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Conserved domains on  [gi|1034649204|ref|XP_016866002|]
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ankyrin repeat domain-containing protein 6 isoform X33 [Homo sapiens]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

Gene Ontology:  GO:0005515
PubMed:  17176038
SCOP:  4000366

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-177 9.96e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.86  E-value: 9.96e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVnARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  93 ALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKgsvsAGDTPSSEQAVARKEEAREEFLSASPEPR 172
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN----DGKTALDLAAENGNLEIVKLLLEAGADLN 246


                  ....*
gi 1034649204 173 AKDDR 177
Cdd:COG0666   247 AKDKD 251
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-177 9.96e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.86  E-value: 9.96e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVnARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  93 ALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKgsvsAGDTPSSEQAVARKEEAREEFLSASPEPR 172
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN----DGKTALDLAAENGNLEIVKLLLEAGADLN 246


                  ....*
gi 1034649204 173 AKDDR 177
Cdd:COG0666   247 AKDKD 251
Ank_2 pfam12796
Ankyrin repeats (3 copies);
46-138 5.53e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.56  E-value: 5.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  46 LHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIhEGCALDRQDkDGNTALHEASWHGFSQSAK 125
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1034649204 126 LLIKAGANVLAKN 138
Cdd:pfam12796  79 LLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 42-222 2.10e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.82  E-value: 2.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIH------------------------- 96
Cdd:PLN03192  558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfasisdphaagdllctaakrndlta 637

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  97 ------EGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVlakNKGSVSAGDTPSSEQAVARKEEA--REEFLSAS 168
Cdd:PLN03192  638 mkellkQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV---DKANTDDDFSPTELRELLQKRELghSITIVDSV 714

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034649204 169 PEPRAKDDRRRKSRPKVSAfsdpTPPADQQPGHQKNLHaHNHPKKRNRHRCSSP 222
Cdd:PLN03192  715 PADEPDLGRDGGSRPGRLQ----GTSSDNQCRPRVSIY-KGHPLLRNERCCNEA 763
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 41-70 3.31e-06

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: 43.73  E-value: 3.31e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034649204   41 HGRTPLHLAANKGHLPVVQILLKAGCDLDV 70
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 41-113 5.08e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 39.68  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  41 HGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEIIAALIHEGCALDRQDK 106
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADS 206


                  ....*..
gi 1034649204 107 DGNTALH 113
Cdd:TIGR00870 207 LGNTLLH 213
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 42-113 6.07e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 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.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 39.45  E-value: 6.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGD-------------QTALHRATVVGNTEIIAALI---HEGCALDRQD 105
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVENGADVHARACGRffqkkqgtcfyfgELPLSLAACTKQWDVVNYLLenpHQPASLQAQD 173


                  ....*...
gi 1034649204 106 KDGNTALH 113
Cdd:cd22197   174 SLGNTVLH 181
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-177 9.96e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.86  E-value: 9.96e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVnARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  93 ALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKgsvsAGDTPSSEQAVARKEEAREEFLSASPEPR 172
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN----DGKTALDLAAENGNLEIVKLLLEAGADLN 246


                  ....*
gi 1034649204 173 AKDDR 177
Cdd:COG0666   247 AKDKD 251
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-163 7.38e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.38  E-value: 7.38e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGADVnAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034649204  93 ALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKGSVSAGDTPSSEQAVARKEEAREE 163
Cdd:COG0666   204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-177 1.25e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.52  E-value: 1.25e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADInAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  93 ALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKGsvsaGDTPSSEQAVARKEEAREEFLSASPEPR 172
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND----GETPLHLAAENGHLEIVKLLLEAGADVN 213


                  ....*
gi 1034649204 173 AKDDR 177
Cdd:COG0666   214 AKDND 218
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-139 1.00e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 104.27  E-value: 1.00e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666   157 LHLAAANGNLEIVKLLLEAGADVnARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVK 236

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1034649204  93 ALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNK 139
Cdd:COG0666   237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
Ank_2 pfam12796
Ankyrin repeats (3 copies);
46-138 5.53e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.56  E-value: 5.53e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  46 LHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIhEGCALDRQDkDGNTALHEASWHGFSQSAK 125
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1034649204 126 LLIKAGANVLAKN 138
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-148 5.59e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 87.70  E-value: 5.59e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204   1 MSQQDAVAALSERLLVAAYKGQTENVVQLINKGARVAVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALH 80
Cdd:COG0666    13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034649204  81 RATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKGsvsaGDTP 148
Cdd:COG0666    93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND----GNTP 156
Ank_2 pfam12796
Ankyrin repeats (3 copies);
14-105 1.12e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 1.12e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKaGCDLDVQDDGdQTALHRATVVGNTEIIA 92
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAnLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNG-RTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1034649204  93 ALIHEGCALDRQD 105
Cdd:pfam12796  79 LLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 42-222 2.10e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.82  E-value: 2.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIH------------------------- 96
Cdd:PLN03192  558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfasisdphaagdllctaakrndlta 637

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  97 ------EGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVlakNKGSVSAGDTPSSEQAVARKEEA--REEFLSAS 168
Cdd:PLN03192  638 mkellkQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV---DKANTDDDFSPTELRELLQKRELghSITIVDSV 714

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034649204 169 PEPRAKDDRRRKSRPKVSAfsdpTPPADQQPGHQKNLHaHNHPKKRNRHRCSSP 222
Cdd:PLN03192  715 PADEPDLGRDGGSRPGRLQ----GTSSDNQCRPRVSIY-KGHPLLRNERCCNEA 763
PHA03095 PHA03095
ankyrin-like protein; Provisional
 24-179 3.25e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.82  E-value: 3.25e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  24 ENVVQLINKGARVAVTK-HGRTPLHLAANKGHLP---VVQILLKAGCDLDVQDDGDQTALHRATVVGNTE-IIAALIHEG 98
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGeYGKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  99 CALDRQDKDGNTALHeASWHGFSQSAK---LLIKAGANVLAKNKGSVSAGDtpsseqAVARKEEAREE----FLSASPEP 171
Cdd:PHA03095  108 ADVNAKDKVGRTPLH-VYLSGFNINPKvirLLLRKGADVNALDLYGMTPLA------VLLKSRNANVEllrlLIDAGADV 180


                  ....*...
gi 1034649204 172 RAKDDRRR 179
Cdd:PHA03095  181 YAVDDRFR 188
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
14-112 4.51e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 63.82  E-value: 4.51e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  14 LLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGADVnAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269

                          90       100
                  ....*....|....*....|
gi 1034649204  93 ALIHEGCALDRQDKDGNTAL 112
Cdd:COG0666   270 LLLLALLLLAAALLDLLTLL 289
Ank_4 pfam13637
Ankyrin repeats (many copies);
42-95 4.86e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.05  E-value: 4.86e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034649204  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALI 95
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 22-143 1.33e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.44  E-value: 1.33e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  22 QTENVVQLINKGARVAV-TKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCA 100
Cdd:PHA02874  103 EKDMIKTILDCGIDVNIkDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAY 182

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1034649204 101 LDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKGSVS 143
Cdd:PHA02874  183 ANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFT 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-177 6.71e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 60.35  E-value: 6.71e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  24 ENVVQLINKGARVAVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDR 103
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034649204 104 QDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKGsvsaGDTPSSEQAVARKEEAREEFLSASPEPRAKDDR 177
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD----GETPLHLAAYNGNLEIVKLLLEAGADVNAQDND 152
PHA03095 PHA03095
ankyrin-like protein; Provisional
 29-196 9.10e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.19  E-value: 9.10e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  29 LINKGARV-AVTKHGRTPLH-LAANKG-HLPVVQILLKAGCDLDVQDDGDQTALH------RAtvvgNTEIIAALIHEGC 99
Cdd:PHA03095  138 LLRKGADVnALDLYGMTPLAvLLKSRNaNVELLRLLIDAGADVYAVDDRFRSLLHhhlqsfKP----RARIVRELIRAGC 213

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204 100 ALDRQDKDGNTALHEASWHGFSQSAKL--LIKAGANVLAKNKgsvsAGDTPSSEQAVARKEEAREEFLS--ASPEPRAKD 175
Cdd:PHA03095  214 DPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNR----YGQTPLHYAAVFNNPRACRRLIAlgADINAVSSD 289

