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Conserved domains on  [gi|966939897|ref|XP_014992381|]
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ankyrin repeat domain-containing protein 6 isoform X4 [Macaca mulatta]

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 1.50e-45

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 164.36  E-value: 1.50e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897  97 KEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLVKAGANVLAKNKAGNTALHLACQN 176
Cdd:COG0666   51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 177 SHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLSAFCSVHEKNQAGDTALHIAAALNHKKVAKILLEAGA 256
Cdd:COG0666  131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210

                        170       180       190
                 ....*....|....*....|....*....|.
gi 966939897 257 DTTIVNNAGQTPLETARCHNNPEVALLLTKA 287
Cdd:COG0666  211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
97-287 1.50e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 164.36  E-value: 1.50e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897  97 KEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLVKAGANVLAKNKAGNTALHLACQN 176
Cdd:COG0666   51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 177 SHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLSAFCSVHEKNQAGDTALHIAAALNHKKVAKILLEAGA 256
Cdd:COG0666  131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210

                        170       180       190
                 ....*....|....*....|....*....|.
gi 966939897 257 DTTIVNNAGQTPLETARCHNNPEVALLLTKA 287
Cdd:COG0666  211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
Ank_2 pfam12796
Ankyrin repeats (3 copies);
170-262 6.66e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.48  E-value: 6.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897  170 LHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLSAFCSvhEKNQAGDTALHIAAALNHKKVAK 249
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 966939897  250 ILLEAGADTTIVN 262
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 97-323 4.48e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 93.94  E-value: 4.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897  97 KEGDQTALH---RATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQS-AKLLVKAGANVLAKNKAGNTALHL 172
Cdd:PHA03095  44 GEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDvIKLLIKAGADVNAKDKVGRTPLHV 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 173 ACQN----------------------------------SHSQST---RVLLLAGSRADLKNNAGDTCLHVAARYNHLS-- 213
Cdd:PHA03095 124 YLSGfninpkvirlllrkgadvnaldlygmtplavllkSRNANVellRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRar 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 214 IIRLLLSAFCSVHEKNQAGDTALHIAAALNHKKVAKI--LLEAGADTTIVNNAGQTPLETARCHNNPEVALLLTKA---P 288
Cdd:PHA03095 204 IVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALgadI 283

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 966939897 289 QGSVSAGDTPSSEqAVARREE-AREEFLSASPEPRA 323
Cdd:PHA03095 284 NAVSSDGNTPLSL-MVRNNNGrAVRAALAKNPSAET 318
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 150-269 7.17e-08

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: 55.79  E-value: 7.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 150 KLLVKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRadLKNNA-------GDTCLHVAARYNHLSIIRLLLS-- 220
Cdd:cd22192   35 KLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyqGETALHIAVVNQNLNLVRELIArg 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966939897 221 ----------AFCSVHEKNQA--GDTALHIAAALNHKKVAKILLEAGADTTIVNNAGQTPL 269
Cdd:cd22192  113 advvspratgTFFRPGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 170-301 3.94e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.00  E-value: 3.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897  170 LHLACQNSHSQSTRVLLLAGSRADLknnaGDTCLHvAARYNHLSIIRLLLSAFCSVHEKN--------------QAGDTA 235
Cdd:TIGR00870  57 FVAAIENENLELTELLLNLSCRGAV----GDTLLH-AISLEYVDAVEAILLHLLAAFRKSgplelandqytsefTPGITA 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897  236 LHIAAALNHKKVAKILLEAGADTTIVNNA--------------GQTPLETARCHNNPEVALLLTKAPQgSVSAGDTPSSE 301
Cdd:TIGR00870 132 LHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPA-DILTADSLGNT 210
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 232-260 1.36e-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: 39.49  E-value: 1.36e-04
                           10        20
                   ....*....|....*....|....*....
gi 966939897   232 GDTALHIAAALNHKKVAKILLEAGADTTI 260
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
97-287 1.50e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 164.36  E-value: 1.50e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897  97 KEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLVKAGANVLAKNKAGNTALHLACQN 176
Cdd:COG0666   51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 177 SHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLSAFCSVHEKNQAGDTALHIAAALNHKKVAKILLEAGA 256
Cdd:COG0666  131 GNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGA 210

                        170       180       190
                 ....*....|....*....|....*....|.
gi 966939897 257 DTTIVNNAGQTPLETARCHNNPEVALLLTKA 287
Cdd:COG0666  211 DVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
23-287 2.96e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.19  E-value: 2.96e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897  23 YATPGANSLLLPANPVNSHWSADAISDWSMSNHIAPASEIVQDAVAAVKAMKEDKNKKNHRGKVRKDPRrsereKEGDQT 102
Cdd:COG0666   15 LLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK-----DDGGNT 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 103 ALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLVKAGANVLAKNKAGNTALHLACQNSHSQST 182
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 183 RVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLSAFCSVHEKNQAGDTALHIAAALNHKKVAKILLEAGADTTIVN 262
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKD 249

