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Conserved domains on  [gi|24111253|ref|NP_035038|]
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NF-kappa-B inhibitor beta [Mus musculus]

Protein Classification

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

ankyrin repeat (ANK) domain-containing protein is involved in mediating protein-protein interactions

Gene Ontology:  GO:0005515
PubMed:  33435370|17176038

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-310 1.38e-26

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 106.96  E-value: 1.38e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  56 EDGDTALHLAVIHQHEPFLDFLLgfsAGTEYLDLQNDLGQTALHLAAILGEASTVEKLYAAGAGVLVAERGGHTALHLAC 135
Cdd:COG0666  52 ALGALLLLAAALAGDLLVALLLL---AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAA 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253 136 RVRAHTCACVLLQprpshprdasdtyltqsqdctpdtshAPAAVDSQpnpeneeeprdedwrlqleaeNYDGHTPLHVAV 215
Cdd:COG0666 129 YNGNLEIVKLLLE--------------------------AGADVNAQ---------------------DNDGNTPLHLAA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253 216 IHKDAEMVRLLRDAGADLNKPEPTcGRTPLHLAVEAQAASVLELLLKAGADPTARMYGGRTPLGSALLRPNPILARLLRA 295
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                       250
                ....*....|....*
gi 24111253 296 HGAPEPEDEDDKLSP 310
Cdd:COG0666 241 AGADLNAKDKDGLTA 255
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-310 1.38e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 106.96  E-value: 1.38e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  56 EDGDTALHLAVIHQHEPFLDFLLgfsAGTEYLDLQNDLGQTALHLAAILGEASTVEKLYAAGAGVLVAERGGHTALHLAC 135
Cdd:COG0666  52 ALGALLLLAAALAGDLLVALLLL---AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAA 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253 136 RVRAHTCACVLLQprpshprdasdtyltqsqdctpdtshAPAAVDSQpnpeneeeprdedwrlqleaeNYDGHTPLHVAV 215
Cdd:COG0666 129 YNGNLEIVKLLLE--------------------------AGADVNAQ---------------------DNDGNTPLHLAA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253 216 IHKDAEMVRLLRDAGADLNKPEPTcGRTPLHLAVEAQAASVLELLLKAGADPTARMYGGRTPLGSALLRPNPILARLLRA 295
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                       250
                ....*....|....*
gi 24111253 296 HGAPEPEDEDDKLSP 310
Cdd:COG0666 241 AGADLNAKDKDGLTA 255
PHA03095 PHA03095
ankyrin-like protein; Provisional
 186-298 2.42e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 79.68  E-value: 2.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  186 ENEEEPRDEDWRLQLEA---ENYDGH---TPLHVAV---IHKDAEMVRLLRDAGADLNKPEpTCGRTPLHLAVE-AQAAS 255
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAgadVNFRGEygkTPLHLYLhysSEKVKDIVRLLLEAGADVNAPE-RCGFTPLHLYLYnATTLD 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 24111253  256 VLELLLKAGADPTARMYGGRTPLGSAL--LRPNPILARLLRAHGA 298
Cdd:PHA03095  99 VIKLLIKAGADVNAKDKVGRTPLHVYLsgFNINPKVIRLLLRKGA 143
Ank_2 pfam12796
Ankyrin repeats (3 copies);
206-270 6.02e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 6.02e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24111253   206 DGHTPLHVAVIHKDAEMVRLLRDaGADLNkpEPTCGRTPLHLAVEAQAASVLELLLKAGADPTAR 270
Cdd:pfam12796  29 NGRTALHLAAKNGHLEIVKLLLE-HADVN--LKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 205-290 1.96e-09

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: 58.87  E-value: 1.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253 205 YDGHTPLHVAVIHKDAEMVRLLRDAGADLNKPEPT-------------CGRTPLHLAVEAQAASVLELLLKAGADPTARM 271
Cdd:cd22192  87 YQGETALHIAVVNQNLNLVRELIARGADVVSPRATgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166

