NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|125820436|ref|XP_696186|]
View 

ankyrin repeat domain-containing protein 53 isoform X1 [Danio rerio]

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

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
19-186 1.72e-28

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.27  E-value: 1.72e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  19 ESDMFHAAASGARDWLSLTLKKARKPLITDKHGLSVLHIAALHGHLDCMELLLAGGyADVNVSCPHGRRPLHMMltAQSQ 98
Cdd:COG0666   88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLA--AANG 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  99 pntHAGLI-YLLEHGAHISVSTDEGLTPLHQAAAEGLTDCTETLVRHGANTHTPDTSGHTPLDLARIWGHRDTARFLKDA 177
Cdd:COG0666  165 ---NLEIVkLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241


                 ....*....
gi 125820436 178 MWRKDKEQQ 186
Cdd:COG0666  242 GADLNAKDK 250
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
19-186 1.72e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.27  E-value: 1.72e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  19 ESDMFHAAASGARDWLSLTLKKARKPLITDKHGLSVLHIAALHGHLDCMELLLAGGyADVNVSCPHGRRPLHMMltAQSQ 98
Cdd:COG0666   88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLA--AANG 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  99 pntHAGLI-YLLEHGAHISVSTDEGLTPLHQAAAEGLTDCTETLVRHGANTHTPDTSGHTPLDLARIWGHRDTARFLKDA 177
Cdd:COG0666  165 ---NLEIVkLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241


                 ....*....
gi 125820436 178 MWRKDKEQQ 186
Cdd:COG0666  242 GADLNAKDK 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
55-152 1.06e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 1.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436   55 LHIAALHGHLDCMELLLAGGyADVNVSCPHGRRPLHMmltAQSQPNTHAgLIYLLEHGAhiSVSTDEGLTPLHQAAAEGL 134
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHL---AAKNGHLEI-VKLLLEHAD--VNLKDNGRTALHYAARSGH 73

                          90
                  ....*....|....*...
gi 125820436  135 TDCTETLVRHGANTHTPD 152
Cdd:pfam12796  74 LEIVKLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 20-174 6.08e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.81  E-value: 6.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  20 SDMFHAAASGARDWLSLTLKKARKPLITDKHGLSVLHIAALHGHLDCMELLLAGGyADVNVSCPHGRRPLHMMLTAQsqp 99
Cdd:PLN03192 527 SNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDANGNTALWNAISAK--- 602

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 125820436 100 ntHAGLIYLLEHGAHISVSTDEGlTPLHQAAAEGLTDCTETLVRHGANTHTPDTSGHTPLDLARIWGHRDTARFL 174
Cdd:PLN03192 603 --HHKIFRILYHFASISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 50-159 5.32e-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: 43.85  E-value: 5.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  50 HGLSVLHIAALHGHLDCMELLLAGGYADVNVSCP----HGRRPLHMMLTAQSQPNTHAgliyLLEHGAhiSVSTDE---- 121
Cdd:cd22192   50 LGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVVNQNLNLVRE----LIARGA--DVVSPRatgt 123

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 125820436 122 ------------GLTPLHQAAAEGLTDCTETLVRHGANTHTPDTSGHTPL 159
Cdd:cd22192  124 ffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 1-162 3.26e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.61  E-value: 3.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436    1 MSVLRKDNNEAVVGGSppesdMFHAAASGARD----WLSLTLKKARK----PLITDK------HGLSVLHIAALHGHLDC 66
Cdd:TIGR00870  69 TELLLNLSCRGAVGDT-----LLHAISLEYVDaveaILLHLLAAFRKsgplELANDQytseftPGITALHLAAHRQNYEI 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436   67 MELLLAGGyADVNVSCP--------------HGRRPLHMMlTAQSQPNTHAgliYLLEHGAHISVSTDEGLTPLHQAAAE 132
Cdd:TIGR00870 144 VKLLLERG-ASVPARACgdffvksqgvdsfyHGESPLNAA-ACLGSPSIVA---LLSEDPADILTADSLGNTLLHLLVME 218

