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Conserved domains on  [gi|767942279|ref|XP_011533898|]
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ankyrin repeat domain-containing protein 6 isoform X5 [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];
95-254 1.72e-42

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.88  E-value: 1.72e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279  95 REKEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLAC 174
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 175 QNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 254
Cdd:COG0666  162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
95-254 1.72e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.88  E-value: 1.72e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279  95 REKEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLAC 174
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 175 QNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 254
Cdd:COG0666  162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
137-229 1.08e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 1.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279  137 LHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRvLLLAGSRADLKNNaGDTALHVAAALNHKKVAK 216
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 767942279  217 ILLEAGADTTIVN 229
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 105-257 6.32e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.76  E-value: 6.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 105 HRATVvgntEIIAALIHEGCALDRQDKDGNTALHEaswhgFSQSAK-------LLIKAGANVLAKNKAGNTALHLACQNS 177
Cdd:PHA03095 163 RNANV----ELLRLLIDAGADVYAVDDRFRSLLHH-----HLQSFKprarivrELIRAGCDPAATDMLGNTPLHSMATGS 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 178 HSQSTRV--LLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPE-VALLLTKA 254
Cdd:PHA03095 234 SCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRaVRAALAKN 313


                 ...
gi 767942279 255 PQV 257
Cdd:PHA03095 314 PSA 316
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 101-247 3.28e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 47.31  E-value: 3.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 101 QTALHRATVVGNTEIIAALIHEGCALDRQDK-----DGNTALHEASWHGFSQSAKLLIKAGANVlAKNKAGNTALHL--- 172
Cdd:cd22192   52 ETALHVAALYDNLEAAVVLMEAAPELVNEPMtsdlyQGETALHIAVVNQNLNLVRELIARGADV-VSPRATGTFFRPgpk 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 173 -------------ACQNsHSQSTRVLLLAGsrADLKN--NAGDTALHVAAALNHKKVAK-----IL-LEAGADT----TI 227
Cdd:cd22192  131 nliyygehplsfaACVG-NEEIVRLLIEHG--ADIRAqdSLGNTVLHILVLQPNKTFACqmydlILsYDKEDDLqpldLV 207

                        170       180
                 ....*....|....*....|
gi 767942279 228 VNNAGQTPLETARYHNNPEV 247
Cdd:cd22192  208 PNNQGLTPFKLAAKEGNIVM 227
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 199-227 2.02e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 2.02e-04
                           10        20
                   ....*....|....*....|....*....
gi 767942279   199 GDTALHVAAALNHKKVAKILLEAGADTTI 227
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 59-220 3.98e-04

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: 43.92  E-value: 3.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279   59 ASEIVQDAVATVKAMKEDKNKKNHRGKVRKDPRRSEREKegDQTALHRATVVGNTEIIAALIHEG-------CALDRQDK 131
Cdd:TIGR00870  89 ISLEYVDAVEAILLHLLAAFRKSGPLELANDQYTSEFTP--GITALHLAAHRQNYEIVKLLLERGasvparaCGDFFVKS 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279  132 DGNTALHeaswHG---------FSQSA--KLLIKAGANVLAKNKAGNTALHLACQNS-----------HSQSTRVLLLAG 189
Cdd:TIGR00870 167 QGVDSFY----HGesplnaaacLGSPSivALLSEDPADILTADSLGNTLLHLLVMENefkaeyeelscQMYNFALSLLDK 242

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 767942279  190 SR-----ADLKNNAGDTALHVAAALNHKKVAKILLE 220
Cdd:TIGR00870 243 LRdskelEVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
95-254 1.72e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.88  E-value: 1.72e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279  95 REKEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLAC 174
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 175 QNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 254
Cdd:COG0666  162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
97-254 4.68e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.47  E-value: 4.68e-37
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279  97 KEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQN 176
Cdd:COG0666   51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 767942279 177 SHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 254
Cdd:COG0666  131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
98-254 3.18e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.16  E-value: 3.18e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279  98 EGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNS 177
Cdd:COG0666  118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG 197

