NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|55741426|ref|NP_110494|]
View 

NF-kappa-B inhibitor beta [Rattus norvegicus]

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];
56-310 3.86e-26

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 105.81  E-value: 3.86e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426  56 EDGDTALHLAVIHQHEPFLDFLLgfsAGTEYLDLQNDLGQTALHLAAILGEASTVEKLYAAGAGVLVTERGGHTALHLAC 135
Cdd:COG0666  52 ALGALLLLAAALAGDLLVALLLL---AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAA 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426 136 RVRAHTCAYVLLQprpshprdasdtyltqsqdhtpdtSHAPVatdpqpnpgneeelrdedwrlqlEAENYDGHTPLHVAV 215
Cdd:COG0666 129 YNGNLEIVKLLLE------------------------AGADV-----------------------NAQDNDGNTPLHLAA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426 216 IHKDAEMVQLLRDAGADLNKPEPTcGRTPLHLAVEGQAAGVLALLLKAGADPTARMYGGRTPLGSALLRPNPVLARLLRA 295
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                       250
                ....*....|....*
gi 55741426 296 HGAPEPEDEDDKLSP 310
Cdd:COG0666 241 AGADLNAKDKDGLTA 255
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-310 3.86e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 105.81  E-value: 3.86e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426  56 EDGDTALHLAVIHQHEPFLDFLLgfsAGTEYLDLQNDLGQTALHLAAILGEASTVEKLYAAGAGVLVTERGGHTALHLAC 135
Cdd:COG0666  52 ALGALLLLAAALAGDLLVALLLL---AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAA 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426 136 RVRAHTCAYVLLQprpshprdasdtyltqsqdhtpdtSHAPVatdpqpnpgneeelrdedwrlqlEAENYDGHTPLHVAV 215
Cdd:COG0666 129 YNGNLEIVKLLLE------------------------AGADV-----------------------NAQDNDGNTPLHLAA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426 216 IHKDAEMVQLLRDAGADLNKPEPTcGRTPLHLAVEGQAAGVLALLLKAGADPTARMYGGRTPLGSALLRPNPVLARLLRA 295
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                       250
                ....*....|....*
gi 55741426 296 HGAPEPEDEDDKLSP 310
Cdd:COG0666 241 AGADLNAKDKDGLTA 255
PHA03095 PHA03095
ankyrin-like protein; Provisional
 203-298 5.04e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.83  E-value: 5.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426  203 ENYDGH---TPLHVAV---IHKDAEMVQLLRDAGADLNKPEpTCGRTPLHLAVE-GQAAGVLALLLKAGADPTARMYGGR 275
Cdd:PHA03095  40 VNFRGEygkTPLHLYLhysSEKVKDIVRLLLEAGADVNAPE-RCGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGR 118

                         90       100
                 ....*....|....*....|....*
gi 55741426  276 TPLGSAL--LRPNPVLARLLRAHGA 298
Cdd:PHA03095 119 TPLHVYLsgFNINPKVIRLLLRKGA 143
Ank_2 pfam12796
Ankyrin repeats (3 copies);
62-148 2.38e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 2.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426    62 LHLAVIHQHEPFLDFLLGFSAGteyLDLQNDLGQTALHLAAILGEASTVEKLYAAGAGVLVTErgGHTALHLACRVRAHT 141
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD---ANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLE 75


                  ....*..
gi 55741426   142 CAYVLLQ 148
Cdd:pfam12796  76 IVKLLLE 82
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 205-290 1.34e-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: 56.17  E-value: 1.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426 205 YDGHTPLHVAVIHKDAEMVQLLRDAGADLNKPEPT-------------CGRTPLHLAVEGQAAGVLALLLKAGADPTARM 271
Cdd:cd22192  87 YQGETALHIAVVNQNLNLVRELIARGADVVSPRATgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166