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 125820436  133 GL---------TDCTETLVRHGANTHT-------PDTSGHTPLDLA 162
Cdd:TIGR00870 219 NEfkaeyeelsCQMYNFALSLLDKLRDskeleviLNHQGLTPLKLA 264
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 50-80 1.52e-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: 1.52e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 125820436    50 HGLSVLHIAALHGHLDCMELLLAGGyADVNV 80
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKG-ADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
19-186 1.72e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.27  E-value: 1.72e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  19 ESDMFHAAASGARDWLSLTLKKARKPLITDKHGLSVLHIAALHGHLDCMELLLAGGyADVNVSCPHGRRPLHMMltAQSQ 98
Cdd:COG0666   88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAG-ADVNAQDNDGNTPLHLA--AANG 164

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  99 pntHAGLI-YLLEHGAHISVSTDEGLTPLHQAAAEGLTDCTETLVRHGANTHTPDTSGHTPLDLARIWGHRDTARFLKDA 177
Cdd:COG0666  165 ---NLEIVkLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEA 241


                 ....*....
gi 125820436 178 MWRKDKEQQ 186
Cdd:COG0666  242 GADLNAKDK 250
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
21-177 1.19e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.95  E-value: 1.19e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  21 DMFHAAASGARDWLSLTLKKARKPLITDKHGLSVLHIAALHGHLDCMELLLAGGyADVNVSCPHGRRPLHMMltaqSQPN 100
Cdd:COG0666   57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAG-ADVNARDKDGETPLHLA----AYNG 131

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 125820436 101 THAGLIYLLEHGAHISVSTDEGLTPLHQAAAEGLTDCTETLVRHGANTHTPDTSGHTPLDLARIWGHRDTARFLKDA 177
Cdd:COG0666  132 NLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEA 208
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-177 1.15e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.47  E-value: 1.15e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  22 MFHAAASGARDWLSLTLKKARKPLITDKHGLSVLHIAALHGHLDCMELLLAGGyADVNVSCPHGRRPLHMMLTAQsqpnt 101
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAG-ADVNARDNDGETPLHLAAENG----- 197

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 125820436 102 HAGLI-YLLEHGAHISVSTDEGLTPLHQAAAEGLTDCTETLVRHGANTHTPDTSGHTPLDLARIWGHRDTARFLKDA 177
Cdd:COG0666  198 HLEIVkLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
Ank_2 pfam12796
Ankyrin repeats (3 copies);
55-152 1.06e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 1.06e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436   55 LHIAALHGHLDCMELLLAGGyADVNVSCPHGRRPLHMmltAQSQPNTHAgLIYLLEHGAhiSVSTDEGLTPLHQAAAEGL 134
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENG-ADANLQDKNGRTALHL---AAKNGHLEI-VKLLLEHAD--VNLKDNGRTALHYAARSGH 73

                          90
                  ....*....|....*...
gi 125820436  135 TDCTETLVRHGANTHTPD 152
Cdd:pfam12796  74 LEIVKLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 20-174 6.08e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.81  E-value: 6.08e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  20 SDMFHAAASGARDWLSLTLKKARKPLITDKHGLSVLHIAALHGHLDCMELLLAGGyADVNVSCPHGRRPLHMMLTAQsqp 99
Cdd:PLN03192 527 SNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA-CNVHIRDANGNTALWNAISAK--- 602

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 125820436 100 ntHAGLIYLLEHGAHISVSTDEGlTPLHQAAAEGLTDCTETLVRHGANTHTPDTSGHTPLDLARIWGHRDTARFL 174
Cdd:PLN03192 603 --HHKIFRILYHFASISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
34-177 3.11e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.20  E-value: 3.11e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  34 LSLTLKKARKPLITDKHGLSVLHIAALHGHLDCMELLLAGGYADVNVscphgRRPLHMMLTAQSQPNTHAGLIYLLEHGA 113
Cdd:COG0666    4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALA-----DALGALLLLAAALAGDLLVALLLLAAGA 78

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 125820436 114 HISVSTDEGLTPLHQAAAEGLTDCTETLVRHGANTHTPDTSGHTPLDLARIWGHRDTARFLKDA 177
Cdd:COG0666   79 DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEA 142
PHA03095 PHA03095
ankyrin-like protein; Provisional
 48-160 4.97e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.80  E-value: 4.97e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  48 DKHGLSVLHIAALHGH-LDCMELLLAGGyADVNVSCPHGRRPLHMMLTAqsqPNTHAGLI-YLLEHGAHISVSTDEGLTP 125
Cdd:PHA03095  80 ERCGFTPLHLYLYNATtLDVIKLLIKAG-ADVNAKDKVGRTPLHVYLSG---FNINPKVIrLLLRKGADVNALDLYGMTP 155

