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Conserved domains on  [gi|39812133|ref|NP_065082|]
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ankyrin repeat domain-containing protein 2 isoform a [Homo sapiens]

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];
100-319 5.80e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.48  E-value: 5.80e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133 100 LDLRREIIDVGGIQNLIELRKKRKQKKRDALAASHEPPPEPEEITGPVDEETFLKAAVEGKMKVIEKFLADGGSADTCDQ 179
Cdd:COG0666   6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133 180 FRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQ 259
Cdd:COG0666  86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133 260 VEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTDL 319
Cdd:COG0666 166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
100-319 5.80e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.48  E-value: 5.80e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133 100 LDLRREIIDVGGIQNLIELRKKRKQKKRDALAASHEPPPEPEEITGPVDEETFLKAAVEGKMKVIEKFLADGGSADTCDQ 179
Cdd:COG0666   6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133 180 FRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQ 259
Cdd:COG0666  86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133 260 VEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTDL 319
Cdd:COG0666 166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
Ank_2 pfam12796
Ankyrin repeats (3 copies);
185-277 4.92e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 4.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133   185 LHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHgADTNVRDKLLsTPLHVAVRTGQVEIVE 264
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 39812133   265 HFLSLGLEINARD 277
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 160-316 1.88e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 92.01  E-value: 1.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  160 KMKVIEKFLADGGSADTCDQFRRTALH---RASLEGHMEILEKLLDNGATVDFQDRLDCTAMH-WACRGGHLEVVKLLQS 235
Cdd:PHA03095  26 TVEEVRRLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  236 HGADTNVRDKLLSTPLHV-----AVRTGQVEIVehfLSLGLEINARDREGDTALHDAVRLNR--YKIIKLLLLHGADMMT 308
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHVylsgfNINPKVIRLL---LRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYA 182


                 ....*...
gi 39812133  309 KNLAGKTP 316
Cdd:PHA03095 183 VDDRFRSL 190
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 153-285 5.59e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 57.72  E-value: 5.59e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133 153 LKAAVEGKMKVIEKFLadggSADTCDQFRR-----TALHRASLEGHMEILEKLLDNG-------ATVDFQdrLDCTAMHW 220
Cdd:cd22192  22 LLAAKENDVQAIKKLL----KCPSCDLFQRgalgeTALHVAALYDNLEAAVVLMEAApelvnepMTSDLY--QGETALHI 95

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 39812133 221 ACRGGHLEVVKLLQSHGADTNV-----------RDKLL---STPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALH 285
Cdd:cd22192  96 AVVNQNLNLVRELIARGADVVSpratgtffrpgPKNLIyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 214-242 7.60e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 7.60e-06
                           10        20
                   ....*....|....*....|....*....
gi 39812133    214 DCTAMHWACRGGHLEVVKLLQSHGADTNV 242
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 191-305 8.77e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 44.30  E-value: 8.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133   191 EGHMEILEKLLDNGATVDFQ--DRLDCTAMHW-ACRGGHLEVVKLLQSHGADTNVRDKLLstplHVAvRTGQVEIVEHFL 267
Cdd:TIGR00870  27 RGDLASVYRDLEEPKKLNINcpDRLGRSALFVaAIENENLELTELLLNLSCRGAVGDTLL----HAI-SLEYVDAVEAIL 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 39812133   268 SLgLEINARDR---------------EGDTALHDAVRLNRYKIIKLLLLHGAD 305
Cdd:TIGR00870 102 LH-LLAAFRKSgplelandqytseftPGITALHLAAHRQNYEIVKLLLERGAS 153
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
100-319 5.80e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.48  E-value: 5.80e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133 100 LDLRREIIDVGGIQNLIELRKKRKQKKRDALAASHEPPPEPEEITGPVDEETFLKAAVEGKMKVIEKFLADGGSADTCDQ 179
Cdd:COG0666   6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133 180 FRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQ 259
Cdd:COG0666  86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133 260 VEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTDL 319
Cdd:COG0666 166 LEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
70-319 1.53e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 1.53e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  70 LLVLEDEKHHGAQSAALQKVKGQERVRKTSLDLRREIIDVGGIQNLIELRKKRKQKKRDALAASHEPPPEPEEITGPVDE 149
Cdd:COG0666   9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133 150 ETFLKAAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEV 229
Cdd:COG0666  89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133 230 VKLLQSHGADTNVRDKLLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTK 309
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248