                        90
                ....*....|....*....
gi 24111253 272 YGGRTPLGSALLRPNPILA 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 1.31e-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: 44.12  E-value: 1.31e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 24111253    206 DGHTPLHVAVIHKDAEMVRLLRDAGADLNK 235
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 203-270 5.25e-06

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: 48.15  E-value: 5.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253   203 ENYDGHTPLHVAVIHKDAEMVRLLRDAGADLN----------KPEPTC---GRTPLHLAVEAQAASVLELLLKAGADPTA 269
Cdd:TIGR00870 124 EFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDSfyhGESPLNAAACLGSPSIVALLSEDPADILT 203


                  .
gi 24111253   270 R 270
Cdd:TIGR00870 204 A 204
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-310 1.38e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 106.96  E-value: 1.38e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  56 EDGDTALHLAVIHQHEPFLDFLLgfsAGTEYLDLQNDLGQTALHLAAILGEASTVEKLYAAGAGVLVAERGGHTALHLAC 135
Cdd:COG0666  52 ALGALLLLAAALAGDLLVALLLL---AAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAA 128

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253 136 RVRAHTCACVLLQprpshprdasdtyltqsqdctpdtshAPAAVDSQpnpeneeeprdedwrlqleaeNYDGHTPLHVAV 215
Cdd:COG0666 129 YNGNLEIVKLLLE--------------------------AGADVNAQ---------------------DNDGNTPLHLAA 161

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253 216 IHKDAEMVRLLRDAGADLNKPEPTcGRTPLHLAVEAQAASVLELLLKAGADPTARMYGGRTPLGSALLRPNPILARLLRA 295
Cdd:COG0666 162 ANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240

                       250
                ....*....|....*
gi 24111253 296 HGAPEPEDEDDKLSP 310
Cdd:COG0666 241 AGADLNAKDKDGLTA 255
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-308 1.32e-23

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 98.87  E-value: 1.32e-23
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  53 YVTEDGDTALHLAVIHQHEPFLDFLLgfSAGTEyLDLQNDLGQTALHLAAILGEASTVEKLYAAGAGVLVAERGGHTALH 132
Cdd:COG0666  82 AKDDGGNTLLHAAARNGDLEIVKLLL--EAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLH 158

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253 133 LACRVRAHTCACVLLQprpshprdasdtyltqsqdctpdtshAPAAVDsqpnpeneeeprdedwrlqleAENYDGHTPLH 212
Cdd:COG0666 159 LAAANGNLEIVKLLLE--------------------------AGADVN---------------------ARDNDGETPLH 191

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253 213 VAVIHKDAEMVRLLRDAGADLNKPEPTcGRTPLHLAVEAQAASVLELLLKAGADPTARMYGGRTPLGSALLRPNPILARL 292
Cdd:COG0666 192 LAAENGHLEIVKLLLEAGADVNAKDND-GKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKL 270

                       250
                ....*....|....*.
gi 24111253 293 LRAHGAPEPEDEDDKL 308
Cdd:COG0666 271 LLLALLLLAAALLDLL 286
PHA03095 PHA03095
ankyrin-like protein; Provisional
 186-298 2.42e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 79.68  E-value: 2.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  186 ENEEEPRDEDWRLQLEA---ENYDGH---TPLHVAV---IHKDAEMVRLLRDAGADLNKPEpTCGRTPLHLAVE-AQAAS 255
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAgadVNFRGEygkTPLHLYLhysSEKVKDIVRLLLEAGADVNAPE-RCGFTPLHLYLYnATTLD 98