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 125820436 126 LHqaAAEGLTDCT----ETLVRHGANTHTPDTSGHTPLD 160
Cdd:PHA03095 156 LA--VLLKSRNANvellRLLIDAGADVYAVDDRFRSLLH 192
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 46-165 5.17e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.74  E-value: 5.17e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  46 ITDKHGLSVLHIAALHGHLDCMELLLAGGyADVNVSCPHGRRPLHMMLtaqsQPNTHAGLIYLLEHGAHISVSTDEGLTP 125
Cdd:PHA02874 119 IKDAELKTFLHYAIKKGDLESIKMLFEYG-ADVNIEDDNGCYPIHIAI----KHNFFDIIKLLLEKGAYANVKDNNGESP 193

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 125820436 126 LHQAAAEGLTDCTETLVRHGANTHTPDTSGHTPLDLARIW 165
Cdd:PHA02874 194 LHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH 233
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 46-176 7.84e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.35  E-value: 7.84e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  46 ITDKHGLSVLHIAALHGHLDCMELLLAGGyADVNVSCPHGRRPLHMmltaQSQPNTHAGLIYLLEHGAHISVSTDEGLTP 125
Cdd:PHA02874 152 IEDDNGCYPIHIAIKHNFFDIIKLLLEKG-AYANVKDNNGESPLHN----AAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436 126 LHQAA--------------------AEGLT------------DCTETLVRHGANTHTPDTSGHTPLDLARIWGHRDTArf 173
Cdd:PHA02874 227 LHNAIihnrsaiellinnasindqdIDGSTplhhainppcdiDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPV-- 304


                 ...
gi 125820436 174 LKD 176
Cdd:PHA02874 305 IKD 307
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 53-177 6.50e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 52.69  E-value: 6.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  53 SVLHIAALHGHLDCMELLL-AGGYADvNVSCPHGRRPLHMMLTAQSQPNTHAgliyLLEHGAHISVSTDEGLTPLHQAAA 131
Cdd:PHA02875  70 SELHDAVEEGDVKAVEELLdLGKFAD-DVFYKDGMTPLHLATILKKLDIMKL----LIARGADPDIPNTDKFSPLHLAVM 144

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 125820436 132 EGLTDCTETLVRHGANTHTPDTSGHTPLDLARIWGHRDTARFLKDA 177
Cdd:PHA02875 145 MGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDS 190
PHA03095 PHA03095
ankyrin-like protein; Provisional
 64-174 2.22e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.18  E-value: 2.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  64 LDCMELLLAGGyADVNVSCPHGRRPLHMMLTAQSQPNTHAGLIyLLEHGAHISVSTDEGLTPLHQAAAEGLT-DCTETLV 142
Cdd:PHA03095  27 VEEVRRLLAAG-ADVNFRGEYGKTPLHLYLHYSSEKVKDIVRL-LLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLI 104

                         90       100       110
                 ....*....|....*....|....*....|....
gi 125820436 143 RHGANTHTPDTSGHTPLD--LARIWGHRDTARFL 174
Cdd:PHA03095 105 KAGADVNAKDKVGRTPLHvyLSGFNINPKVIRLL 138
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 56-174 3.15e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.64  E-value: 3.15e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  56 HIAALHGhLDCMELLLAGGYADVNVSCPHGrrplhmMLTAQSQPNThAGLIYLLEHGAHISVSTDEGLTPLHQAAAEGLT 135
Cdd:PLN03192 500 HHKELHD-LNVGDLLGDNGGEHDDPNMASN------LLTVASTGNA-ALLEELLKAKLDPDIGDSKGRTPLHIAASKGYE 571

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 125820436 136 DCTETLVRHGANTHTPDTSGHTPLDLARIWGHRDTARFL 174
Cdd:PLN03192 572 DCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL 610
PHA03095 PHA03095
ankyrin-like protein; Provisional
 64-160 1.52e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.48  E-value: 1.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  64 LDCMELLLAGGyADVNVSCPHGRRPLHMMLTAQsqpNTHAGLIYLLEHGAHISVSTDEGLTPLHqAAAEGL---TDCTET 140
Cdd:PHA03095  63 KDIVRLLLEAG-ADVNAPERCGFTPLHLYLYNA---TTLDVIKLLIKAGADVNAKDKVGRTPLH-VYLSGFninPKVIRL 137