                        90
                ....*....|....*....
gi 55741426 272 YGGRTPLGSALLRPNPVLA 290
Cdd:cd22192 167 SLGNTVLHILVLQPNKTFA 185
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 206-235 2.16e-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: 2.16e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 55741426    206 DGHTPLHVAVIHKDAEMVQLLRDAGADLNK 235
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 203-270 4.37e-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: 45.46  E-value: 4.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426   203 ENYDGHTPLHVAVIHKDAEMVQLLRDAGADLN----------KPEPTC---GRTPLHLAVEGQAAGVLALLLKAGADPTA 269
Cdd:TIGR00870 124 EFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDSfyhGESPLNAAACLGSPSIVALLSEDPADILT 203


                  .
gi 55741426   270 R 270
Cdd:TIGR00870 204 A 204
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-310 3.86e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 105.81  E-value: 3.86e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426  56 EDGDTALHLAVIHQHEPFLDFLLgfsAGTEYLDLQNDLGQTALHLAAILGEASTVEKLYAAGAGVLVTERGGHTALHLAC 135
Cdd:COG0666  52 ALGALLLLAAALAGDLLVALLLL---AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAA 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426 136 RVRAHTCAYVLLQprpshprdasdtyltqsqdhtpdtSHAPVatdpqpnpgneeelrdedwrlqlEAENYDGHTPLHVAV 215
Cdd:COG0666 129 YNGNLEIVKLLLE------------------------AGADV-----------------------NAQDNDGNTPLHLAA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426 216 IHKDAEMVQLLRDAGADLNKPEPTcGRTPLHLAVEGQAAGVLALLLKAGADPTARMYGGRTPLGSALLRPNPVLARLLRA 295
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                       250
                ....*....|....*
gi 55741426 296 HGAPEPEDEDDKLSP 310
Cdd:COG0666 241 AGADLNAKDKDGLTA 255
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-308 3.04e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.72  E-value: 3.04e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426  53 YVTEDGDTALHLAVIHQHEPFLDFLLgfSAGTEyLDLQNDLGQTALHLAAILGEASTVEKLYAAGAGVLVTERGGHTALH 132
Cdd:COG0666  82 AKDDGGNTLLHAAARNGDLEIVKLLL--EAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLH 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426 133 LACRVRAHTCAYVLLqprpshprdasdtyltqsqDHTPDtshapvatdpqpnpgneeelrdedwrlqLEAENYDGHTPLH 212
Cdd:COG0666 159 LAAANGNLEIVKLLL-------------------EAGAD----------------------------VNARDNDGETPLH 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426 213 VAVIHKDAEMVQLLRDAGADLNKPEPTcGRTPLHLAVEGQAAGVLALLLKAGADPTARMYGGRTPLGSALLRPNPVLARL 292
Cdd:COG0666 192 LAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                       250
                ....*....|....*.
gi 55741426 293 LRAHGAPEPEDEDDKL 308
Cdd:COG0666 271 LLLALLLLAAALLDLL 286
PHA03095 PHA03095
ankyrin-like protein; Provisional
 203-298 5.04e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.83  E-value: 5.04e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426  203 ENYDGH---TPLHVAV---IHKDAEMVQLLRDAGADLNKPEpTCGRTPLHLAVE-GQAAGVLALLLKAGADPTARMYGGR 275
Cdd:PHA03095  40 VNFRGEygkTPLHLYLhysSEKVKDIVRLLLEAGADVNAPE-RCGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGR 118

                         90       100
                 ....*....|....*....|....*
gi 55741426  276 TPLGSAL--LRPNPVLARLLRAHGA 298
Cdd:PHA03095 119 TPLHVYLsgFNINPKVIRLLLRKGA 143
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-278 2.22e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 72.68  E-value: 2.22e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426  56 EDGDTALHLAVIHQHEPFLDFLLgfSAGTEyLDLQNDLGQTALHLAAILGEASTVEKLYAAGAGVLVTERGGHTALHLAC 135
Cdd:COG0666 118 KDGETPLHLAAYNGNLEIVKLLL--EAGAD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426 136 RVRAHTCAYVLLqprpshprdasdtyltqsqDHTPDtshapvatdpqpnpgneeelrdedwrlqLEAENYDGHTPLHVAV 215
Cdd:COG0666 195 ENGHLEIVKLLL-------------------EAGAD----------------------------VNAKDNDGKTALDLAA 227