                        250       260
                 ....*....|....*....|....*
gi 966939897 263 NAGQTPLETARCHNNPEVALLLTKA 287
Cdd:COG0666  250 KDGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
98-269 1.24e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.62  E-value: 1.24e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897  98 EGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLVKAGANVLAKNKAGNTALHLACQNS 177
Cdd:COG0666  118 KDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENG 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 178 HSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLSAFCSVHEKNQAGDTALHIAAALNHKKVAKILLEAGAD 257
Cdd:COG0666  198 HLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277

                        170
                 ....*....|..
gi 966939897 258 TTIVNNAGQTPL 269
Cdd:COG0666  278 LAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
114-284 2.02e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.66  E-value: 2.02e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 114 EIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLVKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRAD 193
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 194 LKNNAGDTCLHVAARYNHLSIIRLLLSAFCSVHEKNQAGDTALHIAAALNHKKVAKILLEAGADTTIVNNAGQTPLETAR 273
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA 161

                        170
                 ....*....|.
gi 966939897 274 CHNNPEVALLL 284
Cdd:COG0666  162 ANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
170-262 6.66e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.48  E-value: 6.66e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897  170 LHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLSAFCSvhEKNQAGDTALHIAAALNHKKVAK 249
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 966939897  250 ILLEAGADTTIVN 262
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 97-323 4.48e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 93.94  E-value: 4.48e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897  97 KEGDQTALH---RATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQS-AKLLVKAGANVLAKNKAGNTALHL 172
Cdd:PHA03095  44 GEYGKTPLHlylHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDvIKLLIKAGADVNAKDKVGRTPLHV 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 173 ACQN----------------------------------SHSQST---RVLLLAGSRADLKNNAGDTCLHVAARYNHLS-- 213
Cdd:PHA03095 124 YLSGfninpkvirlllrkgadvnaldlygmtplavllkSRNANVellRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRar 203

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 214 IIRLLLSAFCSVHEKNQAGDTALHIAAALNHKKVAKI--LLEAGADTTIVNNAGQTPLETARCHNNPEVALLLTKA---P 288
Cdd:PHA03095 204 IVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALgadI 283

                        250       260       270
                 ....*....|....*....|....*....|....*.
gi 966939897 289 QGSVSAGDTPSSEqAVARREE-AREEFLSASPEPRA 323
Cdd:PHA03095 284 NAVSSDGNTPLSL-MVRNNNGrAVRAALAKNPSAET 318
Ank_2 pfam12796
Ankyrin repeats (3 copies);
137-229 3.18e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 3.18e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897  137 LHEASWHGFSQSAKLLVKAGANVLAKNKAGNTALHLACQNSHSQSTRvLLLAGSRADLKNNaGDTCLHVAARYNHLSIIR 216
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 966939897  217 LLLSAFCSVHEKN 229
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 113-272 7.64e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 86.86  E-value: 7.64e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 113 TEIIAALIHEGCALDRQDKD-GNTALHEASWHGFSQSAKLLVKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSR 191
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 192 ADLKNNAGDTCLHVAARY-NHLSIIRLLLSAFCSVHEKNQA-GDTALHIAaaLNHKKVAKILLEAGADTTIVNNAGQTPL 269
Cdd:PHA02878 227 TDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYIlGLTALHSS--IKSERKLKLLLEYGADINSLNSYKLTPL 304


                 ...
gi 966939897 270 ETA 272
Cdd:PHA02878 305 SSA 307
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 112-288 3.47e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 84.72  E-value: 3.47e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 112 NTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQS-----AKLLVKAGANVLAKNKAGNTALHLACQNSHSQSTRV-- 184
Cdd:PHA03100  47 NIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLTdvkeiVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVey 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 185 LLLAGSRADLKNNAGDTCLHVAARYNH--LSIIRLL----------------LSAFCSVHEKNQAGDTALHIAAALNHKK 246
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLidkgvdinaknrvnylLSYGVPINIKDVYGFTPLHYAVYNNNPE 206

