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Conserved domains on  [gi|922304323|ref|NP_998349|]
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nuclear factor of kappa light polypeptide gene enhancer in B-cells inhibitor, alpha a [Danio rerio]

Protein Classification

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

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

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

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-278 6.16e-30

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.05  E-value: 6.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323  54 MEKLTIASLKETICEPWAKVVTEDGDTYLHLAIIHEAEDYAVQIIKQCQNDPYLNRQNNQRQTALHLAVVTEQPQMVERL 133
Cdd:COG0666   27 AAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 134 LKAGCDPQLVDQSGNTALHLACKQGSLACFSVLTQ----IQTQhlrsiltfpNYSGHTCLHIAAINNYLSMVESLVQLGA 209
Cdd:COG0666  107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEagadVNAQ---------DNDGNTPLHLAAANGNLEIVKLLLEAGA 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 922304323 210 DVDAKEQcSGRTSLHLAVDLQNLDLVHTLIALGADANSLTYGGYTAYHLTFGRHNSEIQRQLYSRTALK 278
Cdd:COG0666  178 DVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-278 6.16e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.05  E-value: 6.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323  54 MEKLTIASLKETICEPWAKVVTEDGDTYLHLAIIHEAEDYAVQIIKQCQNDPYLNRQNNQRQTALHLAVVTEQPQMVERL 133
Cdd:COG0666   27 AAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 134 LKAGCDPQLVDQSGNTALHLACKQGSLACFSVLTQ----IQTQhlrsiltfpNYSGHTCLHIAAINNYLSMVESLVQLGA 209
Cdd:COG0666  107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEagadVNAQ---------DNDGNTPLHLAAANGNLEIVKLLLEAGA 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 922304323 210 DVDAKEQcSGRTSLHLAVDLQNLDLVHTLIALGADANSLTYGGYTAYHLTFGRHNSEIQRQLYSRTALK 278
Cdd:COG0666  178 DVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
Ank_2 pfam12796
Ankyrin repeats (3 copies);
118-214 1.05e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.69  E-value: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323  118 LHLAVVTEQPQMVERLLKAGCDPQLVDQSGNTALHLACKQGSLACFSVLtqiqtqhLRSILTFPNYSGHTCLHIAAINNY 197
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-------LEHADVNLKDNGRTALHYAARSGH 73

                          90
                  ....*....|....*..
gi 922304323  198 LSMVESLVQLGADVDAK 214
Cdd:pfam12796  74 LEIVKLLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 94-267 1.21e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.60  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323  94 AVQIIKQCQNDPYLNRQNNQRQTA-LHLAVVTEQPQMVERLLKAGCDPQLVDQSGNTALHLACKQGSL------------ 160
Cdd:PHA03100  14 KVKNIKYIIMEDDLNDYSYKKPVLpLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkeivklll 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 161 ---ACFSVLTQIQTQHLR----------SILTF----------PNYSGHTCLHIAAINNY--LSMVESLVQLGADVDAKE 215
Cdd:PHA03100  94 eygANVNAPDNNGITPLLyaiskksnsySIVEYlldnganvniKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922304323 216 QCS---------------GRTSLHLAVDLQNLDLVHTLIALGADANSLTYGGYTAYHLTFGRHNSEI 267
Cdd:PHA03100 174 RVNyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI 240
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 107-272 2.41e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.94  E-value: 2.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 107 LNRQNNQR--QTALHLAVVTEQPQMVERLLK-AGCDPQLVDQSGNTALHLACKQGSLACFSVLTQIQTQHLRSILTFPNY 183
Cdd:cd22192    8 LHLLQQKRisESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDLY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 184 SGHTCLHIAAINNYLSMVESLVQLGADVDAKEQCS-------------GRTSLHLAVDLQNLDLVHTLIALGADANSLTY 250
Cdd:cd22192   88 QGETALHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDS 167

