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Conserved domains on  [gi|2462543509|ref|XP_054233630|]
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GA-binding protein subunit beta-1 isoform X1 [Homo sapiens]

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];
34-203 7.28e-46

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.12  E-value: 7.28e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  34 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVE 112
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509 113 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQNQINTNP 192
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         170
                  ....*....|.
gi 2462543509 193 ESPDTVTIHAA 203
Cdd:COG0666   251 DGLTALLLAAA 261
ERM_helical super family cl48646
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 365-411 5.98e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


The actual alignment was detected with superfamily member pfam20492:

Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 36.43  E-value: 5.98e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2462543509 365 SAEIEEREALQKQLDEANREAQKYRQQLLKKEQEAEAYRQKLEAMTR 411
Cdd:pfam20492  72 EMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEARE 118
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
34-203 7.28e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.12  E-value: 7.28e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  34 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVE 112
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509 113 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQNQINTNP 192
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         170
                  ....*....|.
gi 2462543509 193 ESPDTVTIHAA 203
Cdd:COG0666   251 DGLTALLLAAA 261
Ank_2 pfam12796
Ankyrin repeats (3 copies);
66-157 1.11e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 99.81  E-value: 1.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  66 LHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHgADVNAKDMlKMTALHWATEHNHQEVVE 145
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 2462543509 146 LLIKYGADVHTQ 157
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 44-167 1.67e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.31  E-value: 1.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  44 DEVRILMANGAPF-TTDWLGTSPLHLaaqYGHYSTTE----VLLRAGVSRDARTKVDRTPLHMAAS--EGHASIVEVLLK 116
Cdd:PHA03095   64 DIVRLLLEAGADVnAPERCGFTPLHL---YLYNATTLdvikLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLR 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462543509 117 HGADVNAKDMLKMTALHWATEhNHQ---EVVELLIKYGADVHTQSKFCKTAFDI 167
Cdd:PHA03095  141 KGADVNALDLYGMTPLAVLLK-SRNanvELLRLLIDAGADVYAVDDRFRSLLHH 193
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 34-205 9.06e-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: 9.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  34 LLEAARAGQDDEVRILMANGA--PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAgvsrdARTKVD----------RTPLHM 101
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCPScdLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509 102 AASEGHASIVEVLLKHGADVNAKD------MLKMTALHWATEH--------NHQEVVELLIKYGADVHTQSKFCKTAFDI 167
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVVSPRatgtffRPGPKNLIYYGEHplsfaacvGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462543509 168 SIDNGNEDLA-EILQIAMQNQINTNPESPDTVTIHAA-TP 205
Cdd:cd22192   176 LVLQPNKTFAcQMYDLILSYDKEDDLQPLDLVPNNQGlTP 215
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 95-123 1.39e-07

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: 47.20  E-value: 1.39e-07
                           10        20
                   ....*....|....*....|....*....
gi 2462543509   95 DRTPLHMAASEGHASIVEVLLKHGADVNA 123
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 27-182 2.98e-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: 49.31  E-value: 2.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  27 LVDLGKKLLEAARAGQDDEV----RILMANGAPFTTDWL-----------GTSPLHLAAQYGHYSTTEVLLRAGVSRDAR 91
Cdd:TIGR00870  78 RGAVGDTLLHAISLEYVDAVeailLHLLAAFRKSGPLELandqytseftpGITALHLAAHRQNYEIVKLLLERGASVPAR 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  92 TKVD--------------RTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNH---------QEVVELLI 148
Cdd:TIGR00870 158 ACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEfkaeyeelsCQMYNFAL 237

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462543509 149 KYGADVHTQSKF-------CKTAFDISIDNGNEDLAE-ILQI 182
Cdd:TIGR00870 238 SLLDKLRDSKELevilnhqGLTPLKLAAKEGRIVLFRlKLAI 279
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 365-411 5.98e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 36.43  E-value: 5.98e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2462543509 365 SAEIEEREALQKQLDEANREAQKYRQQLLKKEQEAEAYRQKLEAMTR 411
Cdd:pfam20492  72 EMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEARE 118
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
34-203 7.28e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.12  E-value: 7.28e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  34 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVE 112
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509 113 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQNQINTNP 192
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         170
                  ....*....|.
gi 2462543509 193 ESPDTVTIHAA 203
Cdd:COG0666   251 DGLTALLLAAA 261
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
34-180 6.30e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.24  E-value: 6.30e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  34 LLEAARAGQDDEVRILMANGAP-FTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVE 112
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADiNAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462543509 113 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL 180
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
34-191 2.01e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.08  E-value: 2.01e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  34 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVE 112
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGAdVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462543509 113 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQNQINTN 191
Cdd:COG0666   204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
34-180 5.72e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 111.97  E-value: 5.72e-28
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  34 LLEAARAGQDDEVRILMANGAPFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEV 113
Cdd:COG0666    26 LAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKL 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462543509 114 LLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL 180
Cdd:COG0666   106 LLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
66-157 1.11e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 99.81  E-value: 1.11e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  66 LHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHgADVNAKDMlKMTALHWATEHNHQEVVE 145
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 2462543509 146 LLIKYGADVHTQ 157
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
34-125 6.78e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 6.78e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  34 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDarTKVDRTPLHMAASEGHASIVE 112
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2462543509 113 VLLKHGADVNAKD 125
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 44-167 1.67e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.31  E-value: 1.67e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  44 DEVRILMANGAPF-TTDWLGTSPLHLaaqYGHYSTTE----VLLRAGVSRDARTKVDRTPLHMAAS--EGHASIVEVLLK 116
Cdd:PHA03095   64 DIVRLLLEAGADVnAPERCGFTPLHL---YLYNATTLdvikLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLR 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462543509 117 HGADVNAKDMLKMTALHWATEhNHQ---EVVELLIKYGADVHTQSKFCKTAFDI 167
Cdd:PHA03095  141 KGADVNALDLYGMTPLAVLLK-SRNanvELLRLLIDAGADVYAVDDRFRSLLHH 193
Ank_2 pfam12796
Ankyrin repeats (3 copies);
99-180 2.96e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.31  E-value: 2.96e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  99 LHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYgADVHTQSKFcKTAFDISIDNGNEDLAE 178
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78


                  ..
gi 2462543509 179 IL 180
Cdd:pfam12796  79 LL 80
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 46-192 8.44e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.55  E-value: 8.44e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  46 VRILMANGAPFT-TDWLGTSPLHLAAQY--GHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHA--SIVEVLLKHGAD 120
Cdd:PHA03100   89 VKLLLEYGANVNaPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVD 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509 121 ----------------VNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEdlaEILQIAM 184
Cdd:PHA03100  169 inaknrvnyllsygvpINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK---EIFKLLL 245


                  ....*...
gi 2462543509 185 QNQINTNP 192
Cdd:PHA03100  246 NNGPSIKT 253
PHA03095 PHA03095
ankyrin-like protein; Provisional
 44-177 1.44e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.14  E-value: 1.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  44 DEVRILMANGAPFT-TDWLGTSPLHLAAQYGHYSTTEV---LLRAGVSRDARTKVDRTPLH---MAASEghASIVEVLLK 116
Cdd:PHA03095   28 EEVRRLLAAGADVNfRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHlylYNATT--LDVIKLLIK 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2462543509 117 HGADVNAKDMLKMTALH--WATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLA 177
Cdd:PHA03095  106 AGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVE 168
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
48-180 5.23e-15

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 74.99  E-value: 5.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  48 ILMANGAPFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDML 127
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462543509 128 KMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL 180
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
PHA03095 PHA03095
ankyrin-like protein; Provisional
 46-198 4.41e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.52  E-value: 4.41e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  46 VRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTT--EVLLRAGVSRDARTKVDRTPLHMAA--SEGHASIVEVLLKHGAD 120
Cdd:PHA03095  170 LRLLIDAGAdVYAVDDRFRSLLHHHLQSFKPRARivRELIRAGCDPAATDMLGNTPLHSMAtgSSCKRSLVLPLLIAGIS 249

