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Conserved domains on  [gi|152112314|sp|A1X154|]
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RecName: Full=Ankyrin repeat, SAM and basic leucine zipper domain-containing protein 1; AltName: Full=Germ cell-specific ankyrin, SAM and basic leucine zipper domain-containing protein

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 12789531)

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
47-234 6.77e-40

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.48  E-value: 6.77e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  47 NEMFKKALTTGDTSLVEELLNAGISVDSSFRYGWTPLMFAASIANVNLVRVLLNRGAN-ASFEKDKQTVLMTACsargsQ 125
Cdd:COG0666   55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADvNARDKDGETPLHLAA-----Y 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 126 EQIIKCVELLLSRNADPNVACRRQMTPIMYAARGGHPQVVALLVAHGAEVNAQDENGYTALTWAAYQGHKNVILKLLELG 205
Cdd:COG0666  130 NGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209

                        170       180
                 ....*....|....*....|....*....
gi 152112314 206 ANKMLQTKDGKTPSEIANRNKHPEIFSLL 234
Cdd:COG0666  210 ADVNAKDNDGKTALDLAAENGNLEIVKLL 238
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 272-333 4.45e-21

SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine Zipper) also known as GASZ (Germ cell-specific Ankyrin, SAM, leucine Zipper) subfamily is a potential protein-protein interaction domain. Proteins of this group are involved in the repression of transposable elements during spermatogenesis, oogenesis, and preimplantation embryogenesis. They support synthesis of PIWI-interacting RNA via association with some PIWI proteins, such as MILI and MIWI. This association is required for initiation and maintenance of retrotransposon repression during the meiosis. In mice lacking ASZ1, DNA damage and delayed germ cell maturation was observed due to retrotransposons releasing from their repressed state.


:

Pssm-ID: 188920  Cd Length: 64  Bit Score: 86.57  E-value: 4.45e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 152112314 272 SYTAFGELDLFLHGLGLEHMTDLLKERDISLRHLMTMKKDEFLKNGITN-KDQQKILSALKEL 333
Cdd:cd09521    1 SYSKLDDLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQpGDQKKILDAIKEV 63
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
47-234 6.77e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.48  E-value: 6.77e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  47 NEMFKKALTTGDTSLVEELLNAGISVDSSFRYGWTPLMFAASIANVNLVRVLLNRGAN-ASFEKDKQTVLMTACsargsQ 125
Cdd:COG0666   55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADvNARDKDGETPLHLAA-----Y 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 126 EQIIKCVELLLSRNADPNVACRRQMTPIMYAARGGHPQVVALLVAHGAEVNAQDENGYTALTWAAYQGHKNVILKLLELG 205
Cdd:COG0666  130 NGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209

                        170       180
                 ....*....|....*....|....*....
gi 152112314 206 ANKMLQTKDGKTPSEIANRNKHPEIFSLL 234
Cdd:COG0666  210 ADVNAKDNDGKTALDLAAENGNLEIVKLL 238
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 60-234 5.09e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.81  E-value: 5.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  60 SLVEELLNAGISVDSSFRYGWTPLMFAASI-----ANVNLVRVLLNRGANASFEKDKQTVLMTACSARGSQEqiIKCVEL 134
Cdd:PHA03100  49 DVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNS--YSIVEY 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 135 LLSRNADPNVACRRQMTPIMYAARGGHP--QVVALLVAHGAEVNAQ----------------DENGYTALTWAAYQGHKN 196
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKnrvnyllsygvpinikDVYGFTPLHYAVYNNNPE 206

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 152112314 197 VILKLLELGANKMLQTKDGKTPSEIANRNKHPEIFSLL 234
Cdd:PHA03100 207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 272-333 4.45e-21

SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine Zipper) also known as GASZ (Germ cell-specific Ankyrin, SAM, leucine Zipper) subfamily is a potential protein-protein interaction domain. Proteins of this group are involved in the repression of transposable elements during spermatogenesis, oogenesis, and preimplantation embryogenesis. They support synthesis of PIWI-interacting RNA via association with some PIWI proteins, such as MILI and MIWI. This association is required for initiation and maintenance of retrotransposon repression during the meiosis. In mice lacking ASZ1, DNA damage and delayed germ cell maturation was observed due to retrotransposons releasing from their repressed state.


Pssm-ID: 188920  Cd Length: 64  Bit Score: 86.57  E-value: 4.45e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 152112314 272 SYTAFGELDLFLHGLGLEHMTDLLKERDISLRHLMTMKKDEFLKNGITN-KDQQKILSALKEL 333
Cdd:cd09521    1 SYSKLDDLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQpGDQKKILDAIKEV 63
Ank_2 pfam12796
Ankyrin repeats (3 copies);
115-211 1.06e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 1.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  115 LMTACSaRGSQEqiikCVELLLSRNADPNVACRRQMTPIMYAARGGHPQVVALLVAHgAEVNAQDeNGYTALTWAAYQGH 194
Cdd:pfam12796   1 LHLAAK-NGNLE----LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGH 73

                          90
                  ....*....|....*..
gi 152112314  195 KNVILKLLELGANKMLQ 211
Cdd:pfam12796  74 LEIVKLLLEKGADINVK 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 62-231 2.09e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.48  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  62 VEELLNAGISvdSSFRYGWTPLMFAASIANVNLVRVLLNRGAnasfekDKQTVLMTACSARGSQEQIIKCVELLLSrnad 141
Cdd:cd22192   74 APELVNEPMT--SDLYQGETALHIAVVNQNLNLVRELIARGA------DVVSPRATGTFFRPGPKNLIYYGEHPLS---- 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 142 pnvacrrqmtpimYAARGGHPQVVALLVAHGAEVNAQDENGYTALTWAAYQGHK-------NVIL---KLLELGANKMLQ 211
Cdd:cd22192  142 -------------FAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKtfacqmyDLILsydKEDDLQPLDLVP 208

                        170       180
                 ....*....|....*....|
gi 152112314 212 TKDGKTPSEIANRNKHPEIF 231
Cdd:cd22192  209 NNQGLTPFKLAAKEGNIVMF 228
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 272-333 2.20e-06

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 44.95  E-value: 2.20e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 152112314  272 SYTAFGELDLFLHGLGLEHMTDLLKERDISLRHLMTMKKDEFLKNGITNK-DQQKILSALKEL 333
Cdd:pfam00536   1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLgHRKKILYAIQRL 63
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 74-186 3.73e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.23  E-value: 3.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314   74 SSFRYGWTPLMFAASIANVNLVRVLLNRGANasfekdkqtVLMTACsargsqeqiikCVELLLSRNADpnvACRRQMTPI 153
Cdd:TIGR00870 123 SEFTPGITALHLAAHRQNYEIVKLLLERGAS---------VPARAC-----------GDFFVKSQGVD---SFYHGESPL 179

                          90       100       110
                  ....*....|....*....|....*....|...
gi 152112314  154 MYAARGGHPQVVALLVAHGAEVNAQDENGYTAL 186
Cdd:TIGR00870 180 NAAACLGSPSIVALLSEDPADILTADSLGNTLL 212
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 150-177 9.32e-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: 36.41  E-value: 9.32e-04
                           10        20
                   ....*....|....*....|....*...
gi 152112314   150 MTPIMYAARGGHPQVVALLVAHGAEVNA 177
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
47-234 6.77e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.48  E-value: 6.77e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  47 NEMFKKALTTGDTSLVEELLNAGISVDSSFRYGWTPLMFAASIANVNLVRVLLNRGAN-ASFEKDKQTVLMTACsargsQ 125
Cdd:COG0666   55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADvNARDKDGETPLHLAA-----Y 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 126 EQIIKCVELLLSRNADPNVACRRQMTPIMYAARGGHPQVVALLVAHGAEVNAQDENGYTALTWAAYQGHKNVILKLLELG 205
Cdd:COG0666  130 NGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209

                        170       180
                 ....*....|....*....|....*....
gi 152112314 206 ANKMLQTKDGKTPSEIANRNKHPEIFSLL 234
Cdd:COG0666  210 ADVNAKDNDGKTALDLAAENGNLEIVKLL 238
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
41-250 1.86e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.33  E-value: 1.86e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  41 LPAEEKNEMFKKALTTGDTSLVEELLNAGISVDSSFRYGWTPLMFAASIANVNLVRVLLNRGA--NASfEKDKQTVLMTA 118
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAdvNAQ-DNDGNTPLHLA 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 119 CsARGSqeqiIKCVELLLSRNADPNVACRRQMTPIMYAARGGHPQVVALLVAHGAEVNAQDENGYTALTWAAYQGHKNVI 198
Cdd:COG0666  161 A-ANGN----LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|..
gi 152112314 199 LKLLELGANKMLQTKDGKTPSEIANRNKHPEIFSLLSLTLNPLEGKIQQLTK 250
Cdd:COG0666  236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
60-234 9.23e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.10  E-value: 9.23e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  60 SLVEELLNAGISVDSSFRYGWTPLMFAASIANVNLVRVLLNRGANASFEKDKQTVLMTACSARGsqeqIIKCVELLLSRN 139
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAG----DLLVALLLLAAG 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 140 ADPNVACRRQMTPIMYAARGGHPQVVALLVAHGAEVNAQDENGYTALTWAAYQGHKNVILKLLELGANKMLQTKDGKTPS 219
Cdd:COG0666   78 ADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157

                        170
                 ....*....|....*
gi 152112314 220 EIANRNKHPEIFSLL 234
Cdd:COG0666  158 HLAAANGNLEIVKLL 172
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 60-234 5.09e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.81  E-value: 5.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  60 SLVEELLNAGISVDSSFRYGWTPLMFAASI-----ANVNLVRVLLNRGANASFEKDKQTVLMTACSARGSQEqiIKCVEL 134
Cdd:PHA03100  49 DVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNS--YSIVEY 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 135 LLSRNADPNVACRRQMTPIMYAARGGHP--QVVALLVAHGAEVNAQ----------------DENGYTALTWAAYQGHKN 196
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKnrvnyllsygvpinikDVYGFTPLHYAVYNNNPE 206

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 152112314 197 VILKLLELGANKMLQTKDGKTPSEIANRNKHPEIFSLL 234
Cdd:PHA03100 207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 272-333 4.45e-21

SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine Zipper) also known as GASZ (Germ cell-specific Ankyrin, SAM, leucine Zipper) subfamily is a potential protein-protein interaction domain. Proteins of this group are involved in the repression of transposable elements during spermatogenesis, oogenesis, and preimplantation embryogenesis. They support synthesis of PIWI-interacting RNA via association with some PIWI proteins, such as MILI and MIWI. This association is required for initiation and maintenance of retrotransposon repression during the meiosis. In mice lacking ASZ1, DNA damage and delayed germ cell maturation was observed due to retrotransposons releasing from their repressed state.


Pssm-ID: 188920  Cd Length: 64  Bit Score: 86.57  E-value: 4.45e-21
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 152112314 272 SYTAFGELDLFLHGLGLEHMTDLLKERDISLRHLMTMKKDEFLKNGITN-KDQQKILSALKEL 333
Cdd:cd09521    1 SYSKLDDLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQpGDQKKILDAIKEV 63
Ank_2 pfam12796
Ankyrin repeats (3 copies);
115-211 1.06e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 1.06e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  115 LMTACSaRGSQEqiikCVELLLSRNADPNVACRRQMTPIMYAARGGHPQVVALLVAHgAEVNAQDeNGYTALTWAAYQGH 194
Cdd:pfam12796   1 LHLAAK-NGNLE----LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGH 73

                          90
                  ....*....|....*..
gi 152112314  195 KNVILKLLELGANKMLQ 211
Cdd:pfam12796  74 LEIVKLLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 58-240 2.53e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.31  E-value: 2.53e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  58 DTSLVEELLNAGISVDSSFRYGWTPLmfAASI----ANVNLVRVLLNRGANAsFEKD--KQTVLMTAC-SARGSQeqiiK 130
Cdd:PHA03095 131 NPKVIRLLLRKGADVNALDLYGMTPL--AVLLksrnANVELLRLLIDAGADV-YAVDdrFRSLLHHHLqSFKPRA----R 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 131 CVELLLSRNADPNVACRRQMTPIMYAARGGHPQ--VVALLVAHGAEVNAQDENGYTALTWAAYQGHKNVILKLLELGANK 208
Cdd:PHA03095 204 IVRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADI 283

                        170       180       190
                 ....*....|....*....|....*....|..
gi 152112314 209 MLQTKDGKTPSEIANRNKHPEIFSLLsLTLNP 240
Cdd:PHA03095 284 NAVSSDGNTPLSLMVRNNNGRAVRAA-LAKNP 314
Ank_2 pfam12796
Ankyrin repeats (3 copies);
83-179 3.36e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.61  E-value: 3.36e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314   83 LMFAASIANVNLVRVLLNRGANASF-EKDKQTVLMTACSaRGSQEqiikCVELLLSrNADPNVACRrQMTPIMYAARGGH 161
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLqDKNGRTALHLAAK-NGHLE----IVKLLLE-HADVNLKDN-GRTALHYAARSGH 73

                          90
                  ....*....|....*...
gi 152112314  162 PQVVALLVAHGAEVNAQD 179
Cdd:pfam12796  74 LEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
153-234 2.80e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 2.80e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  153 IMYAARGGHPQVVALLVAHGAEVNAQDENGYTALTWAAYQGHKNVILKLLELGANKMlqTKDGKTPSEIANRNKHPEIFS 232
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78


                  ..
gi 152112314  233 LL 234
Cdd:pfam12796  79 LL 80
Ank_2 pfam12796
Ankyrin repeats (3 copies);
57-144 4.09e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 4.09e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314   57 GDTSLVEELLNAGISVDSSFRYGWTPLMFAASIANVNLVRVLLNRgANASFEKDKQTVLMTACSARgsqeqIIKCVELLL 136
Cdd:pfam12796   8 GNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSG-----HLEIVKLLL 81


                  ....*...
gi 152112314  137 SRNADPNV 144
Cdd:pfam12796  82 EKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 61-276 3.92e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.77  E-value: 3.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  61 LVEELLNAGISVDSSFRYGWTPLMFAAS--IANVNLVRVLLNRGANasfekdkqtvlMTACSARG---------SQEQII 129
Cdd:PHA03100  88 IVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGAN-----------VNIKNSDGenllhlyleSNKIDL 156

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 130 KCVELLLSRNADPNVACR----------------RQMTPIMYAARGGHPQVVALLVAHGAEVNAQDENGYTALTWAAYQG 193
Cdd:PHA03100 157 KILKLLIDKGVDINAKNRvnyllsygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNN 236

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 194 HKNVILKLLELGAN------KMLQTKDgktpSEIANRNKHPEIFSLLS--LTLNPLEGKIQQLTKEETICKMLATDCDKE 265
Cdd:PHA03100 237 NKEIFKLLLNNGPSiktiieTLLYFKD----KDLNTITKIKMLKKSIMymFLLDPGFYKNRKLIENSKSLKDVINECEKE 312

                        250
                 ....*....|....*
gi 152112314 266 ----KDNLFSSYTAF 276
Cdd:PHA03100 313 iermKEIKLNKVTVY 327
Ank_4 pfam13637
Ankyrin repeats (many copies);
149-202 1.40e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.21  E-value: 1.40e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 152112314  149 QMTPIMYAARGGHPQVVALLVAHGAEVNAQDENGYTALTWAAYQGHKNVILKLL 202
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 53-234 2.88e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.93  E-value: 2.88e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  53 ALTTGDTSLVEELLNAGISVDSSFRYGWTPLMFAASIANVNLVRVLLNRGA----------------------------- 103
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipdvkypdieselhdaveegdvkaveell 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 104 ------NASFEKDKQTVLMTAcsargSQEQIIKCVELLLSRNADPNVACRRQMTPIMYAARGGHPQVVALLVAHGAEVNA 177
Cdd:PHA02875  89 dlgkfaDDVFYKDGMTPLHLA-----TILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 152112314 178 QDENGYTALTWAAYQGHKNVILKLLELGANKMLQTKDGK-TPSEIANRNKHPEIFSLL 234
Cdd:PHA02875 164 EDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLF 221
PHA03095 PHA03095
ankyrin-like protein; Provisional
 73-234 1.73e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.65  E-value: 1.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  73 DSSFRYgwtplMFAASIANVNLVRVLLNRGANASFEKDKQTVLMTACsARGSQEQIIKCVELLLSRNADPNVACRRQMTP 152
Cdd:PHA03095  13 AALYDY-----LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLY-LHYSSEKVKDIVRLLLEAGADVNAPERCGFTP 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 153 I-MYAARGGHPQVVALLVAHGAEVNAQDENGYTALTwaAYQG----HKNVILKLLELGANKMLQTKDGKTPSEI--ANRN 225
Cdd:PHA03095  87 LhLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLAVllKSRN 164


                 ....*....
gi 152112314 226 KHPEIFSLL 234
Cdd:PHA03095 165 ANVELLRLL 173
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 165-235 5.52e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.37  E-value: 5.52e-09
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 152112314 165 VALLVAHGAEVNAQDENGYTALTWAAYQGHKNVILKLLELGANKMLQTKDGKTPSEIANRNKHPEIFSLLS 235
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
134-186 1.13e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.19  E-value: 1.13e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 152112314  134 LLLSRNADPNVACRRQMTPIMYAARGGHPQVVALLVAHGAEVNAQDENGYTAL 186
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 55-221 1.42e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.19  E-value: 1.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  55 TTGDTSLVEELLNAGISVDSSFRYGWTPLMFAASIANVNLVRVLLNRGANASFeKDKQ--TVLMTACSARgsqEQIIKCV 132
Cdd:PLN03192 534 STGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI-RDANgnTALWNAISAK---HHKIFRI 609

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 133 ELLLSRNADPNVA----CrrqmtpimYAARGGHPQVVALLVAHGAEVNAQDENGYTALTWAAYQGHKNVILKLLELGAN- 207
Cdd:PLN03192 610 LYHFASISDPHAAgdllC--------TAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADv 681

                        170
                 ....*....|....
gi 152112314 208 KMLQTKDGKTPSEI 221
Cdd:PLN03192 682 DKANTDDDFSPTEL 695
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 41-243 2.52e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.13  E-value: 2.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  41 LPAEEKNEMFKKALTTGDTSLVEELLNAGISVDSSFRYGWTPLMFAASIANVNLVRVLLNRGANAS------FEKDK-QT 113
Cdd:PHA02874  30 ISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSilpipcIEKDMiKT 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 114 VLMTACSARGSQEQI------------IKCVELLLSRNADPNVACRRQMTPIMYAARGGHPQVVALLVAHGAEVNAQDEN 181
Cdd:PHA02874 110 ILDCGIDVNIKDAELktflhyaikkgdLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 152112314 182 GYTALTWAAYQGHKNVILKLLELGANKMLQTKDGKTPSEIA---NRNKHPEIFSLLSLTLNPLEG 243
Cdd:PHA02874 190 GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAiihNRSAIELLINNASINDQDIDG 254
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 46-234 1.02e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 54.30  E-value: 1.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  46 KNEMFKKALTTGDTS-LVEELLNAGISVDSSFRYGWTPL-MFAASIANVNLVRVLLNRGANA-SFEKDKQTVLMTACSAR 122
Cdd:PHA02876 273 KNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLyLMAKNGYDTENIRTLIMLGADVnAADRLYITPLHQASTLD 352

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 123 GSQEQIIKCVELllsrNADPNVACRRQMTPIMYAARGGHPQVVALLVAHGAEVNAQDENGYTALTWAAYQGHKNVILK-L 201
Cdd:PHA02876 353 RNKDIVITLLEL----GANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMSVKtL 428

                        170       180       190
                 ....*....|....*....|....*....|....
gi 152112314 202 LELGANKMLQTKDGKTPSEIA-NRNKHPEIFSLL 234
Cdd:PHA02876 429 IDRGANVNSKNKDLSTPLHYAcKKNCKLDVIEML 462
Ank_5 pfam13857
Ankyrin repeats (many copies);
168-222 1.08e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 1.08e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 152112314  168 LVAHG-AEVNAQDENGYTALTWAAYQGHKNVILKLLELGANKMLQTKDGKTPSEIA 222
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 62-231 2.09e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.48  E-value: 2.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  62 VEELLNAGISvdSSFRYGWTPLMFAASIANVNLVRVLLNRGAnasfekDKQTVLMTACSARGSQEQIIKCVELLLSrnad 141
Cdd:cd22192   74 APELVNEPMT--SDLYQGETALHIAVVNQNLNLVRELIARGA------DVVSPRATGTFFRPGPKNLIYYGEHPLS---- 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 142 pnvacrrqmtpimYAARGGHPQVVALLVAHGAEVNAQDENGYTALTWAAYQGHK-------NVIL---KLLELGANKMLQ 211
Cdd:cd22192  142 -------------FAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKtfacqmyDLILsydKEDDLQPLDLVP 208

                        170       180
                 ....*....|....*....|
gi 152112314 212 TKDGKTPSEIANRNKHPEIF 231
Cdd:cd22192  209 NNQGLTPFKLAAKEGNIVMF 228
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 282-332 4.03e-07

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 46.85  E-value: 4.03e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|..
gi 152112314 282 FLHGLGLEHMTDLLKERDISLRHLMTMKKDEFLKNGITNK-DQQKILSALKE 332
Cdd:cd09487    5 WLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPgHRKKILRAIQR 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 53-313 4.09e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.27  E-value: 4.09e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  53 ALTTGDTSLVEELLNAGISVDSSFRYGWTPLMFAASIANVNLVRVLLNRGANASFEKDKQTVLMTACSARGSqeqiIKCV 132
Cdd:PHA02874 131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGD----YACI 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 133 ELLLSRNADPNVACRRQMTPIMYAARggHPQVVALLVAHGAEVNAQDENGYTALTWA-AYQGHKNVILKLLELGANKMLQ 211
Cdd:PHA02874 207 KLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIK 284

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 212 TKDGKTPSEIANR--NKHPEIFSLLS-LTLNPLEGKIQQLT-------KEETICKMLATDCDKEKDNLfSSYTAFGE--- 278
Cdd:PHA02874 285 DNKGENPIDTAFKyiNKDPVIKDIIAnAVLIKEADKLKDSDflehieiKDNKEFSDFIKECNEEIEDM-KKTKCGCDkni 363

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 152112314 279 LDLFLHGLGL------EHMTDLLKE-RDISLRHLMTMKKDEF 313
Cdd:PHA02874 364 FDLCLIRIKHkfdgneDSIKDYLNClDDNSHRMLKTIDINEF 405
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 41-154 4.71e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.92  E-value: 4.71e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  41 LPAEEKNEMFKKALTTGDTSLVEELLNAGISVDSSFRYGWTPLMFAASIANVNLVRVLLNRGANAS-FEKDKQTVLMtaC 119
Cdd:PHA02875 130 IPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAAL--C 207

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 152112314 120 SArgSQEQIIKCVELLLSRNADPNVacrrqMTPIM 154
Cdd:PHA02875 208 YA--IENNKIDIVRLFIKRGADCNI-----MFMIE 235
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 61-225 1.52e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.83  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  61 LVEELLNAGISVDSSFRYGWTPLMFAASIANVNLVRVLLNRGAN-ASFEKDKQTVLMTACSARGSQEQiikcVELLLSRN 139
Cdd:PHA02876 357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADiEALSQKIGTALHFALCGTNPYMS----VKTLIDRG 432

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 140 ADPNVACRRQMTPIMYAARGG-HPQVVALLVAHGAEVNAQD-ENGYTALTWAAYQGHKNVilkLLELGAnkmlQTKDGKT 217
Cdd:PHA02876 433 ANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINiQNQYPLLIALEYHGIVNI---LLHYGA----ELRDSRV 505


                 ....*...
gi 152112314 218 PSEIANRN 225
Cdd:PHA02876 506 LHKSLNDN 513
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 272-333 2.20e-06

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 44.95  E-value: 2.20e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 152112314  272 SYTAFGELDLFLHGLGLEHMTDLLKERDISLRHLMTMKKDEFLKNGITNK-DQQKILSALKEL 333
Cdd:pfam00536   1 DGWSVEDVGEWLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLgHRKKILYAIQRL 63
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 45-234 7.30e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 7.30e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  45 EKNEMFKKALTTGDTSLVEELLNAGISVDSSFRYGWTPLMFAASIANVNLVRVLLNRGANAS-FEKDKQTVLMTACSARG 123
Cdd:PHA02876 144 EYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNiIALDDLSVLECAVDSKN 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 124 -----------------------------------------SQEQIIKC-----------------VELLLSRNADPNVA 145
Cdd:PHA02876 224 idtikaiidnrsninkndlsllkairnedletslllydagfSVNSIDDCkntplhhasqapslsrlVPKLLERGADVNAK 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 146 CRRQMTPIMYAARGGH-PQVVALLVAHGAEVNAQDENGYTALTWAA-YQGHKNVILKLLELGANKMLQTKDGKTPSEIAN 223
Cdd:PHA02876 304 NIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAA 383

                        250
                 ....*....|..
gi 152112314 224 -RNKHPEIFSLL 234
Cdd:PHA02876 384 vRNNVVIINTLL 395
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
272-333 9.98e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 43.03  E-value: 9.98e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 152112314  272 SYTAFGELDLFLHGLGLEHMTDLLKERDIS-LRHLMTMKKDEFLKNGITNK-DQQKILSALKEL 333
Cdd:pfam07647   2 ESWSLESVADWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLKRLGITSVgHRRKILKKIQEL 65
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 132-234 1.68e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.56  E-value: 1.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 132 VELLLSRNADPNVACRRQMTPIMYAARGGHPQVVALLVAHGAEVNAQDENGYTALtW----------------------- 188
Cdd:PLN03192 541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL-Wnaisakhhkifrilyhfasisdp 619

