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Conserved domains on  [gi|2217360304|ref|XP_047274353|]
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ankyrin repeat domain-containing protein 6 isoform X2 [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];
97-287 6.71e-46

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 165.51  E-value: 6.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304  97 KEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQN 176
Cdd:COG0666    51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 177 SHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGA 256
Cdd:COG0666   131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2217360304 257 DTTIVNNAGQTPLETARYHNNPEVALLLTKA 287
Cdd:COG0666   211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
97-287 6.71e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 165.51  E-value: 6.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304  97 KEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQN 176
Cdd:COG0666    51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 177 SHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGA 256
Cdd:COG0666   131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2217360304 257 DTTIVNNAGQTPLETARYHNNPEVALLLTKA 287
Cdd:COG0666   211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
170-262 9.32e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 9.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 170 LHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLtAFCSVHEKNQaGDTALHVAAALNHKKVAK 249
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2217360304 250 ILLEAGADTTIVN 262
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 112-290 7.03e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 93.55  E-value: 7.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 112 NTEIIAALIHEGCALDRQDKDGNTALHeaswhGFSQSA-------KLLIKAGANVLAKNKAGNTALHLACQNSHSQST-- 182
Cdd:PHA03095  131 NPKVIRLLLRKGADVNALDLYGMTPLA-----VLLKSRnanvellRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARiv 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 183 RVLLLAGSRADLKNNAGDTCLHVAARYNHL--SIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGADTTI 260
Cdd:PHA03095  206 RELIRAGCDPAATDMLGNTPLHSMATGSSCkrSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2217360304 261 VNNAGQTPLETARYHNNPE-VALLLTKAPQV 290
Cdd:PHA03095  286 VSSDGNTPLSLMVRNNNGRaVRAALAKNPSA 316
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 150-269 2.93e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.86  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 150 KLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRadLKNNA-------GDTCLHVAARYNHLSIIRLLL--- 219
Cdd:cd22192    35 KLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyqGETALHIAVVNQNLNLVRELIarg 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217360304 220 ----------TAFcSVHEKNQA--GDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPL 269
Cdd:cd22192   113 advvspratgTFF-RPGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 232-260 2.09e-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: 2.09e-04
                           10        20
                   ....*....|....*....|....*....
gi 2217360304  232 GDTALHVAAALNHKKVAKILLEAGADTTI 260
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 59-219 2.00e-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: 41.61  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304  59 ASEIVQDAVATVKAMKEDKNKKNHRGKVRKDPRRSEREKegDQTALHRATVVGNTEIIAALIHEG-------CALDRQDK 131
Cdd:TIGR00870  89 ISLEYVDAVEAILLHLLAAFRKSGPLELANDQYTSEFTP--GITALHLAAHRQNYEIVKLLLERGasvparaCGDFFVKS 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 132 DGNTALHeaswHG---------FSQSA--KLLIKAGANVLAKNKAGNTALHLACQNS-----------HSQSTRVLLLAG 189
Cdd:TIGR00870 167 QGVDSFY----HGesplnaaacLGSPSivALLSEDPADILTADSLGNTLLHLLVMENefkaeyeelscQMYNFALSLLDK 242

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2217360304 190 SR-----ADLKNNAGDTCLHVAARYNHLSIIRLLL 219
Cdd:TIGR00870 243 LRdskelEVILNHQGLTPLKLAAKEGRIVLFRLKL 277
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
97-287 6.71e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 165.51  E-value: 6.71e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304  97 KEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQN 176
Cdd:COG0666    51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 177 SHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGA 256
Cdd:COG0666   131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2217360304 257 DTTIVNNAGQTPLETARYHNNPEVALLLTKA 287
Cdd:COG0666   211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
95-287 1.90e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.96  E-value: 1.90e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304  95 REKEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLAC 174
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 175 QNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEA 254
Cdd:COG0666   162 ANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241

                         170       180       190
                  ....*....|....*....|....*....|...
gi 2217360304 255 GADTTIVNNAGQTPLETARYHNNPEVALLLTKA 287
Cdd:COG0666   242 GADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
98-269 5.03e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 137.78  E-value: 5.03e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304  98 EGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNS 177
Cdd:COG0666   118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 178 HSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGAD 257
Cdd:COG0666   198 HLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277