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462543509 121 VNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDlaeilqiAMQNQINTNPeSPDTV 198
Cdd:PHA03095  250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGR-------AVRAALAKNP-SAETV 319
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 38-217 3.30e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 71.25  E-value: 3.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  38 ARAGQDDE-VRILMANGAPFT-TDWLGTSPLHLAAQYGHYSTTEV-LLRAGVSRDARTKVDRTPLHMAASEGHASIVEVL 114
Cdd:PHA02876  315 AKNGYDTEnIRTLIMLGADVNaADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509 115 LKHGADVNAKDMLKMTALHWA-TEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEdlAEILQIAMQNQINTNpe 193
Cdd:PHA02876  395 LDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCK--LDVIEMLLDNGADVN-- 470

                         170       180
                  ....*....|....*....|....*
gi 2462543509 194 spdTVTIHAATPQFI-IGPGGVVNL 217
Cdd:PHA02876  471 ---AINIQNQYPLLIaLEYHGIVNI 492
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 11-200 8.11e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.91  E-value: 8.11e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  11 LKESYPRRKFFISFMSLVDLGKK-----LLEAARAGQDDE-----VRILMANGAPFT--TDWLGTSPLHLAAQYGHYSTT 78
Cdd:PHA02878  105 IKDAFNNRNVEIFKIILTNRYKNiqtidLVYIDKKSKDDIieaeiTKLLLSYGADINmkDRHKGNTALHYATENKDQRLT 184

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  79 EVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEH-NHQEVVELLIKYGADVHTQ 157
Cdd:PHA02878  185 ELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAK 264

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*
gi 2462543509 158 SKFCK-TAFDISIDNgNEDLAEILQI-AMQNQINTNPESPDTVTI 200
Cdd:PHA02878  265 SYILGlTALHSSIKS-ERKLKLLLEYgADINSLNSYKLTPLSSAV 308
Ank_4 pfam13637
Ankyrin repeats (many copies);
96-148 2.66e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.14  E-value: 2.66e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2462543509  96 RTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLI 148
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 21-191 2.88e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.77  E-value: 2.88e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  21 FISFMSLVDLGKKLLEaaragqddevRILMANGAPFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLH 100
Cdd:PHA03100    4 YIVLTKSRIIKVKNIK----------YIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLH 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509 101 MAASEGHAS-----IVEVLLKHGADVNAKDMLKMTALHWA--TEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGN 173
Cdd:PHA03100   74 YLSNIKYNLtdvkeIVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNK 153

                         170
                  ....*....|....*...
gi 2462543509 174 EDLaEILQIAMQNQINTN 191
Cdd:PHA03100  154 IDL-KILKLLIDKGVDIN 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 58-186 9.25e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.82  E-value: 9.25e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  58 TDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATE 137
Cdd:PLN03192  521 DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAIS 600

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2462543509 138 HNHQEVVELLIKYGA--DVHTQSK-FCKTA-------------FDISIDNGNEDLAEILQIAMQN 186
Cdd:PLN03192  601 AKHHKIFRILYHFASisDPHAAGDlLCTAAkrndltamkellkQGLNVDSEDHQGATALQVAMAE 665
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 34-205 9.06e-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: 9.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  34 LLEAARAGQDDEVRILMANGA--PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAgvsrdARTKVD----------RTPLHM 101
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCPScdLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509 102 AASEGHASIVEVLLKHGADVNAKD------MLKMTALHWATEH--------NHQEVVELLIKYGADVHTQSKFCKTAFDI 167
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVVSPRatgtffRPGPKNLIYYGEHplsfaacvGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 2462543509 168 SIDNGNEDLA-EILQIAMQNQINTNPESPDTVTIHAA-TP 205
Cdd:cd22192   176 LVLQPNKTFAcQMYDLILSYDKEDDLQPLDLVPNNQGlTP 215
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 67-155 3.06e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 62.22  E-value: 3.06e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  67 HLAAQyGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVEL 146
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ....*....
gi 2462543509 147 LIKYGADVH 155
Cdd:PTZ00322  167 LSRHSQCHF 175
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 34-173 1.03e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.98  E-value: 1.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  34 LLEAARAGQDDEVRILMANGapfttdwLGTSPLHLAAQygHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEV 113
Cdd:PHA02874   72 LLTAIKIGAHDIIKLLIDNG-------VDTSILPIPCI--EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKM 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509 114 LLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGN 173
Cdd:PHA02874  143 LFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGD 202
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
34-132 1.36e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.81  E-value: 1.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  34 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVE 112
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGAdVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269

                          90       100
                  ....*....|....*....|
gi 2462543509 113 VLLKHGADVNAKDMLKMTAL 132
Cdd:COG0666   270 LLLLALLLLAAALLDLLTLL 289
Ank_5 pfam13857
Ankyrin repeats (many copies);
114-167 1.38e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.50  E-value: 1.38e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2462543509 114 LLKHG-ADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDI 167
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 110-191 3.07e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.92  E-value: 3.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509 110 IVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILqIAMQNQIN 189
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAI-IDNRSNIN 238


                  ..
gi 2462543509 190 TN 191
Cdd:PHA02876  239 KN 240
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 94-180 3.14e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.76  E-value: 3.14e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  94 VDRTPLHMAASE-------GHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFD 166
Cdd:PTZ00322   74 IDPVVAHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153

                          90
                  ....*....|....
gi 2462543509 167 ISIDNGNEDLAEIL 180
Cdd:PTZ00322  154 LAEENGFREVVQLL 167
Ank_4 pfam13637
Ankyrin repeats (many copies);
62-115 5.19e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 5.19e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2462543509  62 GTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLL 115
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 29-180 5.92e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.69  E-value: 5.92e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  29 DLGKKLLEAARAGQDDEVRILMANGApFTTDWL---GTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASE 105
Cdd:PHA02875   67 DIESELHDAVEEGDVKAVEELLDLGK-FADDVFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMM 145

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462543509 106 GHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKF-CKTAFDISIDNGNEDLAEIL 180
Cdd:PHA02875  146 GDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLF 221
Ank_4 pfam13637
Ankyrin repeats (many copies);
129-180 8.39e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 8.39e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2462543509 129 MTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL 180
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 97-204 8.51e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.98  E-value: 8.51e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  97 TPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNH-----QEVVELLIKYGADVHTQSKFCKTAFDISIDN 171
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISK 116

                          90       100       110
                  ....*....|....*....|....*....|....
gi 2462543509 172 GNEDLaEILQIAMQNQINTNPESPDTVT-IHAAT 204
Cdd:PHA03100  117 KSNSY-SIVEYLLDNGANVNIKNSDGENlLHLYL 149
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 96-125 1.57e-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: 49.98  E-value: 1.57e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2462543509  96 RTPLHMAA-SEGHASIVEVLLKHGADVNAKD 125
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 44-153 1.93e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 56.15  E-value: 1.93e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  44 DEVRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVN 122
Cdd:PHA02875  116 DIMKLLIARGAdPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2462543509 123 -AKDMLKMTALHWATEHNHQEVVELLIKYGAD 153
Cdd:PHA02875  196 yFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 30-117 2.64e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 2.64e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  30 LGKKLLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHA 108
Cdd:PTZ00322   82 LTVELCQLAASGDAVGARILLTGGAdPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161


                  ....*....
gi 2462543509 109 SIVEVLLKH 117
Cdd:PTZ00322  162 EVVQLLSRH 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 48-154 3.42e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.64  E-value: 3.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  48 ILMANGAPFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVL------------- 114
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhfasisdphaag 623

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2462543509 115 ------------------LKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADV 154
Cdd:PLN03192  624 dllctaakrndltamkelLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 62-180 6.66e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.23  E-value: 6.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  62 GTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLL---KHGADVNAKDmlKMTALHWATEH 138
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLdlgKFADDVFYKD--GMTPLHLATIL 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 2462543509 139 NHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL 180
Cdd:PHA02875  113 KKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 95-123 1.39e-07

