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Conserved domains on  [gi|407728603|ref|NP_001258396|]
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GA-binding protein subunit beta-1 isoform a [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-179 2.16e-45

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.81  E-value: 2.16e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 88
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  89 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQNQINTNP 168
Cdd:COG0666  171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                        170
                 ....*....|.
gi 407728603 169 ESPDTVTIHAA 179
Cdd:COG0666  251 DGLTALLLAAA 261
Oberon_cc super family cl24780
Coiled-coil region of Oberon; Oberon_cc is the coiled-coil region of Oberon proteins from ...
 315-369 6.02e-03

Coiled-coil region of Oberon; Oberon_cc is the coiled-coil region of Oberon proteins from plants. Oberon is necessary for maintenance and/or establishment of both the shoot and root apical meristems in Arabidopsis. Most Oberon proteins carry a PHD finger domain, pfam07227 and this coiled-coil domain. Oberon proteins mediate the TMO7 (the direct target of MP) expression through modification of, or binding to, chromatin at the TMO7 locus. TMO7 stands for the target of Monopteros 7 (or Auxin response factor 7).


The actual alignment was detected with superfamily member pfam16312:

Pssm-ID: 465089 [Multi-domain]  Cd Length: 129  Bit Score: 36.50  E-value: 6.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407728603  315 KRQCMEIIESRVECAEIEErEALQKQLDEANREAQKYRQQLLKKE----------------QEAEAYRQKL 369
Cdd:pfam16312  31 KKQQIEELESIVRLKQAEA-EMFQLKADEARREAEGLQRIALAKSekseeeyasrylklrlEEAEEERRYK 100
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-179 2.16e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.81  E-value: 2.16e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 88
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  89 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQNQINTNP 168
Cdd:COG0666  171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                        170
                 ....*....|.
gi 407728603 169 ESPDTVTIHAA 179
Cdd:COG0666  251 DGLTALLLAAA 261
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-133 1.12e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 99.03  E-value: 1.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603   42 LHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHgADVNAKDMlKMTALHWATEHNHQEVVE 121
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 407728603  122 LLIKYGADVHTQ 133
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 20-143 7.80e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.69  E-value: 7.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  20 DEVRILMANGAPF-TTDWLGTSPLHLaaqYGHFSTTE----VLLRAGVSRDARTKVDRTPLHMAAS--EGHANIVEVLLK 92
Cdd:PHA03095  64 DIVRLLLEAGADVnAPERCGFTPLHL---YLYNATTLdvikLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLR 140

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 407728603  93 HGADVNAKDMLKMTALHWATEhNHQ---EVVELLIKYGADVHTQSKFCKTAFDI 143
Cdd:PHA03095 141 KGADVNALDLYGMTPLAVLLK-SRNanvELLRLLIDAGADVYAVDDRFRSLLHH 193
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 10-181 7.10e-11

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: 63.49  E-value: 7.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  10 LLEAARAGQDDEVRILMANGA--PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAgvsrdARTKVD----------RTPLHM 77
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKCPScdLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  78 AASEGHANIVEVLLKHGADVNAKD------MLKMTALHWATEH--------NHQEVVELLIKYGADVHTQSKFCKTAFDI 143
Cdd:cd22192   96 AVVNQNLNLVRELIARGADVVSPRatgtffRPGPKNLIYYGEHplsfaacvGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 407728603 144 SIDNGNEDLA-EILQIAMQNQINTNPESPDTVTIHAA-TP 181
Cdd:cd22192  176 LVLQPNKTFAcQMYDLILSYDKEDDLQPLDLVPNNQGlTP 215
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 71-99 7.11e-08

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: 47.97  E-value: 7.11e-08
                           10        20
                   ....*....|....*....|....*....
gi 407728603    71 DRTPLHMAASEGHANIVEVLLKHGADVNA 99
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 2-139 3.94e-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: 48.92  E-value: 3.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603    2 SLVDLGKKLLEAARAGQDDEVRILMANGAPF---TTDWLGTSPLHLAAQYG-HFSTTEVLLragvSRDARTKVDRTPLHm 77
Cdd:TIGR00870  13 PLSDEEKAFLPAAERGDLASVYRDLEEPKKLninCPDRLGRSALFVAAIENeNLELTELLL----NLSCRGAVGDTLLH- 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407728603   78 AASEGHANIVEVLLKHGADVNAKDMLK--------------MTALHWATEHNHQEVVELLIKYGADVHTQSK--FCKT 139
Cdd:TIGR00870  88 AISLEYVDAVEAILLHLLAAFRKSGPLelandqytseftpgITALHLAAHRQNYEIVKLLLERGASVPARACgdFFVK 165
Oberon_cc pfam16312
Coiled-coil region of Oberon; Oberon_cc is the coiled-coil region of Oberon proteins from ...
 315-369 6.02e-03

Coiled-coil region of Oberon; Oberon_cc is the coiled-coil region of Oberon proteins from plants. Oberon is necessary for maintenance and/or establishment of both the shoot and root apical meristems in Arabidopsis. Most Oberon proteins carry a PHD finger domain, pfam07227 and this coiled-coil domain. Oberon proteins mediate the TMO7 (the direct target of MP) expression through modification of, or binding to, chromatin at the TMO7 locus. TMO7 stands for the target of Monopteros 7 (or Auxin response factor 7).


Pssm-ID: 465089 [Multi-domain]  Cd Length: 129  Bit Score: 36.50  E-value: 6.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407728603  315 KRQCMEIIESRVECAEIEErEALQKQLDEANREAQKYRQQLLKKE----------------QEAEAYRQKL 369
Cdd:pfam16312  31 KKQQIEELESIVRLKQAEA-EMFQLKADEARREAEGLQRIALAKSekseeeyasrylklrlEEAEEERRYK 100
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-179 2.16e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.81  E-value: 2.16e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 88
Cdd:COG0666   91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  89 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQNQINTNP 168
Cdd:COG0666  171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                        170
                 ....*....|.
gi 407728603 169 ESPDTVTIHAA 179
Cdd:COG0666  251 DGLTALLLAAA 261
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-156 2.23e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.93  E-value: 2.23e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  10 LLEAARAGQDDEVRILMANGAP-FTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 88
Cdd:COG0666   58 LLAAALAGDLLVALLLLAAGADiNAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407728603  89 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL 156
Cdd:COG0666  138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-167 3.18e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 3.18e-36
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 88
Cdd:COG0666  124 LHLAAYNGNLEIVKLLLEAGAdVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407728603  89 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQNQINTN 167
Cdd:COG0666  204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-156 9.25e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.81  E-value: 9.25e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  10 LLEAARAGQDDEVRILMANGAPFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEV 89
Cdd:COG0666   26 LAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKL 105

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 407728603  90 LLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL 156
Cdd:COG0666  106 LLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-133 1.12e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 99.03  E-value: 1.12e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603   42 LHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHgADVNAKDMlKMTALHWATEHNHQEVVE 121
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 407728603  122 LLIKYGADVHTQ 133
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-101 2.33e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.09  E-value: 2.33e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603   10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDarTKVDRTPLHMAASEGHANIVE 88
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 407728603   89 VLLKHGADVNAKD 101
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 20-143 7.80e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.69  E-value: 7.80e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  20 DEVRILMANGAPF-TTDWLGTSPLHLaaqYGHFSTTE----VLLRAGVSRDARTKVDRTPLHMAAS--EGHANIVEVLLK 92
Cdd:PHA03095  64 DIVRLLLEAGADVnAPERCGFTPLHL---YLYNATTLdvikLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLR 140

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 407728603  93 HGADVNAKDMLKMTALHWATEhNHQ---EVVELLIKYGADVHTQSKFCKTAFDI 143
Cdd:PHA03095 141 KGADVNALDLYGMTPLAVLLK-SRNanvELLRLLIDAGADVYAVDDRFRSLLHH 193
Ank_2 pfam12796
Ankyrin repeats (3 copies);
75-156 4.28e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 4.28e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603   75 LHMAASEGHANIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYgADVHTQSKFcKTAFDISIDNGNEDLAE 154
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78


                  ..
gi 407728603  155 IL 156
Cdd:pfam12796  79 LL 80
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 22-168 8.52e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.17  E-value: 8.52e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  22 VRILMANGAPFT-TDWLGTSPLHLAAQY--GHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHA--NIVEVLLKHGAD 96
Cdd:PHA03100  89 VKLLLEYGANVNaPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVD 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  97 ----------------VNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEdlaEILQIAM 160
Cdd:PHA03100 169 inaknrvnyllsygvpINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK---EIFKLLL 245


                 ....*...
gi 407728603 161 QNQINTNP 168
Cdd:PHA03100 246 NNGPSIKT 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-156 5.76e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.61  E-value: 5.76e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  24 ILMANGAPFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHGADVNAKDML 103
Cdd:COG0666    7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 407728603 104 KMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL 156
Cdd:COG0666   87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
PHA03095 PHA03095
ankyrin-like protein; Provisional
 22-174 2.90e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.82  E-value: 2.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  22 VRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTT--EVLLRAGVSRDARTKVDRTPLHMAA--SEGHANIVEVLLKHGAD 96
Cdd:PHA03095 170 LRLLIDAGAdVYAVDDRFRSLLHHHLQSFKPRARivRELIRAGCDPAATDMLGNTPLHSMAtgSSCKRSLVLPLLIAGIS 249

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407728603  97 VNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDlaeilqiAMQNQINTNPeSPDTV 174
Cdd:PHA03095 250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGR-------AVRAALAKNP-SAETV 319
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 23-167 1.14e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.92  E-value: 1.14e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  23 RILMANGAPFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHA-----NIVEVLLKHGADV 97
Cdd:PHA03100  20 YIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANV 99

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 407728603  98 NAKDMLKMTALHWA--TEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLaEILQIAMQNQINTN 167
Cdd:PHA03100 100 NAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDL-KILKLLIDKGVDIN 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
72-124 4.78e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 4.78e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 407728603   72 RTPLHMAASEGHANIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLI 124
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 34-162 5.02e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.59  E-value: 5.02e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  34 TDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHGADVNAKDMLKMTALHWATE 113
Cdd:PLN03192 521 DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAIS 600

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 407728603 114 HNHQEVVELLIKYGA--DVHTQSK-FCKTA-------------FDISIDNGNEDLAEILQIAMQN 162
Cdd:PLN03192 601 AKHHKIFRILYHFASisDPHAAGDlLCTAAkrndltamkellkQGLNVDSEDHQGATALQVAMAE 665
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 22-176 7.12e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 66.44  E-value: 7.12e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  22 VRILMANGAPFT--TDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHGADVNA 99
Cdd:PHA02878 150 TKLLLSYGADINmkDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603 100 KDMLKMTALHWATEH-NHQEVVELLIKYGADVHTQSKFCK-TAFDISIDNgNEDLAEILQI-AMQNQINTNPESPDTVTI 176
Cdd:PHA02878 230 RDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGlTALHSSIKS-ERKLKLLLEYgADINSLNSYKLTPLSSAV 308
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 10-181 7.10e-11

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: 63.49  E-value: 7.10e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  10 LLEAARAGQDDEVRILMANGA--PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAgvsrdARTKVD----------RTPLHM 77
Cdd:cd22192   21 LLLAAKENDVQAIKKLLKCPScdLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHI 95

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  78 AASEGHANIVEVLLKHGADVNAKD------MLKMTALHWATEH--------NHQEVVELLIKYGADVHTQSKFCKTAFDI 143
Cdd:cd22192   96 AVVNQNLNLVRELIARGADVVSPRatgtffRPGPKNLIYYGEHplsfaacvGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 407728603 144 SIDNGNEDLA-EILQIAMQNQINTNPESPDTVTIHAA-TP 181
Cdd:cd22192  176 LVLQPNKTFAcQMYDLILSYDKEDDLQPLDLVPNNQGlTP 215
PHA03095 PHA03095
ankyrin-like protein; Provisional
 57-156 2.16e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 61.96  E-value: 2.16e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  57 LLRAGVSRDARTKVDRTPLHM---AASEGHANIVEVLLKHGADVNAKDMLKMTALHWATEHNHQE-VVELLIKYGADVHT 132
Cdd:PHA03095  33 LLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNA 112

                         90       100
                 ....*....|....*....|....*.
gi 407728603 133 QSKFCKTAFDI--SIDNGNEDLAEIL 156
Cdd:PHA03095 113 KDKVGRTPLHVylSGFNINPKVIRLL 138
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 38-169 3.99e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 61.62  E-value: 3.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  38 GTSPLHLAAQYGHFS-TTEVLLRAGVSRDARTKVDRTPLHMAAS-EGHANIVEVLLKHGADVNAKDMLKMTALHWATEHN 115
Cdd:PHA02876 307 GETPLYLMAKNGYDTeNIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRN 386

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 407728603 116 HQEVVELLIKYGADVHTQSKFCKTAFDIS-------------IDNG------NEDLAEILQIAMQNqiNTNPE 169
Cdd:PHA02876 387 NVVIINTLLDYGADIEALSQKIGTALHFAlcgtnpymsvktlIDRGanvnskNKDLSTPLHYACKK--NCKLD 457
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 43-131 7.46e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.68  E-value: 7.46e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  43 HLAAQyGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVEL 122
Cdd:PTZ00322  88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                 ....*....
gi 407728603 123 LIKYGADVH 131
Cdd:PTZ00322 167 LSRHSQCHF 175
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 5-156 8.94e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.00  E-value: 8.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603   5 DLGKKLLEAARAGQDDEVRILMANGApFTTDWL---GTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASE 81
Cdd:PHA02875  67 DIESELHDAVEEGDVKAVEELLDLGK-FADDVFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMM 145

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 407728603  82 GHANIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKF-CKTAFDISIDNGNEDLAEIL 156
Cdd:PHA02875 146 GDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLF 221
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 10-149 1.22e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.59  E-value: 1.22e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  10 LLEAARAGQDDEVRILMANGapfttdwLGTSPLHLAAQygHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEV 89
Cdd:PHA02874  72 LLTAIKIGAHDIIKLLIDNG-------VDTSILPIPCI--EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKM 142

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  90 LLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGN 149
Cdd:PHA02874 143 LFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGD 202
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-108 1.71e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.43  E-value: 1.71e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVE 88
Cdd:COG0666  190 LHLAAENGHLEIVKLLLEAGAdVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269

                         90       100
                 ....*....|....*....|
gi 407728603  89 VLLKHGADVNAKDMLKMTAL 108
Cdd:COG0666  270 LLLLALLLLAAALLDLLTLL 289
Ank_5 pfam13857
Ankyrin repeats (many copies);
90-143 1.80e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.12  E-value: 1.80e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 407728603   90 LLKHG-ADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDI 143
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 86-167 2.75e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.92  E-value: 2.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  86 IVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILqIAMQNQIN 165
Cdd:PHA02876 160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAI-IDNRSNIN 238


                 ..
gi 407728603 166 TN 167
Cdd:PHA02876 239 KN 240
Ank_4 pfam13637
Ankyrin repeats (many copies);
38-91 3.48e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.28  E-value: 3.48e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 407728603   38 GTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLL 91
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 70-156 4.73e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.99  E-value: 4.73e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  70 VDRTPLHMAASE-------GHANIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFD 142
Cdd:PTZ00322  74 IDPVVAHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153

                         90
                 ....*....|....
gi 407728603 143 ISIDNGNEDLAEIL 156
Cdd:PTZ00322 154 LAEENGFREVVQLL 167
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 73-180 6.47e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.37  E-value: 6.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  73 TPLHMAASEGHANIVEVLLKHGADVNAKDMLKMTALHWATEHNH-----QEVVELLIKYGADVHTQSKFCKTAFDISIDN 147
Cdd:PHA03100  37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISK 116

                         90       100       110
                 ....*....|....*....|....*....|....
gi 407728603 148 GNEDLaEILQIAMQNQINTNPESPDTVT-IHAAT 180
Cdd:PHA03100 117 KSNSY-SIVEYLLDNGANVNIKNSDGENlLHLYL 149
Ank_4 pfam13637
Ankyrin repeats (many copies);
105-156 7.62e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 7.62e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 407728603  105 MTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL 156
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 6-93 1.73e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 1.73e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603   6 LGKKLLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHA 84
Cdd:PTZ00322  82 LTVELCQLAASGDAVGARILLTGGAdPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161


                 ....*....
gi 407728603  85 NIVEVLLKH 93
Cdd:PTZ00322 162 EVVQLLSRH 170
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 20-129 2.14e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.77  E-value: 2.14e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  20 DEVRILMANGA-PFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHGADVN 98
Cdd:PHA02875 116 DIMKLLIARGAdPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195

                         90       100       110
                 ....*....|....*....|....*....|..
gi 407728603  99 -AKDMLKMTALHWATEHNHQEVVELLIKYGAD 129
Cdd:PHA02875 196 yFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 72-101 2.76e-08

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 49.21  E-value: 2.76e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 407728603   72 RTPLHMAA-SEGHANIVEVLLKHGADVNAKD 101
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 24-130 6.37e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.49  E-value: 6.37e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  24 ILMANGAPFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEV-------------- 89
Cdd:PLN03192 544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRIlyhfasisdphaag 623

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 407728603  90 -----------------LLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADV 130
Cdd:PLN03192 624 dllctaakrndltamkeLLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 71-99 7.11e-08

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: 47.97  E-value: 7.11e-08
                           10        20
                   ....*....|....*....|....*....
gi 407728603    71 DRTPLHMAASEGHANIVEVLLKHGADVNA 99
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 38-156 7.25e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.84  E-value: 7.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  38 GTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLL---KHGADVNAKDmlKMTALHWATEH 114
Cdd:PHA02875  35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLdlgKFADDVFYKD--GMTPLHLATIL 112

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 407728603 115 NHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL 156
Cdd:PHA02875 113 KKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 47-152 1.48e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.53  E-value: 1.48e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  47 QYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKY 126
Cdd:PHA02876 154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDN 233

                         90       100
                 ....*....|....*....|....*...
gi 407728603 127 GADVHTQskfcktafDISIDNG--NEDL 152
Cdd:PHA02876 234 RSNINKN--------DLSLLKAirNEDL 253
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 13-124 4.45e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.50  E-value: 4.45e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  13 AARAGQDDEVRILMANGAPFTT-DWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLL 91
Cdd:PHA02874 131 AIKKGDLESIKMLFEYGADVNIeDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210

                         90       100       110
                 ....*....|....*....|....*....|...
gi 407728603  92 KHGADVNAKDMLKMTALHWATEHNhQEVVELLI 124
Cdd:PHA02874 211 DHGNHIMNKCKNGFTPLHNAIIHN-RSAIELLI 242
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 72-99 1.62e-06

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 44.17  E-value: 1.62e-06
                          10        20
                  ....*....|....*....|....*...
gi 407728603   72 RTPLHMAASEGHANIVEVLLKHGADVNA 99
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
57-111 1.77e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 1.77e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 407728603   57 LLRAG-VSRDARTKVDRTPLHMAASEGHANIVEVLLKHGADVNAKDMLKMTALHWA 111
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 2-139 3.94e-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: 48.92  E-value: 3.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603    2 SLVDLGKKLLEAARAGQDDEVRILMANGAPF---TTDWLGTSPLHLAAQYG-HFSTTEVLLragvSRDARTKVDRTPLHm 77
Cdd:TIGR00870  13 PLSDEEKAFLPAAERGDLASVYRDLEEPKKLninCPDRLGRSALFVAAIENeNLELTELLL----NLSCRGAVGDTLLH- 87

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407728603   78 AASEGHANIVEVLLKHGADVNAKDMLK--------------MTALHWATEHNHQEVVELLIKYGADVHTQSK--FCKT 139
Cdd:TIGR00870  88 AISLEYVDAVEAILLHLLAAFRKSGPLelandqytseftpgITALHLAAHRQNYEIVKLLLERGASVPARACgdFFVK 165
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 20-131 4.11e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.91  E-value: 4.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  20 DEVRILMANGAPFTT-DWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANI-VEVLLKHGADV 97
Cdd:PHA02876 356 DIVITLLELGANVNArDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANV 435

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 407728603  98 NAKDMLKMTALHWATEHNHQ-EVVELLIKYGADVH 131
Cdd:PHA02876 436 NSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVN 470
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 105-131 4.84e-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: 42.96  E-value: 4.84e-06
                           10        20
                   ....*....|....*....|....*..
gi 407728603   105 MTALHWATEHNHQEVVELLIKYGADVH 131
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 6-109 6.41e-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: 48.09  E-value: 6.41e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603   6 LGKKLLEAARAGQDDEVRILMANGAP------FTTD-WLGTSPLHLAAQYGHFSTTEVLLRAGV--------------SR 64
Cdd:cd22192   50 LGETALHVAALYDNLEAAVVLMEAAPelvnepMTSDlYQGETALHIAVVNQNLNLVRELIARGAdvvspratgtffrpGP 129

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 407728603  65 DARTKVDRTPLHMAASEGHANIVEVLLKHGADVNAKDMLKMTALH 109
Cdd:cd22192  130 KNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 20-101 1.30e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.97  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  20 DEVRILMANGAPF-TTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHGADVN 98
Cdd:PHA03100 173 NRVNYLLSYGVPInIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252


                 ...
gi 407728603  99 AKD 101
Cdd:PHA03100 253 TII 255
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 105-135 1.31e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.51  E-value: 1.31e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 407728603  105 MTALHWATEH-NHQEVVELLIKYGADVHTQSK 135
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02946 PHA02946
ankyin-like protein; Provisional
 55-131 2.45e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.20  E-value: 2.45e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 407728603  55 EVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHGADVNAKDMLKMTALHW--ATEHNHQEVVELLIKYGADVH 131
Cdd:PHA02946  56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKIN 134
PHA03095 PHA03095
ankyrin-like protein; Provisional
 77-150 3.57e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.40  E-value: 3.57e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 407728603  77 MAASEGHANIVEVLLKHGADVNAKDMLKMTALHWATEHNHQ---EVVELLIKYGADVHTQSKFCKTAFDISIDNGNE 150
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATT 96
PHA02741 PHA02741
hypothetical protein; Provisional
 75-157 3.89e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 43.88  E-value: 3.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  75 LHMAAsEGH-----ANIVEVLLKHGADVNAKDMLK-MTALHWAT-EHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDN 147
Cdd:PHA02741  64 IHIAA-EKHeaqlaAEIIDHLIELGADINAQEMLEgDTALHLAAhRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAIDN 142

                         90
                 ....*....|
gi 407728603 148 GNEDLAEILQ 157
Cdd:PHA02741 143 EDVAMMQILR 152
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 42-141 6.52e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.57  E-value: 6.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  42 LHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVE 121
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                         90       100
                 ....*....|....*....|
gi 407728603 122 LLIKYGADVHTQskfCKTAF 141
Cdd:PHA02874 208 LLIDHGNHIMNK---CKNGF 224
PHA02798 PHA02798
ankyrin-like protein; Provisional
 85-167 1.38e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 43.67  E-value: 1.38e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  85 NIVEVLLKHGADVNAKDMLKMTALHWATEH---NHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQ 161
Cdd:PHA02798  90 DIVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHIDIEIIKLLLE 169


                 ....*.
gi 407728603 162 NQINTN 167
Cdd:PHA02798 170 KGVDIN 175
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 66-156 1.39e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 43.43  E-value: 1.39e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  66 ARTKVDRTPLHMAASEGH-ANIVEVLLKHGADVNAK----DMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCK-T 139
Cdd:PHA02884  27 KKNKICIANILYSSIKFHyTDIIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiT 106