                       250
                ....*....|
gi 39812133 310 NLAGKTPTDL 319
Cdd:COG0666 249 DKDGLTALLL 258
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
155-315 7.51e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.52  E-value: 7.51e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133 155 AAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQ 234
Cdd:COG0666 127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133 235 SHGADTNVRDKLLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGK 314
Cdd:COG0666 207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286


                .
gi 39812133 315 T 315
Cdd:COG0666 287 T 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
185-277 4.92e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 89.02  E-value: 4.92e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133   185 LHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHgADTNVRDKLLsTPLHVAVRTGQVEIVE 264
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 39812133   265 HFLSLGLEINARD 277
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
218-310 3.81e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.71  E-value: 3.81e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133   218 MHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQVEIVEHFLSLGlEINARDrEGDTALHDAVRLNRYKIIK 297
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 39812133   298 LLLLHGADMMTKN 310
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 160-316 1.88e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 92.01  E-value: 1.88e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  160 KMKVIEKFLADGGSADTCDQFRRTALH---RASLEGHMEILEKLLDNGATVDFQDRLDCTAMH-WACRGGHLEVVKLLQS 235
Cdd:PHA03095  26 TVEEVRRLLAAGADVNFRGEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIK 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  236 HGADTNVRDKLLSTPLHV-----AVRTGQVEIVehfLSLGLEINARDREGDTALHDAVRLNR--YKIIKLLLLHGADMMT 308
Cdd:PHA03095 106 AGADVNAKDKVGRTPLHVylsgfNINPKVIRLL---LRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYA 182


                 ....*...
gi 39812133  309 KNLAGKTP 316
Cdd:PHA03095 183 VDDRFRSL 190
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 160-316 5.56e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.49  E-value: 5.56e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  160 KMKVIEKFLADGGSADTCDQFRRTALHRASLEGH-----MEILEKLLDNGATVDFQDRLDCTAMHWA--CRGGHLEVVKL 232
Cdd:PHA03100  47 NIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEY 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  233 LQSHGADTNVRDKLLSTPLHVAVRTGQVEI------------------VEHFLSLGLEINARDREGDTALHDAVRLNRYK 294
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPE 206

                        170       180
                 ....*....|....*....|..
gi 39812133  295 IIKLLLLHGADMMTKNLAGKTP 316
Cdd:PHA03100 207 FVKYLLDLGANPNLVNKYGDTP 228
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 195-316 8.19e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 90.02  E-value: 8.19e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  195 EILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQVEIVEHFLSLGLEIN 274
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 39812133  275 ARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTP 316
Cdd:PHA02874 185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
161-316 2.43e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.93  E-value: 2.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133 161 MKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADT 240
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39812133 241 NVRDKLLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTP 316
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP 156
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 159-305 4.38e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 84.72  E-value: 4.38e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  159 GKMKVIEKFLADGGSADTCDQFRRTALHrASLEG---HMEILEKLLDNGATVDFQDRldctamhwacrgghlevVKLLQS 235
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSDGENLLH-LYLESnkiDLKILKLLIDKGVDINAKNR-----------------VNYLLS 180

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  236 HGADTNVRDKLLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGAD 305
Cdd:PHA03100 181 YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
155-244 3.50e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.92  E-value: 3.50e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133   155 AAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNgATVDFQDRlDCTAMHWACRGGHLEVVKLLQ 234
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 39812133   235 SHGADTNVRD 244
Cdd:pfam12796  82 EKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
155-284 1.45e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 79.23  E-value: 1.45e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133 155 AAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQ 234
Cdd:COG0666 160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLL 239

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|
gi 39812133 235 SHGADTNVRDKLLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTAL 284
Cdd:COG0666 240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 194-318 5.21e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.91  E-value: 5.21e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  194 MEILEKLLDNGATVDFQDRLDCTAMHWACRGGH---LEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQVE-IVEHFLSL 269
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKA 106

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 39812133  270 GLEINARDREGDTALHdaVRLN----RYKIIKLLLLHGADMMTKNLAGKTPTD 318
Cdd:PHA03095 107 GADVNAKDKVGRTPLH--VYLSgfniNPKVIRLLLRKGADVNALDLYGMTPLA 157
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 163-334 6.07e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 78.47  E-value: 6.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  163 VIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNV 242
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  243 RDKLLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIikLLLLHGADMMTKNLAGKTPtdlvql 322
Cdd:PHA02874 186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTP------ 257

                        170
                 ....*....|..
gi 39812133  323 wqadTRHALEHP 334
Cdd:PHA02874 258 ----LHHAINPP 265
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 155-305 1.27e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 77.34  E-value: 1.27e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  155 AAVEGKMKVIEKFLADGGSADtcDQFRR---TALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVK 231
Cdd:PHA02875  75 AVEEGDVKAVEELLDLGKFAD--DVFYKdgmTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIE 152

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 39812133  232 LLQSHGADTNVRDKLLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGD-TALHDAVRLNRYKIIKLLLLHGAD 305
Cdd:PHA02875 153 LLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 162-320 1.99e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 77.23  E-value: 1.99e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  162 KVIEKFLADGGSADTCDQFR-RTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADT 240
Cdd:PHA02878 148 EITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  241 NVRDKLLSTPLHVAV-RTGQVEIVEHFLSLGLEINARDR-EGDTALHDAVRLNRykIIKLLLLHGADMMTKNLAGKTPTD 318
Cdd:PHA02878 228 DARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLS 305


                 ..
gi 39812133  319 LV 320
Cdd:PHA02878 306 SA 307
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 144-324 2.98e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 77.22  E-value: 2.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  144 TGPVDEETFLKAAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACR 223
Cdd:PLN03192 521 DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAIS 600

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  224 GGHLEVVKLLQ--SHGADTNVRDKLLSTplhvAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLL 301
Cdd:PLN03192 601 AKHHKIFRILYhfASISDPHAAGDLLCT----AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIM 676

                        170       180
                 ....*....|....*....|....
gi 39812133  302 HGADMMTKNLAGK-TPTDLVQLWQ 324
Cdd:PLN03192 677 NGADVDKANTDDDfSPTELRELLQ 700
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 195-316 2.07e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 70.85  E-value: 2.07e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  195 EILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLH-----VAVRTGQVEIVEHFLSL 269
Cdd:PHA03100  16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEY 95

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 39812133  270 GLEINARDREGDTALHDAV--RLNRYKIIKLLLLHGADMMTKNLAGKTP 316
Cdd:PHA03100  96 GANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENL 144
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 182-319 5.11e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 69.63  E-value: 5.11e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  182 RTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQVE 261
Cdd:PHA02875   3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 39812133  262 IVEHFLSLGLEIN-ARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTDL 319
Cdd:PHA02875  83 AVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHL 141
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 171-318 8.02e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 66.63  E-value: 8.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  171 GGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGH-LEVVKLLQSHGADTNVRDKLLST 249
Cdd:PHA02876 365 GANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNpYMSVKTLIDRGANVNSKNKDLST 444

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  250 PLHVAVRTG-QVEIVEHFLSLGLEINARDREGDTALhdAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTD 318
Cdd:PHA02876 445 PLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPL--LIALEYHGIVNILLHYGAELRDSRVLHKSLND 512
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 150-318 1.06e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 65.76  E-value: 1.06e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  150 ETFLKAAVE-GKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLE 228
Cdd:PHA02874 125 KTFLHYAIKkGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYA 204

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  229 VVKLLQSHGADTNVRDKLLSTPLHVAVRTGQVEIveHFLSLGLEINARDREGDTALHDAVRLNRYK-IIKLLLLHGADMM 307
Cdd:PHA02874 205 CIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINDQDIDGSTPLHHAINPPCDIdIIDILLYHKADIS 282

                        170
                 ....*....|.
gi 39812133  308 TKNLAGKTPTD 318
Cdd:PHA02874 283 IKDNKGENPID 293
PHA03095 PHA03095
ankyrin-like protein; Provisional
 166-300 1.17e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.43  E-value: 1.17e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  166 KFLADGGSAD-TCDQFRRTALHRaslegHME-------ILEKLLDNGATVDFQDRLDCTAMHWA---CRGGHLEVVKLLQ 234
Cdd:PHA03095 171 RLLIDAGADVyAVDDRFRSLLHH-----HLQsfkprarIVRELIRAGCDPAATDMLGNTPLHSMatgSSCKRSLVLPLLI 245

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39812133  235 sHGADTNVRDKLLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLL 300
Cdd:PHA03095 246 -AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
181-233 2.22e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 2.22e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 39812133   181 RRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLL 233
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA03095 PHA03095
ankyrin-like protein; Provisional
 162-316 2.58e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.66  E-value: 2.58e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  162 KVIEKFLADGGSADTCDQFRRTALHR--ASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACR--GGHLEVVKLLQSHG 237
Cdd:PHA03095  98 DVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKsrNANVELLRLLIDAG 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  238 ADTNVRDKLLSTPLH---VAVRTGQvEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKL--LLLHGADMMTKNLA 312
Cdd:PHA03095 178 ADVYAVDDRFRSLLHhhlQSFKPRA-RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRY 256


                 ....
gi 39812133  313 GKTP 316
Cdd:PHA03095 257 GQTP 260
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 180-302 4.37e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.07  E-value: 4.37e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  180 FRRTALHR---ASLEGHMEILEKLLDNGATVDF----QDRLDCTAMHWA----CR---GGHLEVVKLLQSHGADTNVRDK 245
Cdd:PTZ00322  34 FERMAAIQeeiARIDTHLEALEATENKDATPDHnlttEEVIDPVVAHMLtvelCQlaaSGDAVGARILLTGGADPNCRDY 113

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 39812133  246 LLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLH 302
Cdd:PTZ00322 114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 162-316 1.50e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.31  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  162 KVIEKFLADGGSADTCDQFRRTALHRASLEGH-MEILEKLLDNGATVDFQDRLDCTAMHWACR-GGHLEVVKLLQSHGAD 239
Cdd:PHA02876 288 RLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGAN 367

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39812133  240 TNVRDKLLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAV-RLNRYKIIKLLLLHGADMMTKNLAGKTP 316
Cdd:PHA02876 368 VNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALcGTNPYMSVKTLIDRGANVNSKNKDLSTP 445
Ank_2 pfam12796
Ankyrin repeats (3 copies);
251-316 1.74e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.35  E-value: 1.74e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 39812133   251 LHVAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNlaGKTP 316
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTA 64
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 192-316 4.66e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 57.67  E-value: 4.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  192 GHMEILEKLLDN-GATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQVEIVE------ 264
Cdd:PHA02874  12 GDIEAIEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKllidng 91

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 39812133  265 -----------------HFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTP 316
Cdd:PHA02874  92 vdtsilpipciekdmikTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYP 160
Ank_4 pfam13637
Ankyrin repeats (many copies);
216-267 4.78e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 4.78e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 39812133   216 TAMHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQVEIVEHFL 267
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 153-285 5.59e-09

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 57.72  E-value: 5.59e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133 153 LKAAVEGKMKVIEKFLadggSADTCDQFRR-----TALHRASLEGHMEILEKLLDNG-------ATVDFQdrLDCTAMHW 220
Cdd:cd22192  22 LLAAKENDVQAIKKLL----KCPSCDLFQRgalgeTALHVAALYDNLEAAVVLMEAApelvnepMTSDLY--QGETALHI 95

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 39812133 221 ACRGGHLEVVKLLQSHGADTNV-----------RDKLL---STPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALH 285
Cdd:cd22192  96 AVVNQNLNLVRELIARGADVVSpratgtffrpgPKNLIyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
Ank_5 pfam13857
Ankyrin repeats (many copies);
232-285 3.57e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 3.57e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 39812133   232 LLQSHGADTNVRDKLLSTPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALH 285
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
248-300 7.03e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 7.03e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 39812133   248 STPLHVAVRTGQVEIVEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLL 300
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 191-320 1.04e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.53  E-value: 1.04e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  191 EGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQVEIVEHF---- 266
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIidnr 234

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  267 -------LSL------------------GLEINARDREGDTALHDAVRL-NRYKIIKLLLLHGADMMTKNLAGKTPTDLV 320
Cdd:PHA02876 235 sninkndLSLlkairnedletslllydaGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLM 314
PHA02798 PHA02798
ankyrin-like protein; Provisional
 185-310 2.71e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 49.06  E-value: 2.71e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  185 LHRASLEghMEILEKLLDNGATVDFQDRLD----CTAMHWACRGGH-LEVVKLLQSHGADTNVRDKLLSTPLHVAVRTGQ 259
Cdd:PHA02798  44 LQRDSPS--TDIVKLFINLGANVNGLDNEYstplCTILSNIKDYKHmLDIVKILIENGADINKKNSDGETPLYCLLSNGY 121

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 39812133  260 V---EIVEHFLSLGLEINARDREGDTALHDAVRLNRY---KIIKLLLLHGADMMTKN 310
Cdd:PHA02798 122 InnlEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHN 178
Ank_5 pfam13857
Ankyrin repeats (many copies);
200-254 4.50e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.49  E-value: 4.50e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 39812133   200 LLDNG-ATVDFQDRLDCTAMHWACRGGHLEVVKLLQSHGADTNVRDKLLSTPLHVA 254
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 214-242 7.60e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 7.60e-06
                           10        20
                   ....*....|....*....|....*....
gi 39812133    214 DCTAMHWACRGGHLEVVKLLQSHGADTNV 242
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02741 PHA02741
hypothetical protein; Provisional
 219-321 1.00e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 45.42  E-value: 1.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  219 HWACRGGHLEVVKLL------QSHGADTNVRDKLLSTPLHVAVRTGQ----VEIVEHFLSLGLEINARDR-EGDTALHDA 287
Cdd:PHA02741  26 HEAARCGCFDIIARFtpfirgDCHAAALNATDDAGQMCIHIAAEKHEaqlaAEIIDHLIELGADINAQEMlEGDTALHLA 105

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 39812133  288 VRLNRYKIIKLLLLH-GADMMTKNLAGKTPTDLVQ 321
Cdd:PHA02741 106 AHRRDHDLAEWLCCQpGIDLHFCNADNKSPFELAI 140
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 162-257 1.02e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.18  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  162 KVIEKFLADGGSADTCDQFRRTALHRASleGHM---EILEKLLDNGATVDFQDR-LDCTAMHWACRGGhlEVVKLLQSHG 237
Cdd:PHA02878 215 PIVHILLENGASTDARDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYG 290

                         90       100
                 ....*....|....*....|
gi 39812133  238 ADTNVRDKLLSTPLHVAVRT 257
Cdd:PHA02878 291 ADINSLNSYKLTPLSSAVKQ 310
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 175-321 1.10e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.97  E-value: 1.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  175 DTCDQFRRTALHrASLEG---HMEILEKLLDNGATVDFQDRLD-CTAMHWAC---RGGHLEVVKLLQSHGADTNVRDKLL 247
Cdd:PHA02859  45 NDCNDLYETPIF-SCLEKdkvNVEILKFLIENGADVNFKTRDNnLSALHHYLsfnKNVEPEILKILIDSGSSITEEDEDG 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39812133  248 STPLHVAVR--TGQVEIVEHFLSLGLEINARDREGDTALHDAVRL-NRYKIIKLLLLHGADMMTKNLAGKTPTDLVQ 321
Cdd:PHA02859 124 KNLLHMYMCnfNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFhSDKKIFDFLTSLGIDINETNKSGYNCYDLIK 200
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 168-236 1.44e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 1.44e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 39812133  168 LADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQSH 236
Cdd:PTZ00322 102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 215-245 1.83e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.12  E-value: 1.83e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 39812133   215 CTAMHWAC-RGGHLEVVKLLQSHGADTNVRDK 245
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 218-316 2.91e-05

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 43.71  E-value: 2.91e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  218 MHWACRGGhlEVVKLLQSHGADTNVRDKLLS-------TPLHVAVRTGQVEIVEHFLSL---GLEINARDR-EGDTALHD 286
Cdd:PHA02736  21 LHYLCRNG--GVTDLLAFKNAISDENRYLVLeynrhgkQCVHIVSNPDKADPQEKLKLLmewGADINGKERvFGNTPLHI 98

                         90       100       110
                 ....*....|....*....|....*....|.
gi 39812133  287 AVRLNRYKIIKLLLLH-GADMMTKNLAGKTP 316
Cdd:PHA02736  99 AVYTQNYELATWLCNQpGVNMEILNYAFKTP 129
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 148-242 5.27e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.98  E-value: 5.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  148 DEETFLKAAV-EGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLLDNGATVD-FQDRLDCTAMHWACRGG 225
Cdd:PHA02875 134 DKFSPLHLAVmMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENN 213

                         90
                 ....*....|....*..
gi 39812133  226 HLEVVKLLQSHGADTNV 242
Cdd:PHA02875 214 KIDIVRLFIKRGADCNI 230
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 267-338 7.65e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 7.65e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 39812133  267 LSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTDLV------QLWQADTRHALEHPEPGA 338
Cdd:PTZ00322 102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAeengfrEVVQLLSRHSQCHFELGA 179
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 191-305 8.77e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 44.30  E-value: 8.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133   191 EGHMEILEKLLDNGATVDFQ--DRLDCTAMHW-ACRGGHLEVVKLLQSHGADTNVRDKLLstplHVAvRTGQVEIVEHFL 267
Cdd:TIGR00870  27 RGDLASVYRDLEEPKKLNINcpDRLGRSALFVaAIENENLELTELLLNLSCRGAVGDTLL----HAI-SLEYVDAVEAIL 101

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 39812133   268 SLgLEINARDR---------------EGDTALHDAVRLNRYKIIKLLLLHGAD 305
Cdd:TIGR00870 102 LH-LLAAFRKSgplelandqytseftPGITALHLAAHRQNYEIVKLLLERGAS 153
Ank_5 pfam13857
Ankyrin repeats (many copies);
262-320 1.44e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 1.44e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 39812133   262 IVEHFLslgLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTPTDLV 320
Cdd:pfam13857   1 LLEHGP---IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
150-201 2.08e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 2.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 39812133   150 ETFLKAAVEGKMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILEKLL 201
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 249-275 2.87e-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: 37.57  E-value: 2.87e-04
                           10        20
                   ....*....|....*....|....*..
gi 39812133    249 TPLHVAVRTGQVEIVEHFLSLGLEINA 275
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 185-316 3.07e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.56  E-value: 3.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  185 LHRASLEGHMEILEKLLDNGATVDFQDRLDCTAMHWACRGGHLEVVKLLQS------------------HGADTNVRDKL 246
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsinkcsvfytlvaikdafNNRNVEIFKII 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  247 LSTPLH-------VAVRTG------QVEIVEHFLSLGLEINARDRE-GDTALHDAVRLNRYKIIKLLLLHGADMMTKNLA 312
Cdd:PHA02878 121 LTNRYKniqtidlVYIDKKskddiiEAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200


                 ....
gi 39812133  313 GKTP 316
Cdd:PHA02878 201 NNSP 204
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 216-242 4.88e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.24  E-value: 4.88e-04
                          10        20
                  ....*....|....*....|....*..
gi 39812133   216 TAMHWACRGGHLEVVKLLQSHGADTNV 242
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 148-288 5.56e-04

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 42.05  E-value: 5.56e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133 148 DEETFLKAAVEGKMKVIEKFLADggSADTCDQFR------------------RTALHRASL---EGHMEILEKLLDNGAT 206
Cdd:cd22194  45 DKKKRLKKVSEAAVEELGELLKE--LKDLSRRRRktdvpdflmhkltasdtgKTCLMKALLninENTKEIVRILLAFAEE 122

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133 207 VDFQDRL-----------DCTAMHWACRGGHLEVVKLLQSHGADTNVRDK--------------LLSTPLHVAVRTGQVE 261
Cdd:cd22194 123 NGILDRFinaeyteeayeGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPE 202

                       170       180
                ....*....|....*....|....*...
gi 39812133 262 IVEHFLSLG-LEINARDREGDTALHDAV 288
Cdd:cd22194 203 IVQLLMEKEsTDITSQDSRGNTVLHALV 230
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 230-304 7.33e-04

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 39.80  E-value: 7.33e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 39812133  230 VKLLQSHGADTNVRDKLL-STPLHVAVRTGQVEIVEHFL-SLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGA 304
Cdd:PHA02743  76 IELLVNMGADINARELGTgNTLLHIAASTKNYELAEWLCrQLGVNLGAINYQHETAYHIAYKMRDRRMMEILRANGA 152
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 279-306 8.45e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 8.45e-04
                           10        20
                   ....*....|....*....|....*...
gi 39812133    279 EGDTALHDAVRLNRYKIIKLLLLHGADM 306
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 182-208 9.79e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 9.79e-04
                           10        20
                   ....*....|....*....|....*..
gi 39812133    182 RTALHRASLEGHMEILEKLLDNGATVD 208
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02946 PHA02946
ankyin-like protein; Provisional
 263-316 1.24e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.42  E-value: 1.24e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....
gi 39812133  263 VEHFLSLGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKTP 316
Cdd:PHA02946  55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTP 108
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 194-316 1.62e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 40.28  E-value: 1.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  194 MEILEKLLDNGATVDFQDRLDCTAMH-WACRGG-HLEVVKLLQSHGADTNVRDKLLSTPLHVavrtgqveivehFLSLGL 271
Cdd:PHA02716 297 ISVVYSFLQPGVKLHYKDSAGRTCLHqYILRHNiSTDIIKLLHEYGNDLNEPDNIGNTVLHT------------YLSMLS 364

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 39812133  272 EINARDREGDTALhdavrlnRYKIIKLLLLHGADMMTKNLAGKTP 316
Cdd:PHA02716 365 VVNILDPETDNDI-------RLDVIQCLISLGADITAVNCLGYTP 402
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 279-310 1.91e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 1.91e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 39812133   279 EGDTALHDAV-RLNRYKIIKLLLLHGADMMTKN 310
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 231-308 2.02e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.00  E-value: 2.02e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133 231 KLLQSHGADTNVRDKLLSTPLHVAVRTGQVEIVEHFLS-----LGLEINARDREGDTALHDAVRLNRYKIIKLLLLHGAD 305
Cdd:cd22192  35 KLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEaapelVNEPMTSDLYQGETALHIAVVNQNLNLVRELIARGAD 114


                ...
gi 39812133 306 MMT 308
Cdd:cd22192 115 VVS 117
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 249-278 2.83e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 2.83e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 39812133   249 TPLHVAV-RTGQVEIVEHFLSLGLEINARDR 278
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02798 PHA02798
ankyrin-like protein; Provisional
 260-316 4.30e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.05  E-value: 4.30e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 39812133  260 VEIVEHFLSLGLEINARDREGDTALHDAV-RLNRYK----IIKLLLLHGADMMTKNLAGKTP 316
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPLCTILsNIKDYKhmldIVKILIENGADINKKNSDGETP 112
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 279-305 4.33e-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: 4.33e-03
                          10        20
                  ....*....|....*....|....*..
gi 39812133   279 EGDTALHDAVRLNRYKIIKLLLLHGAD 305
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 182-212 5.32e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.19  E-value: 5.32e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 39812133   182 RTALHRASLE-GHMEILEKLLDNGATVDFQDR 212
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 249-275 6.35e-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: 33.77  E-value: 6.35e-03
                          10        20
                  ....*....|....*....|....*..
gi 39812133   249 TPLHVAVRTGQVEIVEHFLSLGLEINA 275
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 182-208 7.50e-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: 33.77  E-value: 7.50e-03
                          10        20
                  ....*....|....*....|....*..
gi 39812133   182 RTALHRASLEGHMEILEKLLDNGATVD 208
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02917 PHA02917
ankyrin-like protein; Provisional
 272-315 8.98e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 38.06  E-value: 8.98e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 39812133  272 EINARDREGDTALHDAVRLNRYKIIKLLLLHGADMMTKNLAGKT 315
Cdd:PHA02917 444 DINMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYT 487
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 160-285 9.34e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 37.94  E-value: 9.34e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133 160 KMKVIEKFLADGGSADTCDQFRRTALHRASLEGHMEILE--KLLDNGATVDFQDRLDC-----TAMHWACRGGHLEVVKL 232
Cdd:cd21882  12 RWYLTDSAYQRGATGKTCLHKAALNLNDGVNEAIMLLLEaaPDSGNPKELVNAPCTDEfyqgqTALHIAIENRNLNLVRL 91

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 39812133 233 LQSHGADTNVR---DKLLST----------PLHVAVRTGQVEIVEHFLSLGLEI---NARDREGDTALH 285
Cdd:cd21882  92 LVENGADVSARatgRFFRKSpgnlfyfgelPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNTVLH 160
PHA02946 PHA02946
ankyin-like protein; Provisional
 162-320 9.60e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 37.73  E-value: 9.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  162 KVIEKFLADGGSADTCDQFRRTALHRASLEGHmEILEK---LLDNGATVDFQ-DRLDCTAMhWACRGGHLEVVKLLQSHG 237
Cdd:PHA02946  86 RIVAMLLTHGADPNACDKQHKTPLYYLSGTDD-EVIERinlLVQYGAKINNSvDEEGCGPL-LACTDPSERVFKKIMSIG 163

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133  238 ADTNVRDKLLSTPLHVAVRTG--QVEIVEHFLSLGLEINARDREGDTALHDAVR--LNRYKIIKlLLLHGADMMTKNLAG 313
Cdd:PHA02946 164 FEARIVDKFGKNHIHRHLMSDnpKASTISWMMKLGISPSKPDHDGNTPLHIVCSktVKNVDIIN-LLLPSTDVNKQNKFG 242


                 ....*..
gi 39812133  314 KTPTDLV 320
Cdd:PHA02946 243 DSPLTLL 249
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 146-294 9.97e-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: 37.75  E-value: 9.97e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133   146 PVDEETFLKAAVEGK----MKVIEKFLADGGSADTCdqfrrtaLHRASLEGHM---EILEKLLDNG------------AT 206
Cdd:TIGR00870  50 RLGRSALFVAAIENEnlelTELLLNLSCRGAVGDTL-------LHAISLEYVDaveAILLHLLAAFrksgplelandqYT 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 39812133   207 VDFQdrLDCTAMHWACRGGHLEVVKLLQSHGADTNVR---DKLLST-----------PLHVAVRTGQVEIVEHFLSLGLE 272
Cdd:TIGR00870 123 SEFT--PGITALHLAAHRQNYEIVKLLLERGASVPARacgDFFVKSqgvdsfyhgesPLNAAACLGSPSIVALLSEDPAD 200

                         170       180
                  ....*....|....*....|..
gi 39812133   273 INARDREGDTALHDAVRLNRYK 294
Cdd:TIGR00870 201 ILTADSLGNTLLHLLVMENEFK 222
 
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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