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: 47.20  E-value: 1.39e-07
                           10        20
                   ....*....|....*....|....*....
gi 2462543509   95 DRTPLHMAASEGHASIVEVLLKHGADVNA 123
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 79-176 1.76e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.53  E-value: 1.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  79 EVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQs 158
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKN- 240

                          90       100
                  ....*....|....*....|
gi 2462543509 159 kfcktafDISIDNG--NEDL 176
Cdd:PHA02876  241 -------DLSLLKAirNEDL 253
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 37-148 3.10e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.27  E-value: 3.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  37 AARAGQDDEVRILMANGAPFTT-DWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLL 115
Cdd:PHA02874  131 AIKKGDLESIKMLFEYGADVNIeDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210

                          90       100       110
                  ....*....|....*....|....*....|...
gi 2462543509 116 KHGADVNAKDMLKMTALHWATEHNhQEVVELLI 148
Cdd:PHA02874  211 DHGNHIMNKCKNGFTPLHNAIIHN-RSAIELLI 242
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 96-123 2.22e-06

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 43.79  E-value: 2.22e-06
                          10        20
                  ....*....|....*....|....*...
gi 2462543509  96 RTPLHMAASEGHASIVEVLLKHGADVNA 123
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
81-135 2.24e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 2.24e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2462543509  81 LLRAG-VSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWA 135
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 27-182 2.98e-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: 49.31  E-value: 2.98e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  27 LVDLGKKLLEAARAGQDDEV----RILMANGAPFTTDWL-----------GTSPLHLAAQYGHYSTTEVLLRAGVSRDAR 91
Cdd:TIGR00870  78 RGAVGDTLLHAISLEYVDAVeailLHLLAAFRKSGPLELandqytseftpGITALHLAAHRQNYEIVKLLLERGASVPAR 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  92 TKVD--------------RTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNH---------QEVVELLI 148
Cdd:TIGR00870 158 ACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEfkaeyeelsCQMYNFAL 237

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2462543509 149 KYGADVHTQSKF-------CKTAFDISIDNGNEDLAE-ILQI 182
Cdd:TIGR00870 238 SLLDKLRDSKELevilnhqGLTPLKLAAKEGRIVLFRlKLAI 279
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 129-155 4.48e-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: 4.48e-06
                           10        20
                   ....*....|....*....|....*..
gi 2462543509  129 MTALHWATEHNHQEVVELLIKYGADVH 155
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 129-159 9.05e-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. 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: 42.28  E-value: 9.05e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 2462543509 129 MTALHWATEH-NHQEVVELLIKYGADVHTQSK 159
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 30-133 2.81e-05

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: 46.16  E-value: 2.81e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  30 LGKKLLEAARAGQDDEVRILMANGAP------FTTD-WLGTSPLHLAAQYGHYSTTEVLLRAGV--------------SR 88
Cdd:cd22192    50 LGETALHVAALYDNLEAAVVLMEAAPelvnepMTSDlYQGETALHIAVVNQNLNLVRELIARGAdvvspratgtffrpGP 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 2462543509  89 DARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALH 133
Cdd:cd22192   130 KNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
PHA02741 PHA02741
hypothetical protein; Provisional
 99-181 2.89e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 44.26  E-value: 2.89e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  99 LHMAAsEGH-----ASIVEVLLKHGADVNAKDMLK-MTALHWAT-EHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDN 171
Cdd:PHA02741   64 IHIAA-EKHeaqlaAEIIDHLIELGADINAQEMLEgDTALHLAAhRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAIDN 142

                          90
                  ....*....|
gi 2462543509 172 GNEDLAEILQ 181
Cdd:PHA02741  143 EDVAMMQILR 152
PHA02946 PHA02946
ankyin-like protein; Provisional
 79-155 3.18e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.82  E-value: 3.18e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2462543509  79 EVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHW--ATEHNHQEVVELLIKYGADVH 155
Cdd:PHA02946   56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKIN 134
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 44-125 5.63e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.04  E-value: 5.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  44 DEVRILMANGAPF-TTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVN 122
Cdd:PHA03100  173 NRVNYLLSYGVPInIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252