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55741426 216 IHKDAEMVQLLRDAGADLNKPEPTcGRTPLHLAVEGQAAGVLALLLKAGADPTARMYGGRTPL 278
Cdd:COG0666 228 ENGNLEIVKLLLEAGADLNAKDKD-GLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 58-302 5.80e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.75  E-value: 5.80e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426   58 GDTALHLAVIHQH-EPFLDFLLGFSAGTEYldlQNDLGQTALH--LAAILGEASTVEKLYAAGAGVLVTERGGHTALHLA 134
Cdd:PHA03095  83 GFTPLHLYLYNATtLDVIKLLIKAGADVNA---KDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVL 159

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426  135 CRVRAHTCAYV-LLQPRPSHPRDASDTYLTQSQDHtpdtshapvATDPQPNPGNEEELRDEDWRLQleAENYDGHTPLHV 213
Cdd:PHA03095 160 LKSRNANVELLrLLIDAGADVYAVDDRFRSLLHHH---------LQSFKPRARIVRELIRAGCDPA--ATDMLGNTPLHS 228

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426  214 AVIH---KDAEMVQLLrDAGADLNKPEPTcGRTPLHLAVEGQAAGVLALLLKAGADPTARMYGGRTPLGSALLRPNpvlA 290
Cdd:PHA03095 229 MATGsscKRSLVLPLL-IAGISINARNRY-GQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNN---G 303

                        250
                 ....*....|....
gi 55741426  291 RLLRA--HGAPEPE 302
Cdd:PHA03095 304 RAVRAalAKNPSAE 317
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
184-298 7.23e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 62.28  E-value: 7.23e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426 184 NPGNEEELRDEDWRLQLEAENYDGHTPLHVAVIHKDAEMVQLLRDAGADLNKPEPTcGRTPLHLAVEGQAAGVLALLLKA 263
Cdd:COG0666  31 LLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG-GNTLLHAAARNGDLEIVKLLLEA 109

                        90       100       110
                ....*....|....*....|....*....|....*
gi 55741426 264 GADPTARMYGGRTPLGSALLRPNPVLARLLRAHGA 298
Cdd:COG0666 110 GADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGA 144
Ank_2 pfam12796
Ankyrin repeats (3 copies);
62-148 2.38e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 2.38e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426    62 LHLAVIHQHEPFLDFLLGFSAGteyLDLQNDLGQTALHLAAILGEASTVEKLYAAGAGVLVTErgGHTALHLACRVRAHT 141
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD---ANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLE 75


                  ....*..
gi 55741426   142 CAYVLLQ 148
Cdd:pfam12796  76 IVKLLLE 82
Ank_2 pfam12796
Ankyrin repeats (3 copies);
211-298 1.72e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.35  E-value: 1.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426   211 LHVAVIHKDAEMVQLLRDAGADLNKPEPtCGRTPLHLAVEGQAAGVLALLLKaGADPTARMYgGRTPLGSALLRPNPVLA 290
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIV 77


                  ....*...
gi 55741426   291 RLLRAHGA 298
Cdd:pfam12796  78 KLLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
206-270 2.05e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.97  E-value: 2.05e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 55741426   206 DGHTPLHVAVIHKDAEMVQLLRDaGADLNkpEPTCGRTPLHLAVEGQAAGVLALLLKAGADPTAR 270
Cdd:pfam12796  29 NGRTALHLAAKNGHLEIVKLLLE-HADVN--LKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
98-234 2.13e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.97  E-value: 2.13e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426    98 LHLAAILGEASTVEKLYAAGAGVLVTERGGHTALHLACRVRAHTCAYVLLqprpshprdasdtyltqsqdhtpdtshapv 177
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL------------------------------ 50

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 55741426   178 atdpqpnpgNEEELRDEDwrlqleaenyDGHTPLHVAVIHKDAEMVQLLRDAGADLN 234
Cdd:pfam12796  51 ---------EHADVNLKD----------NGRTALHYAARSGHLEIVKLLLEKGADIN 88
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 204-298 1.07e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.21  E-value: 1.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426  204 NYDGHTPLHVAV--IHKDAEMVQLLRDAGADLN----------KPEPT-----CGRTPLHLAVEGQAAGVLALLLKAGAD 266
Cdd:PHA03100 138 NSDGENLLHLYLesNKIDLKILKLLIDKGVDINaknrvnyllsYGVPInikdvYGFTPLHYAVYNNNPEFVKYLLDLGAN 217