                         170
                  ....*....|..
gi 2217360304 258 TTIVNNAGQTPL 269
Cdd:COG0666   278 LAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
102-287 3.19e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.47  E-value: 3.19e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 102 TALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQS 181
Cdd:COG0666    23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 182 TRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGADTTIV 261
Cdd:COG0666   103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182

                         170       180
                  ....*....|....*....|....*.
gi 2217360304 262 NNAGQTPLETARYHNNPEVALLLTKA 287
Cdd:COG0666   183 DNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
114-284 1.23e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.43  E-value: 1.23e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 114 EIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRAD 193
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 194 LKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETAR 273
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                         170
                  ....*....|.
gi 2217360304 274 YHNNPEVALLL 284
Cdd:COG0666   162 ANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
170-262 9.32e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 9.32e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 170 LHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLtAFCSVHEKNQaGDTALHVAAALNHKKVAK 249
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2217360304 250 ILLEAGADTTIVN 262
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 112-290 7.03e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 93.55  E-value: 7.03e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 112 NTEIIAALIHEGCALDRQDKDGNTALHeaswhGFSQSA-------KLLIKAGANVLAKNKAGNTALHLACQNSHSQST-- 182
Cdd:PHA03095  131 NPKVIRLLLRKGADVNALDLYGMTPLA-----VLLKSRnanvellRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARiv 205

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 183 RVLLLAGSRADLKNNAGDTCLHVAARYNHL--SIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGADTTI 260
Cdd:PHA03095  206 RELIRAGCDPAATDMLGNTPLHSMATGSSCkrSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285

                         170       180       190
                  ....*....|....*....|....*....|.
gi 2217360304 261 VNNAGQTPLETARYHNNPE-VALLLTKAPQV 290
Cdd:PHA03095  286 VSSDGNTPLSLMVRNNNGRaVRAALAKNPSA 316
PHA03095 PHA03095
ankyrin-like protein; Provisional
 97-287 1.11e-19

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 92.78  E-value: 1.11e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304  97 KEGDQTALH---RATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQS-AKLLIKAGANVLAKNKAGNTALHL 172
Cdd:PHA03095   44 GEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDvIKLLIKAGADVNAKDKVGRTPLHV 123

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 173 ACQN----------------------------------SHSQST---RVLLLAGSRADLKNNAGDTCLHVAARYNHLS-- 213
Cdd:PHA03095  124 YLSGfninpkvirlllrkgadvnaldlygmtplavllkSRNANVellRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRar 203

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217360304 214 IIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKI--LLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 287
Cdd:PHA03095  204 IVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIAL 279
Ank_2 pfam12796
Ankyrin repeats (3 copies);
137-229 2.25e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.55  E-value: 2.25e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 137 LHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRvLLLAGSRADLKNNaGDTCLHVAARYNHLSIIR 216
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2217360304 217 LLLTAFCSVHEKN 229
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 112-290 8.63e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 86.64  E-value: 8.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 112 NTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQS-----AKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRV-- 184
Cdd:PHA03100   47 NIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTdvkeiVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVey 126

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 185 LLLAGSRADLKNNAGDTCLHVAARYNH--LSIIRLL----------------LTAFCSVHEKNQAGDTALHVAAALNHKK 246
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLidkgvdinaknrvnylLSYGVPINIKDVYGFTPLHYAVYNNNPE 206

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2217360304 247 VAKILLEAGADTTIVNNAGQTPLETARYHNNPE-VALLLTKAPQV 290
Cdd:PHA03100  207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEiFKLLLNNGPSI 251
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 113-272 1.07e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 86.86  E-value: 1.07e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 113 TEIIAALIHEGCALDRQDKD-GNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSR 191
Cdd:PHA02878  147 AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 192 ADLKNNAGDTCLHVAARY-NHLSIIRLLLTAFCSVHEKNQA-GDTALHVAaaLNHKKVAKILLEAGADTTIVNNAGQTPL 269
Cdd:PHA02878  227 TDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHSS--IKSERKLKLLLEYGADINSLNSYKLTPL 304


                  ...
gi 2217360304 270 ETA 272
Cdd:PHA02878  305 SSA 307
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 32-272 1.16e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 86.17  E-value: 1.16e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304  32 LLPANRVNSHWSANAISDWSMSNHIAPASEIVQDAVATVKAMKEDKNKKNHRGKvrkdprrserekegdqTALHRATVVG 111
Cdd:PHA02874   72 LLTAIKIGAHDIIKLLIDNGVDTSILPIPCIEKDMIKTILDCGIDVNIKDAELK----------------TFLHYAIKKG 135