                         90
                 ....*....|....*..
gi 407728603 140 AFDISIDNGNEDLAEIL 156
Cdd:PHA02884 107 PLYISVLHGCLKCLEIL 123
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-58 1.43e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 1.43e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 407728603   10 LLEAARAGQDDEVRILMANGAPF-TTDWLGTSPLHLAAQYGHFSTTEVLL 58
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADInAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 37-130 2.44e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 2.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  37 LGTSpLHLAAqYGH--FSTTEVLLRAGVSRDARTKVDRTPLHMAASEG-HANIVEVLLKHGADVNAKDMLKMTALHWATE 113
Cdd:PHA02876 408 IGTA-LHFAL-CGTnpYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALE 485

                         90
                 ....*....|....*..
gi 407728603 114 HNhqEVVELLIKYGADV 130
Cdd:PHA02876 486 YH--GIVNILLHYGAEL 500
Ank_5 pfam13857
Ankyrin repeats (many copies);
30-78 2.85e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 2.85e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 407728603   30 APFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMA 78
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 54-162 4.95e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.13  E-value: 4.95e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  54 TEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLL---KHGADVNAKDMLKMTALHWATEHNHQ---EVVELLIKYG 127
Cdd:PHA02798  92 VKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKG 171

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 407728603 128 ADVHTQS-KFCKTAFDISID-NGNEDLAEILQIAMQN 162
Cdd:PHA02798 172 VDINTHNnKEKYDTLHCYFKyNIDRIDADILKLFVDN 208
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 73-171 7.32e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.49  E-value: 7.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  73 TPLHMAASEGHANIVEVLLKHGADVN-----------------AKDMLKM------------------------------ 105
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINhintkiphplltaikigAHDIIKLlidngvdtsilpipciekdmiktildcgid 116

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 407728603 106 ---------TALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL--QIAMQNQINTNPESP 171
Cdd:PHA02874 117 vnikdaelkTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLleKGAYANVKDNNGESP 193
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 51-139 8.11e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.59  E-value: 8.11e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  51 FSTTEVLLRAGVSRDARTKVDRTPLHMAA-SEGHANIVEVLLKHGADVNAKDMLKMTALHWATEHNHQ-EVVELLIKYGA 128
Cdd:PHA02876 253 LETSLLLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGA 332

                         90
                 ....*....|.
gi 407728603 129 DVHTQSKFCKT 139
Cdd:PHA02876 333 DVNAADRLYIT 343
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 105-132 8.96e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.47  E-value: 8.96e-04
                          10        20
                  ....*....|....*....|....*...
gi 407728603  105 MTALHWATEHNHQEVVELLIKYGADVHT 132
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 46-130 1.31e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 41.05  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  46 AQYGHFSTTEVLLRAGVSRDARTKVDRTPLH--MAASEGHANIVEVLLKHGADVNAKDMLKMTALH-----------WAT 112
Cdd:PHA02716 292 ARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvvniLDP 371

                         90       100
                 ....*....|....*....|.
gi 407728603 113 EHNHQ---EVVELLIKYGADV 130
Cdd:PHA02716 372 ETDNDirlDVIQCLISLGADI 392
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 38-69 2.13e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 2.13e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 407728603   38 GTSPLHLAA-QYGHFSTTEVLLRAGVSRDARTK 69
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02798 PHA02798
ankyrin-like protein; Provisional
 85-149 2.23e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.82  E-value: 2.23e-03
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 407728603  85 NIVEVLLKHgADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGN 149
Cdd:PHA02798 240 NILDFIFSY-IDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINIITELGNTCLFTAFENES 303
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 73-149 2.31e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.03  E-value: 2.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  73 TPLHMAASEGHAN--IVEVLLKHGADVNAKDM-LKMTALHWATEHN---HQEVVELLIKYGADVHTQSKFCKTAFDISID 146
Cdd:PHA02859  53 TPIFSCLEKDKVNveILKFLIENGADVNFKTRdNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHMYMC 132


                 ...
gi 407728603 147 NGN 149
Cdd:PHA02859 133 NFN 135
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 86-177 2.50e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.65  E-value: 2.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  86 IVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGN--EDLAEILQIAMQNq 163
Cdd:PHA03100  17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnlTDVKEIVKLLLEY- 95

                         90
                 ....*....|....
gi 407728603 164 iNTNPESPDTVTIH 177
Cdd:PHA03100  96 -GANVNAPDNNGIT 108
PHA02791 PHA02791
ankyrin-like protein; Provisional
 18-125 3.05e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 39.25  E-value: 3.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 407728603  18 QDDEVRILMANGAPFTTDWLGTSPLHLAAQYGHFSTTEVLLRAGVSRDARTkvDRTPLHMAASEGHANIVEVLLKHGADV 97
Cdd:PHA02791  10 KSKQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLE--NEFPLHQAATLEDTKIVKILLFSGMDD 87

                         90       100
                 ....*....|....*....|....*...
gi 407728603  98 NAKDMLKMTALHWATEHNHQEVVELLIK 125
Cdd:PHA02791  88 SQFDDKGNTALYYAVDSGNMQTVKLFVK 115
Oberon_cc pfam16312
Coiled-coil region of Oberon; Oberon_cc is the coiled-coil region of Oberon proteins from ...
 315-369 6.02e-03

Coiled-coil region of Oberon; Oberon_cc is the coiled-coil region of Oberon proteins from plants. Oberon is necessary for maintenance and/or establishment of both the shoot and root apical meristems in Arabidopsis. Most Oberon proteins carry a PHD finger domain, pfam07227 and this coiled-coil domain. Oberon proteins mediate the TMO7 (the direct target of MP) expression through modification of, or binding to, chromatin at the TMO7 locus. TMO7 stands for the target of Monopteros 7 (or Auxin response factor 7).


Pssm-ID: 465089 [Multi-domain]  Cd Length: 129  Bit Score: 36.50  E-value: 6.02e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 407728603  315 KRQCMEIIESRVECAEIEErEALQKQLDEANREAQKYRQQLLKKE----------------QEAEAYRQKL 369
Cdd:pfam16312  31 KKQQIEELESIVRLKQAEA-EMFQLKADEARREAEGLQRIALAKSekseeeyasrylklrlEEAEEERRYK 100
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 42-99 6.05e-03

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 38.70  E-value: 6.05e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 407728603  42 LHLAAQYGHFSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHANIVEVLLKHGADVNA 99
Cdd:PLN03192 626 LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
CREPT pfam16566
Cell-cycle alteration and expression-elevated protein in tumour; CREPT (Cell-cycle alteration ...
 329-377 7.70e-03

Cell-cycle alteration and expression-elevated protein in tumour; CREPT (Cell-cycle alteration and expression-elevated protein in tumour) is a family of eukaryotic transcriptional regulators that ptromote the binding of RNA-polymerase to the CYCLIN D1, CCDN1, promoter and other genes involved in the cell-cycle. It promotes the formation of a chromatin loop in the CYCLIN D1 gene, and is preferentially expressed in a range of different human tumours.


Pssm-ID: 465181 [Multi-domain]  Cd Length: 147  Bit Score: 36.44  E-value: 7.70e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 407728603  329 AEIEEREALQKQLDEAnreAQKYRQQLLKKEQEAEAYRQKLEAMTRIQT 377
Cdd:pfam16566  69 AELEDRKKVAQMLRDF---LQLQKELLAQAEERLEEYKEKLEKVSQVRK 114
Stathmin pfam00836
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ...
 293-370 9.40e-03

Stathmin family; The Stathmin family of proteins play an important role in the regulation of the microtubule cytoskeleton. They regulate microtubule dynamics by promoting depolymerization of microtubules and/or preventing polymerization of tubulin heterodimers.


Pssm-ID: 459956 [Multi-domain]  Cd Length: 136  Bit Score: 36.17  E-value: 9.40e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 407728603  293 QVLTVPATDIAEETVISEEPPAKRQCMEIIESRVECAEiEEREALqkqldeanrEAQKYRQQLLKKEQEAEAYRQKLE 370
Cdd:pfam00836  18 EVILKPPSVNAAPPKLSLSPKKKDSSLEEIQKKLEAAE-ERRKSL---------EAQKLKQLAEKREKEEEALQKADE 85
 
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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