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Conserved domains on  [gi|2000138002|emb|CAF0316078|]
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unnamed protein product, partial [Bigelowiella sp. RCC560]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-206 6.66e-24

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.56  E-value: 6.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  12 ALVKASKENNLQEVSLLLSQKTDPNGATGHGISPLLVACTNGNVEIVRELIKAKAKIGVKKKNGQTTLLCAAASGSVETV 91
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  92 QCILEAKADLTHTDNQNWSAYSFACHNGYNNILSLLVKAK-LPSLKNLN--SLLRLAAQVDQANCCQYLLDLKANPNDQD 168
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGaDVNAKDNDgkTALDLAAENGNLEIVKLLLEAGADLNAKD 249

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2000138002 169 LDNFTASMYAIENRCNIKTLRTLLNAKAHIGVDNFDIA 206
Cdd:COG0666   250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-206 6.66e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.56  E-value: 6.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  12 ALVKASKENNLQEVSLLLSQKTDPNGATGHGISPLLVACTNGNVEIVRELIKAKAKIGVKKKNGQTTLLCAAASGSVETV 91
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  92 QCILEAKADLTHTDNQNWSAYSFACHNGYNNILSLLVKAK-LPSLKNLN--SLLRLAAQVDQANCCQYLLDLKANPNDQD 168
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGaDVNAKDNDgkTALDLAAENGNLEIVKLLLEAGADLNAKD 249

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2000138002 169 LDNFTASMYAIENRCNIKTLRTLLNAKAHIGVDNFDIA 206
Cdd:COG0666   250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
13-105 1.68e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.59  E-value: 1.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  13 LVKASKENNLQEVSLLLSQKTDPNGATGHGISPLLVACTNGNVEIVRELIKAKAkiGVKKKNGQTTLLCAAASGSVETVQ 92
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2000138002  93 CILEAKADLTHTD 105
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 10-202 1.50e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.12  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  10 KIALVKASKENNLQEVSLLLSQKTDPNGATGHGISPLLVACTNGNVEIVRELIKAKAKIGVKKKNGQTTLLCAAASGSVE 89
Cdd:PHA02874  125 KTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYA 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  90 TVQCIleakadLTHTDNqnwsaYSFACHNGYNNILSLLV--KAKLPSLKNLNSLlrlaaqvdqanccqylldlkanpNDQ 167
Cdd:PHA02874  205 CIKLL------IDHGNH-----IMNKCKNGFTPLHNAIIhnRSAIELLINNASI-----------------------NDQ 250

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2000138002 168 DLDNFTASMYAIENRCNIKTLRTLLNAKAHIGV-DN 202
Cdd:PHA02874  251 DIDGSTPLHHAINPPCDIDIIDILLYHKADISIkDN 286
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 8-100 9.36e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.08  E-value: 9.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002   8 IAKIALVKASKENNLQEVS-LLLSQKTDPNGATGHGISPLLVACTNGNVEIVRELIKA-----KAKIGVKKKNGQTTLLC 81
Cdd:cd22192    16 ISESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHI 95

                          90
                  ....*....|....*....
gi 2000138002  82 AAASGSVETVQCILEAKAD 100
Cdd:cd22192    96 AVVNQNLNLVRELIARGAD 114
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 41-68 6.63e-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: 33.33  E-value: 6.63e-03
                           10        20
                   ....*....|....*....|....*...
gi 2000138002   41 HGISPLLVACTNGNVEIVRELIKAKAKI 68
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 12-101 9.56e-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: 36.98  E-value: 9.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  12 ALVKASKENNLQEV-SLLLSQKTDpnGATGHGispLLVACTNGNVEIVRELIKAKAKIGVKKKN--------------GQ 76
Cdd:TIGR00870  55 ALFVAAIENENLELtELLLNLSCR--GAVGDT---LLHAISLEYVDAVEAILLHLLAAFRKSGPlelandqytseftpGI 129

                          90       100
                  ....*....|....*....|....*
gi 2000138002  77 TTLLCAAASGSVETVQCILEAKADL 101
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASV 154
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-206 6.66e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 96.56  E-value: 6.66e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  12 ALVKASKENNLQEVSLLLSQKTDPNGATGHGISPLLVACTNGNVEIVRELIKAKAKIGVKKKNGQTTLLCAAASGSVETV 91
Cdd:COG0666    90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  92 QCILEAKADLTHTDNQNWSAYSFACHNGYNNILSLLVKAK-LPSLKNLN--SLLRLAAQVDQANCCQYLLDLKANPNDQD 168
Cdd:COG0666   170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGaDVNAKDNDgkTALDLAAENGNLEIVKLLLEAGADLNAKD 249

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 2000138002 169 LDNFTASMYAIENRCNIKTLRTLLNAKAHIGVDNFDIA 206
Cdd:COG0666   250 KDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
3-230 3.31e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.64  E-value: 3.31e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002   3 LKMASIAKIALVKASKENNLQEVSLLLSQKTDPNGATGHGISPLLVACTNGNVEIVRELIKAKAKIGVKKKNGQTTLLCA 82
Cdd:COG0666    48 ALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  83 AASGSVETVQCILEAKADLTHTDNQNWSAYSFACHNGYNNILSLLVKAKLP---SLKNLNSLLRLAAQVDQANCCQYLLD 159
Cdd:COG0666   128 AYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADvnaRDNDGETPLHLAAENGHLEIVKLLLE 207

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2000138002 160 LKANPNDQDLDNFTASMYAIENRcNIKTLRTLLNAKAHIGVDNFDIARLSCPIRSVKHAKHTVIIERKPRI 230
Cdd:COG0666   208 AGADVNAKDNDGKTALDLAAENG-NLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-174 5.58e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.86  E-value: 5.58e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  12 ALVKASKENNLQEVSLLLSQKTDPNGATGHGISPLLVACTNGNVEIVRELIKAKAKIGVKKKNGQTTLLCAAASGSVETV 91
Cdd:COG0666   123 PLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  92 QCILEAKADLTHTDNQNWSAYSFACHNGYNNILSLLVKA---KLPSLKNLNSLLRLAAQVDQANCCQYLLDLKANPNDQD 168
Cdd:COG0666   203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAgadLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282


                  ....*.
gi 2000138002 169 LDNFTA 174
Cdd:COG0666   283 LDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-198 4.73e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.07  E-value: 4.73e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002   2 KLKMASIAKIALVKASKENNLQEVSLLLSQKTDPNGATGHGISPLLVACTNGNVEIVRELIKAKAKIGVKKKNGQTTLLC 81
Cdd:COG0666    14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHA 93

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  82 AAASGSVETVQCILEAKADLTHTDNQNWSAYSFACHNGYNNILSLLVKAKLP---SLKNLNSLLRLAAQVDQANCCQYLL 158
Cdd:COG0666    94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADvnaQDNDGNTPLHLAAANGNLEIVKLLL 173

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2000138002 159 DLKANPNDQDLDNFTASMYAIENRcNIKTLRTLLNAKAHI 198
Cdd:COG0666   174 EAGADVNARDNDGETPLHLAAENG-HLEIVKLLLEAGADV 212
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
12-145 1.18e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 71.52  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  12 ALVKASKENNLQEVSLLLSQKTDPNGATGHGISPLLVACTNGNVEIVRELIKAKAKIGVKKKNGQTTLLCAAASGSVETV 91
Cdd:COG0666   156 PLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIV 235

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2000138002  92 QCILEAKADLTHTDNQNWSAYSFACHNGYNNILSLLVKAKLPSLKNLNSLLRLA 145
Cdd:COG0666   236 KLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
13-105 1.68e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.59  E-value: 1.68e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  13 LVKASKENNLQEVSLLLSQKTDPNGATGHGISPLLVACTNGNVEIVRELIKAKAkiGVKKKNGQTTLLCAAASGSVETVQ 92
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2000138002  93 CILEAKADLTHTD 105
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
46-129 1.19e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 1.19e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  46 LLVACTNGNVEIVRELIKAKAKIGVKKKNGQTTLLCAAASGSVETVQCILEaKADLTHTDNqNWSAYSFACHNGYNNILS 125
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ....
gi 2000138002 126 LLVK 129
Cdd:pfam12796  79 LLLE 82
Ank_2 pfam12796
Ankyrin repeats (3 copies);
79-168 8.04e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.97  E-value: 8.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  79 LLCAAASGSVETVQCILEAKADLTHTDNQNWSAYSFACHNGYNNILSLLVKAKLPSLKNL-NSLLRLAAQVDQANCCQYL 157
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNgRTALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 2000138002 158 LDLKANPNDQD 168
Cdd:pfam12796  81 LEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 10-202 1.50e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.12  E-value: 1.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  10 KIALVKASKENNLQEVSLLLSQKTDPNGATGHGISPLLVACTNGNVEIVRELIKAKAKIGVKKKNGQTTLLCAAASGSVE 89
Cdd:PHA02874  125 KTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYA 204

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  90 TVQCIleakadLTHTDNqnwsaYSFACHNGYNNILSLLV--KAKLPSLKNLNSLlrlaaqvdqanccqylldlkanpNDQ 167
Cdd:PHA02874  205 CIKLL------IDHGNH-----IMNKCKNGFTPLHNAIIhnRSAIELLINNASI-----------------------NDQ 250

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2000138002 168 DLDNFTASMYAIENRCNIKTLRTLLNAKAHIGV-DN 202
Cdd:PHA02874  251 DIDGSTPLHHAINPPCDIDIIDILLYHKADISIkDN 286
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 25-95 1.28e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.74  E-value: 1.28e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2000138002  25 VSLLLSQKTDPNGATGHGISPLLVACTNGNVEIVRELIKAKAKIGVKKKNGQTTLLCAAASGSVETVQCIL 95
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 16-129 2.32e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.68  E-value: 2.32e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  16 ASKENNLQEVSLLLSQKTDPNGATGHGISPLLVACTNGNVEIVRELIKAKAKIGVKKKNGQTTLLCAAASGSVETVQCIL 95
Cdd:PHA02875  109 ATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLL 188

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2000138002  96 EAKADLTH-TDNQNWSAYSFACHNGYNNILSLLVK 129
Cdd:PHA02875  189 DSGANIDYfGKNGCVAALCYAIENNKIDIVRLFIK 223
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 10-198 3.16e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.35  E-value: 3.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  10 KIALVKASKENNLQEVSLLLSQKTDPNGATGHGISPLLVACTN--GNVEIVRELIKAKAKIGVKKKNGQTTLLCAAASGS 87
Cdd:PHA03100   74 YLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNK 153

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  88 VET--VQCILEAKADLthtdnqnwsaysfachNGYNNILSLLVKAKLPSLKNL--NSLLRLAAQVDQANCCQYLLDLKAN 163
Cdd:PHA03100  154 IDLkiLKLLIDKGVDI----------------NAKNRVNYLLSYGVPINIKDVygFTPLHYAVYNNNPEFVKYLLDLGAN 217

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2000138002 164 PNDQDLDNFTASMYAIENrCNIKTLRTLLNAKAHI 198
Cdd:PHA03100  218 PNLVNKYGDTPLHIAILN-NNKEIFKLLLNNGPSI 251
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 10-198 6.98e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.14  E-value: 6.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  10 KIALVKASKENNLQEVSLLLSQKTDPNGATGHGISPLLVACTNGNVEIVRELIKAKAKIGVKKKNGQTTLLCAAASGSVE 89
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  90 TVQCILEAKA---DLTHTDNQnwSAYSFACHNGYNNILSLLVKAKL-PSLKNLN--SLLRLAAQVDQANCCQYLLDLKAN 163
Cdd:PHA02875   83 AVEELLDLGKfadDVFYKDGM--TPLHLATILKKLDIMKLLIARGAdPDIPNTDkfSPLHLAVMMGDIKGIELLIDHKAC 160

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2000138002 164 PNDQDLDNFTASMYAIENRcNIKTLRTLLNAKAHI 198
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKG-DIAICKMLLDSGANI 194
PHA03095 PHA03095
ankyrin-like protein; Provisional
 24-203 9.49e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.79  E-value: 9.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  24 EVSLLLSQKTDPNGATGHGISPL--LVACTNGNV-EIVRELIKAKAKIGVKKKNGQTTLLCAAASGSVETV-QCILEAKA 99
Cdd:PHA03095   29 EVRRLLAAGADVNFRGEYGKTPLhlYLHYSSEKVkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDViKLLIKAGA 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002 100 DLThtdnqnwsaysfACHNGYNNILSLlvkaklpSLKNLNsllrlaaqVDqANCCQYLLDLKANPNDQDLDNFTA-SMYA 178
Cdd:PHA03095  109 DVN------------AKDKVGRTPLHV-------YLSGFN--------IN-PKVIRLLLRKGADVNALDLYGMTPlAVLL 160

                         170       180
                  ....*....|....*....|....*.
gi 2000138002 179 IENRCNIKTLRTLLNAKAHI-GVDNF 203
Cdd:PHA03095  161 KSRNANVELLRLLIDAGADVyAVDDR 186
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 16-181 4.53e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.83  E-value: 4.53e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  16 ASKENNLQEVSLLLSQKTDPNGATGHGISPLLVACTNGNVEIVRELIKAKAKIG-VKKKNGQTTLLCAAASGSVETVQCI 94
Cdd:PHA02875   42 AMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLL 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  95 LEAKADLTHTDNQNWSAYSFACHNGYNNILSLLVKAK----LPSLKNLNSLLRLAAQVDQAnCCQYLLDLKANPNDQDLD 170
Cdd:PHA02875  122 IARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKacldIEDCCGCTPLIIAMAKGDIA-ICKMLLDSGANIDYFGKN 200

                         170
                  ....*....|..
gi 2000138002 171 NFTASM-YAIEN 181
Cdd:PHA02875  201 GCVAALcYAIEN 212
Ank_4 pfam13637
Ankyrin repeats (many copies);
44-95 7.98e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 7.98e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2000138002  44 SPLLVACTNGNVEIVRELIKAKAKIGVKKKNGQTTLLCAAASGSVETVQCIL 95
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 8-100 9.36e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.08  E-value: 9.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002   8 IAKIALVKASKENNLQEVS-LLLSQKTDPNGATGHGISPLLVACTNGNVEIVRELIKA-----KAKIGVKKKNGQTTLLC 81
Cdd:cd22192    16 ISESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAapelvNEPMTSDLYQGETALHI 95

                          90
                  ....*....|....*....
gi 2000138002  82 AAASGSVETVQCILEAKAD 100
Cdd:cd22192    96 AVVNQNLNLVRELIARGAD 114
Ank_4 pfam13637
Ankyrin repeats (many copies);
12-62 1.09e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 1.09e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2000138002  12 ALVKASKENNLQEVSLLLSQKTDPNGATGHGISPLLVACTNGNVEIVRELI 62
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 25-195 1.16e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 42.70  E-value: 1.16e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  25 VSLLLSQKTDPNGATGHGISPL--LVACTNGNVEIVRELIKAKAKIGVKKKNGQTTL--LCAAASGSVETVQCILEAKAD 100
Cdd:PHA03095  135 IRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLhhHLQSFKPRARIVRELIRAGCD 214

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002 101 LTHTDN-QNWSAYSFACHNGYNNILSLLVKAKLPSLKNLNSLLR----LAAQVDQANCCQYLLDLKANPNDQDLDNFTAS 175
Cdd:PHA03095  215 PAATDMlGNTPLHSMATGSSCKRSLVLPLLIAGISINARNRYGQtplhYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294

                         170       180
                  ....*....|....*....|
gi 2000138002 176 MYAIENrCNIKTLRTLLNAK 195
Cdd:PHA03095  295 SLMVRN-NNGRAVRAALAKN 313
Ank_4 pfam13637
Ankyrin repeats (many copies);
77-128 1.30e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 1.30e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2000138002  77 TTLLCAAASGSVETVQCILEAKADLTHTDNQNWSAYSFACHNGYNNILSLLV 128
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 25-230 2.47e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.57  E-value: 2.47e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  25 VSLLLSQKTDPNGATGHGISPL-----LVACTNGNVEIVRELIKAKAKIGVKKKNGQTTLLCAAA--SGSVETVQCILEA 97
Cdd:PHA03100   51 VKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDN 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  98 KADLTHTDNQNWsaysfachngynNILSLLVKAKLPSLKNLNSLLRLAAQVDQANCCQYLLDLKANPNDQDLDNFTASMY 177
Cdd:PHA03100  131 GANVNIKNSDGE------------NLLHLYLESNKIDLKILKLLIDKGVDINAKNRVNYLLSYGVPINIKDVYGFTPLHY 198

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2000138002 178 AIENRcNIKTLRTLLNAKAHIG-VDNFDIARLSCPIRSVKHAKHTVIIERKPRI 230
Cdd:PHA03100  199 AVYNN-NPEFVKYLLDLGANPNlVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 31-181 4.44e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.01  E-value: 4.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  31 QKTDPNGAtghgiSPLLVACTNGNVEIVRELIKAKAKIGVKKKNGQTTLLCAAASGSVETVQCILEAKADLTHTDNQN-- 108
Cdd:PLN03192  519 EHDDPNMA-----SNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGnt 593

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2000138002 109 --WSAYSfACHNGYNNILSLLVKAKLPSLKnlNSLLRLAAQVDQANCCQYLLDLKANPNDQDLDNFTASMYAIEN 181
Cdd:PLN03192  594 alWNAIS-AKHHKIFRILYHFASISDPHAA--GDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAE 665
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 7-105 7.66e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.05  E-value: 7.66e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002   7 SIAKIALVKAS-KENNLQEVSLLLSQKTDPNGATGHGISPLLVACTNGNVEIVRELIKAKAKIGVKKKNGQTTLLCAAAS 85
Cdd:PHA02876  142 SIEYMKLIKERiQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDS 221

                          90       100
                  ....*....|....*....|
gi 2000138002  86 GSVETVQCILEAKADLTHTD 105
Cdd:PHA02876  222 KNIDTIKAIIDNRSNINKND 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
142-204 2.30e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 36.25  E-value: 2.30e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2000138002 142 LRLAAQVDQANCCQYLLDLKANPNDQDLDNFTASMYAIENRcNIKTLRTLLNakaHIGVDNFD 204
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNG-HLEIVKLLLE---HADVNLKD 59
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 7-107 2.51e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.49  E-value: 2.51e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002   7 SIAKIALVKASKENNLQEVSLLLSQKTDPNGATGHGISPLLVACTNGNVEIVRELIKAKAKIGVKKKNGQTTLLCAAASG 86
Cdd:PHA03100  157 KILKLLIDKGVDINAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNN 236

                          90       100
                  ....*....|....*....|.
gi 2000138002  87 SVETVQCILEAKADLTHTDNQ 107
Cdd:PHA03100  237 NKEIFKLLLNNGPSIKTIIET 257
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 41-68 6.44e-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: 33.38  E-value: 6.44e-03
                          10        20
                  ....*....|....*....|....*...
gi 2000138002  41 HGISPLLVACTNGNVEIVRELIKAKAKI 68
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 41-68 6.63e-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: 33.33  E-value: 6.63e-03
                           10        20
                   ....*....|....*....|....*...
gi 2000138002   41 HGISPLLVACTNGNVEIVRELIKAKAKI 68
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 12-101 9.56e-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: 36.98  E-value: 9.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2000138002  12 ALVKASKENNLQEV-SLLLSQKTDpnGATGHGispLLVACTNGNVEIVRELIKAKAKIGVKKKN--------------GQ 76
Cdd:TIGR00870  55 ALFVAAIENENLELtELLLNLSCR--GAVGDT---LLHAISLEYVDAVEAILLHLLAAFRKSGPlelandqytseftpGI 129

                          90       100
                  ....*....|....*....|....*
gi 2000138002  77 TTLLCAAASGSVETVQCILEAKADL 101
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASV 154
 
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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