                         90       100
                 ....*....|....*....|
gi 125820436 141 LVRHGANTHTPDTSGHTPLD 160
Cdd:PHA03095 138 LLRKGADVNALDLYGMTPLA 157
Ank_2 pfam12796
Ankyrin repeats (3 copies);
126-187 2.48e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.72  E-value: 2.48e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 125820436  126 LHQAAAEGLTDCTETLVRHGANTHTPDTSGHTPLDLARIWGHRDTARFLKDAMWRKDKEQQM 187
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGR 62
PHA03095 PHA03095
ankyrin-like protein; Provisional
 59-159 6.44e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 6.44e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  59 ALHGHL-------DCMELLLAGGyADVNVSCPHGRRPLHMMLtaqSQPNTHAGLI-YLLEHGAHISVSTDEGLTPLHQAA 130
Cdd:PHA03095 120 PLHVYLsgfninpKVIRLLLRKG-ADVNALDLYGMTPLAVLL---KSRNANVELLrLLIDAGADVYAVDDRFRSLLHHHL 195

                         90       100       110
                 ....*....|....*....|....*....|.
gi 125820436 131 --AEGLTDCTETLVRHGANTHTPDTSGHTPL 159
Cdd:PHA03095 196 qsFKPRARIVRELIRAGCDPAATDMLGNTPL 226
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 68-162 9.47e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.03  E-value: 9.47e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  68 ELLLAGGyADVNVSCPH-GRRPLHMMLTAQSQPNTHagliYLLEHGAHISVSTDEGLTPLHQAAAEGLTDCTETLVRHGA 146
Cdd:PHA02878 151 KLLLSYG-ADINMKDRHkGNTALHYATENKDQRLTE----LLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                         90
                 ....*....|....*.
gi 125820436 147 NTHTPDTSGHTPLDLA 162
Cdd:PHA02878 226 STDARDKCGNTPLHIS 241
Ank_5 pfam13857
Ankyrin repeats (many copies);
108-162 1.00e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 1.00e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 125820436  108 LLEHGAHISVSTD-EGLTPLHQAAAEGLTDCTETLVRHGANTHTPDTSGHTPLDLA 162
Cdd:pfam13857   1 LLEHGPIDLNRLDgEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 47-162 1.19e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.81  E-value: 1.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  47 TDKHGLSVLHIAALH--GHLDCMELLLAGGyADVNVSCPHGRRPLHMMLtaqSQPNTHAGLI-----------------Y 107
Cdd:PHA03100 102 PDNNGITPLLYAISKksNSYSIVEYLLDNG-ANVNIKNSDGENLLHLYL---ESNKIDLKILkllidkgvdinaknrvnY 177

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 125820436 108 LLEHGAHISVSTDEGLTPLHQAAAEGLTDCTETLVRHGANTHTPDTSGHTPLDLA 162
Cdd:PHA03100 178 LLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
Ank_5 pfam13857
Ankyrin repeats (many copies);
44-91 1.58e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 1.58e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 125820436   44 PLITDKHGLSVLHIAALHGHLDCMELLLAGGyADVNVSCPHGRRPLHM 91
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYG-VDLNLKDEEGLTALDL 55
PHA03095 PHA03095
ankyrin-like protein; Provisional
 59-175 1.71e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.40  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  59 ALHGHLD-------CMELLLAGGyADVNVSCPHGRRPLHMMLTAQSQPNTHagLIYLLEHGAHISVSTDEGLTPLHQAAA 131
Cdd:PHA03095 190 LLHHHLQsfkprarIVRELIRAG-CDPAATDMLGNTPLHSMATGSSCKRSL--VLPLLIAGISINARNRYGQTPLHYAAV 266

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 125820436 132 EGLTDCTETLVRHGANTHTPDTSGHTPLDLARIWGHRDTAR-FLK 175
Cdd:PHA03095 267 FNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRaALA 311
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 49-158 2.44e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.60  E-value: 2.44e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  49 KHGLSVLHIAALHGHLDCMELLLAGGyADVNVSCPHGRRPLHMMLTAQSQPNTHagliYLLEHGAHISVSTDEGLTPLHQ 128
Cdd:PHA02875 100 KDGMTPLHLATILKKLDIMKLLIARG-ADPDIPNTDKFSPLHLAVMMGDIKGIE----LLIDHKACLDIEDCCGCTPLII 174