                         170       180
                  ....*....|....*....|....*...
gi 1034649204 176 DR-------RRKSRPKVSAFSDPTPPAD 196
Cdd:PHA03095  290 GNtplslmvRNNNGRAVRAALAKNPSAE 317
Ank_5 pfam13857
Ankyrin repeats (many copies);
40-82 2.12e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.50  E-value: 2.12e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1034649204  40 KHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRA 82
Cdd:pfam13857  14 GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
77-128 4.50e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 4.50e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034649204  77 TALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLI 128
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 17-134 9.90e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.69  E-value: 9.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  17 AAYKGQTENVVQLI--NKGARVAVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAAL 94
Cdd:PHA02875   75 AVEEGDVKAVEELLdlGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034649204  95 IHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANV 134
Cdd:PHA02875  155 IDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANI 194
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 22-138 1.09e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.58  E-value: 1.09e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  22 QTENVVQLINKGARV-AVTKH-GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGC 99
Cdd:PHA02878  146 EAEITKLLLSYGADInMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1034649204 100 ALDRQDKDGNTALHEASWHGFSQSA-KLLIKAGANVLAKN 138
Cdd:PHA02878  226 STDARDKCGNTPLHISVGYCKDYDIlKLLLEHGVDVNAKS 265
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 15-139 1.90e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.38  E-value: 1.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  15 LVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAAN-KGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:PHA02876  313 LMAKNGYDTENIRTLIMLGADVnAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIIN 392

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1034649204  93 ALIHEGCALDRQDKDGNTALHEAsWHGFS--QSAKLLIKAGANVLAKNK 139
Cdd:PHA02876  393 TLLDYGADIEALSQKIGTALHFA-LCGTNpyMSVKTLIDRGANVNSKNK 440
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 29-169 2.31e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.60  E-value: 2.31e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  29 LINKGARV-AVTKHGRTPLHLAANK--GHLPVVQILLKAGCDLDVQDDGDQTALHRATVVG--NTEIIAALIHEG----- 98
Cdd:PHA03100   92 LLEYGANVnAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNkiDLKILKLLIDKGvdina 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  99 -----------CALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKgsvsAGDTPSSEQAVARKEEAREEFLSA 167
Cdd:PHA03100  172 knrvnyllsygVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNK----YGDTPLHIAILNNNKEIFKLLLNN 247


                  ..
gi 1034649204 168 SP 169
Cdd:PHA03100  248 GP 249
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 41-73 2.59e-08

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: 49.60  E-value: 2.59e-08
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1034649204  41 HGRTPLHLAANK-GHLPVVQILLKAGCDLDVQDD 73
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 41-70 3.31e-06

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: 43.73  E-value: 3.31e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1034649204   41 HGRTPLHLAANKGHLPVVQILLKAGCDLDV 70
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 57-148 3.64e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.49  E-value: 3.64e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  57 VVQILLKAGCDLDVQD-DGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVL 135
Cdd:PHA02878  149 ITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD 228

                          90
                  ....*....|...
gi 1034649204 136 AKNKgsvsAGDTP 148
Cdd:PHA02878  229 ARDK----CGNTP 237
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 41-70 5.37e-06

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: 43.01  E-value: 5.37e-06
                          10        20        30
                  ....*....|....*....|....*....|
gi 1034649204  41 HGRTPLHLAANKGHLPVVQILLKAGCDLDV 70
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 14-134 8.04e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.42  E-value: 8.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  14 LLVAAYKGQTENVVQLINKGARVAVTK-HGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIA 92
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDdNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1034649204  93 ALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANV 134
Cdd:PHA02874  208 LLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIELLINNASIND 249
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 107-139 1.43e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.89  E-value: 1.43e-05
                          10        20        30
                  ....*....|....*....|....*....|....
gi 1034649204 107 DGNTALHEASWH-GFSQSAKLLIKAGANVLAKNK 139
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 10-111 1.55e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 1.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  10 LSERLLVAAYKGQTENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNT 88
Cdd:PTZ00322   82 LTVELCQLAASGDAVGARILLTGGADPnCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161

                          90       100
                  ....*....|....*....|...
gi 1034649204  89 EIIAALIheGCALDRQDKDGNTA 111
Cdd:PTZ00322  162 EVVQLLS--RHSQCHFELGANAK 182
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 49-115 2.06e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.56  E-value: 2.06e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1034649204  49 AANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEA 115
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNA 598
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 40-139 4.61e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.81  E-value: 4.61e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  40 KHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVG-----NTEIIAALIHEGCALDRQDKDGNTALHE 114
Cdd:PHA03100   33 KKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKynltdVKEIVKLLLEYGANVNAPDNNGITPLLY 112

                          90       100
                  ....*....|....*....|....*..
gi 1034649204 115 ASWHGFSQSA--KLLIKAGANVLAKNK 139
Cdd:PHA03100  113 AISKKSNSYSivEYLLDNGANVNIKNS 139
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 29-113 8.00e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.04  E-value: 8.00e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  29 LINKGARV-AVTKH-GRTPLH--LAANKGHLP-VVQILLKAGCDLDVQDDGDQTALHR--ATVVGNTEIIAALIHEGCAL 101
Cdd:PHA02859   72 LIENGADVnFKTRDnNLSALHhyLSFNKNVEPeILKILIDSGSSITEEDEDGKNLLHMymCNFNVRINVIKLLIDSGVSF 151