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 966939897 247 VAKILLEAGADTTIVNNAGQTPLETARCHNNPE-VALLLTKAP 288
Cdd:PHA03100 207 FVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEiFKLLLNNGP 249
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 32-272 1.01e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 83.09  E-value: 1.01e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897  32 LLPANPVNSHWSADAISDWSMSNHIAPASEIVQDAVAAVKAMKEDKNKKNHRGKvrkdprrserekegdqTALHRATVVG 111
Cdd:PHA02874  72 LLTAIKIGAHDIIKLLIDNGVDTSILPIPCIEKDMIKTILDCGIDVNIKDAELK----------------TFLHYAIKKG 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 112 NTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLVKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSR 191
Cdd:PHA02874 136 DLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNH 215

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 192 ADLKNNAGDTCLHVAARYNHlSIIRLLLSAfCSVHEKNQAGDTALHiaAALNH---KKVAKILLEAGADTTIVNNAGQTP 268
Cdd:PHA02874 216 IMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASINDQDIDGSTPLH--HAINPpcdIDIIDILLYHKADISIKDNKGENP 291


                 ....
gi 966939897 269 LETA 272
Cdd:PHA02874 292 IDTA 295
Ank_2 pfam12796
Ankyrin repeats (3 copies);
203-284 2.59e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 2.59e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897  203 LHVAARYNHLSIIRLLLSAFCSVHEKNQAGDTALHIAAALNHKKVAKILLEaGADTTIVNNaGQTPLETARCHNNPEVAL 282
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ..
gi 966939897  283 LL 284
Cdd:pfam12796  79 LL 80
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
149-287 1.00e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.46  E-value: 1.00e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 149 AKLLVKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLSAFCSVHEK 228
Cdd:COG0666    4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 966939897 229 NQAGDTALHIAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARCHNNPEVALLLTKA 287
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 111-372 3.06e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 79.91  E-value: 3.06e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 111 GNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLVKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGS 190
Cdd:PLN03192 536 GNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS 615

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 191 RADlKNNAGDTcLHVAARYNHLSIIRLLLSAFCSVHEKNQAGDTALHIAAALNHKKVAKILLEAGADTTIVN-NAGQTPL 269
Cdd:PLN03192 616 ISD-PHAAGDL-LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANtDDDFSPT 693

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 270 ETARchnnpevalLLTKAPQG-SVSAGDT-PSSEQAVARREEAREEFLSASPEprakddrRRKSRPKVSAFSdptppadq 347
Cdd:PLN03192 694 ELRE---------LLQKRELGhSITIVDSvPADEPDLGRDGGSRPGRLQGTSS-------DNQCRPRVSIYK-------- 749

                        250       260
                 ....*....|....*....|....*
gi 966939897 348 qpghqknlhahNHPKKRNRHRCSSP 372
Cdd:PLN03192 750 -----------GHPLLRNERCCNEA 763
PHA03095 PHA03095
ankyrin-like protein; Provisional
 150-269 4.08e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.53  E-value: 4.08e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 150 KLLVKAGANVLAKNKAGNTALHLACQNSHSQSTRV---LLLAGSRADLKNNAGDTCLHVAARY-NHLSIIRLLLSAFCSV 225
Cdd:PHA03095  31 RRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNaTTLDVIKLLIKAGADV 110

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 966939897 226 HEKNQAGDTALHI-AAALN-HKKVAKILLEAGADTTIVNNAGQTPL 269
Cdd:PHA03095 111 NAKDKVGRTPLHVyLSGFNiNPKVIRLLLRKGADVNALDLYGMTPL 156
Ank_2 pfam12796
Ankyrin repeats (3 copies);
104-196 1.48e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.37  E-value: 1.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897  104 LHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLVKaGANVLAKNKaGNTALHLACQNSHSQSTR 183
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 966939897  184 VLLLAGSRADLKN 196
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 112-263 8.37e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 73.93  E-value: 8.37e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 112 NTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSA--KLLVKAGANVLAKNKAGNTALHLACQNSHS---------- 179
Cdd:PHA03100  85 VKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSivEYLLDNGANVNIKNSDGENLLHLYLESNKIdlkilkllid 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 180 ------QSTRV--LLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLSAFCSVHEKNQAGDTALHIAAALNHKKVAKIL 251
Cdd:PHA03100 165 kgvdinAKNRVnyLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244

                        170
                 ....*....|..
gi 966939897 252 LEAGADTTIVNN 263
Cdd:PHA03100 245 LNNGPSIKTIIE 256
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 150-287 2.17e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 72.69  E-value: 2.17e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 150 KLLVKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLSAFCSVHEKN 229
Cdd:PHA02874 108 KTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 966939897 230 QAGDTALHIAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARCHNNPEVALLLTKA 287
Cdd:PHA02874 188 NNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNA 245
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 102-225 1.11e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.30  E-value: 1.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 102 TALHRA--TVVGNTEIIAALIHEGCALDRQDKDGNTALHEA--SWHGFSQSAKLLVKAGANVLAKNKA------------ 165
Cdd:PHA03100 108 TPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYleSNKIDLKILKLLIDKGVDINAKNRVnyllsygvpini 187

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966939897 166 ----GNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLSAFCSV 225
Cdd:PHA03100 188 kdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 112-286 1.05e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.16  E-value: 1.05e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 112 NTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLVKAGA---NVLAKNkaGNTALHLACQNSHSQSTRVLLLA 188
Cdd:PHA02875  47 DSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfadDVFYKD--GMTPLHLATILKKLDIMKLLIAR 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 189 GSRADLKNNAGDTCLHVAARYNHLSIIRLLLSAFCSVHEKNQAGDTALHIAAALNHKKVAKILLEAGADttiVNNAGQTP 268
Cdd:PHA02875 125 GADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN---IDYFGKNG 201

                        170       180
                 ....*....|....*....|..
gi 966939897 269 LETARCH----NNPEVALLLTK 286
Cdd:PHA02875 202 CVAALCYaienNKIDIVRLFIK 223
Ank_2 pfam12796
Ankyrin repeats (3 copies);
101-163 1.14e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.51  E-value: 1.14e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 966939897  101 QTALHRATVVGNTEIIAALIhEGCALDRQDkDGNTALHEASWHGFSQSAKLLVKAGANVLAKN 163
Cdd:pfam12796  31 RTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 110-278 1.50e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.23  E-value: 1.50e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 110 VGNTEIIAALI--HEGCALDRQDKDGNTALHEASWH-GFSQSAKLLVKAGANVLAKNKAGNTALHLACQNSH-SQSTRVL 185
Cdd:PHA02876 248 IRNEDLETSLLlyDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTL 327

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 186 LLAGSRADLKNNAGDTCLHVAA---RYNHLSIIRLLLSAfcSVHEKNQAGDTALHIAAALNHKKVAKILLEAGADTTIVN 262
Cdd:PHA02876 328 IMLGADVNAADRLYITPLHQAStldRNKDIVITLLELGA--NVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALS 405

                        170
                 ....*....|....*.
gi 966939897 263 NAGQTPLETARCHNNP 278
Cdd:PHA02876 406 QKIGTALHFALCGTNP 421
Ank_4 pfam13637
Ankyrin repeats (many copies);
199-252 1.63e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 1.63e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 966939897  199 GDTCLHVAARYNHLSIIRLLLSAFCSVHEKNQAGDTALHIAAALNHKKVAKILL 252
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 99-261 1.77e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.39  E-value: 1.77e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897  99 GDQTALHRATVVGNTEIIAALIHEGC-ALDRQDKDGNTALHEASWHGFSQSAKLLVKAGANVLAKNKAGNTALHLACQNS 177
Cdd:PHA02875  67 DIESELHDAVEEGDVKAVEELLDLGKfADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMG 146

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 178 HSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLSAFCSVHEKNQAGDTALHIAAALNHK-KVAKILLEAGA 256
Cdd:PHA02875 147 DIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKiDIVRLFIKRGA 226


                 ....*
gi 966939897 257 DTTIV 261
Cdd:PHA02875 227 DCNIM 231
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 104-284 2.45e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.28  E-value: 2.45e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 104 LHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLVKaganVLAKNKAGNT--ALHLACQNSH--- 178
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR----SINKCSVFYTlvAIKDAFNNRNvei 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 179 ------------------------------SQSTRVLLLAGSRADLKN-NAGDTCLHVAARYNHLSIIRLLLSAFCSVHE 227
Cdd:PHA02878 117 fkiiltnrykniqtidlvyidkkskddiieAEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNI 196

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 966939897 228 KNQAGDTALHIAAALNHKKVAKILLEAGADTTIVNNAGQTPLETA--RCHNNPEVALLL 284
Cdd:PHA02878 197 PDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvgYCKDYDILKLLL 255
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 112-272 5.39e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.31  E-value: 5.39e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 112 NTEIIAALIHEGCALDRQDKDGNTALHEAS-WHGFSQSAKLLVKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGS 190
Cdd:PHA02876 320 DTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGA 399

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 191 RADLKNNAGDTCLHVA-ARYNHLSIIRLLLSAFCSVHEKNQAGDTALHIAAALNHK-KVAKILLEAGADTTIVNNAGQTP 268
Cdd:PHA02876 400 DIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYP 479


                 ....
gi 966939897 269 LETA 272
Cdd:PHA02876 480 LLIA 483
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 215-295 9.00e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.76  E-value: 9.00e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 215 IRLLLSAFCSVHEKNQAGDTALHIAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARCHNNPEVALLLTKAPQGSVSA 294
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177