                         90       100       110
                 ....*....|....*....|....*....|
gi 125820436 129 AAAEGLTDCTETLVRHGANthtPDTSGHTP 158
Cdd:PHA02875 175 AMAKGDIAICKMLLDSGAN---IDYFGKNG 201
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 69-155 4.12e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 4.12e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  69 LLLAGGyADVNVSCPHGRRPLHMMLTaqsqpNTHAGLI-YLLEHGAHISVSTDEGLTPLHQAAAEGLTDCTETLVRHGAN 147
Cdd:PTZ00322 100 ILLTGG-ADPNCRDYDGRTPLHIACA-----NGHVQVVrVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173


                 ....*...
gi 125820436 148 THTPDTSG 155
Cdd:PTZ00322 174 HFELGANA 181
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 50-159 5.32e-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: 43.85  E-value: 5.32e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  50 HGLSVLHIAALHGHLDCMELLLAGGYADVNVSCP----HGRRPLHMMLTAQSQPNTHAgliyLLEHGAhiSVSTDE---- 121
Cdd:cd22192   50 LGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdlyQGETALHIAVVNQNLNLVRE----LIARGA--DVVSPRatgt 123

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 125820436 122 ------------GLTPLHQAAAEGLTDCTETLVRHGANTHTPDTSGHTPL 159
Cdd:cd22192  124 ffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
Ank_5 pfam13857
Ankyrin repeats (many copies);
70-129 1.78e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 1.78e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436   70 LLAGGYADVNVSCPHGRRPLHMMLTAQSQPnthaGLIYLLEHGAHISVSTDEGLTPLHQA 129
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALE----IVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
122-174 1.99e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.41  E-value: 1.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 125820436  122 GLTPLHQAAAEGLTDCTETLVRHGANTHTPDTSGHTPLDLARIWGHRDTARFL 174
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 1-162 3.26e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.61  E-value: 3.26e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436    1 MSVLRKDNNEAVVGGSppesdMFHAAASGARD----WLSLTLKKARK----PLITDK------HGLSVLHIAALHGHLDC 66
Cdd:TIGR00870  69 TELLLNLSCRGAVGDT-----LLHAISLEYVDaveaILLHLLAAFRKsgplELANDQytseftPGITALHLAAHRQNYEI 143

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436   67 MELLLAGGyADVNVSCP--------------HGRRPLHMMlTAQSQPNTHAgliYLLEHGAHISVSTDEGLTPLHQAAAE 132
Cdd:TIGR00870 144 VKLLLERG-ASVPARACgdffvksqgvdsfyHGESPLNAA-ACLGSPSIVA---LLSEDPADILTADSLGNTLLHLLVME 218

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 125820436  133 GL---------TDCTETLVRHGANTHT-------PDTSGHTPLDLA 162
Cdd:TIGR00870 219 NEfkaeyeelsCQMYNFALSLLDKLRDskeleviLNHQGLTPLKLA 264
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 89-174 7.94e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 7.94e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  89 LHMM---LTAQSQPNTHAGLIYLLEHGAHISVSTDEGLTPLHQAAAEGLTDCTETLVRHGANTHTPDTSGHTPLDLARIW 165
Cdd:PTZ00322  79 AHMLtveLCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEEN 158


                 ....*....
gi 125820436 166 GHRDTARFL 174
Cdd:PTZ00322 159 GFREVVQLL 167
Ank_4 pfam13637
Ankyrin repeats (many copies);
51-142 1.28e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 1.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436   51 GLSVLHIAALHGHLDCMElllaggyadvnvscphgrrplhmmltaqsqpnthagliYLLEHGAHISVSTDEGLTPLHQAA 130
Cdd:pfam13637   1 ELTALHAAAASGHLELLR--------------------------------------LLLEKGADINAVDGNGETALHFAA 42

                          90
                  ....*....|..
gi 125820436  131 AEGLTDCTETLV 142
Cdd:pfam13637  43 SNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 44-150 1.31e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 39.62  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  44 PLITDKHGLSVLHIAALHG---HLDCMELLLAGgyADVNVSCPHGRRPLHMmltAQSQPNTHAGLiYLLEHGAHISVSTD 120
Cdd:PHA03095 215 PAATDMLGNTPLHSMATGSsckRSLVLPLLIAG--ISINARNRYGQTPLHY---AAVFNNPRACR-RLIALGADINAVSS 288