                          90
                  ....*....|..
gi 1034649204 102 DRQDKDGNTALH 113
Cdd:PHA02859  152 LNKDFDNNNILY 163
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 47-129 1.07e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.27  E-value: 1.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  47 HLAANkGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKL 126
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ...
gi 1034649204 127 LIK 129
Cdd:PTZ00322  167 LSR 169
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 24-138 1.17e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 1.17e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  24 ENVVQLINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEI-IAALIHEGCAL 101
Cdd:PHA02876  356 DIVITLLELGANVnARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANV 435

                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1034649204 102 DRQDKDGNTALHEASWHGFS-QSAKLLIKAGANVLAKN 138
Cdd:PHA02876  436 NSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAIN 473
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 57-148 1.93e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.18  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  57 VVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLA 136
Cdd:PHA02874  106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185

                          90
                  ....*....|..
gi 1034649204 137 KNkgsvSAGDTP 148
Cdd:PHA02874  186 KD----NNGESP 193
PHA02791 PHA02791
ankyrin-like protein; Provisional
 41-129 4.79e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 42.34  E-value: 4.79e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  41 HGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDgdQTALHRATVVGNTEIIAALIHEGCALDRQDKDGNTALHEASWHGF 120
Cdd:PHA02791   29 HGHSALYYAIADNNVRLVCTLLNAGALKNLLEN--EFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGN 106


                  ....*....
gi 1034649204 121 SQSAKLLIK 129
Cdd:PHA02791  107 MQTVKLFVK 115
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 29-148 9.10e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.97  E-value: 9.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  29 LINKGARV-AVTKHGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHE---------- 97
Cdd:PHA02876  164 LLEGGADVnAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNrsninkndls 243

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034649204  98 -------------------GCALDRQDKDGNTALHEASWH-GFSQSAKLLIKAGANVLAKNkgsvSAGDTP 148
Cdd:PHA02876  244 llkairnedletslllydaGFSVNSIDDCKNTPLHHASQApSLSRLVPKLLERGADVNAKN----IKGETP 310
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 29-133 1.00e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.90  E-value: 1.00e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  29 LINKGARVAVTKHGR-TPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGCALDRQDKD 107
Cdd:PHA02875  121 LIARGADPDIPNTDKfSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKN 200

                          90       100
                  ....*....|....*....|....*..
gi 1034649204 108 GN-TALHEASWHGFSQSAKLLIKAGAN 133
Cdd:PHA02875  201 GCvAALCYAIENNKIDIVRLFIKRGAD 227
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 107-134 3.20e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 3.20e-03
                           10        20
                   ....*....|....*....|....*...
gi 1034649204  107 DGNTALHEASWHGFSQSAKLLIKAGANV 134
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 41-113 5.08e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 39.68  E-value: 5.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  41 HGRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGD--------------QTALHRATVVGNTEIIAALIHEGCALDRQDK 106
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADS 206


                  ....*..
gi 1034649204 107 DGNTALH 113
Cdd:TIGR00870 207 LGNTLLH 213
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 42-113 6.07e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 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 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.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 39.45  E-value: 6.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGD-------------QTALHRATVVGNTEIIAALI---HEGCALDRQD 105
Cdd:cd22197    94 GHSALHIAIEKRSLQCVKLLVENGADVHARACGRffqkkqgtcfyfgELPLSLAACTKQWDVVNYLLenpHQPASLQAQD 173


                  ....*...
gi 1034649204 106 KDGNTALH 113
Cdd:cd22197   174 SLGNTVLH 181
Ank_5 pfam13857
Ankyrin repeats (many copies);
96-148 7.02e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 7.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034649204  96 HEGCALDRQDKDGNTALHEASWHGFSQSAKLLIKAGANVLAKNKGsvsaGDTP 148
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE----GLTA 52
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 42-133 7.39e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 38.82  E-value: 7.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034649204  42 GRTPLHLAANKGHLPVVQILLKAGCDLDVQDDGDQTALHRATVVGNTEIIAALIHEGC-ALDRQDKDGNTALHEASWHGF 120
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKfADDVFYKDGMTPLHLATILKK 114

                          90
                  ....*....|...
gi 1034649204 121 SQSAKLLIKAGAN 133
Cdd:PHA02875  115 LDIMKLLIARGAD 127
 
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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