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767942279 178 HSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 254
Cdd:COG0666  198 HLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
101-236 9.70e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 113.51  E-value: 9.70e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 101 QTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQ 180
Cdd:COG0666  154 NTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 767942279 181 STRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPL 236
Cdd:COG0666  234 IVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
102-251 1.02e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 105.04  E-value: 1.02e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 102 TALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQS 181
Cdd:COG0666   23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 182 TRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLL 251
Cdd:COG0666  103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
137-229 1.08e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 1.08e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279  137 LHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRvLLLAGSRADLKNNaGDTALHVAAALNHKKVAK 216
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 767942279  217 ILLEAGADTTIVN 229
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
114-254 5.29e-17

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 82.31  E-value: 5.29e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 114 EIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRAD 193
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767942279 194 LKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 254
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
PHA03095 PHA03095
ankyrin-like protein; Provisional
 105-257 6.32e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.76  E-value: 6.32e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 105 HRATVvgntEIIAALIHEGCALDRQDKDGNTALHEaswhgFSQSAK-------LLIKAGANVLAKNKAGNTALHLACQNS 177
Cdd:PHA03095 163 RNANV----ELLRLLIDAGADVYAVDDRFRSLLHH-----HLQSFKprarivrELIRAGCDPAATDMLGNTPLHSMATGS 233

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 178 HSQSTRV--LLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPE-VALLLTKA 254
Cdd:PHA03095 234 SCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRaVRAALAKN 313


                 ...
gi 767942279 255 PQV 257
Cdd:PHA03095 314 PSA 316
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 95-239 1.59e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 76.84  E-value: 1.59e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279  95 REKEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLAC 174
Cdd:PHA02878 163 KDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV 242

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767942279 175 QNSHSQST-RVLLLAGSRADLKNNA-GDTALHVaaALNHKKVAKILLEAGADTTIVNNAGQTPLETA 239
Cdd:PHA02878 243 GYCKDYDIlKLLLEHGVDVNAKSYIlGLTALHS--SIKSERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 112-254 5.23e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 74.61  E-value: 5.23e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 112 NTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSR 191
Cdd:PHA02874 103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767942279 192 ADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 254
Cdd:PHA02874 183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNA 245
Ank_2 pfam12796
Ankyrin repeats (3 copies);
170-251 5.96e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.83  E-value: 5.96e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279  170 LHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEaGADTTIVNNaGQTPLETARYHNNPEVAL 249
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ..
gi 767942279  250 LL 251
Cdd:pfam12796  79 LL 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
100-203 8.64e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 72.68  E-value: 8.64e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 100 DQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHS 179
Cdd:COG0666  186 GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAA 265

                         90       100
                 ....*....|....*....|....
gi 767942279 180 QSTRVLLLAGSRADLKNNAGDTAL 203
Cdd:COG0666  266 LIVKLLLLALLLLAAALLDLLTLL 289
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 112-257 3.91e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.01  E-value: 3.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 112 NTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSA--KLLIKAGANVLAKNKAGNTALHLACQNSHS---------- 179
Cdd:PHA03100  85 VKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSivEYLLDNGANVNIKNSDGENLLHLYLESNKIdlkilkllid 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 180 ------QSTRV--LLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPE-VALL 250
Cdd:PHA03100 165 kgvdinAKNRVnyLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEiFKLL 244


                 ....*..
gi 767942279 251 LTKAPQV 257
Cdd:PHA03100 245 LNNGPSI 251
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 32-293 3.34e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.22  E-value: 3.34e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279  32 LLPANRVNSHWSANAISDWSMSNHIAPASEIVQDAVATVKAMKEDKNKKNHRGKvrkdprrserekegdqTALHRATVVG 111
Cdd:PHA02874  72 LLTAIKIGAHDIIKLLIDNGVDTSILPIPCIEKDMIKTILDCGIDVNIKDAELK----------------TFLHYAIKKG 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 112 NTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSR 191
Cdd:PHA02874 136 DLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNH 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 192 ADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNnaGQTPLETA-RYHNNPEV--ALLLTKAPQVLRFSRGRSLRK 268
Cdd:PHA02874 216 IMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDID--GSTPLHHAiNPPCDIDIidILLYHKADISIKDNKGENPID 293

