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Conserved domains on  [gi|19921030|ref|NP_609333|]
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uncharacterized protein Dmel_CG5846, isoform A [Drosophila melanogaster]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
92-232 1.01e-29

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 112.35  E-value: 1.01e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030  92 NIDYKDAHGFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHNEIVRFLLEHGADSGHMDIVGNTALM 171
Cdd:COG0666 112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLH 191

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19921030 172 YAAAGNHPHTCNELLAKDLDLSATNEDGDTAYSLAVEHGAHLAQALLEQYMTAIITAGAFG 232
Cdd:COG0666 192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
92-232 1.01e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 112.35  E-value: 1.01e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030  92 NIDYKDAHGFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHNEIVRFLLEHGADSGHMDIVGNTALM 171
Cdd:COG0666 112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLH 191

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19921030 172 YAAAGNHPHTCNELLAKDLDLSATNEDGDTAYSLAVEHGAHLAQALLEQYMTAIITAGAFG 232
Cdd:COG0666 192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252
Ank_2 pfam12796
Ankyrin repeats (3 copies);
104-196 1.76e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.08  E-value: 1.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030   104 LHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHNEIVRFLLEHGAdsGHMDIVGNTALMYAAAGNHPHTCN 183
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 19921030   184 ELLAKDLDLSATN 196
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 92-207 8.14e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 8.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030   92 NIDYKDAHGFTALHWAASY--GQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHN--EIVRFLLEHGADSGHM----- 162
Cdd:PHA03100  98 NVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKnrvny 177

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19921030  163 -----------DIVGNTALMYAAAGNHPHTCNELLAKDLDLSATNEDGDTAYSLAV 207
Cdd:PHA03100 178 llsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 100-210 1.29e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 54.63  E-value: 1.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030 100 GFTALHWAASYGQLVSVQLLVAAGANVNTM----------APDLI----SPLLLAAAGGHNEIVRFLLEHGADSGHMDIV 165
Cdd:cd22192  89 GETALHIAVVNQNLNLVRELIARGADVVSPratgtffrpgPKNLIyygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19921030 166 GNTAL-MYAAAGNHPHTC---NELLAKD-------LDLsATNEDGDTAYSLAVEHG 210
Cdd:cd22192 169 GNTVLhILVLQPNKTFACqmyDLILSYDkeddlqpLDL-VPNNQGLTPFKLAAKEG 223
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 99-225 4.60e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.08  E-value: 4.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030    99 HGFTALHWAASYGQLVSVQLLVAAGANVNTMA----------PDLI----SPLLLAAAGGHNEIVRFLLEHGADSGHMDI 164
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgVDSFyhgeSPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19921030   165 VGNTALMYAAAGNHPHTCNELLA---KDLDLSA-------------TNEDGDTAYSLAVEHGAHlaqaLLEQYMTAI 225
Cdd:TIGR00870 207 LGNTLLHLLVMENEFKAEYEELScqmYNFALSLldklrdskeleviLNHQGLTPLKLAAKEGRI----VLFRLKLAI 279
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 99-127 1.36e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 1.36e-04
                           10        20
                   ....*....|....*....|....*....
gi 19921030     99 HGFTALHWAASYGQLVSVQLLVAAGANVN 127
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
92-232 1.01e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 112.35  E-value: 1.01e-29
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030  92 NIDYKDAHGFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHNEIVRFLLEHGADSGHMDIVGNTALM 171
Cdd:COG0666 112 DVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLH 191

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19921030 172 YAAAGNHPHTCNELLAKDLDLSATNEDGDTAYSLAVEHGAHLAQALLEQYMTAIITAGAFG 232
Cdd:COG0666 192 LAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDG 252
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
80-220 1.66e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.88  E-value: 1.66e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030  80 EEQVAAERARQQNIDYKDAHGFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHNEIVRFLLEHGADS 159
Cdd:COG0666  67 LLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADV 146

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19921030 160 GHMDIVGNTALMYAAAGNHPHTCNELLAKDLDLSATNEDGDTAYSLAVEHG-AHLAQALLEQ 220
Cdd:COG0666 147 NAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGhLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
92-218 6.05e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 99.64  E-value: 6.05e-25
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030  92 NIDYKDAHGFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHNEIVRFLLEHGADSGHMDIVGNTALM 171
Cdd:COG0666 145 DVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALD 224

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*..
gi 19921030 172 YAAAGNHPHTCNELLAKDLDLSATNEDGDTAYSLAVEHGAHLAQALL 218
Cdd:COG0666 225 LAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
Ank_2 pfam12796
Ankyrin repeats (3 copies);
104-196 1.76e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.08  E-value: 1.76e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030   104 LHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHNEIVRFLLEHGAdsGHMDIVGNTALMYAAAGNHPHTCN 183
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 19921030   184 ELLAKDLDLSATN 196
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
80-220 3.69e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.46  E-value: 3.69e-17
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030  80 EEQVAAERARQQNIDYKDAHGFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHNEIVRFLLEHGADS 159
Cdd:COG0666  34 LLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADV 113

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19921030 160 GHMDIVGNTALMYAAAGNHPHTCNELLAKDLDLSATNEDGDTAYSLAVEHG-AHLAQALLEQ 220
Cdd:COG0666 114 NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGnLEIVKLLLEA 175
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
92-202 5.12e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 75.38  E-value: 5.12e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030  92 NIDYKDAHGFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHNEIVRFLLEHGADSGHMDIVGNTALM 171
Cdd:COG0666 178 DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257

                        90       100       110
                ....*....|....*....|....*....|.
gi 19921030 172 YAAAGNHPHTCNELLAKDLDLSATNEDGDTA 202
Cdd:COG0666 258 LAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
Ank_2 pfam12796
Ankyrin repeats (3 copies);
92-163 7.00e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.35  E-value: 7.00e-10
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19921030    92 NIDYKDAHGFTALHWAASYGQLVSVQLLVaAGANVNtMAPDLISPLLLAAAGGHNEIVRFLLEHGADSGHMD 163
Cdd:pfam12796  22 DANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVN-LKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 92-207 8.14e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 8.14e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030   92 NIDYKDAHGFTALHWAASY--GQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHN--EIVRFLLEHGADSGHM----- 162
Cdd:PHA03100  98 NVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKnrvny 177

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19921030  163 -----------DIVGNTALMYAAAGNHPHTCNELLAKDLDLSATNEDGDTAYSLAV 207
Cdd:PHA03100 178 llsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAI 233
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
92-219 9.04e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 54.57  E-value: 9.04e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030  92 NIDYKDAHGFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHNEIVRFLLEHGADSGHMDIVGNTALM 171
Cdd:COG0666  13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*....
gi 19921030 172 YAAAGNHPHTCNELLAKDLDLSATNEDGDTAYSLAVEHG-AHLAQALLE 219
Cdd:COG0666  93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGnLEIVKLLLE 141
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 100-210 1.29e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 54.63  E-value: 1.29e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030 100 GFTALHWAASYGQLVSVQLLVAAGANVNTM----------APDLI----SPLLLAAAGGHNEIVRFLLEHGADSGHMDIV 165
Cdd:cd22192  89 GETALHIAVVNQNLNLVRELIARGADVVSPratgtffrpgPKNLIyygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19921030 166 GNTAL-MYAAAGNHPHTC---NELLAKD-------LDLsATNEDGDTAYSLAVEHG 210
Cdd:cd22192 169 GNTVLhILVLQPNKTFACqmyDLILSYDkeddlqpLDL-VPNNQGLTPFKLAAKEG 223
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 92-163 2.15e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.90  E-value: 2.15e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19921030   92 NIDYKDAHGFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHNEIVRFLLEHGADSGHMD 163
Cdd:PHA03100 184 PINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
PHA03095 PHA03095
ankyrin-like protein; Provisional
 75-202 6.82e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.33  E-value: 6.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030   75 QGEITEEQVAAERARQQNIDYKDAHGFTALHWAASYGQLVS---VQLLVAAGANVNtmAPDL--ISPL-LLAAAGGHNEI 148
Cdd:PHA03095  22 ASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVN--APERcgFTPLhLYLYNATTLDV 99

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19921030  149 VRFLLEHGADSGHMDIVGNTAL-MYAAAGN-HPHTCNELLAKDLDLSATNEDGDTA 202
Cdd:PHA03095 100 IKLLIKAGADVNAKDKVGRTPLhVYLSGFNiNPKVIRLLLRKGADVNALDLYGMTP 155
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 45-177 1.04e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030   45 STVLTNLQRGNTEATFCPVEVSLSFHERAG-QGEI------------TEEQVAA---ERARQQNIDYKDAHGFTA--LHW 106
Cdd:PTZ00322  10 SSAFAAQLFFGTEGSRKRRAKPISFERMAAiQEEIaridthlealeaTENKDATpdhNLTTEEVIDPVVAHMLTVelCQL 89

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 19921030  107 AASyGQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHNEIVRFLLEHGADSGHMDIVGNTALMYAAAGN 177
Cdd:PTZ00322  90 AAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
Ank_4 pfam13637
Ankyrin repeats (many copies);
135-186 1.86e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 1.86e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 19921030   135 SPLLLAAAGGHNEIVRFLLEHGADSGHMDIVGNTALMYAAAGNHPHTCNELL 186
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 94-210 2.19e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.02  E-value: 2.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030   94 DYKDAHGFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHNEIVRfLLEHGADSGHMDIVGNTaLMYA 173
Cdd:PLN03192 552 DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR-ILYHFASISDPHAAGDL-LCTA 629

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 19921030  174 AAGNHPHTCNELLAKDLDLSATNEDGDTAYSLAVEHG 210
Cdd:PLN03192 630 AKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAED 666
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 92-173 2.28e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.65  E-value: 2.28e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030   92 NIDYKDAH-GFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHNEIVRFLLEHGADSGHMDIVGNTAL 170
Cdd:PHA02878 159 DINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238


                 ...
gi 19921030  171 MYA 173
Cdd:PHA02878 239 HIS 241
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 100-215 2.33e-07

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: 51.03  E-value: 2.33e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030 100 GFTALHWAASYGQLVSVQLLVAAGANVNTMAP---------DLI----SPLLLAAAGGHNEIVRFLLEHGAD---SGHMD 163
Cdd:cd21882  73 GQTALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgNLFyfgeLPLSLAACTNQEEIVRLLLENGAQpaaLEAQD 152

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19921030 164 IVGNTAL--MYAAAGNHP-------HTCNELLAKDLDLSAT-------NEDGDTAYSLAVEHG-----AHLAQ 215
Cdd:cd21882 153 SLGNTVLhaLVLQADNTPensafvcQMYNLLLSYGAHLDPTqqleeipNHQGLTPLKLAAVEGkivmfQHILQ 225
PHA03095 PHA03095
ankyrin-like protein; Provisional
 92-214 2.58e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.41  E-value: 2.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030   92 NIDYKDAHGFTALHWAASYGQLVS--VQLLVAAGANVNTMAPDLISPLLLAAAGG--HNEIVRFLLEHGADSGHMDIVGN 167
Cdd:PHA03095 179 DVYAVDDRFRSLLHHHLQSFKPRAriVRELIRAGCDPAATDMLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQ 258

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 19921030  168 TALMYAAAGNHPHTCNELLAKDLDLSATNEDGDTAYSLAVEHGAHLA 214
Cdd:PHA03095 259 TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRA 305
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 99-225 4.60e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.08  E-value: 4.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030    99 HGFTALHWAASYGQLVSVQLLVAAGANVNTMA----------PDLI----SPLLLAAAGGHNEIVRFLLEHGADSGHMDI 164
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgVDSFyhgeSPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19921030   165 VGNTALMYAAAGNHPHTCNELLA---KDLDLSA-------------TNEDGDTAYSLAVEHGAHlaqaLLEQYMTAI 225
Cdd:TIGR00870 207 LGNTLLHLLVMENEFKAEYEELScqmYNFALSLldklrdskeleviLNHQGLTPLKLAAKEGRI----VLFRLKLAI 279
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 55-170 1.06e-06

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: 48.99  E-value: 1.06e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030  55 NTEATfcpVEVSLSFHERAGqgeITEEQVAAERARQqniDYKdahGFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLI 134
Cdd:cd22194 108 NTKEI---VRILLAFAEENG---ILDRFINAEYTEE---AYE---GQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVF 175

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 19921030 135 --------------SPLLLAAAGGHNEIVRFLLEHGADSGHM-DIVGNTAL 170
Cdd:cd22194 176 fnpkykhegfyfgeTPLALAACTNQPEIVQLLMEKESTDITSqDSRGNTVL 226
PHA03095 PHA03095
ankyrin-like protein; Provisional
 92-210 1.17e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.48  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030   92 NIDYKDAHGFTALHWAASyGQLVS---VQLLVAAGANVNTMAPDLISPL--LLAAAGGHNEIVRFLLEHGADSGHMDIVG 166
Cdd:PHA03095 109 DVNAKDKVGRTPLHVYLS-GFNINpkvIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRF 187

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 19921030  167 NTALMYAAAGNHPHTC--NELLAKDLDLSATNEDGDTAYSLAVEHG 210
Cdd:PHA03095 188 RSLLHHHLQSFKPRARivRELIRAGCDPAATDMLGNTPLHSMATGS 233
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 92-186 1.25e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.51  E-value: 1.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030   92 NIDYKDAHGFTALHWAASYGQ--LVSVQLLVAAGANVNTM--------------APDLI--SPLLLAAAGGHNEIVRFLL 153
Cdd:PHA03100 133 NVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKnrvnyllsygvpinIKDVYgfTPLHYAVYNNNPEFVKYLL 212

                         90       100       110
                 ....*....|....*....|....*....|...
gi 19921030  154 EHGADSGHMDIVGNTALMYAAAGNHPHTCNELL 186
Cdd:PHA03100 213 DLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 69-209 1.55e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.06  E-value: 1.55e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030   69 FHERAGQGEITE-EQVAAERARQQNIDYKDahGFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHNE 147
Cdd:PHA02875  72 LHDAVEEGDVKAvEELLDLGKFADDVFYKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19921030  148 IVRFLLEHGADSGHMDIVGNTALMYAAAGNHPHTCNELLAKDLDLSATNEDGD-TAYSLAVEH 209
Cdd:PHA02875 150 GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIEN 212
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 92-210 3.80e-06

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: 47.10  E-value: 3.80e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030  92 NIDYKDAH--GFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLI--------------SPLLLAAAGGHNEIVRFLLEH 155
Cdd:cd22193  66 NAEYTDEYyeGQTALHIAIERRQGDIVALLVENGADVHAHAKGRFfqpkyqgegfyfgeLPLSLAACTNQPDIVQYLLEN 145

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19921030 156 G---ADSGHMDIVGNTAL--MYAAAGNHP-------HTCNELLAK------DLDLSA-TNEDGDTAYSLAVEHG 210
Cdd:cd22193 146 EhqpADIEAQDSRGNTVLhaLVTVADNTKentkfvtRMYDMILIRgaklcpTVELEEiRNNDGLTPLQLAAKMG 219
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 92-210 4.41e-06

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 47.11  E-value: 4.41e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030  92 NIDYKDAH--GFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLIS--------------PLLLAAAGGHNEIVRFLLEH 155
Cdd:cd22196  84 NAAYTDSYykGQTALHIAIERRNMHLVELLVQNGADVHARASGEFFkkkkggpgfyfgelPLSLAACTNQLDIVKFLLEN 163

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19921030 156 ---GADSGHMDIVGNTAL--MYAAAGNHPHTC-------NELLAKDLDL-------SATNEDGDTAYSLAVEHG 210
Cdd:cd22196 164 phsPADISARDSMGNTVLhaLVEVADNTPENTkfvtkmyNEILILGAKIrpllkleEITNKKGLTPLKLAAKTG 237
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 63-210 5.79e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 5.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030   63 VEVSLSFHERAGQGEITEEQVAAERArqQNIDYKDAHGFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLAAA 142
Cdd:PHA02876 143 IEYMKLIKERIQQDELLIAEMLLEGG--ADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVD 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030  143 GGHNEIVRFLLEHGA-------------------------DSG----HMDIVGNTALMYAA-AGNHPHTCNELLAKDLDL 192
Cdd:PHA02876 221 SKNIDTIKAIIDNRSninkndlsllkairnedletslllyDAGfsvnSIDDCKNTPLHHASqAPSLSRLVPKLLERGADV 300

                        170
                 ....*....|....*...
gi 19921030  193 SATNEDGDTAYSLAVEHG 210
Cdd:PHA02876 301 NAKNIKGETPLYLMAKNG 318
Ank_4 pfam13637
Ankyrin repeats (many copies);
102-153 7.15e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 7.15e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 19921030   102 TALHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHNEIVRFLL 153
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 93-208 1.25e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.43  E-value: 1.25e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030   93 IDYKDAHGFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHN-----EIVRFLLEHGADSGHMDIVGN 167
Cdd:PHA03100  28 NDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGI 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 19921030  168 TALMYAAAG--NHPHTCNELLAKDLDLSATNEDGDTAYSLAVE 208
Cdd:PHA03100 108 TPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLE 150
PHA03095 PHA03095
ankyrin-like protein; Provisional
 96-194 1.45e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.40  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030   96 KDAHGFTALHWAASYGQLVS--VQLLVAAGANVNTMAPDLISPLLLAAAGGHNEIVRFLLEHGADSGHMDIVGNTALMYA 173
Cdd:PHA03095 218 TDMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297

                         90       100
                 ....*....|....*....|.
gi 19921030  174 AAGNHPHTCNELLAKDLDLSA 194
Cdd:PHA03095 298 VRNNNGRAVRAALAKNPSAET 318
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 92-174 2.35e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.57  E-value: 2.35e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030   92 NIDYKDAHGFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHNEIVRFLLEHGADSGHMDIVGNTALM 171
Cdd:PHA02874 116 DVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLH 195


                 ...
gi 19921030  172 YAA 174
Cdd:PHA02874 196 NAA 198
PHA03095 PHA03095
ankyrin-like protein; Provisional
 93-154 2.39e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 2.39e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19921030   93 IDYKDAHGFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHNEIVRFLLE 154
Cdd:PHA03095 250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
PHA02791 PHA02791
ankyrin-like protein; Provisional
 97-228 2.49e-05

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 44.26  E-value: 2.49e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030   97 DAHGFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLisPLLLAAAGGHNEIVRFLLEHGADSGHMDIVGNTALMYAAAG 176
Cdd:PHA02791  27 DVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENEF--PLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDS 104

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 19921030  177 NHPHTCNELLAKDLDLSATnedGDTAYSLAVEHGAHLAQALLEQYMTAIITA 228
Cdd:PHA02791 105 GNMQTVKLFVKKNWRLMFY---GKTGWKTSFYHAVMLNDVSIVSYFLSEIPS 153
PHA03095 PHA03095
ankyrin-like protein; Provisional
 92-202 2.69e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.63  E-value: 2.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030   92 NIDYKDAHGFTALHWAASYGQLVSV-QLLVAAGANVNtmAPDLI--SPLLLAAAGG--HNEIVRFLLEHGADSGHMDIVG 166
Cdd:PHA03095  75 DVNAPERCGFTPLHLYLYNATTLDViKLLIKAGADVN--AKDKVgrTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYG 152

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 19921030  167 NTALmYAAAGNH---PHTCNELLAKDLDLSATNEDGDTA 202
Cdd:PHA03095 153 MTPL-AVLLKSRnanVELLRLLIDAGADVYAVDDRFRSL 190
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 88-191 5.33e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.44  E-value: 5.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030   88 ARQQNIDYKDAHGFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHNEIVRFLLEHGADSGHMDIVGN 167
Cdd:PHA02875 123 ARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGC 202

                         90       100
                 ....*....|....*....|....*
gi 19921030  168 TALM-YAAAGNHPHTCNELLAKDLD 191
Cdd:PHA02875 203 VAALcYAIENNKIDIVRLFIKRGAD 227
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 141-230 7.43e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 43.35  E-value: 7.43e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030  141 AAGGHNEIVRFLLEHGADSGHMDIVGNTALMYAAAGNHPHTCNELLAKDLDLSATNEDGDTAYSLAVEHGAHLAQALLEQ 220
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169

                         90
                 ....*....|
gi 19921030  221 YMTAIITAGA 230
Cdd:PTZ00322 170 HSQCHFELGA 179
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
92-170 1.13e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 42.25  E-value: 1.13e-04
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 19921030  92 NIDYKDAHGFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHNEIVRFLLEHGADSGHMDIVGNTAL 170
Cdd:COG0666 211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_5 pfam13857
Ankyrin repeats (many copies);
152-206 1.28e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 1.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 19921030   152 LLEHG-ADSGHMDIVGNTALMYAAAGNHPHTCNELLAKDLDLSATNEDGDTAYSLA 206
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 99-127 1.36e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 1.36e-04
                           10        20
                   ....*....|....*....|....*....
gi 19921030     99 HGFTALHWAASYGQLVSVQLLVAAGANVN 127
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 93-167 2.07e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 2.07e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19921030   93 IDYKDAHGFTALHWAASYGQLVSVQLLVAAGANVNTMA--PDlISPLLLAAAGGHNEIVRFLLEHGADSGHMDIVGN 167
Cdd:PHA02875 161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGknGC-VAALCYAIENNKIDIVRLFIKRGADCNIMFMIEG 236
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 99-127 2.60e-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: 37.27  E-value: 2.60e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 19921030    99 HGFTALHWAA-SYGQLVSVQLLVAAGANVN 127
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVN 30
Ank_2 pfam12796
Ankyrin repeats (3 copies);
170-234 3.15e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.56  E-value: 3.15e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19921030   170 LMYAAAGNHPHTCNELLAKDLDLSATNEDGDTAYSLAVEHG-AHLAQALLEQY--------MTAIITAGAFGSI 234
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGhLEIVKLLLEHAdvnlkdngRTALHYAARSGHL 74
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 89-207 3.63e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.20  E-value: 3.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030   89 RQQNIDYKDAHGFTALHWAASYG-QLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHN-EIVRFLLEHGADSGHMDIVG 166
Cdd:PHA02876 296 RGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCD 375

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 19921030  167 NTALMYAAAGNHPHTCNELLAKDLDLSATNEDGDTAYSLAV 207
Cdd:PHA02876 376 KTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL 416
Ank_5 pfam13857
Ankyrin repeats (many copies);
87-140 4.45e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 4.45e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 19921030    87 RARQQNIDYKDAHGFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLA 140
Cdd:pfam13857   3 EHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 96-209 6.24e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 6.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030   96 KDAHGFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLAAAggHNEIVRFLLEHGADSGHMDIVGNTALMYAAa 175
Cdd:PHA02874 186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAI- 262

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 19921030  176 gNHP---HTCNELLAKDLDLSATNEDGDTAYSLAVEH 209
Cdd:PHA02874 263 -NPPcdiDIIDILLYHKADISIKDNKGENPIDTAFKY 298
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 94-155 6.91e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 6.91e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19921030   94 DYKDAHGFTALHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHNEIVRFLLEH 155
Cdd:PTZ00322 109 NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 102-173 9.38e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.05  E-value: 9.38e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19921030  102 TALHWAAsYGQ--LVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHN-EIVRFLLEHGADSGHMDIVGNTALMYA 173
Cdd:PHA02876 410 TALHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIA 483
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 102-220 1.69e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.18  E-value: 1.69e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030  102 TALHWAASYGQLVSVQLLVAAGANVNTMAPDLISPLLLAAAGGHNEIVRFLLEHGADSGHM------------------- 162
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILpipciekdmiktildcgid 116

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19921030  163 ----DIVGNTALMYAAAGNHPHTCNELLAKDLDLSATNEDGDTAYSLAVEHGAH-LAQALLEQ 220
Cdd:PHA02874 117 vnikDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFdIIKLLLEK 179
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 99-128 2.34e-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: 34.54  E-value: 2.34e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 19921030    99 HGFTALHWAASYGQLVSVQLLVAAGANVNT 128
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
166-210 3.95e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.56  E-value: 3.95e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 19921030   166 GNTALMYAAAGNHPHTCNELLAKDLDLSATNEDGDTAYSLAVEHG 210
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNG 45
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 132-158 3.95e-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: 34.16  E-value: 3.95e-03
                          10        20
                  ....*....|....*....|....*..
gi 19921030   132 DLISPLLLAAAGGHNEIVRFLLEHGAD 158
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 132-158 4.57e-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: 33.72  E-value: 4.57e-03
                           10        20
                   ....*....|....*....|....*..
gi 19921030    132 DLISPLLLAAAGGHNEIVRFLLEHGAD 158
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 100-170 4.73e-03

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: 37.91  E-value: 4.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030 100 GFTALHWAASYGQLVSVQLLVAAGANVNTMAP-DLIS------------PLLLAAAGGHNEIVRFLLEHGADSGHM---D 163
Cdd:cd22197  94 GHSALHIAIEKRSLQCVKLLVENGADVHARACgRFFQkkqgtcfyfgelPLSLAACTKQWDVVNYLLENPHQPASLqaqD 173


                ....*..
gi 19921030 164 IVGNTAL 170
Cdd:cd22197 174 SLGNTVL 180
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 92-205 5.51e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 36.72  E-value: 5.51e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030   92 NIDYKDAH-GFTALHWAASYGQLVS---VQLLVAAGANVNTMAPDLISPL--LLAAAGGHNEIVRFLLEHGADSGHMDIV 165
Cdd:PHA02859  78 DVNFKTRDnNLSALHHYLSFNKNVEpeiLKILIDSGSSITEEDEDGKNLLhmYMCNFNVRINVIKLLIDSGVSFLNKDFD 157

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 19921030  166 GNTAL-MYAAAGNHPHTCNELLAKDLDLSATNEDGDTAYSL 205
Cdd:PHA02859 158 NNNILySYILFHSDKKIFDFLTSLGIDINETNKSGYNCYDL 198
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 115-210 5.78e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 37.25  E-value: 5.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19921030  115 SVQLLVAAGANVNTMAPDLISPLLLAAAGGHNEIVRFLLEHGADSGHMDIVGNTALMYAAAGNHPHTCNELLAKDLDLSA 194
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                         90
                 ....*....|....*.
gi 19921030  195 TNEDGDTAYSLAVEHG 210
Cdd:PHA02874 186 KDNNGESPLHNAAEYG 201
 
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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