                        170       180
                 ....*....|....*....|..
gi 922304323 251 GGYTAYHLTFGRHNSEIQRQLY 272
Cdd:cd22192  168 LGNTVLHILVLQPNKTFACQMY 189
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 84-273 1.47e-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: 49.69  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323   84 LAIIHEAEDYAVQIIKQCQNDPYLNRQNNQRQTALHLAVVTEQPQ-MVERLLKAGCDPQLvdqsGNTALHLACK---QGS 159
Cdd:TIGR00870  22 LPAAERGDLASVYRDLEEPKKLNINCPDRLGRSALFVAAIENENLeLTELLLNLSCRGAV----GDTLLHAISLeyvDAV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323  160 LACFSVLTQIQTQHLRSILTFPNYS-----GHTCLHIAAINNYLSMVESLVQLGADVDAKEQCS-------------GRT 221
Cdd:TIGR00870  98 EAILLHLLAAFRKSGPLELANDQYTseftpGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhGES 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323  222 SLHLAVDLQNLDLVHTLIALGAD---ANSLtygGYTAYHL-----TFGRHNSEIQRQLYS 273
Cdd:TIGR00870 178 PLNAAACLGSPSIVALLSEDPADiltADSL---GNTLLHLlvmenEFKAEYEELSCQMYN 234
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 185-213 7.97e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 7.97e-04
                           10        20
                   ....*....|....*....|....*....
gi 922304323   185 GHTCLHIAAINNYLSMVESLVQLGADVDA 213
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-278 6.16e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.05  E-value: 6.16e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323  54 MEKLTIASLKETICEPWAKVVTEDGDTYLHLAIIHEAEDYAVQIIKQCQNDPYLNRQNNQRQTALHLAVVTEQPQMVERL 133
Cdd:COG0666   27 AAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLL 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 134 LKAGCDPQLVDQSGNTALHLACKQGSLACFSVLTQ----IQTQhlrsiltfpNYSGHTCLHIAAINNYLSMVESLVQLGA 209
Cdd:COG0666  107 LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEagadVNAQ---------DNDGNTPLHLAAANGNLEIVKLLLEAGA 177

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 922304323 210 DVDAKEQcSGRTSLHLAVDLQNLDLVHTLIALGADANSLTYGGYTAYHLTFGRHNSEIQRQLYSRTALK 278
Cdd:COG0666  178 DVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADL 245
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
75-271 5.84e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.66  E-value: 5.84e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323  75 TEDGDTYLHLAIIHEAEDYAVQIIKqcqNDPYLNRQNNQRQTALHLAVVTEQPQMVERLLKAGCDPQLVDQSGNTALHLA 154
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLE---AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 155 CKQGSLACFSVLtqiqtqhLRS--ILTFPNYSGHTCLHIAAINNYLSMVESLVQLGADVDAKEQcSGRTSLHLAVDLQNL 232
Cdd:COG0666  161 AANGNLEIVKLL-------LEAgaDVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNL 232

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 922304323 233 DLVHTLIALGADANSLTYGGYTAYHLTFGRHNSEIQRQL 271
Cdd:COG0666  233 EIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
79-267 3.69e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.17  E-value: 3.69e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323  79 DTYLHLAIIHEAEDYAVQIIKQCQNDPYLNRQNNQRQTALHLAVVTEQPQMVERLLKAGCDPQLVDQSGNTALHLACKQG 158
Cdd:COG0666   19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNG 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 159 SLACFSVLTQiqtqhLRSILTFPNYSGHTCLHIAAINNYLSMVESLVQLGADVDAKEQcSGRTSLHLAVDLQNLDLVHTL 238
Cdd:COG0666   99 DLEIVKLLLE-----AGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDN-DGNTPLHLAAANGNLEIVKLL 172

                        170       180
                 ....*....|....*....|....*....
gi 922304323 239 IALGADANSLTYGGYTAYHLTFGRHNSEI 267
Cdd:COG0666  173 LEAGADVNARDNDGETPLHLAAENGHLEI 201
Ank_2 pfam12796
Ankyrin repeats (3 copies);
118-214 1.05e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.69  E-value: 1.05e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323  118 LHLAVVTEQPQMVERLLKAGCDPQLVDQSGNTALHLACKQGSLACFSVLtqiqtqhLRSILTFPNYSGHTCLHIAAINNY 197
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-------LEHADVNLKDNGRTALHYAARSGH 73

                          90
                  ....*....|....*..
gi 922304323  198 LSMVESLVQLGADVDAK 214
Cdd:pfam12796  74 LEIVKLLLEKGADINVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 94-267 1.21e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.60  E-value: 1.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323  94 AVQIIKQCQNDPYLNRQNNQRQTA-LHLAVVTEQPQMVERLLKAGCDPQLVDQSGNTALHLACKQGSL------------ 160
Cdd:PHA03100  14 KVKNIKYIIMEDDLNDYSYKKPVLpLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkeivklll 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 161 ---ACFSVLTQIQTQHLR----------SILTF----------PNYSGHTCLHIAAINNY--LSMVESLVQLGADVDAKE 215
Cdd:PHA03100  94 eygANVNAPDNNGITPLLyaiskksnsySIVEYlldnganvniKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKN 173

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922304323 216 QCS---------------GRTSLHLAVDLQNLDLVHTLIALGADANSLTYGGYTAYHLTFGRHNSEI 267
Cdd:PHA03100 174 RVNyllsygvpinikdvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI 240
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 139-276 4.53e-10

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 57.52  E-value: 4.53e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 139 DPQLVDQSGNTaLHLACKQGSLACFSVLTQIQTQHlRSILTFPNYSGHTCLHIAA---INNYLSMVESLVQLGADVDAKE 215
Cdd:PHA02743  13 AVEIDEDEQNT-FLRICRTGNIYELMEVAPFISGD-GHLLHRYDHHGRQCTHMVAwydRANAVMKIELLVNMGADINARE 90

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 922304323 216 QCSGRTSLHLAVDLQNLDLVHTLI-ALGADANSLTYGGYTAYHLTFGRHNSEIQRQLYSRTA 276
Cdd:PHA02743  91 LGTGNTLLHIAASTKNYELAEWLCrQLGVNLGAINYQHETAYHIAYKMRDRRMMEILRANGA 152
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 144-267 1.26e-09

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 56.04  E-value: 1.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 144 DQSGNTALHLACKQGSLACFSVLTQIQTQHLRSILTFPNYSGHTCLHIAAINNYLSMVESLVQL---GADVDAKEQCSGR 220
Cdd:PHA02736  14 DIEGENILHYLCRNGGVTDLLAFKNAISDENRYLVLEYNRHGKQCVHIVSNPDKADPQEKLKLLmewGADINGKERVFGN 93

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 922304323 221 TSLHLAVDLQNLDLVHTLIAL-GADANSLTYGGYTAYHLTFGRHNSEI 267
Cdd:PHA02736  94 TPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKM 141
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 115-244 1.66e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.73  E-value: 1.66e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 115 QTALHLAVVTEQPQMVERLLKAGCDPQLVDQSGNTALHLACKQGSLACFSVLTQIqtqhlrSILTFPNYSGHTcLHIAAI 194
Cdd:PLN03192 559 RTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF------ASISDPHAAGDL-LCTAAK 631

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 922304323 195 NNYLSMVESLVQLGADVDAKEQcSGRTSLHLAVDLQNLDLVHTLIALGAD 244
Cdd:PLN03192 632 RNDLTAMKELLKQGLNVDSEDH-QGATALQVAMAEDHVDMVRLLIMNGAD 680
PHA03095 PHA03095
ankyrin-like protein; Provisional
 111-240 2.42e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.73  E-value: 2.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 111 NNQRQTALH--LAVVTEQPQMVERLLKAGCDPQLVDQSGNTALHLACKQGSLACFSVLtqiqtQHLRSILTF--PNYSGH 186
Cdd:PHA03095 184 DDRFRSLLHhhLQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVL-----PLLIAGISInaRNRYGQ 258

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 922304323 187 TCLHIAAINNYLSMVESLVQLGADVDAKEQCsGRTSLHLAVDLQNLDLVHTLIA 240
Cdd:PHA03095 259 TPLHYAAVFNNPRACRRLIALGADINAVSSD-GNTPLSLMVRNNNGRAVRAALA 311
Ank_2 pfam12796
Ankyrin repeats (3 copies);
82-166 1.10e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 51.66  E-value: 1.10e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323   82 LHLAIIHEAEDyAVQIIKQCQNDPYLNRQNNQrqTALHLAVVTEQPQMVERLLKaGCDPQLVDQsGNTALHLACKQGSLA 161
Cdd:pfam12796   1 LHLAAKNGNLE-LVKLLLENGADANLQDKNGR--TALHLAAKNGHLEIVKLLLE-HADVNLKDN-GRTALHYAARSGHLE 75


                  ....*
gi 922304323  162 CFSVL 166
Cdd:pfam12796  76 IVKLL 80
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 107-272 2.41e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 51.94  E-value: 2.41e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 107 LNRQNNQR--QTALHLAVVTEQPQMVERLLK-AGCDPQLVDQSGNTALHLACKQGSLACFSVLTQIQTQHLRSILTFPNY 183
Cdd:cd22192    8 LHLLQQKRisESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDLY 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 184 SGHTCLHIAAINNYLSMVESLVQLGADVDAKEQCS-------------GRTSLHLAVDLQNLDLVHTLIALGADANSLTY 250
Cdd:cd22192   88 QGETALHIAVVNQNLNLVRELIARGADVVSPRATGtffrpgpknliyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDS 167

                        170       180
                 ....*....|....*....|..
gi 922304323 251 GGYTAYHLTFGRHNSEIQRQLY 272
Cdd:cd22192  168 LGNTVLHILVLQPNKTFACQMY 189
PHA02741 PHA02741
hypothetical protein; Provisional
 147-238 2.70e-07

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 49.66  E-value: 2.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 147 GNTALHLACKQGslaCFSVLTQ----IQTQHLRSILTFPNYSGHTCLHIAAINN----YLSMVESLVQLGADVDAKEQCS 218
Cdd:PHA02741  21 GENFFHEAARCG---CFDIIARftpfIRGDCHAAALNATDDAGQMCIHIAAEKHeaqlAAEIIDHLIELGADINAQEMLE 97

                         90       100
                 ....*....|....*....|
gi 922304323 219 GRTSLHLAVDLQNLDLVHTL 238
Cdd:PHA02741  98 GDTALHLAAHRRDHDLAEWL 117
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 115-258 2.93e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.53  E-value: 2.93e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 115 QTALHLAVVTEQPQMVERLLKAGCDPQLVDQSGNTALHLACKqgslacFSVLTQIQTqhLRSILTFPNYSG---HTCLHI 191
Cdd:PHA02875   3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMK------FRDSEAIKL--LMKHGAIPDVKYpdiESELHD 74

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922304323 192 AAINNYLSMVESLVQLGADVDAKEQCSGRTSLHLAVDLQNLDLVHTLIALGADANSLTYGGYTAYHL 258
Cdd:PHA02875  75 AVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHL 141
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 107-260 4.82e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.22  E-value: 4.82e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 107 LNRQNNQRQTALHLAVVTEQ-PQMVERLLKAGCDPQLVDQSGNTALHLACKQGslacfsvltqIQTQHLRSILTF----- 180
Cdd:PHA02876 266 VNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNG----------YDTENIRTLIMLgadvn 335

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 181 -PNYSGHTCLHIAA-INNYLSMVESLVQLGADVDAKEQCSgRTSLHLAVDLQNLDLVHTLIALGADANSLTYGGYTAYHL 258
Cdd:PHA02876 336 aADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCD-KTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHF 414


                 ..
gi 922304323 259 TF 260
Cdd:PHA02876 415 AL 416
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 116-249 5.90e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 50.37  E-value: 5.90e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 116 TALHLAVVTEQPQMVERLLKAGCDPQLVDQSGNTALHLACKQGSLAcfsvLTQIQTQHlRSILTFPNYSGHTCLHIAAIN 195
Cdd:PHA02875 104 TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK----GIELLIDH-KACLDIEDCCGCTPLIIAMAK 178

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 922304323 196 NYLSMVESLVQLGADVDAKEQCSGRTSLHLAVDLQNLDLVHTLIALGADANSLT 249
Cdd:PHA02875 179 GDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNIMF 232
PHA03095 PHA03095
ankyrin-like protein; Provisional
 127-278 6.33e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.41  E-value: 6.33e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 127 PQMVERLLKAGCDPQLVDQSGNTALH---LACKQgSLACFSVLTQiqtqhLRSILTFPNYSGHTCLHIAAINNYL--SMV 201
Cdd:PHA03095 167 VELLRLLIDAGADVYAVDDRFRSLLHhhlQSFKP-RARIVRELIR-----AGCDPAATDMLGNTPLHSMATGSSCkrSLV 240

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922304323 202 ESLVQLGADVDAKEQcSGRTSLHLAVDLQNLDLVHTLIALGADANSLTYGGYTAYHLTFGRHNSEIqrqlySRTALK 278
Cdd:PHA03095 241 LPLLIAGISINARNR-YGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRA-----VRAALA 311
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 130-217 7.92e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.05  E-value: 7.92e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 130 VERLLKAGCDPQLVDQSGNTALHLACKQGSLACFSVLTqiqtqHLRSILTFPNYSGHTCLHIAAINNYLSMVESLVQLGA 209
Cdd:PHA03100 175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLL-----DLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249


                 ....*...
gi 922304323 210 DVDAKEQC 217
Cdd:PHA03100 250 SIKTIIET 257
PHA03095 PHA03095
ankyrin-like protein; Provisional
 130-267 1.07e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.64  E-value: 1.07e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 130 VERLLKAGCDPQLVDQSGNTALHLACKQGSLACFSVLtqiqtqhlRSIL------TFPNYSGHTCLHIAAINNY-LSMVE 202
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIV--------RLLLeagadvNAPERCGFTPLHLYLYNATtLDVIK 101

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 922304323 203 SLVQLGADVDAKEQCsGRTSLH--LAVDLQNLDLVHTLIALGADANSLTYGGYTAYHLTFGRHNSEI 267
Cdd:PHA03095 102 LLIKAGADVNAKDKV-GRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANV 167
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 73-267 1.12e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.06  E-value: 1.12e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323  73 VVTEDGDTYLHLAIIHEAEDYAVQIIKqcqndpylNRQN-NQRQTALHLAVVTEQPQMVERLLKAGCDPQLVDQSGNTAL 151
Cdd:PHA02876 206 IIALDDLSVLECAVDSKNIDTIKAIID--------NRSNiNKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPL 277

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 152 HLACKQGSLAcfSVLTQIQTQHLRsiLTFPNYSGHTCLHIAAINNY-LSMVESLVQLGADVDAKEQCSgRTSLHLAVDL- 229
Cdd:PHA02876 278 HHASQAPSLS--RLVPKLLERGAD--VNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLY-ITPLHQASTLd 352

                        170       180       190
                 ....*....|....*....|....*....|....*...
gi 922304323 230 QNLDLVHTLIALGADANSLTYGGYTAYHLTFGRHNSEI 267
Cdd:PHA02876 353 RNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI 390
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 84-273 1.47e-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: 49.69  E-value: 1.47e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323   84 LAIIHEAEDYAVQIIKQCQNDPYLNRQNNQRQTALHLAVVTEQPQ-MVERLLKAGCDPQLvdqsGNTALHLACK---QGS 159
Cdd:TIGR00870  22 LPAAERGDLASVYRDLEEPKKLNINCPDRLGRSALFVAAIENENLeLTELLLNLSCRGAV----GDTLLHAISLeyvDAV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323  160 LACFSVLTQIQTQHLRSILTFPNYS-----GHTCLHIAAINNYLSMVESLVQLGADVDAKEQCS-------------GRT 221
Cdd:TIGR00870  98 EAILLHLLAAFRKSGPLELANDQYTseftpGITALHLAAHRQNYEIVKLLLERGASVPARACGDffvksqgvdsfyhGES 177

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323  222 SLHLAVDLQNLDLVHTLIALGAD---ANSLtygGYTAYHL-----TFGRHNSEIQRQLYS 273
Cdd:TIGR00870 178 PLNAAACLGSPSIVALLSEDPADiltADSL---GNTLLHLlvmenEFKAEYEELSCQMYN 234
Ank_5 pfam13857
Ankyrin repeats (many copies);
107-154 1.57e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 1.57e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*...
gi 922304323  107 LNRQNNQRQTALHLAVVTEQPQMVERLLKAGCDPQLVDQSGNTALHLA 154
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
116-166 1.75e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 1.75e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 922304323  116 TALHLAVVTEQPQMVERLLKAGCDPQLVDQSGNTALHLACKQGSLACFSVL 166
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 112-250 2.45e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.72  E-value: 2.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 112 NQRQTALHLAVVTEQPQMVERLLKAGCDPQLVDQSGNTALHLACKQGSLACFSVLTQ--IQTQHLrsiltfpNYSGHTCL 189
Cdd:PHA02878 166 HKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLEngASTDAR-------DKCGNTPL 238

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 922304323 190 HIAA--INNYlSMVESLVQLGADVDAKEQCSGRTSLHLAvdLQNLDLVHTLIALGADANSLTY 250
Cdd:PHA02878 239 HISVgyCKDY-DILKLLLEHGVDVNAKSYILGLTALHSS--IKSERKLKLLLEYGADINSLNS 298
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 147-249 2.95e-06

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: 48.72  E-value: 2.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 147 GNTALHLAC---KQGSLACFSVLTQI--QTQHLRSILTFPN----YSGHTCLHIAAINNYLSMVESLVQLGADVDA---- 213
Cdd:cd21882   26 GKTCLHKAAlnlNDGVNEAIMLLLEAapDSGNPKELVNAPCtdefYQGQTALHIAIENRNLNLVRLLVENGADVSAratg 105

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 922304323 214 ----KEQCS----GRTSLHLAVDLQNLDLVHTLIALGADANSLT 249
Cdd:cd21882  106 rffrKSPGNlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALE 149
PHA03095 PHA03095
ankyrin-like protein; Provisional
 107-154 7.82e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.94  E-value: 7.82e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*...
gi 922304323 107 LNRQNNQRQTALHLAVVTEQPQMVERLLKAGCDPQLVDQSGNTALHLA 154
Cdd:PHA03095 250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 73-210 1.05e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.52  E-value: 1.05e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323  73 VVTEDGDTYLHLAIIHEAEDYAVQIIKQcQNDPylNRQNNQRQTALHLAVVTEQPQMVERLLKAGCDPQLVDQSGNTALH 152
Cdd:PHA02875  97 VFYKDGMTPLHLATILKKLDIMKLLIAR-GADP--DIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLI 173

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 922304323 153 LACKQGSLACFSVLTQIQTQhlrsiltfPNYSGH----TCLHIAAINNYLSMVESLVQLGAD 210
Cdd:PHA02875 174 IAMAKGDIAICKMLLDSGAN--------IDYFGKngcvAALCYAIENNKIDIVRLFIKRGAD 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
71-144 1.11e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 43.18  E-value: 1.11e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 922304323   71 AKVVTEDGDTYLHLAIIHEAEDYAVQIIKQCQndpyLNRQNNQRqTALHLAVVTEQPQMVERLLKAGCDPQLVD 144
Cdd:pfam12796  23 ANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD----VNLKDNGR-TALHYAARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 91-257 1.69e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.11  E-value: 1.69e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323  91 EDYAVQIIKQCQNDpyLNRQNNQRQTALHLAVVTEQPQMVERLLKAGCDPQLVDQSGNTALHLACKQGSLACFSVLTQIQ 170
Cdd:PHA02874 103 EKDMIKTILDCGID--VNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKG 180