                        250       260       270
                 ....*....|....*....|....*....|.
gi 767942279 269 ------KRERLKEERRAQSVPRDEVAQSKGS 293
Cdd:PHA02874 294 tafkyiNKDPVIKDIIANAVLIKEADKLKDS 324
PHA03095 PHA03095
ankyrin-like protein; Provisional
 97-238 3.44e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 69.28  E-value: 3.44e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279  97 KEGDQTALH---RATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQS-AKLLIKAGANVLAKNKAGNTALH- 171
Cdd:PHA03095  44 GEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDvIKLLIKAGADVNAKDKVGRTPLHv 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767942279 172 -LACQNSHSQSTRVLLLAGsrADL--KNNAGDTALHV-----AAALnhkKVAKILLEAGADTTIVNNAGQTPLET 238
Cdd:PHA03095 124 yLSGFNINPKVIRLLLRKG--ADVnaLDLYGMTPLAVllksrNANV---ELLRLLIDAGADVYAVDDRFRSLLHH 193
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 102-230 1.86e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.53  E-value: 1.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 102 TALHRA--TVVGNTEIIAALIHEGCALDRQDKDGNTALHEA--SWHGFSQSAKLLIKAGANVLAKNKA------------ 165
Cdd:PHA03100 108 TPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKNRVnyllsygvpini 187

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767942279 166 ----GNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNN 230
Cdd:PHA03100 188 kdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 112-253 2.81e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.15  E-value: 2.81e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 112 NTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQS-----AKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRV-- 184
Cdd:PHA03100  47 NIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTdvkeiVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVey 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 185 LLLAGSRADLKNNAGDTALHVAAALNH--KKVAKILLEAGAD----------------TTIVNNAGQTPLETARYHNNPE 246
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDinaknrvnyllsygvpINIKDVYGFTPLHYAVYNNNPE 206


                 ....*...
gi 767942279 247 -VALLLTK 253
Cdd:PHA03100 207 fVKYLLDL 214
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 150-239 5.40e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.20  E-value: 5.40e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 150 KLLIKAGANVLAKNK-AGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIV 228
Cdd:PHA02878 151 KLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDAR 230

                         90
                 ....*....|.
gi 767942279 229 NNAGQTPLETA 239
Cdd:PHA02878 231 DKCGNTPLHIS 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
101-163 5.41e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 5.41e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767942279  101 QTALHRATVVGNTEIIAALIhEGCALDRQDkDGNTALHEASWHGFSQSAKLLIKAGANVLAKN 163
Cdd:pfam12796  31 RTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 174-256 3.76e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.91  E-value: 3.76e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 174 CQNSHSQST---RVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALL 250
Cdd:PTZ00322  87 CQLAASGDAvgaRILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                 ....*.
gi 767942279 251 LTKAPQ 256
Cdd:PTZ00322 167 LSRHSQ 172
Ank_4 pfam13637
Ankyrin repeats (many copies);
102-153 5.73e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 5.73e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767942279  102 TALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLI 153
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 150-238 6.44e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.88  E-value: 6.44e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 150 KLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRV---LLLAGSRADLKNNAGDTALHVAAALNHK-KVAKILLEAGADT 225
Cdd:PHA03095  31 RRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADV 110

                         90
                 ....*....|...
gi 767942279 226 TIVNNAGQTPLET 238
Cdd:PHA03095 111 NAKDKVGRTPLHV 123
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 97-275 1.47e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.69  E-value: 1.47e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279  97 KEGDqTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQN 176
Cdd:PHA02875 100 KDGM-TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAK 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 177 SHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHK-KVAKILLEAGADTTI---VNNAGQTPLETAR-YHNNPEV-ALL 250
Cdd:PHA02875 179 GDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGADCNImfmIEGEECTILDMICnMCTNLESeAID 258

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767942279 251 LTKAPQVLR-----------FSRGRSLRKKRERLKE 275
Cdd:PHA02875 259 ALIADIAIRihkktirrdegFKNNMSTIEDKEEFKD 294
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 64-229 2.70e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.19  E-value: 2.70e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279  64 QDAVATVKAMKEdKNKKNHRGKVRKDPRRSEREKEGDQTALHRATVV--GNTEIIAALIHEGCALDRQDKDGNTALHEAS 141
Cdd:PLN03192 488 EDNVVILKNFLQ-HHKELHDLNVGDLLGDNGGEHDDPNMASNLLTVAstGNAALLEELLKAKLDPDIGDSKGRTPLHIAA 566

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 142 WHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTR----------------VLLLAGSRADL----------- 194
Cdd:PLN03192 567 SKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRilyhfasisdphaagdLLCTAAKRNDLtamkellkqgl 646