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 24111253  256 VLELLLKAGADPTARMYGGRTPLGSAL--LRPNPILARLLRAHGA 298
Cdd:PHA03095  99 VIKLLIKAGADVNAKDKVGRTPLHVYLsgFNINPKVIRLLLRKGA 143
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-278 1.05e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.45  E-value: 1.05e-14
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  56 EDGDTALHLAVIHQHEPFLDFLLgfSAGTEyLDLQNDLGQTALHLAAILGEASTVEKLYAAGAGVLVAERGGHTALHLAC 135
Cdd:COG0666 118 KDGETPLHLAAYNGNLEIVKLLL--EAGAD-VNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA 194

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253 136 RVRAHTCACVLLQprpshprdasdtyltqsqdctpdtshAPAAVDsqpnpeneeeprdedwrlqleAENYDGHTPLHVAV 215
Cdd:COG0666 195 ENGHLEIVKLLLE--------------------------AGADVN---------------------AKDNDGKTALDLAA 227

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24111253 216 IHKDAEMVRLLRDAGADLNKPEPTcGRTPLHLAVEAQAASVLELLLKAGADPTARMYGGRTPL 278
Cdd:COG0666 228 ENGNLEIVKLLLEAGADLNAKDKD-GLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
 207-298 1.55e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.21  E-value: 1.55e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  207 GHTPLHVAVIHKD-AEMVRLLRDAGADLNKpEPTCGRTPLH--LAVEAQAASVLELLLKAGADPTARMYGGRTPLGsALL 283
Cdd:PHA03095  83 GFTPLHLYLYNATtLDVIKLLIKAGADVNA-KDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLA-VLL 160

                         90
                 ....*....|....*...
gi 24111253  284 RP---NPILARLLRAHGA 298
Cdd:PHA03095 161 KSrnaNVELLRLLIDAGA 178
PHA03095 PHA03095
ankyrin-like protein; Provisional
 58-300 1.30e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.43  E-value: 1.30e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253   58 GDTALHLAVIHQH-EPFLDFLLGFSAGTEYldlQNDLGQTALH--LAAILGEASTVEKLYAAGAGVLVAERGGHTALHla 134
Cdd:PHA03095  83 GFTPLHLYLYNATtLDVIKLLIKAGADVNA---KDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLA-- 157

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  135 CRVRAHTCaCV----LLQPRPSHPRDASDTYLT----QSQDCTPDTSHAPAAVDSQPNPEneeeprdedwrlqleAENYD 206
Cdd:PHA03095 158 VLLKSRNA-NVellrLLIDAGADVYAVDDRFRSllhhHLQSFKPRARIVRELIRAGCDPA---------------ATDML 221

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  207 GHTPLHVAVIH---KDAEMVRLLrDAGADLNKPEPTcGRTPLHLAVEAQAASVLELLLKAGADPTARMYGGRTPLGSALL 283
Cdd:PHA03095 222 GNTPLHSMATGsscKRSLVLPLL-IAGISINARNRY-GQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVR 299

                        250
                 ....*....|....*...
gi 24111253  284 RPNP-ILARLLRAHGAPE 300
Cdd:PHA03095 300 NNNGrAVRAALAKNPSAE 317
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
202-298 3.17e-11

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 63.43  E-value: 3.17e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253 202 AENYDGHTPLHVAVIHKDAEMVRLLRDAGADLNKPEPTcGRTPLHLAVEAQAASVLELLLKAGADPTARMYGGRTPLGSA 281
Cdd:COG0666  49 LADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG-GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLA 127

                        90
                ....*....|....*..
gi 24111253 282 LLRPNPILARLLRAHGA 298
Cdd:COG0666 128 AYNGNLEIVKLLLEAGA 144
Ank_2 pfam12796
Ankyrin repeats (3 copies);
206-270 6.02e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 6.02e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24111253   206 DGHTPLHVAVIHKDAEMVRLLRDaGADLNkpEPTCGRTPLHLAVEAQAASVLELLLKAGADPTAR 270
Cdd:pfam12796  29 NGRTALHLAAKNGHLEIVKLLLE-HADVN--LKDNGRTALHYAARSGHLEIVKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
211-298 2.73e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.66  E-value: 2.73e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253   211 LHVAVIHKDAEMVRLLRDAGADLNKPEPtCGRTPLHLAVEAQAASVLELLLKaGADPTARMYgGRTPLGSALLRPNPILA 290
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLEIV 77


