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Conserved domains on  [gi|74723447|sp|Q86SG2|]
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RecName: Full=Ankyrin repeat domain-containing protein 23; AltName: Full=Diabetes-related ankyrin repeat protein; AltName: Full=Muscle ankyrin repeat protein 3

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];
66-299 4.14e-43

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.72  E-value: 4.14e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  66 RFNLDNLADLENLVQRRKKRLRHRVPPRKPEPLVKPQSQAQVEPVGLEMFLKAAAENQEYLIDKYLTDGGDPNAHDKLHR 145
Cdd:COG0666   9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447 146 TALHWACLKGHSQLVNKLLVAGATVDARDLLDRTPVFWACRGGHLVILKQLLNQGARVNARDKIGSTPLHVAVRTRHPDC 225
Cdd:COG0666  89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74723447 226 LEHLIECGAHLNAQDKEGDTALHEAVRHGSYKAMKLLLLYGAELGVRNAASVTPVQLARDW-QRGIREALQAHVA 299
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENgNLEIVKLLLEAGA 243
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
66-299 4.14e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.72  E-value: 4.14e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  66 RFNLDNLADLENLVQRRKKRLRHRVPPRKPEPLVKPQSQAQVEPVGLEMFLKAAAENQEYLIDKYLTDGGDPNAHDKLHR 145
Cdd:COG0666   9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447 146 TALHWACLKGHSQLVNKLLVAGATVDARDLLDRTPVFWACRGGHLVILKQLLNQGARVNARDKIGSTPLHVAVRTRHPDC 225
Cdd:COG0666  89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74723447 226 LEHLIECGAHLNAQDKEGDTALHEAVRHGSYKAMKLLLLYGAELGVRNAASVTPVQLARDW-QRGIREALQAHVA 299
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENgNLEIVKLLLEAGA 243
Ank_2 pfam12796
Ankyrin repeats (3 copies);
148-240 6.52e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 6.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447   148 LHWACLKGHSQLVNKLLVAGATVDARDLLDRTPVFWACRGGHLVILKQLLNQgARVNARDKiGSTPLHVAVRTRHPDCLE 227
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 74723447   228 HLIECGAHLNAQD 240
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 158-294 7.98e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 88.87  E-value: 7.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  158 QLVNKLLVAGATVDARDLLDRTPVFWACRGGHLVILKQLLNQGARVNARDKIGSTPLHVAVRTRHPDCLEHLIECGAHLN 237
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 74723447  238 AQDKEGDTALHEAVRHGSYKAMKLLLLYGAELGVRNAASVTPVQLARDWQRGIREAL 294
Cdd:PHA02874 185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELL 241
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 116-283 1.22e-06

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: 49.63  E-value: 1.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447 116 LKAAAENQEYLIDKYLT-DGGDPNAHDKLHRTALHWACLKGHSQLVNKLLVAgatvdARDLLD----------RTPVFWA 184
Cdd:cd22192  22 LLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHIA 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447 185 CRGGHLVILKQLLNQGARV------------NARDKI--GSTPLHVAVRTRHPDCLEHLIECGAHLNAQDKEGDTALH-- 248
Cdd:cd22192  97 VVNQNLNLVRELIARGADVvspratgtffrpGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHil 176

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 74723447 249 --EAVRHGSYKAMKLLLLYGAELG------VRNAASVTPVQLA 283
Cdd:cd22192 177 vlQPNKTFACQMYDLILSYDKEDDlqpldlVPNNQGLTPFKLA 219
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 210-238 4.21e-05

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: 39.88  E-value: 4.21e-05
                           10        20
                   ....*....|....*....|....*....
gi 74723447    210 GSTPLHVAVRTRHPDCLEHLIECGAHLNA 238
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 151-272 2.84e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 39.29  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447   151 ACLKGHSQLVNKLLVAGAT--VDARDLLDRTPVFW-ACRGGHLVILKQLLNQGARVnardKIGSTPLHVAVRTRHpDCLE 227
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVaAIENENLELTELLLNLSCRG----AVGDTLLHAISLEYV-DAVE 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74723447   228 hliECGAHLNAQDKEGD-----------------TALHEAVRHGSYKAMKLLLLYGAELGVR 272
Cdd:TIGR00870  99 ---AILLHLLAAFRKSGplelandqytseftpgiTALHLAAHRQNYEIVKLLLERGASVPAR 157
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
66-299 4.14e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.72  E-value: 4.14e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  66 RFNLDNLADLENLVQRRKKRLRHRVPPRKPEPLVKPQSQAQVEPVGLEMFLKAAAENQEYLIDKYLTDGGDPNAHDKLHR 145
Cdd:COG0666   9 LLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGN 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447 146 TALHWACLKGHSQLVNKLLVAGATVDARDLLDRTPVFWACRGGHLVILKQLLNQGARVNARDKIGSTPLHVAVRTRHPDC 225
Cdd:COG0666  89 TLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEI 168