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767942279 195 ----KNNAGDTALHVAAALNHKKVAKILLEAGADTTIVN 229
Cdd:PLN03192 647 nvdsEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 102-243 2.99e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.00  E-value: 2.99e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 102 TALHRATVVG-NTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLA-CQNSHS 179
Cdd:PHA02876 343 TPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPY 422

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767942279 180 QSTRVLLLAGSRADLKNNAGDTALHVAAALNHK-KVAKILLEAGADTTIVNNAGQTPLETA-RYHN 243
Cdd:PHA02876 423 MSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAlEYHG 488
Ank_4 pfam13637
Ankyrin repeats (many copies);
199-251 1.06e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 1.06e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767942279  199 GDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLL 251
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 112-262 1.62e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.23  E-value: 1.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 112 NTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGA---NVLAKNkaGNTALHLACQNSHSQSTRVLLLA 188
Cdd:PHA02875  47 DSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIAR 124

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767942279 189 GSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVA-LLLTKAPQVLRFSR 262
Cdd:PHA02875 125 GADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICkMLLDSGANIDYFGK 199
Ank_5 pfam13857
Ankyrin repeats (many copies);
152-206 4.27e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 47.34  E-value: 4.27e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767942279  152 LIKAG-ANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVA 206
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 100-224 4.47e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.14  E-value: 4.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 100 DQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEAsWHGFS--QSAKLLIKAGANVLAKNKAGNTALHLACQ-N 176
Cdd:PHA02876 375 DKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-LCGTNpyMSVKTLIDRGANVNSKNKDLSTPLHYACKkN 453

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 767942279 177 SHSQSTRVLLLAGSRADLKNNAGDTALHVaaALNHKKVAKILLEAGAD 224
Cdd:PHA02876 454 CKLDVIEMLLDNGADVNAINIQNQYPLLI--ALEYHGIVNILLHYGAE 499
Ank_4 pfam13637
Ankyrin repeats (many copies);
133-186 5.67e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 5.67e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767942279  133 GNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLL 186
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
121-173 6.58e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 6.58e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767942279  121 HEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLA 173
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 102-245 9.67e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.37  E-value: 9.67e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 102 TALHRATVVGN-TEIIAALIHEGCALDRQDKDGNTALHEASWHGF-SQSAKLLIKAGANVLAKNKAGNTALHLACQNSHS 179
Cdd:PHA02876 275 TPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRN 354

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767942279 180 QSTRVLLLA-GSRADLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNP 245
Cdd:PHA02876 355 KDIVITLLElGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNP 421
Ank_4 pfam13637
Ankyrin repeats (many copies);
166-219 1.47e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 1.47e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767942279  166 GNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKILL 219
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
203-265 1.54e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.65  E-value: 1.54e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767942279  203 LHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKAPQVLRFSRGRS 265
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 104-251 4.24e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.88  E-value: 4.24e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 104 LHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKaganVLAKNKAGNT--ALHLACQNSH--- 178
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR----SINKCSVFYTlvAIKDAFNNRNvei 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 179 ------------------------------SQSTRVLLLAGSRADLKN-NAGDTALHVAAALNHKKVAKILLEAGADTTI 227
Cdd:PHA02878 117 fkiiltnrykniqtidlvyidkkskddiieAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNI 196

                        170       180
                 ....*....|....*....|....*
gi 767942279 228 VNNAGQTPLETA-RYHNNPEVALLL 251
Cdd:PHA02878 197 PDKTNNSPLHHAvKHYNKPIVHILL 221
Ank_5 pfam13857
Ankyrin repeats (many copies);
185-239 4.68e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 4.68e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767942279  185 LLLAGSRA-DLKNNAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETA 239
Cdd:pfam13857   1 LLEHGPIDlNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 199-230 1.07e-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: 42.66  E-value: 1.07e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 767942279  199 GDTALHVAAA-LNHKKVAKILLEAGADTTIVNN 230
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
PHA02798 PHA02798
ankyrin-like protein; Provisional
 101-230 1.40e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 48.29  E-value: 1.40e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 101 QTALHRATVvgNTEIIAALIHEGCALDRQDKDGNTAL-----HEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQ 175
Cdd:PHA02798  41 QKYLQRDSP--STDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLS 118