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 112 NTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSR 191
Cdd:PHA02874  136 DLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNH 215

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 192 ADLKNNAGDTCLHVAARYNHlSIIRLLLTAfCSVHEKNQAGDTALHvaAALNH---KKVAKILLEAGADTTIVNNAGQTP 268
Cdd:PHA02874  216 IMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLH--HAINPpcdIDIIDILLYHKADISIKDNKGENP 291


                  ....
gi 2217360304 269 LETA 272
Cdd:PHA02874  292 IDTA 295
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
149-287 1.44e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.77  E-value: 1.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 149 AKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEK 228
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217360304 229 NQAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKA 287
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
Ank_2 pfam12796
Ankyrin repeats (3 copies);
203-284 3.49e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 3.49e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 203 LHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEaGADTTIVNNaGQTPLETARYHNNPEVAL 282
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ..
gi 2217360304 283 LL 284
Cdd:pfam12796  79 LL 80
PHA03095 PHA03095
ankyrin-like protein; Provisional
 150-269 4.81e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.14  E-value: 4.81e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 150 KLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRV---LLLAGSRADLKNNAGDTCLHVAARY-NHLSIIRLLLTAFCSV 225
Cdd:PHA03095   31 RRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNaTTLDVIKLLIKAGADV 110

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 2217360304 226 HEKNQAGDTALHV-AAALN-HKKVAKILLEAGADTTIVNNAGQTPL 269
Cdd:PHA03095  111 NAKDKVGRTPLHVyLSGFNiNPKVIRLLLRKGADVNALDLYGMTPL 156
Ank_2 pfam12796
Ankyrin repeats (3 copies);
104-196 5.76e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 5.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 104 LHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKaGANVLAKNKaGNTALHLACQNSHSQSTR 183
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2217360304 184 VLLLAGSRADLKN 196
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 112-326 3.32e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 75.39  E-value: 3.32e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 112 NTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSR 191
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 192 ADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGADTTIVNnaGQTPLET 271
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASINDQDID--GSTPLHH 260

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217360304 272 A-RYHNNPEV--ALLLTKAPQVLRFSRGRSLRK------KRERLKEERRAQSVPRDEVAQSKGS 326
Cdd:PHA02874  261 AiNPPCDIDIidILLYHKADISIKDNKGENPIDtafkyiNKDPVIKDIIANAVLIKEADKLKDS 324
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 64-262 9.58e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 74.90  E-value: 9.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304  64 QDAVATVKAMKEdKNKKNHRGKVRKDPRRSEREKEGDQTALHRATVV--GNTEIIAALIHEGCALDRQDKDGNTALHEAS 141
Cdd:PLN03192  488 EDNVVILKNFLQ-HHKELHDLNVGDLLGDNGGEHDDPNMASNLLTVAstGNAALLEELLKAKLDPDIGDSKGRTPLHIAA 566

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 142 WHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADlKNNAGDTcLHVAARYNHLSIIRLLLTA 221
Cdd:PLN03192  567 SKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISD-PHAAGDL-LCTAAKRNDLTAMKELLKQ 644

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 2217360304 222 FCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGADTTIVN 262
Cdd:PLN03192  645 GLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 112-263 3.44e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 72.39  E-value: 3.44e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 112 NTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSA--KLLIKAGANVLAKNKAGNTALHLACQNSHS---------- 179
Cdd:PHA03100   85 VKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSivEYLLDNGANVNIKNSDGENLLHLYLESNKIdlkilkllid 164

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 180 ------QSTRV--LLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKIL 251
Cdd:PHA03100  165 kgvdinAKNRVnyLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244

                         170
                  ....*....|..
gi 2217360304 252 LEAGADTTIVNN 263
Cdd:PHA03100  245 LNNGPSIKTIIE 256
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 102-219 7.03e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.07  E-value: 7.03e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 102 TALHRA--TVVGNTEIIAALIHEGCALDRQDKDGNTALHEA--SWHGFSQSAKLLIKAGANVLAKNKA------------ 165
Cdd:PHA03100  108 TPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKNRVnyllsygvpini 187

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217360304 166 ----GNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLL 219
Cdd:PHA03100  188 kdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
Ank_2 pfam12796
Ankyrin repeats (3 copies);
101-163 6.59e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 6.59e-10
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217360304 101 QTALHRATVVGNTEIIAALIhEGCALDRQDkDGNTALHEASWHGFSQSAKLLIKAGANVLAKN 163
Cdd:pfam12796  31 RTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 39-276 2.28e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.85  E-value: 2.28e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304  39 NSHWSANAISDWSMSN-HIAPASEIVQDAVATVKAMKEDKNKKNHRGkvrkdprrserekegdQTALHRATVVG-NTEII 116
Cdd:PHA02876  261 DAGFSVNSIDDCKNTPlHHASQAPSLSRLVPKLLERGADVNAKNIKG----------------ETPLYLMAKNGyDTENI 324

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 117 AALIHEGCALDRQDKDGNTALHEAS-WHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLK 195
Cdd:PHA02876  325 RTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEAL 404

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 196 NNAGDTCLHVA-ARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHK-KVAKILLEAGADTTIVNNAGQTPLETA- 272
Cdd:PHA02876  405 SQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAl 484


                  ....
gi 2217360304 273 RYHN 276
Cdd:PHA02876  485 EYHG 488
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 110-278 3.17e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 60.46  E-value: 3.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 110 VGNTEIIAALI--HEGCALDRQDKDGNTALHEASWH-GFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSH-SQSTRVL 185
Cdd:PHA02876  248 IRNEDLETSLLlyDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTL 327

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 186 LLAGSRADLKNNAGDTCLHVAA---RYNHLSIIRLLLTAfcSVHEKNQAGDTALHVAAALNHKKVAKILLEAGADTTIVN 262
Cdd:PHA02876  328 IMLGADVNAADRLYITPLHQAStldRNKDIVITLLELGA--NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALS 405

                         170
                  ....*....|....*.
gi 2217360304 263 NAGQTPLETARYHNNP 278
Cdd:PHA02876  406 QKIGTALHFALCGTNP 421
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 104-272 5.58e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.12  E-value: 5.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 104 LHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKaganVLAKNKAGNT--ALHLACQNSH--- 178
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR----SINKCSVFYTlvAIKDAFNNRNvei 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 179 ------------------------------SQSTRVLLLAGSRADLKN-NAGDTCLHVAARYNHLSIIRLLLTAFCSVHE 227
Cdd:PHA02878  117 fkiiltnrykniqtidlvyidkkskddiieAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNI 196

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2217360304 228 KNQAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETA 272
Cdd:PHA02878  197 PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
Ank_4 pfam13637
Ankyrin repeats (many copies);
102-153 6.63e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 6.63e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217360304 102 TALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLI 153
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 112-286 1.20e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.08  E-value: 1.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 112 NTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGA---NVLAKNkaGNTALHLACQNSHSQSTRVLLLA 188
Cdd:PHA02875   47 DSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIAR 124

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 189 GSRADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQ-T 267
Cdd:PHA02875  125 GADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCvA 204

                         170
                  ....*....|....*....
gi 2217360304 268 PLETARYHNNPEVALLLTK 286
Cdd:PHA02875  205 ALCYAIENNKIDIVRLFIK 223
Ank_4 pfam13637
Ankyrin repeats (many copies);
199-252 2.72e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 2.72e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217360304 199 GDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILL 252
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 215-289 3.44e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 3.44e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217360304 215 IRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKAPQ 289
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172
Ank_4 pfam13637
Ankyrin repeats (many copies);
166-219 4.10e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 4.10e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217360304 166 GNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLL 219
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
232-284 1.19e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 1.19e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217360304 232 GDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLL 284
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 150-269 2.93e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.86  E-value: 2.93e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 150 KLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRadLKNNA-------GDTCLHVAARYNHLSIIRLLL--- 219
Cdd:cd22192    35 KLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyqGETALHIAVVNQNLNLVRELIarg 112

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217360304 220 ----------TAFcSVHEKNQA--GDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPL 269
Cdd:cd22192   113 advvspratgTFF-RPGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 200-290 3.14e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 53.86  E-value: 3.14e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 200 DTCLHVAARYNHL-SIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKILLEagADTTIVNNA-------GQTPLET 271
Cdd:cd22192    18 ESPLLLAAKENDVqAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPmtsdlyqGETALHI 95

                          90       100
                  ....*....|....*....|
gi 2217360304 272 ARYHNNPE-VALLLTKAPQV 290
Cdd:cd22192    96 AVVNQNLNlVRELIARGADV 115
Ank_4 pfam13637
Ankyrin repeats (many copies);
133-186 6.26e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 6.26e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217360304 133 GNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLL 186
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
121-173 1.04e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 1.04e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217360304 121 HEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLA 173
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
185-239 1.64e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 1.64e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217360304 185 LLLAGSRA-DLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVA 239
Cdd:pfam13857   1 LLEHGPIDlNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_2 pfam12796
Ankyrin repeats (3 copies);
236-298 1.89e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.65  E-value: 1.89e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217360304 236 LHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARYHNNPEVALLLTKAPQVLRFSRGRS 298
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRT 63
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 133-280 2.19e-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: 51.17  E-value: 2.19e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 133 GNTALHEASWHGFSQSAKLLIKAgANVLAKNK------AGNTALHLACQNSHSQSTRVLLLAGsrADLKN---------- 196
Cdd:cd22192    51 GETALHVAALYDNLEAAVVLMEA-APELVNEPmtsdlyQGETALHIAVVNQNLNLVRELIARG--ADVVSpratgtffrp 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 197 NAGDTC------LHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAK-----IL-LEAGADT----TI 260
Cdd:cd22192   128 GPKNLIyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACqmydlILsYDKEDDLqpldLV 207

                         170       180
                  ....*....|....*....|
gi 2217360304 261 VNNAGQTPLETARYHNNPEV 280
Cdd:cd22192   208 PNNQGLTPFKLAAKEGNIVM 227
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 100-219 2.71e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.83  E-value: 2.71e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 100 DQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEAsWHGFS--QSAKLLIKAGANVLAKNKAGNTALHLACQ-N 176
Cdd:PHA02876  375 DKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-LCGTNpyMSVKTLIDRGANVNSKNKDLSTPLHYACKkN 453

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2217360304 177 SHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNhlSIIRLLL 219
Cdd:PHA02876  454 CKLDVIEMLLDNGADVNAINIQNQYPLLIALEYH--GIVNILL 494
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 97-308 8.17e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.83  E-value: 8.17e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304  97 KEGDqTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKaganvlaknkagntalHLACqn 176
Cdd:PHA02875  100 KDGM-TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLID----------------HKAC-- 160

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 177 shsqstrvlllagsrADLKNNAGDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHK-KVAKILLEAG 255
Cdd:PHA02875  161 ---------------LDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRG 225

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217360304 256 ADTTI---VNNAGQTPLETAR-YHNNPEV-ALLLTKAPQVLR-----------FSRGRSLRKKRERLKE 308
Cdd:PHA02875  226 ADCNImfmIEGEECTILDMICnMCTNLESeAIDALIADIAIRihkktirrdegFKNNMSTIEDKEEFKD 294
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 137-227 9.38e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.13  E-value: 9.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 137 LHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIR 216
Cdd:PTZ00322   86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                          90
                  ....*....|.
gi 2217360304 217 LLLTAFCSVHE 227
Cdd:PTZ00322  166 LLSRHSQCHFE 176
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 152-269 1.13e-05

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 48.75  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 152 LIKAGANVLAKNKAGNTA--LHLACQNSHSQSTRVL---LLAGSRADLKNNAGDTCLH--VAARYNHLSIIRLLLTAFCS 224
Cdd:PHA02716  265 ITNIYIESLDGNKVKNIPmiLHSYITLARNIDISVVysfLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGND 344

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2217360304 225 VHEKNQAGDTALH-------VAAALNHK-------KVAKILLEAGADTTIVNNAGQTPL 269
Cdd:PHA02716  345 LNEPDNIGNTVLHtylsmlsVVNILDPEtdndirlDVIQCLISLGADITAVNCLGYTPL 403
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 102-277 1.28e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 1.28e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 102 TALHRATVVGNTEIIAALIHEG---------------CALDRQDKD--------------GNTALHEASWHGFSQSAKLL 152
Cdd:PHA02876  180 TPIHYAAERGNAKMVNLLLSYGadvniialddlsvleCAVDSKNIDtikaiidnrsninkNDLSLLKAIRNEDLETSLLL 259

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 153 IKAGANVLAKNKAGNTALHLACQN-SHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNH-LSIIRLLLTAFCSVHEKNQ 230
Cdd:PHA02876  260 YDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADR 339

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 2217360304 231 AGDTALHVAAALN-HKKVAKILLEAGADTTIVNNAGQTPLETARYHNN 277
Cdd:PHA02876  340 LYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNN 387
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 232-263 1.67e-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: 42.28  E-value: 1.67e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2217360304 232 GDTALHVAAA-LNHKKVAKILLEAGADTTIVNN 263
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
Ank_5 pfam13857
Ankyrin repeats (many copies);
152-206 1.76e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 1.76e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217360304 152 LIKAG-ANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVA 206
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
218-272 1.94e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 1.94e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217360304 218 LLTAF-CSVHEKNQAGDTALHVAAALNHKKVAKILLEAGADTTIVNNAGQTPLETA 272
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 132-164 2.95e-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: 41.51  E-value: 2.95e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2217360304 132 DGNTALHEASWH-GFSQSAKLLIKAGANVLAKNK 164
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 150-276 5.81e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.81  E-value: 5.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 150 KLLIKAGANVLAKNKAGN-TALHLAC---QNSHSQSTRVLLLAGSRADLKNNAGDTCLHV-AARYN-HLSIIRLLLTAFC 223
Cdd:PHA02859   70 KFLIENGADVNFKTRDNNlSALHHYLsfnKNVEPEILKILIDSGSSITEEDEDGKNLLHMyMCNFNvRINVIKLLIDSGV 149

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217360304 224 SVHEKNQAGDTALHVAAAL-NHKKVAKILLEAGADTTIVNNAGQTPLETARYHN 276
Cdd:PHA02859  150 SFLNKDFDNNNILYSYILFhSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 90-186 1.74e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 1.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304  90 PRRSEREKEGDQTALHRATV-------VGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAK 162
Cdd:PTZ00322   65 DHNLTTEEVIDPVVAHMLTVelcqlaaSGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLL 144

                          90       100
                  ....*....|....*....|....
gi 2217360304 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 ...
 232-260 2.09e-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: 2.09e-04
                           10        20
                   ....*....|....*....|....*....
gi 2217360304  232 GDTALHVAAALNHKKVAKILLEAGADTTI 260
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 115-269 2.15e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.67  E-value: 2.15e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 115 IIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLlaGSRADL 194
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII--DNRSNI 237

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2217360304 195 KNNagDTCLHVAARYNHLSIIRLLLTAFCSVHEKNQAGDTALHVAA-ALNHKKVAKILLEAGADTTIVNNAGQTPL 269
Cdd:PHA02876  238 NKN--DLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPL 311
PHA02791 PHA02791
ankyrin-like protein; Provisional
 100-229 2.38e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 43.88  E-value: 2.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 100 DQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKAG--NTALHLACQNS 177
Cdd:PHA02791   61 NEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGwkTSFYHAVMLND 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217360304 178 HSQSTRVLLLAGSRADLKNNAgdTCLHVAARYNHLSIIRLLLTAFCSVHEKN 229
Cdd:PHA02791  141 VSIVSYFLSEIPSTFDLAILL--SCIHITIKNGHVDMMILLLDYMTSTNTNN 190
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 101-212 3.62e-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: 3.62e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 101 QTALHRATVVGNTEIIAALIHEG-----------CALDRQDKD---GNTALHEASWHGFSQSAKLLIKAGANVLAKNKAG 166
Cdd:cd22192    90 ETALHIAVVNQNLNLVRELIARGadvvspratgtFFRPGPKNLiyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2217360304 167 NTALH-LACQNSHSQSTRV--LLLAGSRAD-------LKNNAGDTCLHVAAR------YNHL 212
Cdd:cd22192   170 NTVLHiLVLQPNKTFACQMydLILSYDKEDdlqpldlVPNNQGLTPFKLAAKegnivmFQHL 231
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 199-227 3.70e-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: 38.34  E-value: 3.70e-04
                           10        20
                   ....*....|....*....|....*....
gi 2217360304  199 GDTCLHVAARYNHLSIIRLLLTAFCSVHE 227
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 199-229 4.79e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 4.79e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2217360304 199 GDTCLHVAA-RYNHLSIIRLLLTAFCSVHEKN 229
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 172-286 6.21e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 41.02  E-value: 6.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 172 LACQNSHSQSTRVLLLAgsradlKNNAGDTCLHVAARYNHLSII---RLLLTAFCSVHEKNQA-GDTALHVAAALNHKKV 247
Cdd:PHA02736   34 LAFKNAISDENRYLVLE------YNRHGKQCVHIVSNPDKADPQeklKLLMEWGADINGKERVfGNTPLHIAVYTQNYEL 107