                  ....*...
gi 24111253   291 RLLRAHGA 298
Cdd:pfam12796  78 KLLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
62-148 3.04e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 3.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253    62 LHLAVIHQHEPFLDFLLGFSAGteyLDLQNDLGQTALHLAAILGEASTVEKLYAAGAGVLVAErgGHTALHLACRVRAHT 141
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD---ANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAARSGHLE 75


                  ....*..
gi 24111253   142 CACVLLQ 148
Cdd:pfam12796  76 IVKLLLE 82
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 204-298 6.02e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.06  E-value: 6.02e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  204 NYDGHTPLHVAV--IHKDAEMVRLLRDAGADLN----------KPEPT-----CGRTPLHLAVEAQAASVLELLLKAGAD 266
Cdd:PHA03100 138 NSDGENLLHLYLesNKIDLKILKLLIDKGVDINaknrvnyllsYGVPInikdvYGFTPLHYAVYNNNPEFVKYLLDLGAN 217

                         90       100       110
                 ....*....|....*....|....*....|..
gi 24111253  267 PTARMYGGRTPLGSALLRPNPILARLLRAHGA 298
Cdd:PHA03100 218 PNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 205-290 1.96e-09

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: 58.87  E-value: 1.96e-09
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253 205 YDGHTPLHVAVIHKDAEMVRLLRDAGADLNKPEPT-------------CGRTPLHLAVEAQAASVLELLLKAGADPTARM 271
Cdd:cd22192  87 YQGETALHIAVVNQNLNLVRELIARGADVVSPRATgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRAQD 166

                        90
                ....*....|....*....
gi 24111253 272 YGGRTPLGSALLRPNPILA 290
Cdd:cd22192 167 SLGNTVLHILVLQPNKTFA 185
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 78-284 1.03e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.43  E-value: 1.03e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253   78 LGFSAGTEYLDLQNDLGQTALHLAAILGEASTVEKLYAAGAGVLVAERGGHTALHLACRVRAHTCACVLLQPRPShpRDA 157
Cdd:PHA02878 152 LLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS--TDA 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  158 SDTYltqsqdctpdtshapaavdsqpnpeneeeprdedwrlqleaenydGHTPLHVAVIH-KDAEMVRLLRDAGADLNKP 236
Cdd:PHA02878 230 RDKC---------------------------------------------GNTPLHISVGYcKDYDILKLLLEHGVDVNAK 264

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 24111253  237 EPTCGRTPLHLAVEAQaaSVLELLLKAGADPTARMYGGRTPLGSALLR 284
Cdd:PHA02878 265 SYILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
Ank_2 pfam12796
Ankyrin repeats (3 copies);
98-234 2.08e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.27  E-value: 2.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253    98 LHLAAILGEASTVEKLYAAGAGVLVAERGGHTALHLACRVRAHTCACVLLQprpshprdasdtyltqsqdctpdtsHAPA 177
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-------------------------HADV 55

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 24111253   178 AVDSqpnpeneeeprdedwrlqleaenyDGHTPLHVAVIHKDAEMVRLLRDAGADLN 234
Cdd:pfam12796  56 NLKD------------------------NGRTALHYAARSGHLEIVKLLLEKGADIN 88
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 204-298 2.49e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.38  E-value: 2.49e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  204 NYDGHTPLHVAVIHKDAEMVRLLRDAGADLNKpEPTCGRTPLHLAVEAQAASVLELLLKAGADPTarmYGGRTP----LG 279
Cdd:PHA02875 132 NTDKFSPLHLAVMMGDIKGIELLIDHKACLDI-EDCCGCTPLIIAMAKGDIAICKMLLDSGANID---YFGKNGcvaaLC 207