                         90       100       110
                 ....*....|....*....|....*....|
gi 125820436 121 EGLTPLHQAAAEGLTDCTETLVRHGANTHT 150
Cdd:PHA03095 289 DGNTPLSLMVRNNNGRAVRAALAKNPSAET 318
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 108-176 1.34e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.56  E-value: 1.34e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 125820436 108 LLEHGAHISVSTDEGLTPLHQAAAEGLTDCTETLVRHGANTHTPDTSGHTPLDLARIWGHRDTARFLKD 176
Cdd:PHA02874 143 LFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLID 211
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 50-80 1.52e-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: 1.52e-03
                           10        20        30
                   ....*....|....*....|....*....|.
gi 125820436    50 HGLSVLHIAALHGHLDCMELLLAGGyADVNV 80
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKG-ADINA 30
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 4-211 1.57e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 39.47  E-value: 1.57e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436   4 LRKDNNEAVVGGSPPESDMFHAAASGARDWLSLTLKKARKPLITDKHGLSVLHIAALHGHLDCMELLlaggYADVNVSCP 83
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIL----YHFASISDP 619

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  84 HGRRPLhmMLTAQSQPNTHAgLIYLLEHGAHISVSTDEGLTPLHQAAAEGLTDCTETLVRHGANTHTPDT-SGHTPLDLA 162
Cdd:PLN03192 620 HAAGDL--LCTAAKRNDLTA-MKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTdDDFSPTELR 696

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 125820436 163 RIWGHRDTARFLKDAMWRKDKEQQMKRSKHQhnlRQELLMMTKSRGKCV 211
Cdd:PLN03192 697 ELLQKRELGHSITIVDSVPADEPDLGRDGGS---RPGRLQGTSSDNQCR 742
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 55-170 2.12e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 38.88  E-value: 2.12e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  55 LHIAALHGHLDCMELLLAGGyADVNVSCPHGRRPLHMMLTAQSQPNTHAGLIY-LLEHGAHISVSTDEGLTPLHQAAAEG 133
Cdd:PHA03100  39 LYLAKEARNIDVVKILLDNG-ADINSSTKNNSTPLHYLSNIKYNLTDVKEIVKlLLEYGANVNAPDNNGITPLLYAISKK 117

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 125820436 134 LTDCT--ETLVRHGANTHTPDTSGHTPLDLARIWGHRDT 170
Cdd:PHA03100 118 SNSYSivEYLLDNGANVNIKNSDGENLLHLYLESNKIDL 156
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 50-80 2.19e-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: 2.19e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 125820436   50 HGLSVLHIAALHGHLDCMELLLAGGyADVNV 80
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENG-ADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 76-164 2.66e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.89  E-value: 2.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  76 ADVNVSCPHGRRPLHMMltAQSQPNTHaGLIYLLEHGAHISVSTDEGLTPLHQAAA-EGLTDCTETLVRHGANTHTPDTS 154
Cdd:PHA02876 298 ADVNAKNIKGETPLYLM--AKNGYDTE-NIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYC 374

                         90
                 ....*....|
gi 125820436 155 GHTPLDLARI 164
Cdd:PHA02876 375 DKTPIHYAAV 384
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 48-162 4.93e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 37.74  E-value: 4.93e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 125820436  48 DKHGLSVLHiAALHGHLDCMELLLAGGYAdVNVSCPHGRRPLHMmltAQSQPNTHAGLIYLLEHGAHISVSTDEGLTPLH 127
Cdd:PHA02876 238 NKNDLSLLK-AIRNEDLETSLLLYDAGFS-VNSIDDCKNTPLHH---ASQAPSLSRLVPKLLERGADVNAKNIKGETPLY 312

                         90       100       110
                 ....*....|....*....|....*....|....*.
gi 125820436 128 QAAAEGL-TDCTETLVRHGANTHTPDTSGHTPLDLA 162
Cdd:PHA02876 313 LMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQA 348
Ank_4 pfam13637
Ankyrin repeats (many copies);
22-71 5.04e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.17  E-value: 5.04e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 125820436   22 MFHAAASGARDWLSLTLKKARKPLITDKHGLSVLHIAALHGHLDCMELLL 71
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 50-80 7.19e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 33.42  E-value: 7.19e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 125820436   50 HGLSVLHIAALH-GHLDCMELLLAGGyADVNV 80
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKG-ADVNA 31
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH