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Conserved domains on  [gi|45359372|gb|AAS58862|]
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POTE2D [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];
138-368 9.13e-51

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.68  E-value: 9.13e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 138 EDLDKLHRAAWWGKVPRKDLIVMLRDTDVNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQ 217
Cdd:COG0666  52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 218 EDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKAN 297
Cdd:COG0666 132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45359372 298 LNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYKEKQMLKI 368
Cdd:COG0666 212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
138-368 9.13e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.68  E-value: 9.13e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 138 EDLDKLHRAAWWGKVPRKDLIVMLRDTDVNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQ 217
Cdd:COG0666  52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 218 EDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKAN 297
Cdd:COG0666 132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45359372 298 LNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYKEKQMLKI 368
Cdd:COG0666 212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 158-361 4.56e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 96.66  E-value: 4.56e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  158 IVMLrDTDVNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTAL-----IKAVQCQEDECALMLLEHGTDP 232
Cdd:PHA03100  21 IIME-DDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  233 NIPDEYGNTTLHYAIYN--EDKLMAKALLLYGADIESKNKHGLTPL--LLGVHEQKQQVVKFLIKKKANLNALDR----- 303
Cdd:PHA03100 100 NAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLhlYLESNKIDLKILKLLIDKGVDINAKNRvnyll 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45359372  304 -----------YGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYK 361
Cdd:PHA03100 180 sygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-269 1.38e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 1.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372   177 LHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGtDPNIPDeYGNTTLHYAIYNEDKLMAK 256
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 45359372   257 ALLLYGADIESKN 269
Cdd:pfam12796  79 LLLEKGADINVKD 91
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 154-362 5.08e-10

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: 61.25  E-value: 5.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372   154 RKDLIVMLRDTDVNKKDKQK------RTAL-HLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEdECALMLL 226
Cdd:TIGR00870  27 RGDLASVYRDLEEPKKLNINcpdrlgRSALfVAAIENENLELTELLLNLSCRGAVGDTLLHAISLEYVDAVE-AILLHLL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372   227 EHgtdpniPDEYGNTTLHYAIYNEDklmakallLYgadiesknkHGLTPLLLGVHEQKQQVVKFLIKKKANLNA------ 300
Cdd:TIGR00870 106 AA------FRKSGPLELANDQYTSE--------FT---------PGITALHLAAHRQNYEIVKLLLERGASVPAracgdf 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372   301 --------LDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVsshhhVICQLLSDYKE 362
Cdd:TIGR00870 163 fvksqgvdSFYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV-----MENEFKAEYEE 227
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 171-340 9.28e-10

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: 60.03  E-value: 9.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 171 KQKRTA---LHLASANGNSEVVK-LLLDRRCqlnvlDNKKR-----TALIKAVQCQEDECALMLLEhgTDP---NIP--- 235
Cdd:cd22192  12 QQKRISespLLLAAKENDVQAIKkLLKCPSC-----DLFQRgalgeTALHVAALYDNLEAAVVLME--AAPelvNEPmts 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 236 DEY-GNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLtplllgvheqkqqvvkFLIKKKANLNaldRYGRTALILAVC 314
Cdd:cd22192  85 DLYqGETALHIAVVNQNLNLVRELIARGADVVSPRATGT----------------FFRPGPKNLI---YYGEHPLSFAAC 145

                       170       180
                ....*....|....*....|....*.
gi 45359372 315 CGSASIVSLLLEQNIDVSSQDLSGQT 340
Cdd:cd22192 146 VGNEEIVRLLIEHGADIRAQDSLGNT 171
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 172-201 6.31e-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: 36.80  E-value: 6.31e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 45359372    172 QKRTALHLASANGNSEVVKLLLDRRCQLNV 201
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
138-368 9.13e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.68  E-value: 9.13e-51
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 138 EDLDKLHRAAWWGKVPRKDLIVMLRDTDVNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQ 217
Cdd:COG0666  52 ALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 218 EDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKAN 297
Cdd:COG0666 132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGAD 211

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45359372 298 LNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYKEKQMLKI 368
Cdd:COG0666 212 VNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
139-374 5.45e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 169.75  E-value: 5.45e-50
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 139 DLDKLHRAAWWGKVPRKDLIVMLRDTDVNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQE 218
Cdd:COG0666  20 LLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGD 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 219 DECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANL 298
Cdd:COG0666 100 LEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45359372 299 NALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYKEKQMLKISSENSN 374
Cdd:COG0666 180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
143-341 3.10e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 154.73  E-value: 3.10e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 143 LHRAAWWGkvpRKDLIVML--RDTDVNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDE 220
Cdd:COG0666  91 LHAAARNG---DLEIVKLLleAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLE 167

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 221 CALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNA 300
Cdd:COG0666 168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 45359372 301 LDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTA 341
Cdd:COG0666 248 KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
157-357 1.58e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.01  E-value: 1.58e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 157 LIVMLRDTDVNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGTDPNIPD 236
Cdd:COG0666   5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 237 EYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCG 316
Cdd:COG0666  85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANG 164

                       170       180       190       200
                ....*....|....*....|....*....|....*....|.
gi 45359372 317 SASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLL 357
Cdd:COG0666 165 NLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
143-309 1.17e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 129.30  E-value: 1.17e-34
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 143 LHRAAWWGKVprkDLIVML--RDTDVNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDE 220
Cdd:COG0666 124 LHLAAYNGNL---EIVKLLleAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 221 CALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNA 300
Cdd:COG0666 201 IVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280


                ....*....
gi 45359372 301 LDRYGRTAL 309
Cdd:COG0666 281 ALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
187-357 1.47e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.87  E-value: 1.47e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 187 EVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIE 266
Cdd:COG0666   2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 267 SKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAV 346
Cdd:COG0666  82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                       170
                ....*....|.
gi 45359372 347 SSHHHVICQLL 357
Cdd:COG0666 162 ANGNLEIVKLL 172
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 158-361 4.56e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 96.66  E-value: 4.56e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  158 IVMLrDTDVNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTAL-----IKAVQCQEDECALMLLEHGTDP 232
Cdd:PHA03100  21 IIME-DDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANV 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  233 NIPDEYGNTTLHYAIYN--EDKLMAKALLLYGADIESKNKHGLTPL--LLGVHEQKQQVVKFLIKKKANLNALDR----- 303
Cdd:PHA03100 100 NAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLhlYLESNKIDLKILKLLIDKGVDINAKNRvnyll 179

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45359372  304 -----------YGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYK 361
Cdd:PHA03100 180 sygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248
Ank_2 pfam12796
Ankyrin repeats (3 copies);
177-269 1.38e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 1.38e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372   177 LHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGtDPNIPDeYGNTTLHYAIYNEDKLMAK 256
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHA-DVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 45359372   257 ALLLYGADIESKN 269
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 154-332 1.10e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 87.03  E-value: 1.10e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  154 RKDLIVMLRDT--DVNKKDKQKRTALHLAS-----ANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALM-- 224
Cdd:PHA03100  47 NIDVVKILLDNgaDINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVey 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  225 LLEHGTDPNIPDEYGNTTLH-YAIYNEDKL-MAKALLL----------------YGADIESKNKHGLTPLLLGVHEQKQQ 286
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHlYLESNKIDLkILKLLIDkgvdinaknrvnyllsYGVPINIKDVYGFTPLHYAVYNNNPE 206

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 45359372  287 VVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVS 332
Cdd:PHA03100 207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 158-304 1.26e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 86.64  E-value: 1.26e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  158 IVMLRDTDVNKKDKQKRTALHLASAN--GNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECAL------------ 223
Cdd:PHA03100  91 LLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKIlkllidkgvdin 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  224 ------MLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKAN 297
Cdd:PHA03100 171 aknrvnYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250


                 ....*..
gi 45359372  298 LNALDRY 304
Cdd:PHA03100 251 IKTIIET 257
Ank_2 pfam12796
Ankyrin repeats (3 copies);
243-335 8.78e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 8.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372   243 LHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIkKKANLNALDrYGRTALILAVCCGSASIVS 322
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 45359372   323 LLLEQNIDVSSQD 335
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 165-360 1.26e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 84.34  E-value: 1.26e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  165 DVNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLD-----------------------------NKKRTALIKAVQ 215
Cdd:PHA02876 170 DVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIAlddlsvlecavdsknidtikaiidnrsniNKNDLSLLKAIR 249

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  216 CQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNE--DKLMAKaLLLYGADIESKNKHGLTPL-LLGVHEQKQQVVKFLI 292
Cdd:PHA02876 250 NEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPslSRLVPK-LLERGADVNAKNIKGETPLyLMAKNGYDTENIRTLI 328

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 45359372  293 KKKANLNALDRYGRTALILAVCCG-SASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDY 360
Cdd:PHA02876 329 MLGADVNAADRLYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDY 397
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 151-361 1.37e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 83.78  E-value: 1.37e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  151 KVPRKDLIVMLRDTDVNKKDKQKRTALHlasaNGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGT 230
Cdd:PHA02878  83 KLGMKEMIRSINKCSVFYTLVAIKDAFN----NRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGA 158

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  231 DPNIPDEY-GNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTAL 309
Cdd:PHA02878 159 DINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 45359372  310 ILAVC-CGSASIVSLLLEQNIDVSSQD-LSGQTAREYAVSSHHhvICQLLSDYK 361
Cdd:PHA02878 239 HISVGyCKDYDILKLLLEHGVDVNAKSyILGLTALHSSIKSER--KLKLLLEYG 290
Ank_2 pfam12796
Ankyrin repeats (3 copies);
143-236 1.09e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 1.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372   143 LHRAAWWGKVprkDLIVML--RDTDVNKKDKQKRTALHLASANGNSEVVKLLLDrRCQLNVlDNKKRTALIKAVQCQEDE 220
Cdd:pfam12796   1 LHLAAKNGNL---ELVKLLleNGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNL-KDNGRTALHYAARSGHLE 75

                          90
                  ....*....|....*.
gi 45359372   221 CALMLLEHGTDPNIPD 236
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 224-349 2.19e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.07  E-value: 2.19e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  224 MLLEHGTDPNIPDEYGNTTLHYAIYN---EDKLMAKALLLYGADIESKNKHGLTPL-LLGVHEQKQQVVKFLIKKKANLN 299
Cdd:PHA03095  32 RLLAAGADVNFRGEYGKTPLHLYLHYsseKVKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVN 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 45359372  300 ALDRYGRTalILAVCCGSASI----VSLLLEQNIDVSSQDLSGQTAREYAVSSH 349
Cdd:PHA03095 112 AKDKVGRT--PLHVYLSGFNInpkvIRLLLRKGADVNALDLYGMTPLAVLLKSR 163
PHA03095 PHA03095
ankyrin-like protein; Provisional
 165-345 3.34e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 79.68  E-value: 3.34e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  165 DVNKKDKQKRTALHLASANGNS---EVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECAL-MLLEHGTDPNIPDEYGN 240
Cdd:PHA03095  39 DVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIkLLIKAGADVNAKDKVGR 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  241 TTLHyaIY----NEDKLMAKALLLYGADIESKNKHGLTPL--LLGVHEQKQQVVKFLIKKKANLNALDRYGRTAL--ILA 312
Cdd:PHA03095 119 TPLH--VYlsgfNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLhhHLQ 196

                        170       180       190
                 ....*....|....*....|....*....|...
gi 45359372  313 VCCGSASIVSLLLEQNIDVSSQDLSGQTAREYA 345
Cdd:PHA03095 197 SFKPRARIVRELIRAGCDPAATDMLGNTPLHSM 229
PHA03095 PHA03095
ankyrin-like protein; Provisional
 165-328 7.00e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.53  E-value: 7.00e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  165 DVNKKDKQKRTALH--LASANGNSEVVKLLLDRRCQLNVLDNKKRTAL-IKAVQCQEDECAL-MLLEHGTDPNIPDEYGN 240
Cdd:PHA03095 144 DVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLhHHLQSFKPRARIVrELIRAGCDPAATDMLGN 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  241 TTLHY-AIYNEDK--LMAKaLLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGS 317
Cdd:PHA03095 224 TPLHSmATGSSCKrsLVLP-LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNN 302

                        170
                 ....*....|.
gi 45359372  318 ASIVSLLLEQN 328
Cdd:PHA03095 303 GRAVRAALAKN 313
PHA03095 PHA03095
ankyrin-like protein; Provisional
 165-353 5.02e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.22  E-value: 5.02e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  165 DVNKKDKQKRTALH--LASANGNSEVVKLLLDRRCQLNVLDNKKRT---ALIKAVQCqEDECALMLLEHGTDPNIPDEYG 239
Cdd:PHA03095 109 DVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTplaVLLKSRNA-NVELLRLLIDAGADVYAVDDRF 187

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  240 NTTLHY-AIY---NEDKLmaKALLLYGADIESKNKHGLTPL--LLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAV 313
Cdd:PHA03095 188 RSLLHHhLQSfkpRARIV--RELIRAGCDPAATDMLGNTPLhsMATGSSCKRSLVLPLLIAGISINARNRYGQTPLHYAA 265

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 45359372  314 CCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVI 353
Cdd:PHA03095 266 VFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRA 305
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 165-359 2.62e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.84  E-value: 2.62e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  165 DVNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLdnkkrtalikAVQCQEDECALMLLEHGTDPNIPDEYGNTTLH 244
Cdd:PHA02874  60 DINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIL----------PIPCIEKDMIKTILDCGIDVNIKDAELKTFLH 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  245 YAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLL 324
Cdd:PHA02874 130 YAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLL 209

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 45359372  325 LEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSD 359
Cdd:PHA02874 210 IDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINN 244
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 143-360 3.21e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.86  E-value: 3.21e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  143 LHRAAWWGKVPRKDLIVMLRDTDVNKKDKQKRTALHLASANG-NSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQED-E 220
Cdd:PHA02876 277 LHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDRNkD 356

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  221 CALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQV-VKFLIKKKANLN 299
Cdd:PHA02876 357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVN 436

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45359372  300 ALDRYGRTALILAvCCGSA--SIVSLLLEQNIDVSSQDLSGQTAREYAVSshHHVICQLLSDY 360
Cdd:PHA02876 437 SKNKDLSTPLHYA-CKKNCklDVIEMLLDNGADVNAINIQNQYPLLIALE--YHGIVNILLHY 496
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 158-330 5.41e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 69.63  E-value: 5.41e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  158 IVMLRDTDVNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLN-VLDNKKRTALIKAVQCQEDECALMLLEHGTDPNIPD 236
Cdd:PHA02875  53 LLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPN 132

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  237 EYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGR-TALILAVCC 315
Cdd:PHA02875 133 TDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvAALCYAIEN 212

                        170
                 ....*....|....*
gi 45359372  316 GSASIVSLLLEQNID 330
Cdd:PHA02875 213 NKIDIVRLFIKRGAD 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 185-346 8.16e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.22  E-value: 8.16e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  185 NSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGAD 264
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  265 IESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVcCGSASIVSLLLeQNIDVSSQDLSGQTAREY 344
Cdd:PHA02874 183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAI-IHNRSAIELLI-NNASINDQDIDGSTPLHH 260


                 ..
gi 45359372  345 AV 346
Cdd:PHA02874 261 AI 262
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 165-280 1.08e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.14  E-value: 1.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  165 DVNKKDKQK-RTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGTDPNIPDEYGNTTL 243
Cdd:PHA02878 159 DINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45359372  244 HYA-----------------------------------IYNEDKLmaKALLLYGADIESKNKHGLTPLLLGV 280
Cdd:PHA02878 239 HISvgyckdydilklllehgvdvnaksyilgltalhssIKSERKL--KLLLEYGADINSLNSYKLTPLSSAV 308
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 156-304 1.82e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 68.74  E-value: 1.82e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  156 DLIVMLRDTDVNkkDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALML--LEHGTDPN 233
Cdd:PLN03192 543 ELLKAKLDPDIG--DSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhFASISDPH 620

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45359372  234 IpdeyGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRY 304
Cdd:PLN03192 621 A----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 175-334 1.14e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.78  E-value: 1.14e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  175 TALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGTDPN-IPDEYGNTTLHYAIYNEDKL 253
Cdd:PHA02875  37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLD 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  254 MAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQ--NIDV 331
Cdd:PHA02875 117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSgaNIDY 196


                 ...
gi 45359372  332 SSQ 334
Cdd:PHA02875 197 FGK 199
Ank_2 pfam12796
Ankyrin repeats (3 copies);
287-367 2.87e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 2.87e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372   287 VVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEqNIDVSSQDlSGQTAREYAVSSHHHVICQLLSDYKEKQML 366
Cdd:pfam12796  12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINV 89


                  .
gi 45359372   367 K 367
Cdd:pfam12796  90 K 90
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 174-359 9.91e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.70  E-value: 9.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  174 RTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKL 253
Cdd:PHA02875   3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  254 MAKALLLYGADIESK-NKHGLTPLLLGVHEQKQQVVKFLIKKKA--NLNALDRYgrTALILAVCCGSASIVSLLLEQNID 330
Cdd:PHA02875  83 AVEELLDLGKFADDVfYKDGMTPLHLATILKKLDIMKLLIARGAdpDIPNTDKF--SPLHLAVMMGDIKGIELLIDHKAC 160

                        170       180
                 ....*....|....*....|....*....
gi 45359372  331 VSSQDLSGQTAREYAVSSHHHVICQLLSD 359
Cdd:PHA02875 161 LDIEDCCGCTPLIIAMAKGDIAICKMLLD 189
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 154-362 5.08e-10

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: 61.25  E-value: 5.08e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372   154 RKDLIVMLRDTDVNKKDKQK------RTAL-HLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEdECALMLL 226
Cdd:TIGR00870  27 RGDLASVYRDLEEPKKLNINcpdrlgRSALfVAAIENENLELTELLLNLSCRGAVGDTLLHAISLEYVDAVE-AILLHLL 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372   227 EHgtdpniPDEYGNTTLHYAIYNEDklmakallLYgadiesknkHGLTPLLLGVHEQKQQVVKFLIKKKANLNA------ 300
Cdd:TIGR00870 106 AA------FRKSGPLELANDQYTSE--------FT---------PGITALHLAAHRQNYEIVKLLLERGASVPAracgdf 162

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372   301 --------LDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVsshhhVICQLLSDYKE 362
Cdd:TIGR00870 163 fvksqgvdSFYHGESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV-----MENEFKAEYEE 227
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 171-340 9.28e-10

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: 60.03  E-value: 9.28e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 171 KQKRTA---LHLASANGNSEVVK-LLLDRRCqlnvlDNKKR-----TALIKAVQCQEDECALMLLEhgTDP---NIP--- 235
Cdd:cd22192  12 QQKRISespLLLAAKENDVQAIKkLLKCPSC-----DLFQRgalgeTALHVAALYDNLEAAVVLME--AAPelvNEPmts 84

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 236 DEY-GNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLtplllgvheqkqqvvkFLIKKKANLNaldRYGRTALILAVC 314
Cdd:cd22192  85 DLYqGETALHIAVVNQNLNLVRELIARGADVVSPRATGT----------------FFRPGPKNLI---YYGEHPLSFAAC 145

                       170       180
                ....*....|....*....|....*.
gi 45359372 315 CGSASIVSLLLEQNIDVSSQDLSGQT 340
Cdd:cd22192 146 VGNEEIVRLLIEHGADIRAQDSLGNT 171
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 217-340 1.36e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.69  E-value: 1.36e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  217 QEDE--CALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKK 294
Cdd:PHA02876 154 QQDEllIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45359372  295 KANL-----------------------------NALDRYGRTALILAVCCGSAS-IVSLLLEQNIDVSSQDLSGQT 340
Cdd:PHA02876 234 RSNInkndlsllkairnedletslllydagfsvNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKNIKGET 309
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 158-367 2.43e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.35  E-value: 2.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  158 IVMLRDTDVNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGTDPNI--- 234
Cdd:PHA02874  20 IIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSIlpi 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  235 PDeygnttlhyaIYNEdklMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVC 314
Cdd:PHA02874 100 PC----------IEKD---MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIK 166

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|...
gi 45359372  315 CGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYKEKQMLK 367
Cdd:PHA02874 167 HNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK 219
Ank_5 pfam13857
Ankyrin repeats (many copies);
165-213 8.76e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 8.76e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 45359372   165 DVNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKA 213
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
225-276 8.85e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 8.85e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 45359372   225 LLEHGT-DPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPL 276
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02798 PHA02798
ankyrin-like protein; Provisional
 157-363 9.34e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 53.69  E-value: 9.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  157 LIVMLRDTDVNKKDKQKRTALHLASANG---NSEVVKLLLDRRCQLNVLDNKKRTALIKAVQ--CQED-ECALMLLEHGT 230
Cdd:PHA02798  93 KILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTMLQVYLQsnHHIDiEIIKLLLEKGV 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  231 DPN-IPDEYGNTTLH-YAIYN---------------------EDKLMAKALLLY---------------------GADIE 266
Cdd:PHA02798 173 DINtHNNKEKYDTLHcYFKYNidridadilklfvdngfiinkENKSHKKKFMEYlnsllydnkrfkknildfifsYIDIN 252

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  267 SKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAV 346
Cdd:PHA02798 253 QVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENESKFIFNSILNKKPNKNTISYTYYKLRKHIL 332

                        250
                 ....*....|....*..
gi 45359372  347 SSHHHVICQLLSDYKEK 363
Cdd:PHA02798 333 NVEGDFINQLEFDIIKK 349
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 172-295 3.81e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.94  E-value: 3.81e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 172 QKRTALHLASANGNSEVVKLLLDRRCQLN------VLDNKKRTALIK--------AVQCQEDECALMLLEHGTDPNIPDE 237
Cdd:cd22192  88 QGETALHIAVVNQNLNLVRELIARGADVVspratgTFFRPGPKNLIYygehplsfAACVGNEEIVRLLIEHGADIRAQDS 167

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 45359372 238 YGNTTLHYAIYNEDKLMAKAL--LLYGADIES--------KNKHGLTPLLLGVHEQKQQVVKFLIKKK 295
Cdd:cd22192 168 LGNTVLHILVLQPNKTFACQMydLILSYDKEDdlqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
Ank_4 pfam13637
Ankyrin repeats (many copies);
272-325 5.88e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 5.88e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 45359372   272 GLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLL 325
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
192-246 7.73e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 7.73e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 45359372   192 LLDRR-CQLNVLDNKKRTALIKAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYA 246
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 256-341 8.27e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.79  E-value: 8.27e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  256 KALLLYGADIESKNKHGLTPLLLGVH---EQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGS-ASIVSLLLEQNIDV 331
Cdd:PHA03095  31 RRLLAAGADVNFRGEYGKTPLHLYLHyssEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADV 110

                         90
                 ....*....|
gi 45359372  332 SSQDLSGQTA 341
Cdd:PHA03095 111 NAKDKVGRTP 120
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 172-295 9.53e-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: 50.65  E-value: 9.53e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 172 QKRTALHLASANGNSEVVKLLLDRRCQLNVLDNK---KRTA----------LIKAVQCQEDECALMLLEHGTDP---NIP 235
Cdd:cd21882  72 QGQTALHIAIENRNLNLVRLLVENGADVSARATGrffRKSPgnlfyfgelpLSLAACTNQEEIVRLLLENGAQPaalEAQ 151

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45359372 236 DEYGNTTLHYAIYNEDKL---------MAKALLLYGADI-------ESKNKHGLTPLLLGVHEQKQQVVKFLIKKK 295
Cdd:cd21882 152 DSLGNTVLHALVLQADNTpensafvcqMYNLLLSYGAHLdptqqleEIPNHQGLTPLKLAAVEGKIVMFQHILQRE 227
Ank_4 pfam13637
Ankyrin repeats (many copies);
143-193 1.16e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 1.16e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 45359372   143 LHRAAWWGKVprkDLIVMLRDT--DVNKKDKQKRTALHLASANGNSEVVKLLL 193
Cdd:pfam13637   5 LHAAAASGHL---ELLRLLLEKgaDINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
207-259 1.34e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 1.34e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 45359372   207 RTALIKAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALL 259
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 185-354 1.73e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 49.67  E-value: 1.73e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  185 NSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLL--YG 262
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERINLLvqYG 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  263 ADI-ESKNKHGLTPlLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGS--ASIVSLLLEQNIDVSSQDLSGQ 339
Cdd:PHA02946 131 AKInNSVDEEGCGP-LLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNpkASTISWMMKLGISPSKPDHDGN 209

                        170
                 ....*....|....*
gi 45359372  340 TAReyavsshhHVIC 354
Cdd:PHA02946 210 TPL--------HIVC 216
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 251-338 6.80e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 6.80e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  251 DKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNID 330
Cdd:PTZ00322  94 DAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173


                 ....*...
gi 45359372  331 VSSQDLSG 338
Cdd:PTZ00322 174 HFELGANA 181
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 222-293 7.89e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 7.89e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45359372  222 ALMLLEHGTDPNIPDEYGNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIK 293
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_2 pfam12796
Ankyrin repeats (3 copies);
309-365 8.02e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.95  E-value: 8.02e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 45359372   309 LILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDYKEKQM 365
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL 57
Ank_5 pfam13857
Ankyrin repeats (many copies);
296-345 8.15e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 8.15e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 45359372   296 ANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYA 345
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 180-357 8.28e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.94  E-value: 8.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  180 ASANGNSEVVKLLLDRRCQLNVLDNKKRTAL-IKAVQCQEDeCALMLLEHGTDPNIPDEYGNTTL-------HYAIYNed 251
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLhIAASKGYED-CVLVLLKHACNVHIRDANGNTALwnaisakHHKIFR-- 608

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  252 klmakaLLLYGADIEskNKHGLTPLLLgvheqkqqvvkfLIKKKANLNALDRygrtalilavccgsasivslLLEQNIDV 331
Cdd:PLN03192 609 ------ILYHFASIS--DPHAAGDLLC------------TAAKRNDLTAMKE--------------------LLKQGLNV 648