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2217360304 248 AKILL-EAGADTTIVNNAGQTPLETARYHNNPEVALLLTK 286
Cdd:PHA02736  108 ATWLCnQPGVNMEILNYAFKTPYYVACERHDAKMMNILRA 147
PHA02798 PHA02798
ankyrin-like protein; Provisional
 101-255 1.44e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 41.74  E-value: 1.44e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 101 QTALHRATVvgNTEIIAALIHEGCALDRQDKDGNTAL-----HEASWHGFSQSAKLLIKAGANVLAKNKAGNTALHLACQ 175
Cdd:PHA02798   41 QKYLQRDSP--STDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLS 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 176 NSHSQSTRVLLLA---GSRADLKNNAGDTCLHVAARYNH---LSIIRLLLTAFCSVHE-KNQAGDTALHVAAALNHKK-- 246
Cdd:PHA02798  119 NGYINNLEILLFMienGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNIDRid 198

                         170
                  ....*....|.
gi 2217360304 247 --VAKILLEAG 255
Cdd:PHA02798  199 adILKLFVDNG 209
PHA03095 PHA03095
ankyrin-like protein; Provisional
 212-287 1.58e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.55  E-value: 1.58e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 212 LSIIRLLLTAFCSVHEKNQAGDTALHVAAALNHKKVAKI---LLEAGADTTIVNNAGQTPLETARYHNN-PEVALLLTKA 287
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKA 106
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 59-219 2.00e-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: 41.61  E-value: 2.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304  59 ASEIVQDAVATVKAMKEDKNKKNHRGKVRKDPRRSEREKegDQTALHRATVVGNTEIIAALIHEG-------CALDRQDK 131
Cdd:TIGR00870  89 ISLEYVDAVEAILLHLLAAFRKSGPLELANDQYTSEFTP--GITALHLAAHRQNYEIVKLLLERGasvparaCGDFFVKS 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 132 DGNTALHeaswHG---------FSQSA--KLLIKAGANVLAKNKAGNTALHLACQNS-----------HSQSTRVLLLAG 189
Cdd:TIGR00870 167 QGVDSFY----HGesplnaaacLGSPSivALLSEDPADILTADSLGNTLLHLLVMENefkaeyeelscQMYNFALSLLDK 242

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 2217360304 190 SR-----ADLKNNAGDTCLHVAARYNHLSIIRLLL 219
Cdd:TIGR00870 243 LRdskelEVILNHQGLTPLKLAAKEGRIVLFRLKL 277
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 227-288 2.14e-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: 41.28  E-value: 2.14e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217360304 227 EKNQAGDTALHVAAALNHKKVAKILLEAGADTTI---------VNNA-----GQTPLETARYHNNPE-VALLLTKAP 288
Cdd:cd22194   136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHegfyfGETPLALAACTNQPEiVQLLMEKES 212
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 170-301 2.54e-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: 41.22  E-value: 2.54e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 170 LHLACQNSHSQSTRVLLLAGSRADLknnaGDTCLHVAARYNHL---SIIRLLLTAF---CSVHEKN-------QAGDTAL 236
Cdd:TIGR00870  57 FVAAIENENLELTELLLNLSCRGAV----GDTLLHAISLEYVDaveAILLHLLAAFrksGPLELANdqytsefTPGITAL 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217360304 237 HVAAALNHKKVAKILLEAGADTTIVNNA--------------GQTPLETARYHNNPEVALLLTKAPQVLR--FSRGRSLR 300
Cdd:TIGR00870 133 HLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPADILtaDSLGNTLL 212


                  .
gi 2217360304 301 K 301
Cdd:TIGR00870 213 H 213
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 199-227 3.85e-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: 35.31  E-value: 3.85e-03
                          10        20
                  ....*....|....*....|....*....
gi 2217360304 199 GDTCLHVAARYNHLSIIRLLLTAFCSVHE 227
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 132-159 4.20e-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: 4.20e-03
                           10        20
                   ....*....|....*....|....*...
gi 2217360304  132 DGNTALHEASWHGFSQSAKLLIKAGANV 159
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_5 pfam13857
Ankyrin repeats (many copies);
86-140 4.31e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 4.31e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217360304  86 VRKDPRRSEREKEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEA 140
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 232-257 5.70e-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: 5.70e-03
                          10        20
                  ....*....|....*....|....*.
gi 2217360304 232 GDTALHVAAALNHKKVAKILLEAGAD 257
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGAD 27
 
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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