                         90
                 ....*....|....*....
gi 24111253  280 SALLRPNPILARLLRAHGA 298
Cdd:PHA02875 208 YAIENNKIDIVRLFIKRGA 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
52-118 9.21e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 49.34  E-value: 9.21e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24111253    52 GYVTEDGDTALHLAVIHQHEPFLDFLLgfsagtEYLDLQN-DLGQTALHLAAILGEASTVEKLYAAGA 118
Cdd:pfam12796  24 NLQDKNGRTALHLAAKNGHLEIVKLLL------EHADVNLkDNGRTALHYAARSGHLEIVKLLLEKGA 85
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 203-310 1.11e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.07  E-value: 1.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  203 ENYDGHTPLHVAVIHKDAEMVRLLRDAGA--DLNKPEPtcgRTPLHLAVEAQAASVLELLLKAGADPTARMY-GGRTPLG 279
Cdd:PHA02875  31 EIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDI---ESELHDAVEEGDVKAVEELLDLGKFADDVFYkDGMTPLH 107

                         90       100       110
                 ....*....|....*....|....*....|.
gi 24111253  280 SALLRPNPILARLLRAHGAPEPEDEDDKLSP 310
Cdd:PHA02875 108 LATILKKLDIMKLLIARGADPDIPNTDKFSP 138
Ank_4 pfam13637
Ankyrin repeats (many copies);
207-261 2.41e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 2.41e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 24111253   207 GHTPLHVAVIHKDAEMVRLLRDAGADLNKPePTCGRTPLHLAVEAQAASVLELLL 261
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAV-DGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 207-298 3.70e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.80  E-value: 3.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  207 GHTPLHVAVIHKDAEMVRLLRDAGADLNKPEpTCGRTPLHLAVEAQAASVLELLLKAGADPTARMYGGRTPLGSALLRPN 286
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPD-KTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCK 246

                         90
                 ....*....|...
gi 24111253  287 PI-LARLLRAHGA 298
Cdd:PHA02878 247 DYdILKLLLEHGV 259
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 207-298 1.15e-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: 50.40  E-value: 1.15e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253 207 GHTPLHVAVIHKDAEMVRLLRDAGADL-NKP---EPTCGRTPLHLAVEAQAASVLELLLKAGAD--------------PT 268
Cdd:cd22192  51 GETALHVAALYDNLEAAVVLMEAAPELvNEPmtsDLYQGETALHIAVVNQNLNLVRELIARGADvvspratgtffrpgPK 130

                        90       100       110
                ....*....|....*....|....*....|
gi 24111253 269 ARMYGGRTPLGSALLRPNPILARLLRAHGA 298
Cdd:cd22192 131 NLIYYGEHPLSFAACVGNEEIVRLLIEHGA 160
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 206-235 1.31e-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: 44.12  E-value: 1.31e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 24111253    206 DGHTPLHVAVIHKDAEMVRLLRDAGADLNK 235
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 204-298 1.66e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.60  E-value: 1.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  204 NYDG-HTPLHVAVIHKDAEMVRLLRDAGADLNKPEPTCGRTPLHLAVEAQAASVLELLLKAGADPTARMYGGRTPLGSAL 282
Cdd:PHA02875  64 KYPDiESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAV 143

                         90
                 ....*....|....*.
gi 24111253  283 LRPNPILARLLRAHGA 298
Cdd:PHA02875 144 MMGDIKGIELLIDHKA 159
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 219-294 2.57e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 49.11  E-value: 2.57e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24111253  219 DAEMVRLLRDAGADLNKPEPTCGRTPLHLAVEAQAASVLELLLKAGADPTARMYGGRTPLGSALL-RPNPILARLLR 294
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKhYNKPIVHILLE 222
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 203-270 5.25e-06