                        170       180
                 ....*....|....*....|....*.
gi 45359372  332 SSQDLSGQTAREYAVSSHHHVICQLL 357
Cdd:PLN03192 649 DSEDHQGATALQVAMAEDHVDMVRLL 674
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 207-340 1.87e-05

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: 46.41  E-value: 1.87e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 207 RTALIKAV---QCQEDECALMLLEHGTDPNIP---------DEY--GNTTLHYAIYNEDKLMAKALLLYGADIESKNKhg 272
Cdd:cd21882  27 KTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPkelvnapctDEFyqGQTALHIAIENRNLNLVRLLVENGADVSARAT-- 104

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45359372 273 ltplllGVHEQKQQVVKFLikkkanlnaldrYGRTALILAVCCGSASIVSLLLE---QNIDVSSQDLSGQT 340
Cdd:cd21882 105 ------GRFFRKSPGNLFY------------FGELPLSLAACTNQEEIVRLLLEngaQPAALEAQDSLGNT 157
Ank_4 pfam13637
Ankyrin repeats (many copies);
239-292 2.63e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 2.63e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 45359372   239 GNTTLHYAIYNEDKLMAKALLLYGADIESKNKHGLTPLLLGVHEQKQQVVKFLI 292
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02798 PHA02798
ankyrin-like protein; Provisional
 178-332 4.76e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.21  E-value: 4.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  178 HLASANGNSEVVKLLLDRRCQLNVLDNKKRTALikavqcqedeCALMllehgtdPNIPDeygnttlhyaiYNEDKLMAKA 257
Cdd:PHA02798  43 YLQRDSPSTDIVKLFINLGANVNGLDNEYSTPL----------CTIL-------SNIKD-----------YKHMLDIVKI 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  258 LLLYGADIESKNKHGLTPLLLGVHE---QKQQVVKFLIKKKANLNALDRYGRTALILAV---CCGSASIVSLLLEQNIDV 331
Cdd:PHA02798  95 LIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLqsnHHIDIEIIKLLLEKGVDI 174


                 .
gi 45359372  332 S 332
Cdd:PHA02798 175 N 175
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 288-360 6.60e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 6.60e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 45359372  288 VKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHHHVICQLLSDY 360
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 280-350 2.20e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 2.20e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 45359372  280 VHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLSGQTAREYAVSSHH 350
Cdd:PHA02876 153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKN 223
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 174-204 2.68e-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: 38.04  E-value: 2.68e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 45359372   174 RTALHLASA-NGNSEVVKLLLDRRCQLNVLDN 204
Cdd:pfam00023   3 NTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 260-340 3.20e-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: 42.82  E-value: 3.20e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 260 LYGADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDR--------------YGRTALILAVCCGSASIVSLLL 325
Cdd:cd22194 129 FINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPEIVQLLM 208

                        90
                ....*....|....*.
gi 45359372 326 EQ-NIDVSSQDLSGQT 340
Cdd:cd22194 209 EKeSTDITSQDSRGNT 224
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 207-340 3.65e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 42.48  E-value: 3.65e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372 207 RTALIKAV---QCQEDECALMLLEHGTDPNIPDEY-----------GNTTLHYAIYNEDKLMAKALLLYGADIESKNKhg 272
Cdd:cd22193  30 KTCLMKALlnlNPGTNDTIRILLDIAEKTDNLKRFinaeytdeyyeGQTALHIAIERRQGDIVALLVENGADVHAHAK-- 107

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 45359372 273 ltplllGVHEQKQ-QVVKFLikkkanlnaldrYGRTALILAVCCGSASIVSLLLE---QNIDVSSQDLSGQT 340
Cdd:cd22193 108 ------GRFFQPKyQGEGFY------------FGELPLSLAACTNQPDIVQYLLEnehQPADIEAQDSRGNT 161
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 183-275 5.97e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 5.97e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  183 NGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVqcqeDECAL------MLLEHGTDPNIPDEYGNTTLH-YAIYNEDKLMA 255
Cdd:PHA02859 100 NVEPEILKILIDSGSSITEEDEDGKNLLHMYM----CNFNVrinvikLLIDSGVSFLNKDFDNNNILYsYILFHSDKKIF 175

                         90       100
                 ....*....|....*....|
gi 45359372  256 KALLLYGADIESKNKHGLTP 275
Cdd:PHA02859 176 DFLTSLGIDINETNKSGYNC 195
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 172-201 6.31e-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: 36.80  E-value: 6.31e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 45359372    172 QKRTALHLASANGNSEVVKLLLDRRCQLNV 201
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 165-228 7.59e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 7.59e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 45359372  165 DVNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEH 228
Cdd:PTZ00322 107 DPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 174-201 8.32e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 8.32e-04
                          10        20
                  ....*....|....*....|....*...
gi 45359372   174 RTALHLASANGNSEVVKLLLDRRCQLNV 201
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 238-270 1.35e-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. 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: 36.11  E-value: 1.35e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 45359372   238 YGNTTLHYAIYNEDKL-MAKALLLYGADIESKNK 270
Cdd:pfam00023   1 DGNTPLHLAAGRRGNLeIVKLLLSKGADVNARDK 34
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 188-278 2.17e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.58  E-value: 2.17e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  188 VVKLLLDRRCQLNVLDNKKRTALIKAVQCQEDECALMLLEHGTDPNIPDEYGNTT-LHYAIYNEDKLMAKALLLYGADIE 266
Cdd:PHA02884  52 ILKLGADPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITpLYISVLHGCLKCLEILLSYGADIN 131

                         90
                 ....*....|..
gi 45359372  267 SKNKHGLTPLLL 278
Cdd:PHA02884 132 IQTNDMVTPIEL 143
PHA02791 PHA02791
ankyrin-like protein; Provisional
 155-247 2.44e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 39.25  E-value: 2.44e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  155 KDLIVMLRDTDVNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLNVLDNKkrTALIKAVQCQEDECALMLLEHGTDPNI 234
Cdd:PHA02791  12 KQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLENE--FPLHQAATLEDTKIVKILLFSGMDDSQ 89

                         90
                 ....*....|...
gi 45359372  235 PDEYGNTTLHYAI 247
Cdd:PHA02791  90 FDDKGNTALYYAV 102
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 224-276 3.41e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 39.51  E-value: 3.41e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 45359372  224 MLLEHGTDPNIPDEYGNTTLHY-------------AIYNEDKL-MAKALLLYGADIESKNKHGLTPL 276
Cdd:PHA02716 337 LLHEYGNDLNEPDNIGNTVLHTylsmlsvvnildpETDNDIRLdVIQCLISLGADITAVNCLGYTPL 403
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 304-335 4.05e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.57  E-value: 4.05e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 45359372   304 YGRTALILAVC-CGSASIVSLLLEQNIDVSSQD 335
Cdd:pfam00023   1 DGNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 109-337 5.84e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.89  E-value: 5.84e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  109 CRGSGKSKVGAWGDYDDSAFMEPRYHVRGEDLDKLHRAAWWGKVPRKDLIVMLRDTDVNKKDKQKRTALHLASANGNSEV 188
Cdd:PHA02876  11 CRGNCIDILSAIDNYDLHKHGANQCENESIPFTAIHQALQLRQIDIVEEIIQQNPELIYITDHKCHSTLHTICIIPNVMD 90

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  189 VKLLLDRRCQLnVLDNKKRTALIKAVQCqeDECALMLLEHGTDPN-IPDEYGNTTLHYA------IYNEDKLMAKALLLY 261
Cdd:PHA02876  91 IVISLTLDCDI-ILDIKYASIILNKHKL--DEACIHILKEAISGNdIHYDKINESIEYMklikerIQQDELLIAEMLLEG 167

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 45359372  262 GADIESKNKHGLTPLLLGVHEQKQQVVKFLIKKKANLNALDRYGRTALILAVCCGSASIVSLLLEQNIDVSSQDLS 337
Cdd:PHA02876 168 GADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDLS 243
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 238-266 7.23e-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: 7.23e-03
                           10        20
                   ....*....|....*....|....*....
gi 45359372    238 YGNTTLHYAIYNEDKLMAKALLLYGADIE 266
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 143-234 9.27e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 38.05  E-value: 9.27e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 45359372  143 LHRAAWWGKVPRKDLIVMLRDTdVNKKDKQKRTALHLASANGNSEVVKLLLDRRCQLN-VLDNKKRTALIKAVQCQEDEC 221
Cdd:PHA02875 139 LHLAVMMGDIKGIELLIDHKAC-LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDI 217

                         90
                 ....*....|...
gi 45359372  222 ALMLLEHGTDPNI 234
Cdd:PHA02875 218 VRLFIKRGADCNI 230
 
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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