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 171 tqhlrSILTFPNYSGHTCLHIAAINNYLSMVESLVQLGADVDAKeqCS-GRTSLHLAVdLQNLDLVHTLIAlGADANSLT 249
Cdd:PHA02874 181 -----AYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNK--CKnGFTPLHNAI-IHNRSAIELLIN-NASINDQD 251


                 ....*...
gi 922304323 250 YGGYTAYH 257
Cdd:PHA02874 252 IDGSTPLH 259
Ank_4 pfam13637
Ankyrin repeats (many copies);
185-239 1.75e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 1.75e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 922304323  185 GHTCLHIAAINNYLSMVESLVQLGADVDAKEQCsGRTSLHLAVDLQNLDLVHTLI 239
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGN-GETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 118-267 2.36e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.64  E-value: 2.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 118 LHLAVVTEQPQMVERLLKAGCDPQLVDQSGNTALHLACKQGSLACFSVLTQIQTQ-----HLRSILTFPNYSGHTCLHIA 192
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKcsvfyTLVAIKDAFNNRNVEIFKII 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 193 AINNY---------------------LSMVESLVQLGADVDAKEQCSGRTSLHLAVDLQNLDLVHTLIALGADANSLTYG 251
Cdd:PHA02878 121 LTNRYkniqtidlvyidkkskddiieAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                        170
                 ....*....|....*.
gi 922304323 252 GYTAYHLTFGRHNSEI 267
Cdd:PHA02878 201 NNSPLHHAVKHYNKPI 216
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 107-247 1.91e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 1.91e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 107 LNRQNNQRQTALHL-AVVTEQPQMVERLLKAGCDPQLVDQSGNTALHlackQGSLACFSVLTQIQTQHLRSILTFPNYSG 185
Cdd:PHA02876 300 VNAKNIKGETPLYLmAKNGYDTENIRTLIMLGADVNAADRLYITPLH----QASTLDRNKDIVITLLELGANVNARDYCD 375

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 922304323 186 HTCLHIAAINNYLSMVESLVQLGADVDAKEQCSGrTSLHLAVDLQNLDL-VHTLIALGADANS 247
Cdd:PHA02876 376 KTPIHYAAVRNNVVIINTLLDYGADIEALSQKIG-TALHFALCGTNPYMsVKTLIDRGANVNS 437
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 185-214 2.22e-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: 2.22e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 922304323  185 GHTCLHIAAI-NNYLSMVESLVQLGADVDAK 214
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNAR 32
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 118-271 4.38e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.52  E-value: 4.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 118 LHLAVVTEQPQMVERLLKAGCDPQLVDQSGNTALHLACKQGSLacfsvltqIQTQHLRSILTFPN----YSGHTCLHIAA 193
Cdd:PHA02875  39 IKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV--------KAVEELLDLGKFADdvfyKDGMTPLHLAT 110

