN 134
PHA02795 PHA02795
ankyrin-like protein; Provisional
 89-169 5.74e-03

ankyrin-like protein; Provisional


Pssm-ID: 165157 [Multi-domain]  Cd Length: 437  Bit Score: 38.05  E-value: 5.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   89 LDVVKILIKAGASVDTPSADGGTPLFVACQGGHVKIVRELLDCGANVNAHMKDRATPVFISAQNG--------HRTVLSL 160
Cdd:PHA02795 201 LEIYKLCIPYIEDINQLDAGGRTLLYRAIYAGYIDLVSWLLENGANVNAVMSNGYTCLDVAVDRGsviarretHLKILEI 280


                 ....*....
gi 24581258  161 LIQAGAEID 169
Cdd:PHA02795 281 LLREPLSID 289
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 239-292 7.69e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 37.96  E-value: 7.69e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 24581258  239 NGESALHAAAMFGHMTVCKQLVAAGSDVLLKNHDGLTALQLAHQQKYTSICDYL 292
Cdd:PTZ00322 114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 90-197 7.94e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 37.66  E-value: 7.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258   90 DVVKILIKAGASVDTPSADG----GTPLFVACQGGHVKIVRELLDCGANVNAHMKD-RATPVFISAQNGHRTVLSLLIQA 164
Cdd:PHA02884  47 DIIDAILKLGADPEAPFPLSenskTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEaKITPLYISVLHGCLKCLEILLSY 126

                         90       100       110
                 ....*....|....*....|....*....|...
gi 24581258  165 GAEIDIKRIDGATPLWIAAQMGQDHICKVLLQN 197
Cdd:PHA02884 127 GADINIQTNDMVTPIELALMICNNFLAFMICDN 159
PHA02798 PHA02798
ankyrin-like protein; Provisional
 122-220 8.95e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 37.51  E-value: 8.95e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258  122 VKIVRELLDCGANVNAHMKDRATPVFisaqnghrTVLSLLIQAGAEIDIkridgatplwiaaqmgqdhiCKVLLQNGANV 201
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPLC--------TILSNIKDYKHMLDI--------------------VKILIENGADI 102

                         90
                 ....*....|....*....
gi 24581258  202 DTVRCDGATPLFKAAHKGH 220
Cdd:PHA02798 103 NKKNSDGETPLYCLLSNGY 121
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 151-303 9.21e-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: 37.85  E-value: 9.21e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258 151 QNGHRTVLSLLIQAGAEIDIKR-----------IDGATPLWIAAQMGQDHICKVLLQNGANVDTVRCD------------ 207
Cdd:cd22193  41 NPGTNDTIRILLDIAEKTDNLKrfinaeytdeyYEGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegf 120

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24581258 208 --GATPLFKAAHKGHAAVITVLLK--YRP--NLGQLPNGESALHAAAMFGHMTVCK-QLVAAGSDVLL------------ 268
Cdd:cd22193 121 yfGELPLSLAACTNQPDIVQYLLEneHQPadIEAQDSRGNTVLHALVTVADNTKENtKFVTRMYDMILirgaklcptvel 200

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 24581258 269 ---KNHDGLTALQLAHQQKYTSICDY-LQERIRTMVARS 303
Cdd:cd22193 201 eeiRNNDGLTPLQLAAKMGKIEILKYiLQREIKEPELRH 239
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH