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Conserved domains on  [gi|1907154184|ref|XP_036019565|]
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ankyrin repeat domain-containing protein 6 isoform X2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-229 9.00e-52

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.92  E-value: 9.00e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184   5 DAVAALSERLLIAAYKGQTENVVQLINKGAKV--AVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRA 82
Cdd:COG0666    48 ALADALGALLLLAAALAGDLLVALLLLAAGADinAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  83 TVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGDTCLHVAARYNHLSVVRLLLN 162
Cdd:COG0666   128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907154184 163 AFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 229
Cdd:COG0666   208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
geminin-like_CC super family cl45898
coiled-coil domain found in the geminin family; The geminin family includes geminin, geminin ...
 389-434 8.70e-03

coiled-coil domain found in the geminin family; The geminin family includes geminin, geminin coiled-coil domain-containing protein 1 (GemC1), and McIdas. Together, geminin, GemC1, and McIdas (also called Idas or multicilin), controls both the cell cycle and differentiation decisions in cells. They were initially identified as cell cycle regulators associated with the chromosome cycle. Geminin is required to ensure once-per-cell-cycle genome replication, while McIdas and GemC1 bind to geminin and are implicated in DNA replication control. Geminin binds to Cdt1, a key component and crucial regulator of pre-replicative complexes (pre-RC), in a timely manner to inhibit DNA replication. Geminin family members also function as early regulators of multiciliogenesis. GemC1 and McIdas specify the multiciliate cell fate by forming complexes with the E2F4/5 transcription factors, resulting in centriole amplification and cilia formation. Geminin family proteins contain a homologous central coiled-coil domain that mediates homo- and heterodimerization; this ability is likely to be important for modulating their function in cycling and differentiating cells. This model represents the central coiled-coil domain of the geminin family.


The actual alignment was detected with superfamily member cd22590:

Pssm-ID: 459243  Cd Length: 64  Bit Score: 35.16  E-value: 8.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1907154184 389 NQLEATVEEIRAELGSVQDKvNAKLGQMESKTQHQMCVLDKLMVER 434
Cdd:cd22590    20 NQLHETLTRKQEEIDSLQER-NVQLKELASQAKHLASVLDKLMTVR 64
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-229 9.00e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.92  E-value: 9.00e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184   5 DAVAALSERLLIAAYKGQTENVVQLINKGAKV--AVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRA 82
Cdd:COG0666    48 ALADALGALLLLAAALAGDLLVALLLLAAGADinAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  83 TVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGDTCLHVAARYNHLSVVRLLLN 162
Cdd:COG0666   128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907154184 163 AFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 229
Cdd:COG0666   208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
PHA03095 PHA03095
ankyrin-like protein; Provisional
 19-232 6.98e-25

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 108.57  E-value: 6.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  19 YKGQTENVVQ-LINKGAKV-AVTKHGRTPLHL-AANKG-HLSVVQILLKAGCDLDVQDDGDQTALH------RATVvgnt 88
Cdd:PHA03095   92 YNATTLDVIKlLIKAGADVnAKDKVGRTPLHVyLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLAvllksrNANV---- 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  89 EILTALIREGCALDRQDKDGNTALHEaawhgFSQSAK-------LLVKAGANVLARNKAGDTCLHVAARYNHL--SVVRL 159
Cdd:PHA03095  168 ELLRLLIDAGADVYAVDDRFRSLLHH-----HLQSFKprarivrELIRAGCDPAATDMLGNTPLHSMATGSSCkrSLVLP 242

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907154184 160 LLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETARYHNNPE-VALLLTKAPQI 232
Cdd:PHA03095  243 LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRaVRAALAKNPSA 316
Ank_2 pfam12796
Ankyrin repeats (3 copies);
112-204 5.21e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.56  E-value: 5.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 112 LHEAAWHGFSQSAKLLVKAGANVLARNKAGDTCLHVAARYNHLSVVRLLLNAFCSvhEKNQAGDTALHVAAALNHKKVVK 191
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1907154184 192 VLLEAGADTTIVN 204
Cdd:pfam12796  79 LLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 44-222 1.03e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 61.57  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  44 TPLHLAANKGHLSVVQILLK-AGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQDK-----DGNTALHEAAW 117
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMtsdlyQGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 118 HGFSQSAKLLVKAGANVLA---------RNKA-----GDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVAAA 183
Cdd:cd22192    99 NQNLNLVRELIARGADVVSpratgtffrPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1907154184 184 LNHKKVVKVL------LEAGADT----TIVNNAGQTPLETARYHNNPEV 222
Cdd:cd22192   179 QPNKTFACQMydlilsYDKEDDLqpldLVPNNQGLTPFKLAAKEGNIVM 227
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 41-70 1.31e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.89  E-value: 1.31e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1907154184   41 HGRTPLHLAANKGHLSVVQILLKAGCDLDV 70
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 42-226 2.81e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.38  E-value: 2.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  42 GRTPLHLAANKG-HLSVVQILLKAGCDLDVQDdgdqTALHRAT--VVGNTEILTALI----REGC----ALDRQDKD--- 107
Cdd:TIGR00870  52 GRSALFVAAIENeNLELTELLLNLSCRGAVGD----TLLHAISleYVDAVEAILLHLlaafRKSGplelANDQYTSEftp 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 108 GNTALHEAAWHGFSQSAKLLVKAGANVLARNKaGDTC---------------LHVAARYNHLSVVRLLLNAFCSVHEKNQ 172
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARAC-GDFFvksqgvdsfyhgespLNAAACLGSPSIVALLSEDPADILTADS 206

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 173 AGDTALHVAAALNHKKV------------VKVLLEAGADTT----IVNNAGQTPLETARYHNNPEVALLL 226
Cdd:TIGR00870 207 LGNTLLHLLVMENEFKAeyeelscqmynfALSLLDKLRDSKelevILNHQGLTPLKLAAKEGRIVLFRLK 276
McIdas_CC cd22590
central coiled-coil domain of McIdas (or multicilin); McIdas (also called Idas or multicilin), ...
 389-434 8.70e-03

central coiled-coil domain of McIdas (or multicilin); McIdas (also called Idas or multicilin), together with geminin coiled-coil domain-containing protein 1 (GemC1) and geminin, controls both the cell cycle and differentiation decisions in cells. Idas binds to geminin and is implicated in DNA replication control. It also functions as an early regulator of multiciliogenesis. GemC1 and McIdas specify the multiciliate cell fate by forming complexes with the E2F4/5 transcription factors, resulting in centriole amplification and cilia formation. Idas belongs to the geminin family of proteins that also includes geminin and GemC1. They share a homologous central coiled-coil domain that mediates homo- and heterodimerization with other family members; this ability is likely to be important for modulating their function in cycling and differentiating cells. This model represents the central coiled-coil domain of McIdas.


Pssm-ID: 439144  Cd Length: 64  Bit Score: 35.16  E-value: 8.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1907154184 389 NQLEATVEEIRAELGSVQDKvNAKLGQMESKTQHQMCVLDKLMVER 434
Cdd:cd22590    20 NQLHETLTRKQEEIDSLQER-NVQLKELASQAKHLASVLDKLMTVR 64
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-229 9.00e-52

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 180.92  E-value: 9.00e-52
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184   5 DAVAALSERLLIAAYKGQTENVVQLINKGAKV--AVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRA 82
Cdd:COG0666    48 ALADALGALLLLAAALAGDLLVALLLLAAGADinAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  83 TVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGDTCLHVAARYNHLSVVRLLLN 162
Cdd:COG0666   128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLE 207

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1907154184 163 AFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 229
Cdd:COG0666   208 AGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-229 2.46e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 177.07  E-value: 2.46e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184   1 MSQQDAVAALSERLLIAAYKGQTENVVQLINKGAKVAVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALH 80
Cdd:COG0666    13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  81 RATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGDTCLHVAARYNHLSVVRLL 160
Cdd:COG0666    93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907154184 161 LNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 229
Cdd:COG0666   173 LEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-211 6.15e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 173.22  E-value: 6.15e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  14 LLIAAYKGQTENVVQLINKGAKV-AVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILT 92
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVnARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  93 ALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQ 172
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907154184 173 AGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPL 211
Cdd:COG0666   251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-229 1.94e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.42  E-value: 1.94e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  24 ENVVQLINKGAKVAVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDR 103
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 104 QDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVAAA 183
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907154184 184 LNHKKVVKVLLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 229
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
55-226 1.25e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.13  E-value: 1.25e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  55 LSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANV 134
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 135 LARNKAGDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETA 214
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         170
                  ....*....|..
gi 1907154184 215 RYHNNPEVALLL 226
Cdd:COG0666   161 AANGNLEIVKLL 172
PHA03095 PHA03095
ankyrin-like protein; Provisional
 19-232 6.98e-25

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 108.57  E-value: 6.98e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  19 YKGQTENVVQ-LINKGAKV-AVTKHGRTPLHL-AANKG-HLSVVQILLKAGCDLDVQDDGDQTALH------RATVvgnt 88
Cdd:PHA03095   92 YNATTLDVIKlLIKAGADVnAKDKVGRTPLHVyLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLAvllksrNANV---- 167

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  89 EILTALIREGCALDRQDKDGNTALHEaawhgFSQSAK-------LLVKAGANVLARNKAGDTCLHVAARYNHL--SVVRL 159
Cdd:PHA03095  168 ELLRLLIDAGADVYAVDDRFRSLLHH-----HLQSFKprarivrELIRAGCDPAATDMLGNTPLHSMATGSSCkrSLVLP 242

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907154184 160 LLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETARYHNNPE-VALLLTKAPQI 232
Cdd:PHA03095  243 LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRaVRAALAKNPSA 316
PHA03095 PHA03095
ankyrin-like protein; Provisional
 24-229 1.17e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 104.72  E-value: 1.17e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  24 ENVVQLINKGAKVAVTK-HGRTPLHLAANKGH---LSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTE-ILTALIREG 98
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGeYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  99 CALDRQDKDGNTALHeAAWHGFSQSAK---LLVKAGANVLARNKAGDTCLHVAARYNHLSV--VRLLLNAFCSVHEK--- 170
Cdd:PHA03095  108 ADVNAKDKVGRTPLH-VYLSGFNINPKvirLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAVddr 186

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 171 --------------------------------NQAGDTALHVAAALNHKKVVKV--LLEAGADTTIVNNAGQTPLETARY 216
Cdd:PHA03095  187 frsllhhhlqsfkprarivreliragcdpaatDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAV 266

                         250
                  ....*....|...
gi 1907154184 217 HNNPEVALLLTKA 229
Cdd:PHA03095  267 FNNPRACRRLIAL 279
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 40-232 1.23e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 100.89  E-value: 1.23e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  40 KHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVG-----NTEILTALIREGCALDRQDKDGNTALHE 114
Cdd:PHA03100   33 KKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYGANVNAPDNNGITPLLY 112

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 115 AAWHGFSQSA--KLLVKAGANVLARNKAGDTCLHVAARYNH--LSVVRLLL------NAFCSV----------HEKNQAG 174
Cdd:PHA03100  113 AISKKSNSYSivEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIdkgvdiNAKNRVnyllsygvpiNIKDVYG 192

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907154184 175 DTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETARYHNNPE-VALLLTKAPQI 232
Cdd:PHA03100  193 FTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEiFKLLLNNGPSI 251
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 22-214 2.70e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 100.04  E-value: 2.70e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  22 QTENVVQLINKGAKVAV-TKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCA 100
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIkDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 101 LDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGDTCLHVAARYNHlSVVRLLLNAfCSVHEKNQAGDTALHv 180
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLH- 259

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1907154184 181 aAALNH---KKVVKVLLEAGADTTIVNNAGQTPLETA 214
Cdd:PHA02874  260 -HAINPpcdIDIIDILLYHKADISIKDNKGENPIDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
112-204 5.21e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.56  E-value: 5.21e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 112 LHEAAWHGFSQSAKLLVKAGANVLARNKAGDTCLHVAARYNHLSVVRLLLNAFCSvhEKNQAGDTALHVAAALNHKKVVK 191
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1907154184 192 VLLEAGADTTIVN 204
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
46-138 1.15e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.79  E-value: 1.15e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  46 LHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIrEGCALDRQDkDGNTALHEAAWHGFSQSAK 125
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1907154184 126 LLVKAGANVLARN 138
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
14-105 2.70e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 2.70e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  14 LLIAAYKGQTENVVQLINKGAKV-AVTKHGRTPLHLAANKGHLSVVQILLKaGCDLDVQDDGdQTALHRATVVGNTEILT 92
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAnLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNG-RTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1907154184  93 ALIREGCALDRQD 105
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 26-205 4.32e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 87.03  E-value: 4.32e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  26 VVQLINKGAKVAV-TKHGRTPLHLAANKGH-----LSVVQILLKAGCDLDVQDDGDQTALHRA--TVVGNTEILTALIRE 97
Cdd:PHA03100   51 VKILLDNGADINSsTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDN 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  98 GCALDRQDKDGNTALHEAAWHGFSQS--AKLLVKAGANV----------------LARNKAGDTCLHVAARYNHLSVVRL 159
Cdd:PHA03100  131 GANVNIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDInaknrvnyllsygvpiNIKDVYGFTPLHYAVYNNNPEFVKY 210

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1907154184 160 LLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTIVNN 205
Cdd:PHA03100  211 LLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 57-214 4.89e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 87.63  E-value: 4.89e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  57 VVQILLKAGCDLDVQD-DGDQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVL 135
Cdd:PHA02878  149 ITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 136 ARNKAGDTCLHVAARY-NHLSVVRLLLNAFCSVHEKNQA-GDTALHVaaALNHKKVVKVLLEAGADTTIVNNAGQTPLET 213
Cdd:PHA02878  229 ARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHS--SIKSERKLKLLLEYGADINSLNSYKLTPLSS 306


                  .
gi 1907154184 214 A 214
Cdd:PHA02878  307 A 307
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
89-229 1.09e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.24  E-value: 1.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  89 EILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGDTCLHVAARYNHLSVVRLLLNAFCSVH 168
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907154184 169 EKNQAGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 229
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
Ank_2 pfam12796
Ankyrin repeats (3 copies);
145-226 8.72e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 8.72e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 145 LHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEaGADTTIVNNaGQTPLETARYHNNPEVAL 224
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ..
gi 1907154184 225 LL 226
Cdd:pfam12796  79 LL 80
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 14-167 1.40e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 79.32  E-value: 1.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  14 LLIAAYK--GQTENVVQLINKGAKV-AVTKHGRTPLHLAA--NKGHLSVVQILLKAGCDLDVQDdgdqtalhratvvgNT 88
Cdd:PHA03100  110 LLYAISKksNSYSIVEYLLDNGANVnIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKN--------------RV 175

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907154184  89 EILtalIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGDTCLHVAARYNHLSVVRLLLNAFCSV 167
Cdd:PHA03100  176 NYL---LSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 15-229 1.51e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.62  E-value: 1.51e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  15 LIAAYKGQTENVVQL-INKGAKVA-VTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQtalhratvvgNTEILT 92
Cdd:PHA02874   39 LIDAIRSGDAKIVELfIKHGADINhINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPIPCI----------EKDMIK 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  93 ALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQ 172
Cdd:PHA02874  109 TILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDN 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907154184 173 AGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 229
Cdd:PHA02874  189 NGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNA 245
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 49-204 3.28e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 79.53  E-value: 3.28e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  49 AANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLV 128
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1907154184 129 KAGAnvLARNKAGDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTIVN 204
Cdd:PLN03192  612 HFAS--ISDPHAAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 26-218 1.02e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 74.71  E-value: 1.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  26 VVQLINKGAKV-AVTKHGRTPLHLAANKGH-LSVVQILLKAGCDLDVQDDGDQTALHRATVVG-NTEILTALIREGCALD 102
Cdd:PHA02876  290 VPKLLERGADVnAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVN 369

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 103 RQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGDTCLHVA-ARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVA 181
Cdd:PHA02876  370 ARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYA 449

                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 1907154184 182 AALNHK-KVVKVLLEAGADTTIVNNAGQTPLETA-RYHN 218
Cdd:PHA02876  450 CKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAlEYHG 488
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 43-221 1.19e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.41  E-value: 1.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  43 RTPLHLAANKGHLSVVQILLKAGCDLD--VQDDGDqTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGF 120
Cdd:PHA02875   69 ESELHDAVEEGDVKAVEELLDLGKFADdvFYKDGM-TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGD 147

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 121 SQSAKLLVKAGANVLARNKAGDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVAAALNHK-KVVKVLLEAGAD 199
Cdd:PHA02875  148 IKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGAD 227

                         170       180
                  ....*....|....*....|....*.
gi 1907154184 200 TTI---VNNAGQTPLETAR-YHNNPE 221
Cdd:PHA02875  228 CNImfmIEGEECTILDMICnMCTNLE 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 14-226 1.55e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.86  E-value: 1.55e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  14 LLIAAYKGQTENVVQLINKGAKV-AVTKHGRTPLHLAANKGHLS-VVQILLKAGCDLDVQDDGDQTALHRATVVG-NTEI 90
Cdd:PHA02876  244 LLKAIRNEDLETSLLLYDAGFSVnSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTEN 323

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  91 LTALIREGCALDRQDKDGNTALHEAA-WHGFSQSAKLLVKAGANVLARNKAGDTCLHVAARYNHLSVVRLLLNAFCSVHE 169
Cdd:PHA02876  324 IRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA 403

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907154184 170 KNQAGDTALHVA-AALNHKKVVKVLLEAGADTTIVNNAGQTPLETARYHN-NPEVALLL 226
Cdd:PHA02876  404 LSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEML 462
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 17-161 3.90e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.40  E-value: 3.90e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  17 AAYKGQTENVVQLI--NKGAKVAVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTAL 94
Cdd:PHA02875   75 AVEEGDVKAVEELLdlGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907154184  95 IREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGD-TCLHVAARYNHLSVVRLLL 161
Cdd:PHA02875  155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFI 222
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 29-219 5.99e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.86  E-value: 5.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  29 LINKGAKV-AVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRAT------------------------ 83
Cdd:PHA02876  164 LLEGGADVnAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVdsknidtikaiidnrsninkndls 243

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  84 ---VVGNTEILTALI--REGCALDRQDKDGNTALHEAAWH-GFSQSAKLLVKAGANVLARNKAGDTCLHVAARYNH-LSV 156
Cdd:PHA02876  244 llkAIRNEDLETSLLlyDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTEN 323

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1907154184 157 VRLLLNAFCSVHEKNQAGDTALHVAAALN-HKKVVKVLLEAGADTTIVNNAGQTPLETARYHNN 219
Cdd:PHA02876  324 IRTLIMLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNN 387
Ank_4 pfam13637
Ankyrin repeats (many copies);
42-95 9.88e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 57.28  E-value: 9.88e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907154184  42 GRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALI 95
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
141-194 5.37e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 5.37e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907154184 141 GDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLL 194
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 44-222 1.03e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 61.57  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  44 TPLHLAANKGHLSVVQILLK-AGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQDK-----DGNTALHEAAW 117
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMtsdlyQGETALHIAVV 98

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 118 HGFSQSAKLLVKAGANVLA---------RNKA-----GDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVAAA 183
Cdd:cd22192    99 NQNLNLVRELIARGADVVSpratgtffrPGPKnliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVL 178

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 1907154184 184 LNHKKVVKVL------LEAGADT----TIVNNAGQTPLETARYHNNPEV 222
Cdd:cd22192   179 QPNKTFACQMydlilsYDKEDDLqpldLVPNNQGLTPFKLAAKEGNIVM 227
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 42-228 1.47e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.78  E-value: 1.47e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  42 GRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGC-ALDRQDKDGNTALHEAAWHGF 120
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfADDVFYKDGMTPLHLATILKK 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 121 SQSAKLLVKAGANVLARNKAGDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADT 200
Cdd:PHA02875  115 LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194

                         170       180
                  ....*....|....*....|....*....
gi 1907154184 201 TIVNNAGQ-TPLETARYHNNPEVALLLTK 228
Cdd:PHA02875  195 DYFGKNGCvAALCYAIENNKIDIVRLFIK 223
Ank_4 pfam13637
Ankyrin repeats (many copies);
108-161 2.62e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 2.62e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1907154184 108 GNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGDTCLHVAARYNHLSVVRLLL 161
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
40-82 4.58e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 52.73  E-value: 4.58e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1907154184  40 KHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRA 82
Cdd:pfam13857  14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
127-181 2.78e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.42  E-value: 2.78e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907154184 127 LVKAG-ANVLARNKAGDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVA 181
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 157-231 2.92e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 2.92e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1907154184 157 VRLLLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKAPQ 231
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172
Ank_4 pfam13637
Ankyrin repeats (many copies);
174-226 3.37e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 3.37e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1907154184 174 GDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETARYHNNPEVALLL 226
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 41-73 3.62e-08

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: 49.60  E-value: 3.62e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907154184  41 HGRTPLHLAANK-GHLSVVQILLKAGCDLDVQDD 73
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 55-211 6.72e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.84  E-value: 6.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  55 LSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANV 134
Cdd:PHA02876  158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1907154184 135 larNKaGDTCLHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVAA-ALNHKKVVKVLLEAGADTTIVNNAGQTPL 211
Cdd:PHA02876  238 ---NK-NDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPL 311
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 131-228 1.14e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 55.02  E-value: 1.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 131 GANVLARNKAGDTCLHVAARYNHL-SVVRLLLNAFCSVHEKNQAGDTALHVAAALNHKKVVKVLLEagADTTIVNNA--- 206
Cdd:cd22192     7 ELHLLQQKRISESPLLLAAKENDVqAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPmts 84

                          90       100
                  ....*....|....*....|....*..
gi 1907154184 207 ----GQTPLETARYHNNPE-VALLLTK 228
Cdd:cd22192    85 dlyqGETALHIAVVNQNLNlVRELIAR 111
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 109-199 2.94e-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: 53.86  E-value: 2.94e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 109 NTALHEAAWHGFSQSAK-LLVKAGANVLARNKAGDTCLHVAARYNHLSVVRLLLNAfcsVHE-KNQA-------GDTALH 179
Cdd:cd22192    18 ESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEA---APElVNEPmtsdlyqGETALH 94

                          90       100
                  ....*....|....*....|
gi 1907154184 180 VAAALNHKKVVKVLLEAGAD 199
Cdd:cd22192    95 IAVVNQNLNLVRELIARGAD 114
Ank_2 pfam12796
Ankyrin repeats (3 copies);
178-240 8.15e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.42  E-value: 8.15e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907154184 178 LHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKAPQILRFSRGRS 240
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 41-70 1.31e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 44.89  E-value: 1.31e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1907154184   41 HGRTPLHLAANKGHLSVVQILLKAGCDLDV 70
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 11-183 1.37e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.55  E-value: 1.37e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  11 SERLLIAAYKgqtENVVQLINKGAKVAVTK------HGRTPLHLAANKGHLSVVQILLKAGCDL-DVQDDGD----QTAL 79
Cdd:cd22192    17 SESPLLLAAK---ENDVQAIKKLLKCPSCDlfqrgaLGETALHVAALYDNLEAAVVLMEAAPELvNEPMTSDlyqgETAL 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  80 HRATVVGNTEILTALIREG-----------CALDRQDKD---GNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGDTCL 145
Cdd:cd22192    94 HIAVVNQNLNLVRELIARGadvvspratgtFFRPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1907154184 146 HVAARYNHLSVVRLLLNAFCSV----------HEKNQAGDTALHVAAA 183
Cdd:cd22192   174 HILVLQPNKTFACQMYDLILSYdkeddlqpldLVPNNQGLTPFKLAAK 221
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 87-218 1.77e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 49.43  E-value: 1.77e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  87 NTEILTALIREGCALDRQDKDGN-TALHeaAWHGFSQSA-----KLLVKAGANVLARNKAGDTCLHV-AARYN-HLSVVR 158
Cdd:PHA02859   65 NVEILKFLIENGADVNFKTRDNNlSALH--HYLSFNKNVepeilKILIDSGSSITEEDEDGKNLLHMyMCNFNvRINVIK 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907154184 159 LLLNAFCSVHEKNQAGDTALHVAAAL-NHKKVVKVLLEAGADTTIVNNAGQTPLETARYHN 218
Cdd:PHA02859  143 LLIDSGVSFLNKDFDNNNILYSYILFhSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
Ank_5 pfam13857
Ankyrin repeats (many copies);
160-214 1.92e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 1.92e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907154184 160 LLNAF-CSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETA 214
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02791 PHA02791
ankyrin-like protein; Provisional
 41-169 4.53e-06

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 48.88  E-value: 4.53e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  41 HGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDgdQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGF 120
Cdd:PHA02791   29 HGHSALYYAIADNNVRLVCTLLNAGALKNLLEN--EFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGN 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1907154184 121 SQSAKLLVKAGANVLARNKAG-DTCLHVAARYNHLSVVRLLLNAFCSVHE 169
Cdd:PHA02791  107 MQTVKLFVKKNWRLMFYGKTGwKTSFYHAVMLNDVSIVSYFLSEIPSTFD 156
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 10-96 4.84e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 4.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  10 LSERLLIAAYKGQTENVVQLINKGAKV-AVTKHGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNT 88
Cdd:PTZ00322   82 LTVELCQLAASGDAVGARILLTGGADPnCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161


                  ....*...
gi 1907154184  89 EILTALIR 96
Cdd:PTZ00322  162 EVVQLLSR 169
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 29-144 4.88e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 47.89  E-value: 4.88e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  29 LINKGAKV-AVTKH-GRTPLH--LAANKG-HLSVVQILLKAGCDLDVQDDGDQTALHR--ATVVGNTEILTALIREGCAL 101
Cdd:PHA02859   72 LIENGADVnFKTRDnNLSALHhyLSFNKNvEPEILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLIDSGVSF 151

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1907154184 102 DRQDKDGNTALHE-AAWHGFSQSAKLLVKAGANVLARNKAGDTC 144
Cdd:PHA02859  152 LNKDFDNNNILYSyILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 174-205 6.09e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 43.43  E-value: 6.09e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1907154184 174 GDTALHVAAA-LNHKKVVKVLLEAGADTTIVNN 205
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 107-139 9.66e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 9.66e-06
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1907154184 107 DGNTALHEAAWH-GFSQSAKLLVKAGANVLARNK 139
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 41-70 1.19e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 42.24  E-value: 1.19e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 1907154184  41 HGRTPLHLAANKGHLSVVQILLKAGCDLDV 70
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 108-214 2.25e-05

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 47.54  E-value: 2.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 108 GNTALHEAAWHGFSQSAKLLVKAGANVLAR------NKAGDTC-------LHVAARYNHLSVVRLLLN---AFCSVHEKN 171
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVENGADVHARacgrffQKKQGTCfyfgelpLSLAACTKQWDVVNYLLEnphQPASLQAQD 173

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1907154184 172 QAGDTALH--VAAALNHKK----VVKV---LLEAGADTT-------IVNNAGQTPLETA 214
Cdd:cd22197   174 SLGNTVLHalVMIADNSPEnsalVIKMydgLLQAGARLCptvqleeISNHEGLTPLKLA 232
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 71-169 2.27e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.59  E-value: 2.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  71 QDDGDQTALHRATV-------VGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGDT 143
Cdd:PTZ00322   71 EEVIDPVVAHMLTVelcqlaaSGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKT 150

                          90       100
                  ....*....|....*....|....*.
gi 1907154184 144 CLHVAARYNHLSVVRLLLNAFCSVHE 169
Cdd:PTZ00322  151 PLELAEENGFREVVQLLSRHSQCHFE 176
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 42-226 2.81e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.38  E-value: 2.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  42 GRTPLHLAANKG-HLSVVQILLKAGCDLDVQDdgdqTALHRAT--VVGNTEILTALI----REGC----ALDRQDKD--- 107
Cdd:TIGR00870  52 GRSALFVAAIENeNLELTELLLNLSCRGAVGD----TLLHAISleYVDAVEAILLHLlaafRKSGplelANDQYTSEftp 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 108 GNTALHEAAWHGFSQSAKLLVKAGANVLARNKaGDTC---------------LHVAARYNHLSVVRLLLNAFCSVHEKNQ 172
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARAC-GDFFvksqgvdsfyhgespLNAAACLGSPSIVALLSEDPADILTADS 206

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 173 AGDTALHVAAALNHKKV------------VKVLLEAGADTT----IVNNAGQTPLETARYHNNPEVALLL 226
Cdd:TIGR00870 207 LGNTLLHLLVMENEFKAeyeelscqmynfALSLLDKLRDSKelevILNHQGLTPLKLAAKEGRIVLFRLK 276
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 13-226 2.95e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.18  E-value: 2.95e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  13 RLLIAAYKGQTENVVQLINKGAKvavTKHGRT--------PLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTALHRATV 84
Cdd:PHA02878    3 KLYKSMYTDNYETILKYIEYIDH---TENYSTsaslipfiPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICK 79

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  85 VGNTEILTALIREgcalDRQDKDGNT--ALHEAAWHGFSQSAKLLVkagANVLARNKAGDTCLHVAARYNHL---SVVRL 159
Cdd:PHA02878   80 EPNKLGMKEMIRS----INKCSVFYTlvAIKDAFNNRNVEIFKIIL---TNRYKNIQTIDLVYIDKKSKDDIieaEITKL 152

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907154184 160 LLNAFCSVHEKNQ-AGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETA-RYHNNPEVALLL 226
Cdd:PHA02878  153 LLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAvKHYNKPIVHILL 221
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 75-230 4.37e-05

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 46.68  E-value: 4.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  75 DQTALHRATVVGNTEILTALIREgcALDRQDKDGNTALHEAAWHGFSQSAK---LLVKAGANVLARNKAGDTCLHVAARY 151
Cdd:cd22194    45 DKKKRLKKVSEAAVEELGELLKE--LKDLSRRRRKTDVPDFLMHKLTASDTgktCLMKALLNINENTKEIVRILLAFAEE 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 152 NhlSVVRLLLNAfcSVHEKNQAGDTALHVAAALNHKKVVKVLLEAGADTTI---------VNNA-----GQTPLETARYH 217
Cdd:cd22194   123 N--GILDRFINA--EYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHegfyfGETPLALAACT 198

                         170
                  ....*....|....
gi 1907154184 218 NNPE-VALLLTKAP 230
Cdd:cd22194   199 NQPEiVQLLMEKES 212
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 29-211 5.27e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 46.44  E-value: 5.27e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  29 LINKGAKVAV-TKHGRTPLHLAANKGHLS--VVQILLKAGCDLDVQddgdqtalhraTVVGNTEILTALIR------EGC 99
Cdd:PHA02716  198 LCNNGVNVNLqNNHLITPLHTYLITGNVCasVIKKIIELGGDMDMK-----------CVNGMSPIMTYIINidninpEIT 266

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 100 ALDRQDKDGNTALH-EAAWHGFSQSA--------KLLVKAGANVLARNKAGDTCLH--VAARYNHLSVVRLLLNAFCSVH 168
Cdd:PHA02716  267 NIYIESLDGNKVKNiPMILHSYITLArnidisvvYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLN 346

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1907154184 169 EKNQAGDTALH-------VAAALNHK-------KVVKVLLEAGADTTIVNNAGQTPL 211
Cdd:PHA02716  347 EPDNIGNTVLHtylsmlsVVNILDPEtdndirlDVIQCLISLGADITAVNCLGYTPL 403
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 47-127 6.86e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 6.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  47 HLAANkGHLSVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKL 126
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  .
gi 1907154184 127 L 127
Cdd:PTZ00322  167 L 167
Ank_5 pfam13857
Ankyrin repeats (many copies);
94-148 8.75e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 8.75e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1907154184  94 LIREG-CALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGDTCLHVA 148
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 174-202 1.01e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.88  E-value: 1.01e-04
                           10        20
                   ....*....|....*....|....*....
gi 1907154184  174 GDTALHVAAALNHKKVVKVLLEAGADTTI 202
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 141-171 1.04e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 39.97  E-value: 1.04e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1907154184 141 GDTCLHVAA-RYNHLSVVRLLLNAFCSVHEKN 171
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 141-169 1.09e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 1.09e-04
                           10        20
                   ....*....|....*....|....*....
gi 1907154184  141 GDTCLHVAARYNHLSVVRLLLNAFCSVHE 169
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 154-229 2.18e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 154 LSVVRLLLNAFCSVHEKNQAGDTALHVAAALNH---KKVVKVLLEAGADTTIVNNAGQTPLETARYHNN-PEVALLLTKA 229
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKA 106
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 42-162 2.38e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 44.36  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  42 GRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEILTaLIREGCALD--RQD 105
Cdd:cd22194   141 GQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIVQ-LLMEKESTDitSQD 219

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1907154184 106 KDGNTALH---EAAWHGFSQSA-------KLLVKAGANVL--ARNKAGDTCLHVAARYNHLSVVRLLLN 162
Cdd:cd22194   220 SRGNTVLHalvTVAEDSKTQNDfvkrmydMILLKSENKNLetIRNNEGLTPLQLAAKMGKAEILKYILS 288
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 174-199 8.75e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 8.75e-04
                          10        20
                  ....*....|....*....|....*.
gi 1907154184 174 GDTALHVAAALNHKKVVKVLLEAGAD 199
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGAD 27
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 108-214 1.01e-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: 42.48  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 108 GNTALHEAAWHGFSQSAKLLVKAGANVLARNKA--------------GDTCLHVAARYNHLSVVRLLL-NAF--CSVHEK 170
Cdd:cd22193    76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLeNEHqpADIEAQ 155

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 171 NQAGDTALH--VAAALNHK-------KVVKVLLEAGAD-------TTIVNNAGQTPLETA 214
Cdd:cd22193   156 DSRGNTVLHalVTVADNTKentkfvtRMYDMILIRGAKlcptvelEEIRNNDGLTPLQLA 215
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 141-169 1.32e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 1.32e-03
                          10        20
                  ....*....|....*....|....*....
gi 1907154184 141 GDTCLHVAARYNHLSVVRLLLNAFCSVHE 169
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 134-228 1.48e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.86  E-value: 1.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 134 VLARNKAGDTCLHVAARYNHL---SVVRLLLNAFCSVHEKNQA-GDTALHVAAALNHKKVVKVLL-EAGADTTIVNNAGQ 208
Cdd:PHA02736   48 VLEYNRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFK 127

                          90       100
                  ....*....|....*....|
gi 1907154184 209 TPLETARYHNNPEVALLLTK 228
Cdd:PHA02736  128 TPYYVACERHDAKMMNILRA 147
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 75-214 1.89e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.13  E-value: 1.89e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  75 DQTALHRATVVGNTEILTALIREGCALDRQDKDGNTALHEAAWHGFSQSAKLLVKAGANVLARNKAGDTCLHVAARYNHL 154
Cdd:PHA02875    2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1907154184 155 SVVRLLL--NAFCS-VHEKNqaGDTALHVAAALNHKKVVKVLLEAGADTTIVNNAGQTPLETA 214
Cdd:PHA02875   82 KAVEELLdlGKFADdVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLA 142
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 107-134 1.98e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 1.98e-03
                           10        20
                   ....*....|....*....|....*...
gi 1907154184  107 DGNTALHEAAWHGFSQSAKLLVKAGANV 134
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02798 PHA02798
ankyrin-like protein; Provisional
 125-212 2.05e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.36  E-value: 2.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 125 KLLVKAGANV--LARNKAGDTC--LHVAARYNH-LSVVRLLLNAFCSVHEKNQAGDTALHVA---AALNHKKVVKVLLEA 196
Cdd:PHA02798   55 KLFINLGANVngLDNEYSTPLCtiLSNIKDYKHmLDIVKILIENGADINKKNSDGETPLYCLlsnGYINNLEILLFMIEN 134

                          90
                  ....*....|....*.
gi 1907154184 197 GADTTIVNNAGQTPLE 212
Cdd:PHA02798  135 GADTTLLDKDGFTMLQ 150
PHA02798 PHA02798
ankyrin-like protein; Provisional
 55-205 2.61e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.97  E-value: 2.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  55 LSVVQILLKAgCDLDV---QDDGDQTALHRATVvgNTEILTALIREGCALDRQDKDGNTAL-----HEAAWHGFSQSAKL 126
Cdd:PHA02798   18 LSTVKLLIKS-CNPNEivnEYSIFQKYLQRDSP--STDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKI 94

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 127 LVKAGANVLARNKAGDT---CLHVAARYNHLSVVRLLLNAFCSVHEKNQAGDTALHVAAALNHK---KVVKVLLEAGADT 200
Cdd:PHA02798   95 LIENGADINKKNSDGETplyCLLSNGYINNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDI 174


                  ....*
gi 1907154184 201 TIVNN 205
Cdd:PHA02798  175 NTHNN 179
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 41-161 3.98e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.45  E-value: 3.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  41 HGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEILTALIREGCALDRQDK 106
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1907154184 107 DGNTALH--------EAAWHGFSQSAK-LLVKAGANV-------LARNKAGDTCLHVAARYNHLSVVRLLL 161
Cdd:TIGR00870 207 LGNTLLHllvmenefKAEYEELSCQMYnFALSLLDKLrdskeleVILNHQGLTPLKLAAKEGRIVLFRLKL 277
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 14-119 5.33e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.00  E-value: 5.33e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184  14 LLIAAYKGQTENVVQLINKGAKVAVTK---------------HGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGDQTA 78
Cdd:cd22192    93 LHIAVVNQNLNLVRELIARGADVVSPRatgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTV 172

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1907154184  79 LHRATVVGNTEILT----------ALIREGCaLDR-QDKDGNTALHEAAWHG 119
Cdd:cd22192   173 LHILVLQPNKTFACqmydlilsydKEDDLQP-LDLvPNNQGLTPFKLAAKEG 223
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 4-113 6.02e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 39.86  E-value: 6.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184   4 QDAVAALSERLLIAAYKgqTENVVQLINKGAKVAVTKhGRTPLHLAANKGHLSVVQILLKAGCDLDVQDDGD-------- 75
Cdd:cd21882    38 NDGVNEAIMLLLEAAPD--SGNPKELVNAPCTDEFYQ-GQTALHIAIENRNLNLVRLLVENGADVSARATGRffrkspgn 114

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1907154184  76 -----QTALHRATVVGNTEILTALIREG---CALDRQDKDGNTALH 113
Cdd:cd21882   115 lfyfgELPLSLAACTNQEEIVRLLLENGaqpAALEAQDSLGNTVLH 160
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 141-234 6.11e-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: 39.68  E-value: 6.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1907154184 141 GDTCLHvAARYNHLSVVRLLLNAFCSVHEKN--------------QAGDTALHVAAALNHKKVVKVLLEAGADTTIVNNA 206
Cdd:TIGR00870  82 GDTLLH-AISLEYVDAVEAILLHLLAAFRKSgplelandqytsefTPGITALHLAAHRQNYEIVKLLLERGASVPARACG 160

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1907154184 207 --------------GQTPLETARYHNNPEVALLLTKAPQILR 234
Cdd:TIGR00870 161 dffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADIL 202
McIdas_CC cd22590
central coiled-coil domain of McIdas (or multicilin); McIdas (also called Idas or multicilin), ...
 389-434 8.70e-03

central coiled-coil domain of McIdas (or multicilin); McIdas (also called Idas or multicilin), together with geminin coiled-coil domain-containing protein 1 (GemC1) and geminin, controls both the cell cycle and differentiation decisions in cells. Idas binds to geminin and is implicated in DNA replication control. It also functions as an early regulator of multiciliogenesis. GemC1 and McIdas specify the multiciliate cell fate by forming complexes with the E2F4/5 transcription factors, resulting in centriole amplification and cilia formation. Idas belongs to the geminin family of proteins that also includes geminin and GemC1. They share a homologous central coiled-coil domain that mediates homo- and heterodimerization with other family members; this ability is likely to be important for modulating their function in cycling and differentiating cells. This model represents the central coiled-coil domain of McIdas.


Pssm-ID: 439144  Cd Length: 64  Bit Score: 35.16  E-value: 8.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1907154184 389 NQLEATVEEIRAELGSVQDKvNAKLGQMESKTQHQMCVLDKLMVER 434
Cdd:cd22590    20 NQLHETLTRKQEEIDSLQER-NVQLKELASQAKHLASVLDKLMTVR 64
 
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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