                  ...
gi 2462543509 123 AKD 125
Cdd:PHA03100  253 TII 255
PHA03095 PHA03095
ankyrin-like protein; Provisional
 101-174 1.09e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 1.09e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2462543509 101 MAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQ---EVVELLIKYGADVHTQSKFCKTAFDISIDNGNE 174
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATT 96
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 66-165 1.55e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.80  E-value: 1.55e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  66 LHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVE 145
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                          90       100
                  ....*....|....*....|
gi 2462543509 146 LLIKYGADVHTQskfCKTAF 165
Cdd:PHA02874  208 LLIDHGNHIMNK---CKNGF 224
Ank_4 pfam13637
Ankyrin repeats (many copies);
34-82 2.29e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 2.29e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462543509  34 LLEAARAGQDDEVRILMANGAPF-TTDWLGTSPLHLAAQYGHYSTTEVLL 82
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADInAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 110-180 2.54e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 42.66  E-value: 2.54e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 2462543509 110 IVEVLLKHGADVNAK----DMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCK-TAFDISIDNGNEDLAEIL 180
Cdd:PHA02884   48 IIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEIL 123
Ank_5 pfam13857
Ankyrin repeats (many copies);
54-102 3.39e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 3.39e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 2462543509  54 APFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMA 102
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 110-191 4.99e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.13  E-value: 4.99e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509 110 IVEVLLKHGADVNAKDMLKMTALHWATEH---NHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQN 186
Cdd:PHA02798   91 IVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHIDIEIIKLLLEK 170


                  ....*
gi 2462543509 187 QINTN 191
Cdd:PHA02798  171 GVDIN 175
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 62-93 9.71e-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: 36.50  E-value: 9.71e-04
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2462543509  62 GTSPLHLAA-QYGHYSTTEVLLRAGVSRDARTK 93
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 129-156 9.81e-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: 9.81e-04
                          10        20
                  ....*....|....*....|....*...
gi 2462543509 129 MTALHWATEHNHQEVVELLIKYGADVHT 156
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 110-201 2.88e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.65  E-value: 2.88e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509 110 IVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGN--EDLAEILQIAMQNq 187
Cdd:PHA03100   17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnlTDVKEIVKLLLEY- 95

                          90
                  ....*....|....
gi 2462543509 188 iNTNPESPDTVTIH 201
Cdd:PHA03100   96 -GANVNAPDNNGIT 108
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 70-154 3.28e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 39.90  E-value: 3.28e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  70 AQYGHYSTTEVLLRAGVSRDARTKVDRTPLH--MAASEGHASIVEVLLKHGADVNAKDMLKMTALH-----------WAT 136
Cdd:PHA02716  292 ARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvvniLDP 371

                          90       100
                  ....*....|....*....|.
gi 2462543509 137 EHNHQ---EVVELLIKYGADV 154
Cdd:PHA02716  372 ETDNDirlDVIQCLISLGADI 392
PHA02798 PHA02798
ankyrin-like protein; Provisional
 78-186 3.94e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.43  E-value: 3.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  78 TEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLL---KHGADVNAKDMLKMTALHWATEHNHQ---EVVELLIKYG 151
Cdd:PHA02798   92 VKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKG 171

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2462543509 152 ADVHTQS-KFCKTAFDISID-NGNEDLAEILQIAMQN 186
Cdd:PHA02798  172 VDINTHNnKEKYDTLHCYFKyNIDRIDADILKLFVDN 208
PHA02791 PHA02791
ankyrin-like protein; Provisional
 42-149 4.80e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 38.48  E-value: 4.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  42 QDDEVRILMANGAPFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTkvDRTPLHMAASEGHASIVEVLLKHGADV 121
Cdd:PHA02791   10 KSKQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLE--NEFPLHQAATLEDTKIVKILLFSGMDD 87