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 152112314 189 ---------AAYQGHKNVILKLLELGANKMLQTKDGKTPSEIANRNKHPEIFSLL 234
Cdd:PLN03192 620 haagdllctAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
Ank_4 pfam13637
Ankyrin repeats (many copies);
52-99 2.01e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 2.01e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 152112314   52 KALTTGDTSLVEELLNAGISVDSSFRYGWTPLMFAASIANVNLVRVLL 99
Cdd:pfam13637   7 AAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 74-186 3.73e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.23  E-value: 3.73e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314   74 SSFRYGWTPLMFAASIANVNLVRVLLNRGANasfekdkqtVLMTACsargsqeqiikCVELLLSRNADpnvACRRQMTPI 153
Cdd:TIGR00870 123 SEFTPGITALHLAAHRQNYEIVKLLLERGAS---------VPARAC-----------GDFFVKSQGVD---SFYHGESPL 179

                          90       100       110
                  ....*....|....*....|....*....|...
gi 152112314  154 MYAARGGHPQVVALLVAHGAEVNAQDENGYTAL 186
Cdd:TIGR00870 180 NAAACLGSPSIVALLSEDPADILTADSLGNTLL 212
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 150-180 3.91e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.74  E-value: 3.91e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 152112314  150 MTPIMYAA-RGGHPQVVALLVAHGAEVNAQDE 180
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 102-207 5.43e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 5.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 102 GANASFEKDKQTV-LMTACSARGSQEQIiKCVELLLSRNADPNVACRRQMTPIMYAARGGHPQVVALLVAHGAEVNAQDE 180
Cdd:PHA02876 131 GNDIHYDKINESIeYMKLIKERIQQDEL-LIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIAL 209

                         90       100
                 ....*....|....*....|....*..
gi 152112314 181 NGYTALTWAAYQGHKNVILKLLELGAN 207
Cdd:PHA02876 210 DDLSVLECAVDSKNIDTIKAIIDNRSN 236
Ank_4 pfam13637
Ankyrin repeats (many copies);
129-169 5.76e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 5.76e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 152112314  129 IKCVELLLSRNADPNVACRRQMTPIMYAARGGHPQVVALLV 169
Cdd:pfam13637  14 LELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 91-234 9.69e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.87  E-value: 9.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  91 NVNLVR-VLLNRGANasfEKDKQTVLMTACSARGSQEQIIkcVELLLSRNADPNVACRRQM-TPIMYAARGGHPQVVALL 168
Cdd:PHA02878 113 NVEIFKiILTNRYKN---IQTIDLVYIDKKSKDDIIEAEI--TKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELL 187

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 152112314 169 VAHGAEVNAQDENGYTALTWAAYQGHKNVILKLLELGANKMLQTKDGKTPSEIA-NRNKHPEIFSLL 234
Cdd:PHA02878 188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLL 254
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 53-192 2.80e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.33  E-value: 2.80e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  53 ALTTGDTSLVEELLNAGISVDSSFRYGWTPLMFAASIANVNLVRVLLNRGANASFEKDKQTVLMTACSARGSQEQIIKcv 132
Cdd:PHA02878 175 ATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILK-- 252

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 152112314 133 eLLLSRNADPNVACR-RQMTPIMYAARGghPQVVALLVAHGAEVNAQDENGYTALTWAAYQ 192
Cdd:PHA02878 253 -LLLEHGVDVNAKSYiLGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA02946 PHA02946
ankyin-like protein; Provisional
 58-260 6.21e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.96  E-value: 6.21e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  58 DTSLVEELLNAGISVDSSFRYGWTPLMFAASIANVNLVRVLLNRGANA-SFEKDKQTVLMTacsARGSQEQIIKCVELLL 136
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPnACDKQHKTPLYY---LSGTDDEVIERINLLV 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 137 SRNADPNVACRRQMTPIMYAARGGHPQVVALLVAHGAEVNAQDENGYTAL--TWAAYQGHKNVILKLLELGANKMLQTKD 214
Cdd:PHA02946 128 QYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHD 207

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 152112314 215 GKTPSEI--ANRNKHPEIFSLL--SLTLN--------PLEGKIQQLTKEETICKMLAT 260
Cdd:PHA02946 208 GNTPLHIvcSKTVKNVDIINLLlpSTDVNkqnkfgdsPLTLLIKTLSPAHLINKLLST 265
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 78-104 8.72e-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: 36.85  E-value: 8.72e-04
                          10        20
                  ....*....|....*....|....*..
gi 152112314   78 YGWTPLMFAASIANVNLVRVLLNRGAN 104
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 150-177 9.32e-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: 36.41  E-value: 9.32e-04
                           10        20
                   ....*....|....*....|....*...
gi 152112314   150 MTPIMYAARGGHPQVVALLVAHGAEVNA 177
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
182-234 1.28e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 1.28e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 152112314  182 GYTALTWAAYQGHKNVILKLLELGANKMLQTKDGKTPSEIANRNKHPEIFSLL 234
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 78-104 1.86e-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: 1.86e-03
                           10        20
                   ....*....|....*....|....*..
gi 152112314    78 YGWTPLMFAASIANVNLVRVLLNRGAN 104
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 58-222 2.00e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.63  E-value: 2.00e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  58 DTSLVEELLNAGISVDSSFRY-GWTPLMFAASIANVNLVRVLLNRGANA-SFEKDKQTVLMTACSARGSqeqiiKCVELL 135
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVnIPDKTNNSPLHHAVKHYNK-----PIVHIL 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 136 LSRNADPNVACRRQMTPIMYA-ARGGHPQVVALLVAHGAEVNAQDE-NGYTALTWAAyqgHKNVILK-LLELGANKMLQT 212
Cdd:PHA02878 221 LENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSI---KSERKLKlLLEYGADINSLN 297

                        170
                 ....*....|
gi 152112314 213 KDGKTPSEIA 222
Cdd:PHA02878 298 SYKLTPLSSA 307
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 181-207 2.17e-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: 2.17e-03
                           10        20
                   ....*....|....*....|....*..
gi 152112314   181 NGYTALTWAAYQGHKNVILKLLELGAN 207
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 150-177 2.73e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 2.73e-03
                          10        20
                  ....*....|....*....|....*...
gi 152112314  150 MTPIMYAARGGHPQVVALLVAHGAEVNA 177
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 52-158 2.83e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.25  E-value: 2.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  52 KALTTGDTSLVEELLNAGISVDSSFRYGWTPLMFAAS-IANVNLVRVLLNRGANASFekdKQTVL-MTACSARGSQEQII 129
Cdd:PHA02878 207 HAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGyCKDYDILKLLLEHGVDVNA---KSYILgLTALHSSIKSERKL 283

                         90       100
                 ....*....|....*....|....*....
gi 152112314 130 KcveLLLSRNADPNVACRRQMTPIMYAAR 158
Cdd:PHA02878 284 K---LLLEYGADINSLNSYKLTPLSSAVK 309
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 78-104 4.56e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.57  E-value: 4.56e-03
                          10        20
                  ....*....|....*....|....*...
gi 152112314   78 YGWTPLMFAASIA-NVNLVRVLLNRGAN 104
Cdd:pfam00023   1 DGNTPLHLAAGRRgNLEIVKLLLSKGAD 28
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 53-104 4.56e-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: 39.61  E-value: 4.56e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 152112314  53 ALTTGDTSLVEELLNAGISVDSS------FR--------YGWTPLMFAASIANVNLVRVLLNRGAN 104
Cdd:cd22192   96 AVVNQNLNLVRELIARGADVVSPratgtfFRpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGAD 161
PHA02798 PHA02798
ankyrin-like protein; Provisional
 92-207 7.09e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 38.66  E-value: 7.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314  92 VNLVRVLLNRGANAS-FEKDKQTVLMTACSARGSQEQIIKCVELLLSRNADPNVACRRQMTPIMYAARGGH---PQVVAL 167
Cdd:PHA02798  51 TDIVKLFINLGANVNgLDNEYSTPLCTILSNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLF 130

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 152112314 168 LVAHGAEVNAQDENGYTALTWAAYQGHK---NVILKLLELGAN 207
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVD 173
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 132-224 8.53e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 38.04  E-value: 8.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 152112314 132 VELLLSRNADPNV----ACRRQMTPIMYAARGGHPQVVALLVAHGAEVNA-QDENGYTALTWAAYQGHKNVILKLLELGA 206
Cdd:PHA02884  49 IDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKITPLYISVLHGCLKCLEILLSYGA 128

                         90
                 ....*....|....*...
gi 152112314 207 NKMLQTKDGKTPSEIANR 224
Cdd:PHA02884 129 DINIQTNDMVTPIELALM 146
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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