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 74723447 226 LEHLIECGAHLNAQDKEGDTALHEAVRHGSYKAMKLLLLYGAELGVRNAASVTPVQLARDW-QRGIREALQAHVA 299
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENgNLEIVKLLLEAGA 243
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
111-283 7.53e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.25  E-value: 7.53e-42
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447 111 GLEMFLKAAAENQEYLIDKYLTDGGDPNAHDKLHRTALHWACLKGHSQLVNKLLVAGATVDARDLLDRTPVFWACRGGHL 190
Cdd:COG0666  87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447 191 VILKQLLNQGARVNARDKIGSTPLHVAVRTRHPDCLEHLIECGAHLNAQDKEGDTALHEAVRHGSYKAMKLLLLYGAELG 270
Cdd:COG0666 167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                       170
                ....*....|...
gi 74723447 271 VRNAASVTPVQLA 283
Cdd:COG0666 247 AKDKDGLTALLLA 259
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
118-275 2.53e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.52  E-value: 2.53e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447 118 AAAENQ----EYLIDKyltdGGDPNAHDKLHRTALHWACLKGHSQLVNKLLVAGATVDARDLLDRTPVFWACRGGHLVIL 193
Cdd:COG0666 127 AAYNGNleivKLLLEA----GADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIV 202

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447 194 KQLLNQGARVNARDKIGSTPLHVAVRTRHPDCLEHLIECGAHLNAQDKEGDTALHEAVRHGSYKAMKLLLLYGAELGVRN 273
Cdd:COG0666 203 KLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282


                ..
gi 74723447 274 AA 275
Cdd:COG0666 283 LD 284
Ank_2 pfam12796
Ankyrin repeats (3 copies);
148-240 6.52e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.86  E-value: 6.52e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447   148 LHWACLKGHSQLVNKLLVAGATVDARDLLDRTPVFWACRGGHLVILKQLLNQgARVNARDKiGSTPLHVAVRTRHPDCLE 227
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 74723447   228 HLIECGAHLNAQD 240
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
182-273 4.62e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 4.62e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447   182 FWACRGGHLVILKQLLNQGARVNARDKIGSTPLHVAVRTRHPDCLEHLIECgAHLNAQDkEGDTALHEAVRHGSYKAMKL 261
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 74723447   262 LLLYGAELGVRN 273
Cdd:pfam12796  80 LLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 158-294 7.98e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 88.87  E-value: 7.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  158 QLVNKLLVAGATVDARDLLDRTPVFWACRGGHLVILKQLLNQGARVNARDKIGSTPLHVAVRTRHPDCLEHLIECGAHLN 237
Cdd:PHA02874 105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 74723447  238 AQDKEGDTALHEAVRHGSYKAMKLLLLYGAELGVRNAASVTPVQLARDWQRGIREAL 294
Cdd:PHA02874 185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELL 241
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 131-283 2.67e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 87.63  E-value: 2.67e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  131 LTDGGDPNAHDK-LHRTALHWACLKGHSQLVNKLLVAGATVDARDLLDRTPVFWACRGGHLVILKQLLNQGARVNARDKI 209
Cdd:PHA02878 154 LSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKC 233

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74723447  210 GSTPLHVAV-RTRHPDCLEHLIECGAHLNAQDK-EGDTALHEAVRhgSYKAMKLLLLYGAELGVRNAASVTPVQLA 283
Cdd:PHA02878 234 GNTPLHISVgYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSA 307
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
116-247 7.04e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 84.62  E-value: 7.04e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447 116 LKAAAENQ-----EYLIDKyltdGGDPNAHDKLHRTALHWACLKGHSQLVNKLLVAGATVDARDLLDRTPVFWACRGGHL 190
Cdd:COG0666 157 LHLAAANGnleivKLLLEA----GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNL 232

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 74723447 191 VILKQLLNQGARVNARDKIGSTPLHVAVRTRHPDCLEHLIECGAHLNAQDKEGDTAL 247
Cdd:COG0666 233 EIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 127-287 1.88e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 79.72  E-value: 1.88e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  127 IDKYLTDGGDPNAHDKLHRTALHWA-CLKGHSQLVNKLLVAGATVDARDLLDRTPVFWACRGGHLVILKQLLNQGARVNA 205
Cdd:PHA02876 324 IRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA 403

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  206 -RDKIGsTPLHVAVRTRHP-DCLEHLIECGAHLNAQDKEGDTALHEAVRHG-SYKAMKLLLLYGAELGVRNAASVTPVQL 282
Cdd:PHA02876 404 lSQKIG-TALHFALCGTNPyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLI 482


                 ....*
gi 74723447  283 ARDWQ 287
Cdd:PHA02876 483 ALEYH 487
Ank_2 pfam12796
Ankyrin repeats (3 copies);
118-207 3.37e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 3.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447   118 AAAENQEYLIDKYLTDGGDPNAHDKLHRTALHWACLKGHSQLVnKLLVAGATVDARDlLDRTPVFWACRGGHLVILKQLL 197
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIV-KLLLEHADVNLKD-NGRTALHYAARSGHLEIVKLLL 81

                          90
                  ....*....|
gi 74723447   198 NQGARVNARD 207
Cdd:pfam12796  82 EKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 129-269 1.56e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.60  E-value: 1.56e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  129 KYLTDGGDPNAHDKLHRTALHwACLKGHSQL----VNKLLVAGATVDARDLLDRTPVF-WACRGGHLVILKQLLNQGARV 203
Cdd:PHA03095  32 RLLAAGADVNFRGEYGKTPLH-LYLHYSSEKvkdiVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIKAGADV 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  204 NARDKIGSTPLHVAVRTR--HPDCLEHLIECGAHLNAQDKEGDTALHEAVRHG--SYKAMKLLLLYGAEL 269
Cdd:PHA03095 111 NAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRnaNVELLRLLIDAGADV 180
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 126-283 1.98e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 76.16  E-value: 1.98e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  126 LIDKYLTDGGDPNAHDKLHRTALHWACLKGHSQLVNKLLVAGATVDARDLLDRTPVFWACRGGHLVILKQLLNQGARVNA 205
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 74723447  206 RDKIGSTPLHVAVRTRHPDCLEHLIECGAHLNAQDKEGDTALHEAVRHGsyKAMKLLLLYGAELGVRNAASVTPVQLA 283
Cdd:PHA02874 186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN--RSAIELLINNASINDQDIDGSTPLHHA 261
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 124-283 2.43e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.86  E-value: 2.43e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  124 EYLIDKyltdGGDPNAHDKLHRTALHWACLKGHSQLVNK-----LLVAGATVDARDLLDRTPVFWA--CRGGHLVILKQL 196
Cdd:PHA03100  52 KILLDN----GADINSSTKNNSTPLHYLSNIKYNLTDVKeivklLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYL 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  197 LNQGARVNARDKIGSTPLHVAVRTRHPDC------------------LEHLIECGAHLNAQDKEGDTALHEAVRHGSYKA 258
Cdd:PHA03100 128 LDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEF 207

                        170       180
                 ....*....|....*....|....*
gi 74723447  259 MKLLLLYGAELGVRNAASVTPVQLA 283
Cdd:PHA03100 208 VKYLLDLGANPNLVNKYGDTPLHIA 232
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 116-252 2.51e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 76.07  E-value: 2.51e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  116 LKAAAENQEYLIDKYL-TDGGDPNAHDKLHRTALHWACLKGHSQLVNKLLVAGATVDARDLLDRTPVFWACrgGHLV--- 191
Cdd:PHA02878 172 LHYATENKDQRLTELLlSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYCKdyd 249

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74723447  192 ILKQLLNQGARVNARDKI-GSTPLHVAVRTrhPDCLEHLIECGAHLNAQDKEGDTALHEAVR 252
Cdd:PHA02878 250 ILKLLLEHGVDVNAKSYIlGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 113-269 1.66e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 73.94  E-value: 1.66e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  113 EMFLKAAAENQEYLIDKYLTDGG-DPNAHDKLHRTALHWAC-LKGHSQLVNKLLVAGATVDARDLLDRTPVFWACRGGHL 190
Cdd:PHA02876 241 DLSLLKAIRNEDLETSLLLYDAGfSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYD 320

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  191 VI-LKQLLNQGARVNARDKIGSTPLHVA-VRTRHPDCLEHLIECGAHLNAQDKEGDTALHEAVRHGSYKAMKLLLLYGAE 268
Cdd:PHA02876 321 TEnIRTLIMLGADVNAADRLYITPLHQAsTLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400


                 .
gi 74723447  269 L 269
Cdd:PHA02876 401 I 401
PHA03095 PHA03095
ankyrin-like protein; Provisional
 160-280 2.07e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.14  E-value: 2.07e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  160 VNKLLVAGATVDARDLLDRTP--VFWACRGGHLV-ILKQLLNQGARVNARDKIGSTPLHVAVRTRH-PDCLEHLIECGAH 235
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKTPlhLYLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGAD 109

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 74723447  236 LNAQDKEGDTALH-----EAVRhgsYKAMKLLLLYGAELGVRNAASVTPV 280
Cdd:PHA03095 110 VNAKDKVGRTPLHvylsgFNIN---PKVIRLLLRKGADVNALDLYGMTPL 156
PHA03095 PHA03095
ankyrin-like protein; Provisional
 125-263 3.48e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.36  E-value: 3.48e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  125 YLIDKyltdGGDPNAHDKLHRTALHWAC--LKGHSQLVNKLLVAGATVDARDLLDRTPV-----FWACRGGHLVilkQLL 197
Cdd:PHA03095 172 LLIDA----GADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLhsmatGSSCKRSLVL---PLL 244

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 74723447  198 NQGARVNARDKIGSTPLHVAVRTRHPDCLEHLIECGAHLNAQDKEGDTALHEAVRHGSYKAMKLLL 263
Cdd:PHA03095 245 IAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA03095 PHA03095
ankyrin-like protein; Provisional
 126-283 3.40e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 69.67  E-value: 3.40e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  126 LIDKyltdGGDPNAHDKLHRTALHwACLKG---HSQLVNKLLVAGATVDARDLLDRTP--VFWACRGGHLVILKQLLNQG 200
Cdd:PHA03095 103 LIKA----GADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPlaVLLKSRNANVELLRLLIDAG 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  201 ARVNARDKIGSTPLH---VAVRTR------------------------------HPDC----LEHLIECGAHLNAQDKEG 243
Cdd:PHA03095 178 ADVYAVDDRFRSLLHhhlQSFKPRarivreliragcdpaatdmlgntplhsmatGSSCkrslVLPLLIAGISINARNRYG 257

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 74723447  244 DTALHEAVRHGSYKAMKLLLLYGAELGVRNAASVTPVQLA 283
Cdd:PHA03095 258 QTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
PHA03095 PHA03095
ankyrin-like protein; Provisional
 192-281 3.87e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 69.28  E-value: 3.87e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  192 ILKQLLNQGARVNARDKIGSTPLHVAVRTRHPDCLE---HLIECGAHLNAQDKEGDTALHEAVRHGS-YKAMKLLLLYGA 267
Cdd:PHA03095  29 EVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDivrLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGA 108

                         90
                 ....*....|....
gi 74723447  268 ELGVRNAASVTPVQ 281
Cdd:PHA03095 109 DVNAKDKVGRTPLH 122
PHA03095 PHA03095
ankyrin-like protein; Provisional
 112-283 1.30e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.74  E-value: 1.30e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  112 LEMFLKAAAENQEYLIDKYLTDGGDPNAHDKLHRTALHwaCLKGHSQLVN--KLLV-AGATVDARDLLDRTPVFwACRGG 188
Cdd:PHA03095  51 LHLYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLH--LYLYNATTLDviKLLIkAGADVNAKDKVGRTPLH-VYLSG 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  189 ---HLVILKQLLNQGARVNARDKIGSTPLHVAVRTR----------------------------H---------PDCLEH 228
Cdd:PHA03095 128 fniNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRnanvellrllidagadvyavddrfrsllHhhlqsfkprARIVRE 207

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 74723447  229 LIECGAHLNAQDKEGDTALHEAVRHGSYKAMKL--LLLYGAELGVRNAASVTPVQLA 283
Cdd:PHA03095 208 LIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYA 264
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 114-267 3.20e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.61  E-value: 3.20e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  114 MFLKAAAENQEYLIDKYLTD-GGDPNAHDKLHRTALHWA--CLKGHSQLVNKLLVAGATVDARDLLDRtpvfwacrgghl 190
Cdd:PHA03100 110 LLYAISKKSNSYSIVEYLLDnGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKNRVNY------------ 177

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74723447  191 vilkqLLNQGARVNARDKIGSTPLHVAVRTRHPDCLEHLIECGAHLNAQDKEGDTALHEAVRHGSYKAMKLLLLYGA 267
Cdd:PHA03100 178 -----LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 157-283 3.61e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.44  E-value: 3.61e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  157 SQLVNKLLVAGATVDARDL-LDRTPVFWACRGGHLVILKQLLNQGARVNARDKIGSTPLHVAVRTRHPDCLEHLIECGAH 235
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 74723447  236 LNAQDKEGDTALHEAV-RHGSYKAMKLLLLYGAELgvrNAAS----VTPVQLA 283
Cdd:PHA02878 227 TDARDKCGNTPLHISVgYCKDYDILKLLLEHGVDV---NAKSyilgLTALHSS 276
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 70-269 3.65e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 63.73  E-value: 3.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447   70 DNLADLENLVQRRKkrlrhRVPPRKPEPLVKPQSQAQVEPVGLEMFLKAAAENQEYLIDKYLTDGGDPNAHDKLHRTALH 149
Cdd:PLN03192 489 DNVVILKNFLQHHK-----ELHDLNVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLH 563

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  150 WACLKGHSQLVNKLLVAGATVDARDLLDRTPVFWACRGGHLVILKqLLNQGARVnARDKIGSTPLHVAVRTRHPDCLEHL 229
Cdd:PLN03192 564 IAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR-ILYHFASI-SDPHAAGDLLCTAAKRNDLTAMKEL 641

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 74723447  230 IECGAHLNAQDKEGDTALHEAVRHGSYKAMKLLLLYGAEL 269
Cdd:PLN03192 642 LKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
Ank_2 pfam12796
Ankyrin repeats (3 copies);
214-263 4.20e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.59  E-value: 4.20e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 74723447   214 LHVAVRTRHPDCLEHLIECGAHLNAQDKEGDTALHEAVRHGSYKAMKLLL 263
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL 50
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 160-241 6.74e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 62.38  E-value: 6.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  160 VNKLLVAGATVDARDLLDRTPVFWACRGGHLVILKQLLNQGARVNARDKIGSTPLHVAVRTRHPDCLEHLIECGAHLNAQ 239
Cdd:PHA03100 175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254


                 ..
gi 74723447  240 DK 241
Cdd:PHA03100 255 IE 256
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 116-288 7.30e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.77  E-value: 7.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  116 LKAAAENQEYLIDKYLTDGG-DPNAHDKLHRTALHWACLKGHSQLVNKLLVAGATVDARDLLDRTPVFWACRGGHLVILK 194
Cdd:PHA02876 149 IKERIQQDELLIAEMLLEGGaDVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  195 QLLNQ-----------------------------GARVNARDKIGSTPLHVAVRTRHPDCL-EHLIECGAHLNAQDKEGD 244
Cdd:PHA02876 229 AIIDNrsninkndlsllkairnedletslllydaGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGE 308

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*
gi 74723447  245 TALHEAVRHG-SYKAMKLLLLYGAELGVRNAASVTPVQLARDWQR 288
Cdd:PHA02876 309 TPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTLDR 353
Ank_4 pfam13637
Ankyrin repeats (many copies);
210-263 3.41e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 3.41e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 74723447   210 GSTPLHVAVRTRHPDCLEHLIECGAHLNAQDKEGDTALHEAVRHGSYKAMKLLL 263
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
196-250 8.32e-10

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.89  E-value: 8.32e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 74723447   196 LLNQG-ARVNARDKIGSTPLHVAVRTRHPDCLEHLIECGAHLNAQDKEGDTALHEA 250
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 179-283 1.82e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.97  E-value: 1.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  179 TPVFWACRGGHLVILKQLLNQGARVNARDKIGSTPLHVAVRTRHPD------------------CLEH-----LIECGAH 235
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDiikllidngvdtsilpipCIEKdmiktILDCGID 116

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 74723447  236 LNAQDKEGDTALHEAVRHGSYKAMKLLLLYGAELGVRNAASVTPVQLA 283
Cdd:PHA02874 117 VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 163-232 4.22e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 4.22e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  163 LLVAGATVDARDLLDRTPVFWACRGGHLVILKQLLNQGARVNARDKIGSTPLHVAVRTRHPDCLEHLIEC 232
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 102-283 5.21e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.10  E-value: 5.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  102 QSQAQVEPVGLEMFLKAAAENQEYLIDKYLTDGGDPNAHDKLHRTALHWACLkGHSQLVNKLLVAGATVDARDLLDRTPV 181
Cdd:PLN03192 484 QTRQEDNVVILKNFLQHHKELHDLNVGDLLGDNGGEHDDPNMASNLLTVAST-GNAALLEELLKAKLDPDIGDSKGRTPL 562

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  182 FWACRGGHLVILKQLLNQGARVNARDKIGSTPLHVAVRTRHPDCLEHLIECgAHLNAQDKEGDTaLHEAVRHGSYKAMKL 261
Cdd:PLN03192 563 HIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-ASISDPHAAGDL-LCTAAKRNDLTAMKE 640

                        170       180
                 ....*....|....*....|..
gi 74723447  262 LLLYGAELGVRNAASVTPVQLA 283
Cdd:PLN03192 641 LLKQGLNVDSEDHQGATALQVA 662
Ank_4 pfam13637
Ankyrin repeats (many copies);
178-230 5.75e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 5.75e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 74723447   178 RTPVFWACRGGHLVILKQLLNQGARVNARDKIGSTPLHVAVRTRHPDCLEHLI 230
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 188-268 3.06e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.44  E-value: 3.06e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  188 GHLVILKQLLNQGARVNARDKIGSTPLHVAVRTRHPDCLEHLIECGAHLNAQDKEGDTALHEAVRHGSYKAMKLLLLYGA 267
Cdd:PTZ00322  93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172


                 .
gi 74723447  268 E 268
Cdd:PTZ00322 173 C 173
Ank_4 pfam13637
Ankyrin repeats (many copies);
144-197 7.02e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 7.02e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 74723447   144 HRTALHWACLKGHSQLVNKLLVAGATVDARDLLDRTPVFWACRGGHLVILKQLL 197
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 137-267 7.99e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.99  E-value: 7.99e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  137 PNAHDKLHRTALHWACLKGHSQLVNKLLVAGATVDarDLLDR---TPVFWACRGGHLVILKQLLNQGARVNARDKIGSTP 213
Cdd:PHA02875  61 PDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAD--DVFYKdgmTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSP 138

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 74723447  214 LHVAVRTRHPDCLEHLIECGAHLNAQDKEGDTALHEAVRHGSYKAMKLLLLYGA 267
Cdd:PHA02875 139 LHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA 192
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 116-283 1.22e-06

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: 49.63  E-value: 1.22e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447 116 LKAAAENQEYLIDKYLT-DGGDPNAHDKLHRTALHWACLKGHSQLVNKLLVAgatvdARDLLD----------RTPVFWA 184
Cdd:cd22192  22 LLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHIA 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447 185 CRGGHLVILKQLLNQGARV------------NARDKI--GSTPLHVAVRTRHPDCLEHLIECGAHLNAQDKEGDTALH-- 248
Cdd:cd22192  97 VVNQNLNLVRELIARGADVvspratgtffrpGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHil 176

                       170       180       190       200
                ....*....|....*....|....*....|....*....|...
gi 74723447 249 --EAVRHGSYKAMKLLLLYGAELG------VRNAASVTPVQLA 283
Cdd:cd22192 177 vlQPNKTFACQMYDLILSYDKEDDlqpldlVPNNQGLTPFKLA 219
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 135-271 3.15e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 3.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  135 GDPNAHDKLHRTALHWACLKGHSQ-----LVNKLLVAGATVDARDLLDRTPVFWACRGGHLVILKQLLNQGARVNARDKI 209
Cdd:PHA02876 131 GNDIHYDKINESIEYMKLIKERIQqdellIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD 210

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74723447  210 GSTPLHVAVRTRHPDCLEHLIECGAHLNaqdkEGDTALHEAVRHGSYKAMklLLLYGAELGV 271
Cdd:PHA02876 211 DLSVLECAVDSKNIDTIKAIIDNRSNIN----KNDLSLLKAIRNEDLETS--LLLYDAGFSV 266
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 131-197 3.66e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 3.66e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 74723447  131 LTDGGDPNAHDKLHRTALHWACLKGHSQLVNKLLVAGATVDARDLLDRTPVFWACRGGHLVILKQLL 197
Cdd:PTZ00322 102 LTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 157-283 4.36e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.68  E-value: 4.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  157 SQLVNKLLVAGATVDARDLLDRTPVFWACRGGHLVILKQLLNQGARVN-ARDKIGSTPLHVAVRTRHPDCLEHLIECGAH 235
Cdd:PHA02875  48 SEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGAD 127

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 74723447  236 LNAQDKEGDTALHEAVRHGSYKAMKLLLLYGAELGVRNAASVTPVQLA 283
Cdd:PHA02875 128 PDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIA 175
PHA02741 PHA02741
hypothetical protein; Provisional
 201-285 5.35e-06

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 45.80  E-value: 5.35e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  201 ARVNARDKIGSTPLHVAVRTRHP----DCLEHLIECGAHLNAQDK-EGDTALHEAVRHGSYKAMKLLLLY-GAELGVRNA 274
Cdd:PHA02741  51 AALNATDDAGQMCIHIAAEKHEAqlaaEIIDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCCQpGIDLHFCNA 130

                         90
                 ....*....|.
gi 74723447  275 ASVTPVQLARD 285
Cdd:PHA02741 131 DNKSPFELAID 141
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 118-269 5.56e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.75  E-value: 5.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  118 AAAENQEYLIDKYLTDGGDPNAHDKLHRTALHWAClkghsqlvnkllvagatvdardlldrtpvfwaCRGGHLVILKQLL 197
Cdd:PHA02876 382 AAVRNNVVIINTLLDYGADIEALSQKIGTALHFAL--------------------------------CGTNPYMSVKTLI 429

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 74723447  198 NQGARVNARDKIGSTPLHVAVRTR-HPDCLEHLIECGAHLNAQDKEGDTALHEAVrhGSYKAMKLLLLYGAEL 269
Cdd:PHA02876 430 DRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAEL 500
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 143-283 5.70e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 47.29  E-value: 5.70e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  143 LHRTALHWACLKGHSQLVNKLLVAGATVDARDLLDRTPVFWACRGGHLVILKQLLNQGARVNARDKIGSTPLHVAVRTRH 222
Cdd:PHA02875   1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74723447  223 PDCLEHLIECGAHLN-AQDKEGDTALHEAVRHGSYKAMKLLLLYGAELGVRNAASVTPVQLA 283
Cdd:PHA02875  81 VKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLA 142
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 210-241 2.21e-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: 40.74  E-value: 2.21e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 74723447   210 GSTPLHVAV-RTRHPDCLEHLIECGAHLNAQDK 241
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
229-283 2.56e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 2.56e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 74723447   229 LIECG-AHLNAQDKEGDTALHEAVRHGSYKAMKLLLLYGAELGVRNAASVTPVQLA 283
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 210-238 4.21e-05

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: 39.88  E-value: 4.21e-05
                           10        20
                   ....*....|....*....|....*....
gi 74723447    210 GSTPLHVAVRTRHPDCLEHLIECGAHLNA 238
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 131-237 5.83e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.21  E-value: 5.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  131 LTDGGDPNAHDKLHRTALHWACLKGHSQLVNKLLVAGATVDARDLLDRTPVFWACRGGHLVILKQLLNQGARVNARDKIG 210
Cdd:PHA02875 122 IARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG 201

                         90       100
                 ....*....|....*....|....*...
gi 74723447  211 S-TPLHVAVRTRHPDCLEHLIECGAHLN 237
Cdd:PHA02875 202 CvAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 146-268 5.83e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.21  E-value: 5.83e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  146 TALHWACLKGHSQLVNKLLVAGATVDARDLLDRTPVFWACRGGHLVILKQLLNQGARVNARDKIGSTPLHVAVRTRHPDC 225
Cdd:PHA02875 104 TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 74723447  226 LEHLIECGAHLNAQDKEGD-TALHEAVRHGSYKAMKLLLLYGAE 268
Cdd:PHA02875 184 CKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGAD 227
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 192-295 8.53e-05

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: 43.98  E-value: 8.53e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447 192 ILKQLLNQGARVNARDK--------------IGSTPLHVAVRTRHPDCLEHLIE-CGAHLNAQDKEGDTALHEAV----- 251
Cdd:cd22194 156 IVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPEIVQLLMEkESTDITSQDSRGNTVLHALVtvaed 235

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 74723447 252 ---RHGSYKAMKLLLLYGAE----LGVRNAASVTPVQLARdwQRGIREALQ 295
Cdd:cd22194 236 sktQNDFVKRMYDMILLKSEnknlETIRNNEGLTPLQLAA--KMGKAEILK 284
PHA02946 PHA02946
ankyin-like protein; Provisional
 118-248 2.07e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 42.73  E-value: 2.07e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  118 AAAENQEYLIDKYLTDGGDPNAHDKLHRTALHWacLKGHS----QLVNKLLVAGATVDARDLLDRTPVFWACRGGHLVIL 193
Cdd:PHA02946  79 ASKINNNRIVAMLLTHGADPNACDKQHKTPLYY--LSGTDdeviERINLLVQYGAKINNSVDEEGCGPLLACTDPSERVF 156

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 74723447  194 KQLLNQGARVNARDKIGSTPLHVAVRTRHPDC--LEHLIECGAHLNAQDKEGDTALH 248
Cdd:PHA02946 157 KKIMSIGFEARIVDKFGKNHIHRHLMSDNPKAstISWMMKLGISPSKPDHDGNTPLH 213
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 196-267 3.75e-04

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 40.57  E-value: 3.75e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74723447  196 LLNQGARVNARD-KIGSTPLHVAVRTRHPDCLEHLI-ECGAHLNAQDKEGDTALHEAVRHGSYKAMKLLLLYGA 267
Cdd:PHA02743  79 LVNMGADINARElGTGNTLLHIAASTKNYELAEWLCrQLGVNLGAINYQHETAYHIAYKMRDRRMMEILRANGA 152
PHA03095 PHA03095
ankyrin-like protein; Provisional
 126-199 4.53e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.55  E-value: 4.53e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 74723447  126 LIDKYLTDGGDPNAHDKLHRTALHWACLKGHSQLVNKLLVAGATVDARDLLDRTPVFWACRGGHLVILKQLLNQ 199
Cdd:PHA03095 239 LVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 210-238 4.90e-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: 36.85  E-value: 4.90e-04
                          10        20
                  ....*....|....*....|....*....
gi 74723447   210 GSTPLHVAVRTRHPDCLEHLIECGAHLNA 238
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 242-269 9.55e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 9.55e-04
                           10        20
                   ....*....|....*....|....*...
gi 74723447    242 EGDTALHEAVRHGSYKAMKLLLLYGAEL 269
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 191-283 9.63e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.35  E-value: 9.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  191 VILKQLLNQGARVNARDKIGSTPLHVAVRTRHPDCLEHLIECGAHLNAQDKEGD-TALHEAVRHGSYKAMKLLLLYGAEL 269
Cdd:PHA02884  51 AILKLGADPEAPFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSYGADI 130

                         90
                 ....*....|....
gi 74723447  270 GVRNAASVTPVQLA 283
Cdd:PHA02884 131 NIQTNDMVTPIELA 144
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 186-283 1.04e-03

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: 40.55  E-value: 1.04e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447 186 RGGHLVILkqLLNQGARVNARDK--------------IGSTPLHVAVRTRHPDCLEHLIECG---AHLNAQDKEGDTALH 248
Cdd:cd22193  87 RQGDIVAL--LVENGADVHAHAKgrffqpkyqgegfyFGELPLSLAACTNQPDIVQYLLENEhqpADIEAQDSRGNTVLH 164

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 74723447 249 EAVRHGS---------YKAMKLLLLYGAEL-------GVRNAASVTPVQLA 283
Cdd:cd22193 165 ALVTVADntkentkfvTRMYDMILIRGAKLcptveleEIRNNDGLTPLQLA 215
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 145-174 1.21e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 1.21e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 74723447   145 RTALHWACLK-GHSQLVNKLLVAGATVDARD 174
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
136-181 1.28e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 1.28e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 74723447   136 DPNAHDKLHRTALHWACLKGHSQLVNKLLVAGATVDARDLLDRTPV 181
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 242-269 1.28e-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: 35.70  E-value: 1.28e-03
                          10        20
                  ....*....|....*....|....*...
gi 74723447   242 EGDTALHEAVRHGSYKAMKLLLLYGAEL 269
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 124-205 1.37e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.03  E-value: 1.37e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  124 EYLIDKyltdGGDPNAHDKLHRTALHWACLKGHSQLVNKLLVAGATVDARDLLDRTPVFWACRGGHLVILKQLLNQGARV 203
Cdd:PHA03100 176 NYLLSY----GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251


                 ..
gi 74723447  204 NA 205
Cdd:PHA03100 252 KT 253
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 177-205 1.37e-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: 35.64  E-value: 1.37e-03
                           10        20
                   ....*....|....*....|....*....
gi 74723447    177 DRTPVFWACRGGHLVILKQLLNQGARVNA 205
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 192-283 1.61e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.65  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  192 ILKQLLNQGARVNARDKIGSTPLHVAVRTRHPDCLEHLIECGAHLNAQDKEGDTALHEAVRHGSY-----KAMKLLLLYG 266
Cdd:PHA03100  17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYG 96

                         90
                 ....*....|....*..
gi 74723447  267 AELGVRNAASVTPVQLA 283
Cdd:PHA03100  97 ANVNAPDNNGITPLLYA 113
Ank_4 pfam13637
Ankyrin repeats (many copies);
117-164 1.99e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 1.99e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 74723447   117 KAAAENQEYLIDKYLTDGGDPNAHDKLHRTALHWACLKGHSQLVNKLL 164
Cdd:pfam13637   7 AAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 151-272 2.84e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 39.29  E-value: 2.84e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447   151 ACLKGHSQLVNKLLVAGAT--VDARDLLDRTPVFW-ACRGGHLVILKQLLNQGARVnardKIGSTPLHVAVRTRHpDCLE 227
Cdd:TIGR00870  24 AAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVaAIENENLELTELLLNLSCRG----AVGDTLLHAISLEYV-DAVE 98

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74723447   228 hliECGAHLNAQDKEGD-----------------TALHEAVRHGSYKAMKLLLLYGAELGVR 272
Cdd:TIGR00870  99 ---AILLHLLAAFRKSGplelandqytseftpgiTALHLAAHRQNYEIVKLLLERGASVPAR 157
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 202-254 2.93e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 38.95  E-value: 2.93e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 74723447  202 RVNARDKIGSTPLHVAVRTRHPDCLEHLIECGAHLNAQDKEGDTALHEAVRHG 254
Cdd:PHA02989 248 KINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHG 300
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 145-218 3.01e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 39.09  E-value: 3.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447 145 RTALHWACLKGHSQLVNKLLVAGATVDAR---DLLDRTP-----------VFWACRgGHLVILKQLLNQGAR---VNARD 207
Cdd:cd21882  74 QTALHIAIENRNLNLVRLLVENGADVSARatgRFFRKSPgnlfyfgelplSLAACT-NQEEIVRLLLENGAQpaaLEAQD 152

                        90
                ....*....|.
gi 74723447 208 KIGSTPLHVAV 218
Cdd:cd21882 153 SLGNTVLHALV 163
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 145-172 3.26e-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: 34.49  E-value: 3.26e-03
                           10        20
                   ....*....|....*....|....*...
gi 74723447    145 RTALHWACLKGHSQLVNKLLVAGATVDA 172
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02917 PHA02917
ankyrin-like protein; Provisional
 225-303 3.45e-03

ankyrin-like protein; Provisional


Pssm-ID: 165231 [Multi-domain]  Cd Length: 661  Bit Score: 38.83  E-value: 3.45e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74723447  225 CLEHLIEcgahLNAQDKEGDTALHEAVRHGSYKAMKLLLLYGAELGVRNAASVTPVQLARDWQRGIrEALQAHVAHPRT 303
Cdd:PHA02917 438 CLPYLKD----INMIDKRGETLLHKAVRYNKQSLVSLLLESGSDVNIRSNNGYTCIAIAINESRNI-ELLKMLLCHKPT 511
Ank_5 pfam13857
Ankyrin repeats (many copies);
170-217 3.74e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 3.74e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 74723447   170 VDARDLLDRTPVFWACRGGHLVILKQLLNQGARVNARDKIGSTPLHVA 217
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
247-283 3.88e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 35.86  E-value: 3.88e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 74723447   247 LHEAVRHGSYKAMKLLLLYGAELGVRNAASVTPVQLA 283
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLA 37
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 193-271 4.05e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.16  E-value: 4.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  193 LKQLLNQGARVNARDKI-GSTPLHVAVRTRHPDCLEHLI-ECGAHLNAQDKEGDTALHEAVRHGSYKAMKLLLLYGAELG 270
Cdd:PHA02736  74 LKLLMEWGADINGKERVfGNTPLHIAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCK 153


                 .
gi 74723447  271 V 271
Cdd:PHA02736 154 V 154
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 178-208 5.23e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.19  E-value: 5.23e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 74723447   178 RTPVFWAC-RGGHLVILKQLLNQGARVNARDK 208
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 229-300 5.69e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 38.34  E-value: 5.69e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 74723447  229 LIECGAHLNAQDKEGDTALHEAVRHGSYKAMKLLLLYGAELGVRNAASVTPVQLARdwQRGIREALQAHVAH 300
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAE--ENGFREVVQLLSRH 170
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 177-301 7.13e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 38.14  E-value: 7.13e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447   177 DRTPVFWACRGGHLVILKQLLNQGARVNAR------------DKI--GSTPLHVAVRTRHPDCLEHLIECGAHLNAQDKE 242
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARacgdffvksqgvDSFyhGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447   243 GDTALHEAVRHGSYKA--------MKLLLL-YGAELG-------VRNAASVTPVQLARDWQRG--IREALQA------HV 298
Cdd:TIGR00870 208 GNTLLHLLVMENEFKAeyeelscqMYNFALsLLDKLRdskelevILNHQGLTPLKLAAKEGRIvlFRLKLAIkykqkkFV 287


                  ...
gi 74723447   299 AHP 301
Cdd:TIGR00870 288 AWP 290
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 213-263 7.40e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 37.94  E-value: 7.40e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 74723447  213 PLHVAVRTRHPDCLEHLIECGAHLNAQDKEGDTALHEAVRHGSYKAMKLLL 263
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI 90
PHA02946 PHA02946
ankyin-like protein; Provisional
 124-258 8.13e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 37.73  E-value: 8.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 74723447  124 EYLIDKYLTDGGDPNAHDKLHRTALHWACLKGHSQLVNKLLVAGATVDARDLLDRTPVFWACRGGHLVI--LKQLLNQGA 201
Cdd:PHA02946  52 ERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGA 131

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 74723447  202 RV-NARDKIGSTPLhVAVRTRHPDCLEHLIECGAHLNAQDKEGDTALHEAVRHGSYKA 258
Cdd:PHA02946 132 KInNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKA 188
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 242-273 8.40e-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: 33.42  E-value: 8.40e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 74723447   242 EGDTALHEAV-RHGSYKAMKLLLLYGAELGVRN 273
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02946 PHA02946
ankyin-like protein; Provisional
 193-269 9.70e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 37.34  E-value: 9.70e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 74723447  193 LKQLLNQGARVNARDKIGSTPLHVAVRTRHPDCLEHLIECGAHLNAQDKEGDTALH--EAVRHGSYKAMKLLLLYGAEL 269
Cdd:PHA02946  55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYylSGTDDEVIERINLLVQYGAKI 133
 
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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