                          90       100
                  ....*....|....*....|....*...
gi 2462543509 122 NAKDMLKMTALHWATEHNHQEVVELLIK 149
Cdd:PHA02791   88 SQFDDKGNTALYYAVDSGNMQTVKLFVK 115
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 365-411 5.98e-03

Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related proteins, ezrin, radixin and moesin. Ezrin was first identified as a constituent of microvilli, radixin as a barbed, end-capping actin-modulating protein from isolated junctional fractions, and moesin as a heparin binding protein. A tumour suppressor molecule responsible for neurofibromatosis type 2 (NF2) is highly similar to ERM proteins and has been designated merlin (moesin-ezrin-radixin-like protein). ERM molecules contain 3 domains, an N-terminal globular domain, an extended alpha-helical domain and a charged C-terminal domain (pfam00769). Ezrin, radixin and merlin also contain a polyproline linker region between the helical and C-terminal domains. The N-terminal domain is highly conserved and is also found in merlin, band 4.1 proteins and members of the band 4.1 superfamily, designated the FERM domain. ERM proteins crosslink actin filaments with plasma membranes. They co-localize with CD44 at actin filament plasma membrane interaction sites, associating with CD44 via their N-terminal domains and with actin filaments via their C-terminal domains. This is the alpha-helical domain, which is involved in intramolecular masking of protein-protein interaction sites, regulating the activity of this proteins.


Pssm-ID: 466641 [Multi-domain]  Cd Length: 120  Bit Score: 36.43  E-value: 5.98e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2462543509 365 SAEIEEREALQKQLDEANREAQKYRQQLLKKEQEAEAYRQKLEAMTR 411
Cdd:pfam20492  72 EMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEARE 118
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 97-173 6.68e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 37.88  E-value: 6.68e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  97 TPLHMAASEGHAS--IVEVLLKHGADVNAKDM-LKMTALHWATEHN---HQEVVELLIKYGADVHTQSKFCKTAFDISID 170
Cdd:PHA02859   53 TPIFSCLEKDKVNveILKFLIENGADVNFKTRdNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHMYMC 132


                  ...
gi 2462543509 171 NGN 173
Cdd:PHA02859  133 NFN 135
Stathmin pfam00836
Stathmin family; The Stathmin family of proteins play an important role in the regulation of ...
 330-407 7.39e-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: 36.56  E-value: 7.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2462543509 330 QVLTVPATDIAEETVISEEPPAKRQCIEIIENRVESAEiEEREALqkqldeanrEAQKYRQQLLKKEQEAEAYRQKLE 407
Cdd:pfam00836  18 EVILKPPSVNAAPPKLSLSPKKKDSSLEEIQKKLEAAE-ERRKSL---------EAQKLKQLAEKREKEEEALQKADE 85
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 67-152 7.95e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 37.10  E-value: 7.95e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2462543509  67 HLAAQYGHYSTT---EVLLRAGVSRDAR-TKVDRTPLHMAASEGHASIVEVLLKH-GADVNAKDMLKMTALHWATEHNHQ 141
Cdd:PHA02743   62 HMVAWYDRANAVmkiELLVNMGADINAReLGTGNTLLHIAASTKNYELAEWLCRQlGVNLGAINYQHETAYHIAYKMRDR 141

                          90
                  ....*....|.
gi 2462543509 142 EVVELLIKYGA 152
Cdd:PHA02743  142 RMMEILRANGA 152
CREPT pfam16566
Cell-cycle alteration and expression-elevated protein in tumour; CREPT (Cell-cycle alteration ...
 365-414 8.00e-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: 36.83  E-value: 8.00e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 2462543509 365 SAEIEEREALQKQLDEAnreAQKYRQQLLKKEQEAEAYRQKLEAMTRLQT 414
Cdd:pfam16566  68 AAELEDRKKVAQMLRDF---LQLQKELLAQAEERLEEYKEKLEKVSQVRK 114
 
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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