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: 48.15  E-value: 5.25e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253   203 ENYDGHTPLHVAVIHKDAEMVRLLRDAGADLN----------KPEPTC---GRTPLHLAVEAQAASVLELLLKAGADPTA 269
Cdd:TIGR00870 124 EFTPGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDSfyhGESPLNAAACLGSPSIVALLSEDPADILT 203


                  .
gi 24111253   270 R 270
Cdd:TIGR00870 204 A 204
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 84-281 1.02e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.27  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253   84 TEYLDLQNDLGQTALHLAAILGEASTVEKLYAAGAGVLVAERGGHTALHLACRVRAHTCACVLLqprpshprdasdtylt 163
Cdd:PHA02874  25 GNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI---------------- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  164 qsqDCTPDTSHAPAavdsqPNPENEEEPRDEDWRLQLEAENYDGHTPLHVAVIHKDAEMVRLLRDAGADLNKpEPTCGRT 243
Cdd:PHA02874  89 ---DNGVDTSILPI-----PCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNI-EDDNGCY 159

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 24111253  244 PLHLAVEAQAASVLELLLKAGADPTARMYGGRTPLGSA 281
Cdd:PHA02874 160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNA 197
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 195-283 1.46e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.50  E-value: 1.46e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  195 DWRLQLEAENYDGHTPLHVAVIHKDAEMVRLLRDAGADLNKPEPTcGRTPLHLAVEAQAASVLELLLKAGADPTARMYGG 274
Cdd:PHA02874 145 EYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN-GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNG 223


                 ....*....
gi 24111253  275 RTPLGSALL 283
Cdd:PHA02874 224 FTPLHNAII 232
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 219-278 1.61e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.82  E-value: 1.61e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  219 DAEMVRLLRDAGADLNKPEPTcGRTPLHLAVEAQAASVLELLLKAGADPTARMYGGRTPL 278
Cdd:PTZ00322  94 DAVGARILLTGGADPNCRDYD-GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL 152
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 193-298 1.89e-05

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 44.10  E-value: 1.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  193 DEDWRLQLEAeNYDGHTPLHVAVIHKDA---EMVRLLRDAGADLNKPEPTCGRTPLHLAVEAQAASVLELLL-KAGADPT 268
Cdd:PHA02736  42 DENRYLVLEY-NRHGKQCVHIVSNPDKAdpqEKLKLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCnQPGVNME 120

                         90       100       110
                 ....*....|....*....|....*....|
gi 24111253  269 ARMYGGRTPLGSALLRPNPILARLLRAHGA 298
Cdd:PHA02736 121 ILNYAFKTPYYVACERHDAKMMNILRAKGA 150
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 200-298 3.98e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 3.98e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  200 LEAENYDGHTPLHVAVIHK-DAEMVRLLRDAGADLNKPEpTCGRTPLHLAVEA-QAASVLELLLKAGADPTARMYGGRTP 277
Cdd:PHA02876 300 VNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAAD-RLYITPLHQASTLdRNKDIVITLLELGANVNARDYCDKTP 378

                         90       100
                 ....*....|....*....|.
gi 24111253  278 LGSALLRPNPILARLLRAHGA 298
Cdd:PHA02876 379 IHYAAVRNNVVIINTLLDYGA 399
Ank_5 pfam13857
Ankyrin repeats (many copies);
225-278 4.60e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 4.60e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 24111253   225 LLRDAGADLNKPEpTCGRTPLHLAVEAQAASVLELLLKAGADPTARMYGGRTPL 278
Cdd:pfam13857   1 LLEHGPIDLNRLD-GEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 204-262 5.96e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 5.96e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24111253  204 NYDGHTPLHVAVIHKDAEMVRLLRDAGAD---LNKPeptcGRTPLHLAVEAQAASVLELLLK 262
Cdd:PTZ00322 112 DYDGRTPLHIACANGHVQVVRVLLEFGADptlLDKD----GKTPLELAEENGFREVVQLLSR 169
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 203-286 6.04e-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: 44.87  E-value: 6.04e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253 203 ENYDGHTPLHVAVIHKDAEMVRLLRDAGADLN---------KPEPTC---GRTPLHLAVEAQAASVLELLLKAGADP--- 267
Cdd:cd21882  69 EFYQGQTALHIAIENRNLNLVRLLVENGADVSaratgrffrKSPGNLfyfGELPLSLAACTNQEEIVRLLLENGAQPaal 148