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 922304323 194 INNYLSMVESLVQLGADVDAKEqcSGRTS-LHLAVDLQNLDLVHTLIALGADANSLTYGGYTAYHLTFGRHNSEIQRQL 271
Cdd:PHA02875 111 ILKKLDIMKLLIARGADPDIPN--TDKFSpLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKML 187
Ank_5 pfam13857
Ankyrin repeats (many copies);
181-226 6.98e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 6.98e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 922304323  181 PNYSGHTCLHIAAINNYLSMVESLVQLGADVDAKEQCsGRTSLHLA 226
Cdd:pfam13857  12 LDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEE-GLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 185-213 7.97e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 7.97e-04
                           10        20
                   ....*....|....*....|....*....
gi 922304323   185 GHTCLHIAAINNYLSMVESLVQLGADVDA 213
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 185-213 1.16e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.70  E-value: 1.16e-03
                          10        20
                  ....*....|....*....|....*....
gi 922304323  185 GHTCLHIAAINNYLSMVESLVQLGADVDA 213
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 182-247 1.99e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.88  E-value: 1.99e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 922304323 182 NYSGHTCLHIAAINNYLSMVESLVQLGADVDAKEQcSGRTSLHLAV-----DLQNLDLVHTLIALGADANS 247
Cdd:PTZ00322 112 DYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDK-DGKTPLELAEengfrEVVQLLSRHSQCHFELGANA 181
PHA03095 PHA03095
ankyrin-like protein; Provisional
 116-257 2.97e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.85  E-value: 2.97e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 116 TALHLAVV--TEQPqMVERLLKAGCDPQLVDQSGNTALHlackqgslACFSVLTqIQTQHLRSILTF------PNYSGHT 187
Cdd:PHA03095  85 TPLHLYLYnaTTLD-VIKLLIKAGADVNAKDKVGRTPLH--------VYLSGFN-INPKVIRLLLRKgadvnaLDLYGMT 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 922304323 188 CLHIAAINN--YLSMVESLVQLGADVDAKEQCsGRTSLHlaVDLQNL----DLVHTLIALGADANSLTYGGYTAYH 257
Cdd:PHA03095 155 PLAVLLKSRnaNVELLRLLIDAGADVYAVDDR-FRSLLH--HHLQSFkpraRIVRELIRAGCDPAATDMLGNTPLH 227
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 219-246 3.93e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.16  E-value: 3.93e-03
                          10        20
                  ....*....|....*....|....*...
gi 922304323  219 GRTSLHLAVDLQNLDLVHTLIALGADAN 246
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 100-254 6.55e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.12  E-value: 6.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 100 QCQND--PYlnrqnnqrqTALHLAVVTEQPQMVERLLKAgcDPQLV---DQSGNTALHLACKQGSLACFSVLTQIQTQHL 174
Cdd:PHA02876  34 QCENEsiPF---------TAIHQALQLRQIDIVEEIIQQ--NPELIyitDHKCHSTLHTICIIPNVMDIVISLTLDCDII 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 175 -----RSILTFPNYSGHTCLHIAA------------IN---------------NYLSMVESLVQLGADVDAKEQCSgRTS 222
Cdd:PHA02876 103 ldikyASIILNKHKLDEACIHILKeaisgndihydkINesieymklikeriqqDELLIAEMLLEGGADVNAKDIYC-ITP 181

                        170       180       190
                 ....*....|....*....|....*....|..
gi 922304323 223 LHLAVDLQNLDLVHTLIALGADANSLTYGGYT 254
Cdd:PHA02876 182 IHYAAERGNAKMVNLLLSYGADVNIIALDDLS 213
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 115-158 7.17e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 37.96  E-value: 7.17e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 922304323 115 QTALHLAVVTEQPQMVERLLKAGCDPQLVDQSGNTALHLACKQG 158
Cdd:PTZ00322 116 RTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 87-265 7.45e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 37.64  E-value: 7.45e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323  87 IHEAEDYAVQ-IIKQCQNdpYLNRQNNQRQTALHLAVVTEQPQMVERLLKAGCDPQLVDQSGNTALHLACKQGSLACFSV 165
Cdd:PHA02874   9 IYSGDIEAIEkIIKNKGN--CINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKL 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 922304323 166 LtqIQTQHLRSILTFPNysghtclhiaaINNylSMVESLVQLGADVDAKEQCSgRTSLHLAVDLQNLDLVHTLIALGADA 245
Cdd:PHA02874  87 L--IDNGVDTSILPIPC-----------IEK--DMIKTILDCGIDVNIKDAEL-KTFLHYAIKKGDLESIKMLFEYGADV 150

                        170       180
                 ....*....|....*....|
gi 922304323 246 NSLTYGGYTAYHLTFgRHNS 265
Cdd:PHA02874 151 NIEDDNGCYPIHIAI-KHNF 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
219-257 8.56e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.17  E-value: 8.56e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 922304323  219 GRTSLHLAVDLQNLDLVHTLIALGADANSLTYGGYTAYH 257
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALH 39
 
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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