                         90       100       110
                 ....*....|....*....|....*....|..
gi 55741426  267 PTARMYGGRTPLGSALLRPNPVLARLLRAHGA 298
Cdd:PHA03100 218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 205-290 1.34e-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: 56.17  E-value: 1.34e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426 205 YDGHTPLHVAVIHKDAEMVQLLRDAGADLNKPEPT-------------CGRTPLHLAVEGQAAGVLALLLKAGADPTARM 271
Cdd:cd22192  87 YQGETALHIAVVNQNLNLVRELIARGADVVSPRATgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166

                        90
                ....*....|....*....
gi 55741426 272 YGGRTPLGSALLRPNPVLA 290
Cdd:cd22192 167 SLGNTVLHILVLQPNKTFA 185
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 78-284 1.51e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.04  E-value: 1.51e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426   78 LGFSAGTEYLDLQNDLGQTALHLAAILGEASTVEKLYAAGAGVLVTERGGHTALHLACRVRAHTCAYVLLQPRPShpRDA 157
Cdd:PHA02878 152 LLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS--TDA 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426  158 SDTYltqsqdhtpdtshapvatdpqpnpgneeelrdedwrlqleaenydGHTPLHVAVIH-KDAEMVQLLRDAGADLNKP 236
Cdd:PHA02878 230 RDKC---------------------------------------------GNTPLHISVGYcKDYDILKLLLEHGVDVNAK 264

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 55741426  237 EPTCGRTPLHLAVEGQAagVLALLLKAGADPTARMYGGRTPLGSALLR 284
Cdd:PHA02878 265 SYILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 204-298 7.21e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.84  E-value: 7.21e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426  204 NYDGHTPLHVAVIHKDAEMVQLLRDAGADLNKpEPTCGRTPLHLAVEGQAAGVLALLLKAGADPTarmYGGRTP----LG 279
Cdd:PHA02875 132 NTDKFSPLHLAVMMGDIKGIELLIDHKACLDI-EDCCGCTPLIIAMAKGDIAICKMLLDSGANID---YFGKNGcvaaLC 207

                         90
                 ....*....|....*....
gi 55741426  280 SALLRPNPVLARLLRAHGA 298
Cdd:PHA02875 208 YAIENNKIDIVRLFIKRGA 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
52-118 8.27e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.34  E-value: 8.27e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 55741426    52 GYVTEDGDTALHLAVIHQHEPFLDFLLgfsagtEYLDLQN-DLGQTALHLAAILGEASTVEKLYAAGA 118
Cdd:pfam12796  24 NLQDKNGRTALHLAAKNGHLEIVKLLL------EHADVNLkDNGRTALHYAARSGHLEIVKLLLEKGA 85
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 203-310 2.16e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.22  E-value: 2.16e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426  203 ENYDGHTPLHVAVIHKDAEMVQLLRDAGA--DLNKPEPtcgRTPLHLAVEGQAAGVLALLLKAGADPTARMY-GGRTPLG 279
Cdd:PHA02875  31 EIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDI---ESELHDAVEEGDVKAVEELLDLGKFADDVFYkDGMTPLH 107

                         90       100       110
                 ....*....|....*....|....*....|.
gi 55741426  280 SALLRPNPVLARLLRAHGAPEPEDEDDKLSP 310
Cdd:PHA02875 108 LATILKKLDIMKLLIARGADPDIPNTDKFSP 138
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 206-235 2.16e-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: 2.16e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 55741426    206 DGHTPLHVAVIHKDAEMVQLLRDAGADLNK 235
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 207-298 2.76e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 49.24  E-value: 2.76e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426 207 GHTPLHVAVIHKDAEMVQLLRDAGADL-NKP---EPTCGRTPLHLAVEGQAAGVLALLLKAGAD--------------PT 268
Cdd:cd22192  51 GETALHVAALYDNLEAAVVLMEAAPELvNEPmtsDLYQGETALHIAVVNQNLNLVRELIARGADvvspratgtffrpgPK 130