                 .
gi 966939897 295 G 295
Cdd:PTZ00322 178 G 178
Ank_2 pfam12796
Ankyrin repeats (3 copies);
236-325 9.98e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.81  E-value: 9.98e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897  236 LHIAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARCHNNPEVA-LLLTKAPQGSVSAGDTPSSEQAVARREEAREEF 314
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVkLLLEHADVNLKDNGRTALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 966939897  315 LSASPEPRAKD 325
Cdd:pfam12796  81 LEKGADINVKD 91
Ank_4 pfam13637
Ankyrin repeats (many copies);
102-153 2.02e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 2.02e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 966939897  102 TALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLV 153
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
166-219 5.17e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 5.17e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 966939897  166 GNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLL 219
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 150-269 7.17e-08

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: 55.79  E-value: 7.17e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 150 KLLVKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRadLKNNA-------GDTCLHVAARYNHLSIIRLLLS-- 220
Cdd:cd22192   35 KLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPE--LVNEPmtsdlyqGETALHIAVVNQNLNLVRELIArg 112

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966939897 221 ----------AFCSVHEKNQA--GDTALHIAAALNHKKVAKILLEAGADTTIVNNAGQTPL 269
Cdd:cd22192  113 advvspratgTFFRPGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 200-286 1.40e-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: 55.02  E-value: 1.40e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 200 DTCLHVAARYNHL-SIIRLLLSAFCSVHEKNQAGDTALHIAAALNHKKVAKILLEagADTTIVNNA-------GQTPLET 271
Cdd:cd22192   18 ESPLLLAAKENDVqAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLME--AAPELVNEPmtsdlyqGETALHI 95

                         90
                 ....*....|....*.
gi 966939897 272 ARCHNNPE-VALLLTK 286
Cdd:cd22192   96 AVVNQNLNlVRELIAR 111
Ank_5 pfam13857
Ankyrin repeats (many copies);
185-239 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 966939897  185 LLLAGSRA-DLKNNAGDTCLHVAARYNHLSIIRLLLSAFCSVHEKNQAGDTALHIA 239
Cdd:pfam13857   1 LLEHGPIDlNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
133-186 1.11e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 1.11e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 966939897  133 GNTALHEASWHGFSQSAKLLVKAGANVLAKNKAGNTALHLACQNSHSQSTRVLL 186
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 133-280 1.14e-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: 51.94  E-value: 1.14e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 133 GNTALHEASWHGFSQSAKLLVKAgANVLAKNK------AGNTALHLACQNSHSQSTRVLLLAGsrADLKN---------- 196
Cdd:cd22192   51 GETALHVAALYDNLEAAVVLMEA-APELVNEPmtsdlyQGETALHIAVVNQNLNLVRELIARG--ADVVSpratgtffrp 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 197 NAGDTC------LHVAARYNHLSIIRLLLSAFCSVHEKNQAGDTALHIAAALNHKKVAK-----IL-LEAGADT----TI 260
Cdd:cd22192  128 GPKNLIyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACqmydlILsYDKEDDLqpldLV 207

                        170       180
                 ....*....|....*....|
gi 966939897 261 VNNAGQTPLETARCHNNPEV 280
Cdd:cd22192  208 PNNQGLTPFKLAAKEGNIVM 227
Ank_5 pfam13857
Ankyrin repeats (many copies);
121-173 1.84e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.42  E-value: 1.84e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 966939897  121 HEGCALDRQDKDGNTALHEASWHGFSQSAKLLVKAGANVLAKNKAGNTALHLA 173
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 157-251 3.68e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.25  E-value: 3.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 157 ANVLAKNKAGNTALhlacqnshsqsTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIRLLLSAFCSVHEKNQAGDTAL 236
Cdd:PLN03192 527 SNLLTVASTGNAAL-----------LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL 595

                         90
                 ....*....|....*
gi 966939897 237 HIAAALNHKKVAKIL 251
Cdd:PLN03192 596 WNAISAKHHKIFRIL 610
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 185-274 3.77e-06

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 50.30  E-value: 3.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 185 LLLAGSRADLKNNAGDTCLH--VAARYNHLSIIRLLLSAFCSVHEKNQAGDTALH-------IAAALNHK-------KVA 248
Cdd:PHA02716 303 FLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsVVNILDPEtdndirlDVI 382

                         90       100
                 ....*....|....*....|....*.
gi 966939897 249 KILLEAGADTTIVNNAGQTPLETARC 274
Cdd:PHA02716 383 QCLISLGADITAVNCLGYTPLTSYIC 408
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 100-219 4.58e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.06  E-value: 4.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 100 DQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEAsWHGFS--QSAKLLVKAGANVLAKNKAGNTALHLACQ-N 176
Cdd:PHA02876 375 DKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-LCGTNpyMSVKTLIDRGANVNSKNKDLSTPLHYACKkN 453

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 966939897 177 SHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNhlSIIRLLL 219
Cdd:PHA02876 454 CKLDVIEMLLDNGADVNAINIQNQYPLLIALEYH--GIVNILL 494
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 137-227 4.83e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 49.90  E-value: 4.83e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 137 LHEASWHGFSQSAKLLVKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNHLSIIR 216
Cdd:PTZ00322  86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQ 165

                         90
                 ....*....|.
gi 966939897 217 LLLSAFCSVHE 227
Cdd:PTZ00322 166 LLSRHSQCHFE 176
Ank_4 pfam13637
Ankyrin repeats (many copies);
232-284 5.41e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 5.41e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 966939897  232 GDTALHIAAALNHKKVAKILLEAGADTTIVNNAGQTPLETARCHNNPEVALLL 284
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 102-277 6.46e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.68  E-value: 6.46e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 102 TALHRATVVGNTEIIAALIHEG---------------CALDRQDKD--------------GNTALHEASWHGFSQSAKLL 152
Cdd:PHA02876 180 TPIHYAAERGNAKMVNLLLSYGadvniialddlsvleCAVDSKNIDtikaiidnrsninkNDLSLLKAIRNEDLETSLLL 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 153 VKAGANVLAKNKAGNTALHLACQN-SHSQSTRVLLLAGSRADLKNNAGDTCLHVAARYNH-LSIIRLLLSAFCSVHEKNQ 230
Cdd:PHA02876 260 YDAGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADR 339

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 966939897 231 AGDTALHIAAALN-HKKVAKILLEAGADTTIVNNAGQTPLETARCHNN 277
Cdd:PHA02876 340 LYITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNN 387
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 97-220 8.67e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.83  E-value: 8.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897  97 KEGDqTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLVKAGANVLAKNKAGNTALHLACQN 176
Cdd:PHA02875 100 KDGM-TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAK 178

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 966939897 177 SHSQSTRVLLLAGSRADLKNNAGD-TCLHVAARYNHLSIIRLLLS 220
Cdd:PHA02875 179 GDIAICKMLLDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIK 223
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 156-284 1.14e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.86  E-value: 1.14e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 156 GANVLAKNKAGNTALHLACQNSHSQSTRVLLLAgSRADL--KNNAGDTCLHVAARYNHLSIIRLLLSAfcsVHE-KNQA- 231
Cdd:cd22192    7 ELHLLQQKRISESPLLLAAKENDVQAIKKLLKC-PSCDLfqRGALGETALHVAALYDNLEAAVVLMEA---APElVNEPm 82

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966939897 232 ------GDTALHIAAALNHKKVAKILLEAGADttiVNNA-----------------GQTPLETARCHNNPEVALLL 284
Cdd:cd22192   83 tsdlyqGETALHIAVVNQNLNLVRELIARGAD---VVSPratgtffrpgpknliyyGEHPLSFAACVGNEEIVRLL 155
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 232-263 1.35e-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: 1.35e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 966939897  232 GDTALHIAAA-LNHKKVAKILLEAGADTTIVNN 263
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARDK 34
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 227-288 1.38e-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: 48.60  E-value: 1.38e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966939897 227 EKNQAGDTALHIAAALNHKKVAKILLEAGADTTI---------VNNA-----GQTPLETARCHNNPE-VALLLTKAP 288
Cdd:cd22194  136 EEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHegfyfGETPLALAACTNQPEiVQLLMEKES 212
Ank_5 pfam13857
Ankyrin repeats (many copies);
218-272 2.10e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 2.10e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 966939897  218 LLSAF-CSVHEKNQAGDTALHIAAALNHKKVAKILLEAGADTTIVNNAGQTPLETA 272
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
152-206 2.60e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 2.60e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 966939897  152 LVKAG-ANVLAKNKAGNTALHLACQNSHSQSTRVLLLAGSRADLKNNAGDTCLHVA 206
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 172-292 3.85e-05

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 44.48  E-value: 3.85e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 172 LACQNSHSQSTRVLLLAgsradlKNNAGDTCLHVAARYNHLSII---RLLLSAFCSVHEKNQA-GDTALHIAAALNHKKV 247
Cdd:PHA02736  34 LAFKNAISDENRYLVLE------YNRHGKQCVHIVSNPDKADPQeklKLLMEWGADINGKERVfGNTPLHIAVYTQNYEL 107

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 966939897 248 AKILL-EAGADTTIVNNAGQTPLETA-RCHNNPEVALLLTKAPQGSV 292
Cdd:PHA02736 108 ATWLCnQPGVNMEILNYAFKTPYYVAcERHDAKMMNILRAKGAQCKV 154
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 170-301 3.94e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.00  E-value: 3.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897  170 LHLACQNSHSQSTRVLLLAGSRADLknnaGDTCLHvAARYNHLSIIRLLLSAFCSVHEKN--------------QAGDTA 235
Cdd:TIGR00870  57 FVAAIENENLELTELLLNLSCRGAV----GDTLLH-AISLEYVDAVEAILLHLLAAFRKSgplelandqytsefTPGITA 131

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897  236 LHIAAALNHKKVAKILLEAGADTTIVNNA--------------GQTPLETARCHNNPEVALLLTKAPQgSVSAGDTPSSE 301
Cdd:TIGR00870 132 LHLAAHRQNYEIVKLLLERGASVPARACGdffvksqgvdsfyhGESPLNAAACLGSPSIVALLSEDPA-DILTADSLGNT 210
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 132-164 6.71e-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: 40.35  E-value: 6.71e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 966939897  132 DGNTALHEASWH-GFSQSAKLLVKAGANVLAKNK 164
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02791 PHA02791
ankyrin-like protein; Provisional
 100-229 1.22e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 44.65  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 100 DQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLVKAGANVLAKNKAG--NTALHLACQNS 177
Cdd:PHA02791  61 NEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLFVKKNWRLMFYGKTGwkTSFYHAVMLND 140

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 966939897 178 HSQSTRVLLLAGSRADLKNNAgdTCLHVAARYNHLSIIRLLLSAFCSVHEKN 229
Cdd:PHA02791 141 VSIVSYFLSEIPSTFDLAILL--SCIHITIKNGHVDMMILLLDYMTSTNTNN 190
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 232-260 1.36e-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: 39.49  E-value: 1.36e-04
                           10        20
                   ....*....|....*....|....*....
gi 966939897   232 GDTALHIAAALNHKKVAKILLEAGADTTI 260
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 90-186 2.01e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 2.01e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897  90 PRRSEREKEGDQTALHRATV-------VGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLVKAGANVLAK 162
Cdd:PTZ00322  65 DHNLTTEEVIDPVVAHMLTVelcqlaaSGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLL 144

                         90       100
                 ....*....|....*....|....
gi 966939897 163 NKAGNTALHLACQNSHSQSTRVLL 186
Cdd:PTZ00322 145 DKDGKTPLELAEENGFREVVQLLS 168
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 115-269 2.09e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.67  E-value: 2.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 115 IIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLVKAGANVLAKNKAGNTALHLACQNSHSQSTRVLLlaGSRADL 194
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII--DNRSNI 237

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966939897 195 KNNagDTCLHVAARYNHLSIIRLLLSAFCSVHEKNQAGDTALHIAA-ALNHKKVAKILLEAGADTTIVNNAGQTPL 269
Cdd:PHA02876 238 NKN--DLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPL 311
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 199-227 2.42e-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: 38.72  E-value: 2.42e-04
                           10        20
                   ....*....|....*....|....*....
gi 966939897   199 GDTCLHVAARYNHLSIIRLLLSAFCSVHE 227
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 199-229 2.53e-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: 38.81  E-value: 2.53e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 966939897  199 GDTCLHVAA-RYNHLSIIRLLLSAFCSVHEKN 229
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 232-297 8.11e-04

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 42.86  E-value: 8.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 232 GDTALHIAAALNHKKVAKILLEAGADTTIVNNA--------------GQTPLETARCHNNPEVALLLTKAPQ--GSVSAG 295
Cdd:cd22193   76 GQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEHqpADIEAQ 155


                 ..
gi 966939897 296 DT 297
Cdd:cd22193  156 DS 157
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 199-288 8.37e-04

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: 42.56  E-value: 8.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 199 GDTCLHVAARYNH---LSIIRLLLSA-----------FCSVHEKNQAGDTALHIAAALNHKKVAKILLEAGADTTIVNNA 264
Cdd:cd21882   26 GKTCLHKAALNLNdgvNEAIMLLLEAapdsgnpkelvNAPCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARATG 105

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 966939897 265 -------------GQTPLETARCHNNPEVALLLTKAP 288
Cdd:cd21882  106 rffrkspgnlfyfGELPLSLAACTNQEEIVRLLLENG 142
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 59-219 1.26e-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: 41.99  E-value: 1.26e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897   59 ASEIVQDAVAAVKAMKEDKNKKNHRGKVRKDPRRSEREKegDQTALHRATVVGNTEIIAALIHEG-------CALDRQDK 131
Cdd:TIGR00870  89 ISLEYVDAVEAILLHLLAAFRKSGPLELANDQYTSEFTP--GITALHLAAHRQNYEIVKLLLERGasvparaCGDFFVKS 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897  132 DGNTALHeaswHG---------FSQSA--KLLVKAGANVLAKNKAGNTALHLACQNS-----------HSQSTRVLLLAG 189
Cdd:TIGR00870 167 QGVDSFY----HGesplnaaacLGSPSivALLSEDPADILTADSLGNTLLHLLVMENefkaeyeelscQMYNFALSLLDK 242

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 966939897  190 SR-----ADLKNNAGDTCLHVAARYNHLSIIRLLL 219
Cdd:TIGR00870 243 LRdskelEVILNHQGLTPLKLAAKEGRIVLFRLKL 277
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 150-270 1.36e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 1.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 150 KLLVKAGANVLAKNKAGN-TALHLAC---QNSHSQSTRVLLLAGSRADLKNNAGDTCLHV-AARYN-HLSIIRLLLSAFC 223
Cdd:PHA02859  70 KFLIENGADVNFKTRDNNlSALHHYLsfnKNVEPEILKILIDSGSSITEEDEDGKNLLHMyMCNFNvRINVIKLLIDSGV 149

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 966939897 224 SVHEKNQAGDTALHIAAAL-NHKKVAKILLEAGADTTIVNNAGQTPLE 270
Cdd:PHA02859 150 SFLNKDFDNNNILYSYILFhSDKKIFDFLTSLGIDINETNKSGYNCYD 197
PHA03095 PHA03095
ankyrin-like protein; Provisional
 212-287 1.65e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 41.55  E-value: 1.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 212 LSIIRLLLSAFCSVHEKNQAGDTALHIAAALNHKKVAKI---LLEAGADTTIVNNAGQTPLETARCHNN-PEVALLLTKA 287
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKA 106
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 201-269 2.42e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.80  E-value: 2.42e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966939897 201 TCLHVAARYNHLSIIRLLLSAFCSVHEKNQAGDTALHIAAALNH-----KKVAKILLEAGADTTIVNNAGQTPL 269
Cdd:PHA03100  37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPL 110
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 199-227 2.75e-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: 2.75e-03
                          10        20
                  ....*....|....*....|....*....
gi 966939897  199 GDTCLHVAARYNHLSIIRLLLSAFCSVHE 227
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 232-257 2.89e-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: 2.89e-03
                          10        20
                  ....*....|....*....|....*.
gi 966939897  232 GDTALHIAAALNHKKVAKILLEAGAD 257
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGAD 27
PHA02798 PHA02798
ankyrin-like protein; Provisional
 101-255 3.38e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.59  E-value: 3.38e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 101 QTALHRATVvgNTEIIAALIHEGCALDRQDKDGNTAL-----HEASWHGFSQSAKLLVKAGANVLAKNKAGNTALHLACQ 175
Cdd:PHA02798  41 QKYLQRDSP--STDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLS 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 176 NSHSQSTRVLLLA---GSRADLKNNAGDTCLHVAARYNH---LSIIRLLLSAFCSVHE-KNQAGDTALHIAAALNHKK-- 246
Cdd:PHA02798 119 NGYINNLEILLFMienGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINThNNKEKYDTLHCYFKYNIDRid 198

                        170
                 ....*....|.
gi 966939897 247 --VAKILLEAG 255
Cdd:PHA02798 199 adILKLFVDNG 209
Ank_5 pfam13857
Ankyrin repeats (many copies);
86-140 5.09e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 5.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 966939897   86 VRKDPRRSEREKEGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEA 140
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02946 PHA02946
ankyin-like protein; Provisional
 93-269 5.74e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 39.65  E-value: 5.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897  93 SEREKEGDQtALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHG--FSQSAKLLVKAGANVLAKNKAGNTAL 170
Cdd:PHA02946  66 NETDDDGNY-PLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDdeVIERINLLVQYGAKINNSVDEEGCGP 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966939897 171 HLACQNSHSQSTRVLLLAGSRADLKNNAGDTCL--HVAARYNHLSIIRLLLSAFCSVHEKNQAGDTALHIAAALNHKKVA 248
Cdd:PHA02946 145 LLACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKTVKNVD 224

                        170       180
                 ....*....|....*....|..
gi 966939897 249 KI-LLEAGADTTIVNNAGQTPL 269
Cdd:PHA02946 225 IInLLLPSTDVNKQNKFGDSPL 246
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 132-159 7.79e-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: 7.79e-03
                           10        20
                   ....*....|....*....|....*...
gi 966939897   132 DGNTALHEASWHGFSQSAKLLVKAGANV 159
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
 
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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