                        90
                ....*....|....*....
gi 24111253 268 TARMYGGRTPLGSALLRPN 286
Cdd:cd21882 149 EAQDSLGNTVLHALVLQAD 167
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 241-269 7.67e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 7.67e-05
                           10        20
                   ....*....|....*....|....*....
gi 24111253    241 GRTPLHLAVEAQAASVLELLLKAGADPTA 269
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
200-248 8.71e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 8.71e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 24111253   200 LEAENYDGHTPLHVAVIHKDAEMVRLLRDAGADLNKPEPtCGRTPLHLA 248
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDE-EGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 206-234 8.87e-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: 39.19  E-value: 8.87e-05
                          10        20        30
                  ....*....|....*....|....*....|
gi 24111253   206 DGHTPLHVAVIH-KDAEMVRLLRDAGADLN 234
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 207-266 1.06e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.89  E-value: 1.06e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24111253  207 GHTPLHVAVIHKDAEMVRLLRDAGADLNkpepTC---GRTPLHLAVEAQAASVLELLLKAGAD 266
Cdd:PHA03100 192 GFTPLHYAVYNNNPEFVKYLLDLGANPN----LVnkyGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 195-266 2.10e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.06  E-value: 2.10e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24111253  195 DWRLQLEAENYDGHTPLHVAVIHKDAEMVRLLRDAGADLNKPEPTCGRTPLHLAVEAQAASVLELLLKAGAD 266
Cdd:PHA02875 156 DHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 241-270 2.59e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 38.04  E-value: 2.59e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 24111253   241 GRTPLHLAV-EAQAASVLELLLKAGADPTAR 270
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 73-235 2.74e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.93  E-value: 2.74e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253   73 FLDFLLgfSAGTEyLDLQNDLGQTALHLAAILGEASTVEKLYAAGAGVLVAERGGHTALHLACRVRAHTCACVLLQ-PRP 151
Cdd:PLN03192 540 LLEELL--KAKLD-PDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfASI 616

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  152 SHPRDASDTYLTQSQdctpdtshapaavdsqpnpENEEEPRDEDWRLQL--EAENYDGHTPLHVAVIHKDAEMVRLLRDA 229
Cdd:PLN03192 617 SDPHAAGDLLCTAAK-------------------RNDLTAMKELLKQGLnvDSEDHQGATALQVAMAEDHVDMVRLLIMN 677


                 ....*.
gi 24111253  230 GADLNK 235
Cdd:PLN03192 678 GADVDK 683
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 206-235 3.92e-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: 37.24  E-value: 3.92e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 24111253   206 DGHTPLHVAVIHKDAEMVRLLRDAGADLNK 235
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
241-293 4.84e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 4.84e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 24111253   241 GRTPLHLAVEAQAASVLELLLKAGADPTARMYGGRTPLGSALLRPNPILARLL 293
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 214-278 6.75e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.59  E-value: 6.75e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24111253  214 AVIHKDAEMVRLLRDAGADLNKPEpTCGRTPLHLAVEAQAASVL-ELLLKAGADPTARMYGGRTPL 278
Cdd:PHA02876 247 AIRNEDLETSLLLYDAGFSVNSID-DCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPL 311
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 201-269 1.13e-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: 40.90  E-value: 1.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253 201 EAENYDGHTPLHVAVIHKDAEMVRLLRDAGADLN----------KPEPTC---GRTPLHLAVEAQAASVLELLLKAGADP 267
Cdd:cd22194 135 TEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNahakgvffnpKYKHEGfyfGETPLALAACTNQPEIVQLLMEKESTD 214


                ..
gi 24111253 268 TA 269
Cdd:cd22194 215 IT 216
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 203-269 1.22e-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: 1.22e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 24111253 203 ENYDGHTPLHVAVIHKDAEMVRLLRDAGADLN---------KPEPTC---GRTPLHLAVEAQAASVLELLLKAGADPTA 269
Cdd:cd22197  90 EYYRGHSALHIAIEKRSLQCVKLLVENGADVHaracgrffqKKQGTCfyfGELPLSLAACTKQWDVVNYLLENPHQPAS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
82-134 1.53e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 1.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 24111253    82 AGTEYLDLQNDLGQTALHLAAILGEASTVEKLYAAGAGVLVAERGGHTALHLA 134
Cdd:pfam13857   4 HGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
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 24111253    58 GDTALHLAVIHQHEPFLDFLLGFSAGteyLDLQNDLGQTALHLAAILGEASTVEKL 113
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGAD---INAVDGNGETALHFAASNGNVEVLKLL 53
Ank_2 pfam12796
Ankyrin repeats (3 copies);
245-305 2.14e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.02  E-value: 2.14e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24111253   245 LHLAVEAQAASVLELLLKAGADPTARMYGGRTPLGSALLRPNPILARLLRAHGAPEPEDED 305
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNG 61
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 240-267 2.17e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.31  E-value: 2.17e-03
                          10        20
                  ....*....|....*....|....*...
gi 24111253   240 CGRTPLHLAVEAQAASVLELLLKAGADP 267
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADI 28
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 207-293 2.82e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.56  E-value: 2.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  207 GHTPLHVAVIHKDAEMVRLLRDAG---ADLNkpeptcGRTPLHLAVEAQAA-SVLELLLKAGADPTARMYGGRTPLGSAL 282
Cdd:PHA02874 223 GFTPLHNAIIHNRSAIELLINNASindQDID------GSTPLHHAINPPCDiDIIDILLYHKADISIKDNKGENPIDTAF 296

                         90
                 ....*....|...
gi 24111253  283 --LRPNPILARLL 293
Cdd:PHA02874 297 kyINKDPVIKDII 309
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 205-309 7.23e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 36.72  E-value: 7.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  205 YDGHTPL--HVAVIH--KDAEM-VRLLRDAGADLNKPEPTCGRTPLHLAVEAQAASVLELLLKA-GADPTARMYGGRTPL 278
Cdd:PHA02743  53 YDHHGRQctHMVAWYdrANAVMkIELLVNMGADINARELGTGNTLLHIAASTKNYELAEWLCRQlGVNLGAINYQHETAY 132

                         90       100       110
                 ....*....|....*....|....*....|.
gi 24111253  279 GSALLRPNPILARLLRAHGAPEPEDEDDKLS 309
Cdd:PHA02743 133 HIAYKMRDRRMMEILRANGAVCDDPLSIGLS 163
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 203-262 8.46e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 38.24  E-value: 8.46e-03
                        10        20        30        40        50        60        70
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 24111253 203 ENYDGHTPLHVAVIHKDAEMVRLLRDAGADLN----------KPEPTC---GRTPLHLAVEAQAASVLELLLK 262
Cdd:cd22193  72 EYYEGQTALHIAIERRQGDIVALLVENGADVHahakgrffqpKYQGEGfyfGELPLSLAACTNQPDIVQYLLE 144
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 204-278 9.49e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 37.72  E-value: 9.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24111253  204 NYDGHTPLHVAVIHKDAEMVRLLRDAGADLNKpEPTCGRTPLHLAVEAQAAS-----VLELLLKAGADPTARMYGGRTPL 278
Cdd:PHA03100  32 YKKPVLPLYLAKEARNIDVVKILLDNGADINS-STKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVNAPDNNGITPL 110
 
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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