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767942279 176 NSHSQSTRVLLLA---GSRADLKNNAGDTALHVAAALNHK---KVAKILLEAGADTTIVNN 230
Cdd:PHA02798 119 NGYINNLEILLFMienGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNN 179
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 137-219 1.67e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 1.67e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 137 LHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTALHVAAALNHKKVAK 216
Cdd:PTZ00322  86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165


                 ...
gi 767942279 217 ILL 219
Cdd:PTZ00322 166 LLS 168
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 132-164 1.93e-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: 41.89  E-value: 1.93e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 767942279  132 DGNTALHEASWH-GFSQSAKLLIKAGANVLAKNK 164
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 101-247 3.28e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 47.31  E-value: 3.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 101 QTALHRATVVGNTEIIAALIHEGCALDRQDK-----DGNTALHEASWHGFSQSAKLLIKAGANVlAKNKAGNTALHL--- 172
Cdd:cd22192   52 ETALHVAALYDNLEAAVVLMEAAPELVNEPMtsdlyQGETALHIAVVNQNLNLVRELIARGADV-VSPRATGTFFRPgpk 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 173 -------------ACQNsHSQSTRVLLLAGsrADLKN--NAGDTALHVAAALNHKKVAK-----IL-LEAGADT----TI 227
Cdd:cd22192  131 nliyygehplsfaACVG-NEEIVRLLIEHG--ADIRAqdSLGNTVLHILVLQPNKTFACqmydlILsYDKEDDLqpldLV 207

                        170       180
                 ....*....|....*....|
gi 767942279 228 VNNAGQTPLETARYHNNPEV 247
Cdd:cd22192  208 PNNQGLTPFKLAAKEGNIVM 227
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 133-236 6.68e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 46.16  E-value: 6.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 133 GNTALHEASWHGFSQSAKLLIKAgANVLAKNK------AGNTALHLACQNSHSQSTRVLLLAGsrADLKNNA-------- 198
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEA-APELVNEPmtsdlyQGETALHIAVVNQNLNLVRELIARG--ADVVSPRatgtffrp 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 767942279 199 --------GDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPL 236
Cdd:cd22192  128 gpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 150-224 1.02e-04

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: 45.77  E-value: 1.02e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 150 KLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRadLKNNA-------GDTALHVAAALNHKKVAKILLEAG 222
Cdd:cd22192   35 KLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyqGETALHIAVVNQNLNLVRELIARG 112


                 ..
gi 767942279 223 AD 224
Cdd:cd22192  113 AD 114
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 90-186 1.67e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 1.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279  90 PRRSEREKEGDQTALHRATV-------VGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAK 162
Cdd:PTZ00322  65 DHNLTTEEVIDPVVAHMLTVelcqlaaSGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLL 144

                         90       100
                 ....*....|....*....|....
gi 767942279 163 NKAGNTALHLACQNSHSQSTRVLL 186
Cdd:PTZ00322 145 DKDGKTPLELAEENGFREVVQLLS 168
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 199-227 2.02e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 2.02e-04
                           10        20
                   ....*....|....*....|....*....
gi 767942279   199 GDTALHVAAALNHKKVAKILLEAGADTTI 227
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 156-257 3.16e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.85  E-value: 3.16e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 156 GANVLAKNKAGNTALHLACQNSHSQSTRVLLLAgSRADL--KNNAGDTALHVAAALNHKKVAKILLEagADTTIVNNA-- 231
Cdd:cd22192    7 ELHLLQQKRISESPLLLAAKENDVQAIKKLLKC-PSCDLfqRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPmt 83

                         90       100       110
                 ....*....|....*....|....*....|..
gi 767942279 232 -----GQTPLETARYHNNPE-VALLLTKAPQV 257
Cdd:cd22192   84 sdlyqGETALHIAVVNQNLNlVRELIARGADV 115
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 59-220 3.98e-04

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: 43.92  E-value: 3.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279   59 ASEIVQDAVATVKAMKEDKNKKNHRGKVRKDPRRSEREKegDQTALHRATVVGNTEIIAALIHEG-------CALDRQDK 131
Cdd:TIGR00870  89 ISLEYVDAVEAILLHLLAAFRKSGPLELANDQYTSEFTP--GITALHLAAHRQNYEIVKLLLERGasvparaCGDFFVKS 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279  132 DGNTALHeaswHG---------FSQSA--KLLIKAGANVLAKNKAGNTALHLACQNS-----------HSQSTRVLLLAG 189
Cdd:TIGR00870 167 QGVDSFY----HGesplnaaacLGSPSivALLSEDPADILTADSLGNTLLHLLVMENefkaeyeelscQMYNFALSLLDK 242

                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 767942279  190 SR-----ADLKNNAGDTALHVAAALNHKKVAKILLE 220
Cdd:TIGR00870 243 LRdskelEVILNHQGLTPLKLAAKEGRIVLFRLKLA 278
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 112-243 1.52e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 1.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 112 NTEIIAALIHEGCALDRQDKDGN-TALHeaSWHGFSQSA-----KLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVL 185
Cdd:PHA02859  65 NVEILKFLIENGADVNFKTRDNNlSALH--HYLSFNKNVepeilKILIDSGSSITEEDEDGKNLLHMYMCNFNVRINVIK 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767942279 186 LL--AGSRADLKNNAGDTALHVAAAL-NHKKVAKILLEAGADTTIVNNAGQTPLETARYHN 243
Cdd:PHA02859 143 LLidSGVSFLNKDFDNNNILYSYILFhSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
Ank_5 pfam13857
Ankyrin repeats (many copies);
86-140 3.00e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 3.00e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767942279   86 VRKDPRRSEREKEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEA 140
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 73-223 3.22e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 39.03  E-value: 3.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279  73 MKEDKNKKNHRGKVRKDprrserekEGDQTALHRATVVGN----TEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQS 148
Cdd:PHA02743   1 MAENGTAGNNLGAVEID--------EDEQNTFLRICRTGNiyelMEVAPFISGDGHLLHRYDHHGRQCTHMVAWYDRANA 72

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 149 A---KLLIKAGANVLAKN-KAGNTALHLACqnshsqSTRVLLLA-------GSRADLKNNAGDTALHVAAALNHKKVAKI 217
Cdd:PHA02743  73 VmkiELLVNMGADINARElGTGNTLLHIAA------STKNYELAewlcrqlGVNLGAINYQHETAYHIAYKMRDRRMMEI 146


                 ....*.
gi 767942279 218 LLEAGA 223
Cdd:PHA02743 147 LRANGA 152
PHA02791 PHA02791
ankyrin-like protein; Provisional
 166-260 3.31e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.03  E-value: 3.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 166 GNTALHLACQNSHSQSTRVLLLAGSRADLKNNagDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNP 245
Cdd:PHA02791  30 GHSALYYAIADNNVRLVCTLLNAGALKNLLEN--EFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNM 107

                         90
                 ....*....|....*
gi 767942279 246 EVALLLTKAPQVLRF 260
Cdd:PHA02791 108 QTVKLFVKKNWRLMF 122
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 132-159 4.04e-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: 35.26  E-value: 4.04e-03
                           10        20
                   ....*....|....*....|....*...
gi 767942279   132 DGNTALHEASWHGFSQSAKLLIKAGANV 159
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 199-224 5.49e-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: 34.93  E-value: 5.49e-03
                          10        20
                  ....*....|....*....|....*.
gi 767942279  199 GDTALHVAAALNHKKVAKILLEAGAD 224
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGAD 27
PHA02946 PHA02946
ankyin-like protein; Provisional
 112-250 6.45e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 39.65  E-value: 6.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767942279 112 NTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSR 191
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIERINLLVQYG 130

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767942279 192 ADLKNNAGDTALH--VAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALL 250
Cdd:PHA02946 131 AKINNSVDEEGCGplLACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKASTI 191
PHA03095 PHA03095
ankyrin-like protein; Provisional
 183-254 9.03e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.24  E-value: 9.03e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767942279 183 RVLLLAGSRADLKNNAGDTALHVAAALNHKKVAKI---LLEAGADTTIVNNAGQTPLETARYHNN-PEVALLLTKA 254
Cdd:PHA03095  31 RRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKA 106
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 195-255 9.93e-03

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: 39.36  E-value: 9.93e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767942279 195 KNNAGDTALHVAAALNHKKVAKILLEAGADTTI---------VNNA-----GQTPLETARYHNNPE-VALLLTKAP 255
Cdd:cd22194  137 EAYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHegfyfGETPLALAACTNQPEiVQLLMEKES 212
 
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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