                        90       100       110
                ....*....|....*....|....*....|
gi 55741426 269 ARMYGGRTPLGSALLRPNPVLARLLRAHGA 298
Cdd:cd22192 131 NLIYYGEHPLSFAACVGNEEIVRLLIEHGA 160
Ank_4 pfam13637
Ankyrin repeats (many copies);
207-261 3.09e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 3.09e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 55741426   207 GHTPLHVAVIHKDAEMVQLLRDAGADLNKPePTCGRTPLHLAVEGQAAGVLALLL 261
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAV-DGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 204-298 3.25e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.45  E-value: 3.25e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426  204 NYDG-HTPLHVAVIHKDAEMVQLLRDAGADLNKPEPTCGRTPLHLAVEGQAAGVLALLLKAGADPTARMYGGRTPLGSAL 282
Cdd:PHA02875  64 KYPDiESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAV 143

                         90
                 ....*....|....*.
gi 55741426  283 LRPNPVLARLLRAHGA 298
Cdd:PHA02875 144 MMGDIKGIELLIDHKA 159
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 207-298 6.63e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.57  E-value: 6.63e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426  207 GHTPLHVAVIHKDAEMVQLLRDAGADLNKPEpTCGRTPLHLAVEGQAAGVLALLLKAGADPTARMYGGRTPLGSALLR-P 285
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPD-KTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcK 246

                         90
                 ....*....|...
gi 55741426  286 NPVLARLLRAHGA 298
Cdd:PHA02878 247 DYDILKLLLEHGV 259
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 84-297 1.60e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.50  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426   84 TEYLDLQNDLGQTALHLAAILGEASTVEKLYAAGAGVLVTERGGHTALHLACRVRAHTCAYVLLqprpshprdasdtylt 163
Cdd:PHA02874  25 GNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI---------------- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426  164 qsqDHTPDTSHAPVatdpqPNPGNEEELRDEDWRLQLEAENYDGHTPLHVAVIHKDAEMVQLLRDAGADLNKpEPTCGRT 243
Cdd:PHA02874  89 ---DNGVDTSILPI-----PCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNI-EDDNGCY 159

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....
gi 55741426  244 PLHLAVEGQAAGVLALLLKAGADPTARMYGGRTPLGSALLRPNPVLARLLRAHG 297
Cdd:PHA02874 160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHG 213
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 57-266 2.11e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.14  E-value: 2.11e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426   57 DGDTALHLAVIHQHEPFLDFLLGFSAgteYLDLQNDLGQTALHLAAILGEASTVEKLYAAGAGVL-VTERGGHTALHLAC 135
Cdd:PHA02875  34 DGISPIKLAMKFRDSEAIKLLMKHGA---IPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLAT 110

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426  136 RVRAHTCAYVLLQpRPSHPrDASDTyltqsqDHTPDTSHAPVATDPQpnpGNEEELrdeDWRLQLEAENYDGHTPLHVAV 215
Cdd:PHA02875 111 ILKKLDIMKLLIA-RGADP-DIPNT------DKFSPLHLAVMMGDIK---GIELLI---DHKACLDIEDCCGCTPLIIAM 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 55741426  216 IHKDAEMVQLLRDAGADLNKPEPTCGRTPLHLAVEGQAAGVLALLLKAGAD 266
Cdd:PHA02875 177 AKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 203-270 4.37e-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: 45.46  E-value: 4.37e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426   203 ENYDGHTPLHVAVIHKDAEMVQLLRDAGADLN----------KPEPTC---GRTPLHLAVEGQAAGVLALLLKAGADPTA 269
Cdd:TIGR00870 124 EFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDSfyhGESPLNAAACLGSPSIVALLSEDPADILT 203


                  .
gi 55741426   270 R 270
Cdd:TIGR00870 204 A 204
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 195-293 5.03e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.95  E-value: 5.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426  195 DWRLQLEAENYDGHTPLHVAVIHKDAEMVQLLRDAGADLNKPEPTcGRTPLHLAVEGQAAGVLALLLKAGADPTARMYGG 274
Cdd:PHA02874 145 EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN-GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNG 223

                         90
                 ....*....|....*....
gi 55741426  275 RTPLGSALLRPNPVLARLL 293
Cdd:PHA02874 224 FTPLHNAIIHNRSAIELLI 242
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 219-294 5.55e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.87  E-value: 5.55e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 55741426  219 DAEMVQLLRDAGADLNKPEPTCGRTPLHLAVEGQAAGVLALLLKAGADPTARMYGGRTPLGSALL-RPNPVLARLLR 294
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKhYNKPIVHILLE 222
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 167-286 7.27e-05

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: 44.49  E-value: 7.27e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426 167 DHTPDTSHAPVATDPQPNPGNEEELRDEdwrlQLEAENYDGHTPLHVAVIHKDAEMVQLLRDAGADLN---------KPE 237
Cdd:cd21882  37 LNDGVNEAIMLLLEAAPDSGNPKELVNA----PCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSaratgrffrKSP 112

                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*
gi 55741426 238 PTC---GRTPLHLAVEGQAAGVLALLLKAGADP---TARMYGGRTPLGSALLRPN 286
Cdd:cd21882 113 GNLfyfGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLGNTVLHALVLQAD 167
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 200-298 7.73e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.67  E-value: 7.73e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426  200 LEAENYDGHTPLHVAVIHK-DAEMVQLLRDAGADLNKPEpTCGRTPLHLAVE-GQAAGVLALLLKAGADPTARMYGGRTP 277
Cdd:PHA02876 300 VNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAAD-RLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTP 378

                         90       100
                 ....*....|....*....|.
gi 55741426  278 LGSALLRPNPVLARLLRAHGA 298
Cdd:PHA02876 379 IHYAAVRNNVVIINTLLDYGA 399
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 73-235 8.52e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 44.47  E-value: 8.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426   73 FLDFLLgfSAGTEyLDLQNDLGQTALHLAAILGEASTVEKLYAAGAGVLVTERGGHTALHLACRVRAHTCAYVLLQ-PRP 151
Cdd:PLN03192 540 LLEELL--KAKLD-PDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfASI 616

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426  152 SHPRDASDTYLTQSQdhtpdtshapvatdpQPNPGNEEELRDEDwrLQLEAENYDGHTPLHVAVIHKDAEMVQLLRDAGA 231
Cdd:PLN03192 617 SDPHAAGDLLCTAAK---------------RNDLTAMKELLKQG--LNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGA 679


                 ....
gi 55741426  232 DLNK 235
Cdd:PLN03192 680 DVDK 683
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 219-278 1.04e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 1.04e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426  219 DAEMVQLLRDAGADLNKPEPTcGRTPLHLAVEGQAAGVLALLLKAGADPTARMYGGRTPL 278
Cdd:PTZ00322  94 DAVGARILLTGGADPNCRDYD-GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL 152
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 206-234 1.30e-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: 1.30e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 55741426   206 DGHTPLHVAVIH-KDAEMVQLLRDAGADLN 234
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
200-248 1.38e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 1.38e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 55741426   200 LEAENYDGHTPLHVAVIHKDAEMVQLLRDAGADLNKPEPtCGRTPLHLA 248
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDE-EGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
225-278 2.78e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 2.78e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 55741426   225 LLRDAGADLNKPEpTCGRTPLHLAVEGQAAGVLALLLKAGADPTARMYGGRTPL 278
Cdd:pfam13857   1 LLEHGPIDLNRLD-GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
82-134 3.16e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 3.16e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 55741426    82 AGTEYLDLQNDLGQTALHLAAILGEASTVEKLYAAGAGVLVTERGGHTALHLA 134
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 193-298 5.79e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 39.86  E-value: 5.79e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426  193 DEDWRLQLEAeNYDGHTPLHVAVIHKDA---EMVQLLRDAGADLNKPEPTCGRTPLHLAVEGQAAGVLALLL-KAGADPT 268
Cdd:PHA02736  42 DENRYLVLEY-NRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCnQPGVNME 120

                         90       100       110
                 ....*....|....*....|....*....|
gi 55741426  269 ARMYGGRTPLGSALLRPNPVLARLLRAHGA 298
Cdd:PHA02736 121 ILNYAFKTPYYVACERHDAKMMNILRAKGA 150
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 206-235 6.10e-04

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.85  E-value: 6.10e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 55741426   206 DGHTPLHVAVIHKDAEMVQLLRDAGADLNK 235
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 207-266 6.72e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.19  E-value: 6.72e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 55741426  207 GHTPLHVAVIHKDAEMVQLLRDAGADLNkpepTC---GRTPLHLAVEGQAAGVLALLLKAGAD 266
Cdd:PHA03100 192 GFTPLHYAVYNNNPEFVKYLLDLGANPN----LVnkyGDTPLHIAILNNNKEIFKLLLNNGPS 250
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 186-269 1.33e-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: 40.61  E-value: 1.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426 186 GNEEELRDEdwrlQLEAENYDGHTPLHVAVIHKDAEMVQLLRDAGADLN---------KPEPTC---GRTPLHLAVEGQA 253
Cdd:cd22197  77 GNPKPLVNA----QCTDEYYRGHSALHIAIEKRSLQCVKLLVENGADVHaracgrffqKKQGTCfyfGELPLSLAACTKQ 152

                        90
                ....*....|....*.
gi 55741426 254 AGVLALLLKAGADPTA 269
Cdd:cd22197 153 WDVVNYLLENPHQPAS 168
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 241-269 1.38e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 1.38e-03
                           10        20
                   ....*....|....*....|....*....
gi 55741426    241 GRTPLHLAVEGQAAGVLALLLKAGADPTA 269
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 204-262 1.55e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 1.55e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 55741426  204 NYDGHTPLHVAVIHKDAEMVQLLRDAGAD---LNKPeptcGRTPLHLAVEGQAAGVLALLLK 262
Cdd:PTZ00322 112 DYDGRTPLHIACANGHVQVVRVLLEFGADptlLDKD----GKTPLELAEENGFREVVQLLSR 169
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 94-187 1.91e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 1.91e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426   94 GQTALHLAAILGEASTVEKLYAAGAGVLVTERGGHTALHLACRVRAHTCAYVLLQPRPSH----PRDASDTYLTQ--SQD 167
Cdd:PTZ00322 115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHfelgANAKPDSFTGKppSLE 194

                         90       100
                 ....*....|....*....|.
gi 55741426  168 HTPDTSHAP-VATDPQPNPGN 187
Cdd:PTZ00322 195 DSPISSHHPdFSAVPQPMMGS 215
Ank_4 pfam13637
Ankyrin repeats (many copies);
58-113 2.08e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 2.08e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 55741426    58 GDTALHLAVIHQHEPFLDFLLGFSAGteyLDLQNDLGQTALHLAAILGEASTVEKL 113
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLL 53
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 241-270 3.00e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 3.00e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 55741426   241 GRTPLHLAV-EGQAAGVLALLLKAGADPTAR 270
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 201-293 4.33e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 38.97  E-value: 4.33e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 55741426 201 EAENYDGHTPLHVAVIHKDAEMVQLLRDAGADLNkpeptcgrtplhlaveGQAAGVLalllkagADPTARM---YGGRTP 277
Cdd:cd22194 135 TEEAYEGQTALNIAIERRQGDIVKLLIAKGADVN----------------AHAKGVF-------FNPKYKHegfYFGETP 191

                        90
                ....*....|....*.
gi 55741426 278 LGSALLRPNPVLARLL 293
Cdd:cd22194 192 LALAACTNQPEIVQLL 207
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 214-278 5.81e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.51  E-value: 5.81e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 55741426  214 AVIHKDAEMVQLLRDAGADLNKPEpTCGRTPLHLAVEGQAAGVLA-LLLKAGADPTARMYGGRTPL 278
Cdd:PHA02876 247 AIRNEDLETSLLLYDAGFSVNSID-DCKNTPLHHASQAPSLSRLVpKLLERGADVNAKNIKGETPL 311
 
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