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Conserved domains on  [gi|1370466417|ref|XP_024305651|]
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GA-binding protein subunit beta-1 isoform X2 [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];
15-184 8.81e-45

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 156.65  E-value: 8.81e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  15 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVE 93
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  94 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQNQINTNP 173
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         170
                  ....*....|.
gi 1370466417 174 ESPDTVTIHAA 184
Cdd:COG0666   251 DGLTALLLAAA 261
MobB_NDR_LATS-like super family cl45907
Mob-binding domain found in the NDR/LATS family serine/threonine protein kinases; The nuclear ...
 340-387 8.67e-03

Mob-binding domain found in the NDR/LATS family serine/threonine protein kinases; The nuclear Dbf2-related (NDR)/large tumor suppressor (LATS) family includes NDR, LATS, CBK1, and Sid2p. They are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. NDR/LATS kinases bind to highly conserved Mob (Mps One binder) coactivators, forming regulatory complexes that control a diverse set of in vivo effector proteins, and are essential and evolutionarily conserved components of "Hippo" signaling pathways. Mob association creates a novel binding pocket that participates in the formation of the active state of NDR/LATS kinases. These kinases contain a regulatory domain located N-terminal to the serine/threonine kinase domain (called the N-terminal regulatory (NTR) domain) and an insert within the catalytic domain that contains an auto-inhibitory sequence. This model corresponds to the NTR or Mob-binding domain of NDR/LATS family serine/threonine protein kinases.


The actual alignment was detected with superfamily member cd21742:

Pssm-ID: 459252  Cd Length: 62  Bit Score: 34.48  E-value: 8.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370466417 340 IENRVESA--EIEERE----ALQKQLDEAN---REAQKYRQQLLKKEQE-AEAYRQKL 387
Cdd:cd21742     5 IENHYTNLlqQLKERRerrkQLEEKLENLNlseEEKEQLRKELLKKESEyLRLQRQKL 62
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-184 8.81e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 156.65  E-value: 8.81e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  15 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVE 93
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  94 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQNQINTNP 173
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         170
                  ....*....|.
gi 1370466417 174 ESPDTVTIHAA 184
Cdd:COG0666   251 DGLTALLLAAA 261
Ank_2 pfam12796
Ankyrin repeats (3 copies);
47-138 2.31e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 98.65  E-value: 2.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  47 LHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHgADVNAKDMlKMTALHWATEHNHQEVVE 126
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 1370466417 127 LLIKYGADVHTQ 138
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 25-148 1.40e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.31  E-value: 1.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  25 DEVRILMANGAPF-TTDWLGTSPLHLaaqYGHYSTTE----VLLRAGVSRDARTKVDRTPLHMAAS--EGHASIVEVLLK 97
Cdd:PHA03095   64 DIVRLLLEAGADVnAPERCGFTPLHL---YLYNATTLdvikLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLR 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370466417  98 HGADVNAKDMLKMTALHWATEhNHQ---EVVELLIKYGADVHTQSKFCKTAFDI 148
Cdd:PHA03095  141 KGADVNALDLYGMTPLAVLLK-SRNanvELLRLLIDAGADVYAVDDRFRSLLHH 193
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 15-186 8.05e-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: 8.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  15 LLEAARAGQDDEVRILMANGA--PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAgvsrdARTKVD----------RTPLHM 82
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCPScdLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  83 AASEGHASIVEVLLKHGADVNAKD------MLKMTALHWATEH--------NHQEVVELLIKYGADVHTQSKFCKTAFDI 148
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVVSPRatgtffRPGPKNLIYYGEHplsfaacvGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1370466417 149 SIDNGNEDLA-EILQIAMQNQINTNPESPDTVTIHAA-TP 186
Cdd:cd22192   176 LVLQPNKTFAcQMYDLILSYDKEDDLQPLDLVPNNQGlTP 215
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 76-104 1.56e-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: 1.56e-07
                           10        20
                   ....*....|....*....|....*....
gi 1370466417   76 DRTPLHMAASEGHASIVEVLLKHGADVNA 104
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 8-163 2.74e-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: 2.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417   8 LVDLGKKLLEAARAGQDDEV----RILMANGAPFTTDWL-----------GTSPLHLAAQYGHYSTTEVLLRAGVSRDAR 72
Cdd:TIGR00870  78 RGAVGDTLLHAISLEYVDAVeailLHLLAAFRKSGPLELandqytseftpGITALHLAAHRQNYEIVKLLLERGASVPAR 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  73 TKVD--------------RTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNH---------QEVVELLI 129
Cdd:TIGR00870 158 ACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEfkaeyeelsCQMYNFAL 237

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1370466417 130 KYGADVHTQSKF-------CKTAFDISIDNGNEDLAE-ILQI 163
Cdd:TIGR00870 238 SLLDKLRDSKELevilnhqGLTPLKLAAKEGRIVLFRlKLAI 279
MobB_NDR_LATS-like cd21742
Mob-binding domain found in the NDR/LATS family serine/threonine protein kinases; The nuclear ...
 340-387 8.67e-03

Mob-binding domain found in the NDR/LATS family serine/threonine protein kinases; The nuclear Dbf2-related (NDR)/large tumor suppressor (LATS) family includes NDR, LATS, CBK1, and Sid2p. They are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. NDR/LATS kinases bind to highly conserved Mob (Mps One binder) coactivators, forming regulatory complexes that control a diverse set of in vivo effector proteins, and are essential and evolutionarily conserved components of "Hippo" signaling pathways. Mob association creates a novel binding pocket that participates in the formation of the active state of NDR/LATS kinases. These kinases contain a regulatory domain located N-terminal to the serine/threonine kinase domain (called the N-terminal regulatory (NTR) domain) and an insert within the catalytic domain that contains an auto-inhibitory sequence. This model corresponds to the NTR or Mob-binding domain of NDR/LATS family serine/threonine protein kinases.


Pssm-ID: 439267  Cd Length: 62  Bit Score: 34.48  E-value: 8.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370466417 340 IENRVESA--EIEERE----ALQKQLDEAN---REAQKYRQQLLKKEQE-AEAYRQKL 387
Cdd:cd21742     5 IENHYTNLlqQLKERRerrkQLEEKLENLNlseEEKEQLRKELLKKESEyLRLQRQKL 62
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 346-392 9.09e-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: 36.05  E-value: 9.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1370466417 346 SAEIEEREALQKQLDEANREAQKYRQQLLKKEQEAEAYRQKLEAMTR 392
Cdd:pfam20492  72 EMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEARE 118
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-184 8.81e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 156.65  E-value: 8.81e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  15 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVE 93
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  94 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQNQINTNP 173
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         170
                  ....*....|.
gi 1370466417 174 ESPDTVTIHAA 184
Cdd:COG0666   251 DGLTALLLAAA 261
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-161 5.00e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 5.00e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  15 LLEAARAGQDDEVRILMANGAP-FTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVE 93
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADiNAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370466417  94 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL 161
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-172 1.41e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.39  E-value: 1.41e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  15 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVE 93
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGAdVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370466417  94 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQNQINTN 172
Cdd:COG0666   204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-161 2.57e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.66  E-value: 2.57e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417   1 MKLVKMSLVDLGKKLLEAARAGQDDEVRILMANGAPFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPL 80
Cdd:COG0666    12 LAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLL 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  81 HMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEI 160
Cdd:COG0666    92 HAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKL 171


                  .
gi 1370466417 161 L 161
Cdd:COG0666   172 L 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
47-138 2.31e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 98.65  E-value: 2.31e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  47 LHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHgADVNAKDMlKMTALHWATEHNHQEVVE 126
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 1370466417 127 LLIKYGADVHTQ 138
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
15-106 1.41e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 1.41e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  15 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDarTKVDRTPLHMAASEGHASIVE 93
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1370466417  94 VLLKHGADVNAKD 106
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 25-148 1.40e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.31  E-value: 1.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  25 DEVRILMANGAPF-TTDWLGTSPLHLaaqYGHYSTTE----VLLRAGVSRDARTKVDRTPLHMAAS--EGHASIVEVLLK 97
Cdd:PHA03095   64 DIVRLLLEAGADVnAPERCGFTPLHL---YLYNATTLdvikLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLR 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370466417  98 HGADVNAKDMLKMTALHWATEhNHQ---EVVELLIKYGADVHTQSKFCKTAFDI 148
Cdd:PHA03095  141 KGADVNALDLYGMTPLAVLLK-SRNanvELLRLLIDAGADVYAVDDRFRSLLHH 193
Ank_2 pfam12796
Ankyrin repeats (3 copies);
80-161 5.48e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 5.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  80 LHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYgADVHTQSKFcKTAFDISIDNGNEDLAE 159
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78


                  ..
gi 1370466417 160 IL 161
Cdd:pfam12796  79 LL 80
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 27-173 7.29e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.55  E-value: 7.29e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  27 VRILMANGAPFT-TDWLGTSPLHLAAQY--GHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHA--SIVEVLLKHGAD 101
Cdd:PHA03100   89 VKLLLEYGANVNaPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVD 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417 102 ----------------VNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEdlaEILQIAM 165
Cdd:PHA03100  169 inaknrvnyllsygvpINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK---EIFKLLL 245


                  ....*...
gi 1370466417 166 QNQINTNP 173
Cdd:PHA03100  246 NNGPSIKT 253
PHA03095 PHA03095
ankyrin-like protein; Provisional
 25-158 1.23e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.14  E-value: 1.23e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  25 DEVRILMANGAPFT-TDWLGTSPLHLAAQYGHYSTTEV---LLRAGVSRDARTKVDRTPLH---MAASEghASIVEVLLK 97
Cdd:PHA03095   28 EEVRRLLAAGADVNfRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHlylYNATT--LDVIKLLIK 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370466417  98 HGADVNAKDMLKMTALH--WATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLA 158
Cdd:PHA03095  106 AGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVE 168
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
29-161 1.35e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.83  E-value: 1.35e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  29 ILMANGAPFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDML 108
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370466417 109 KMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL 161
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
PHA03095 PHA03095
ankyrin-like protein; Provisional
 27-179 3.84e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.52  E-value: 3.84e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  27 VRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTT--EVLLRAGVSRDARTKVDRTPLHMAA--SEGHASIVEVLLKHGAD 101
Cdd:PHA03095  170 LRLLIDAGAdVYAVDDRFRSLLHHHLQSFKPRARivRELIRAGCDPAATDMLGNTPLHSMAtgSSCKRSLVLPLLIAGIS 249

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370466417 102 VNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDlaeilqiAMQNQINTNPeSPDTV 179
Cdd:PHA03095  250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGR-------AVRAALAKNP-SAETV 319
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 19-198 4.84e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.86  E-value: 4.84e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  19 ARAGQDDE-VRILMANGAPFT-TDWLGTSPLHLAAQYGHYSTTEV-LLRAGVSRDARTKVDRTPLHMAASEGHASIVEVL 95
Cdd:PHA02876  315 AKNGYDTEnIRTLIMLGADVNaADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  96 LKHGADVNAKDMLKMTALHWA-TEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEdlAEILQIAMQNQINTNpe 174
Cdd:PHA02876  395 LDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCK--LDVIEMLLDNGADVN-- 470

                         170       180
                  ....*....|....*....|....*
gi 1370466417 175 spdTVTIHAATPQFI-IGPGGVVNL 198
Cdd:PHA02876  471 ---AINIQNQYPLLIaLEYHGIVNI 492
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 5-181 1.83e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.37  E-value: 1.83e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417   5 KMSLVDLGKK-----LLEAARAGQDDE-----VRILMANGAPFT--TDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDAR 72
Cdd:PHA02878  118 KIILTNRYKNiqtidLVYIDKKSKDDIieaeiTKLLLSYGADINmkDRHKGNTALHYATENKDQRLTELLLSYGANVNIP 197

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  73 TKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEH-NHQEVVELLIKYGADVHTQSKFCK-TAFDISI 150
Cdd:PHA02878  198 DKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGlTALHSSI 277

                         170       180       190
                  ....*....|....*....|....*....|..
gi 1370466417 151 DNgNEDLAEILQI-AMQNQINTNPESPDTVTI 181
Cdd:PHA02878  278 KS-ERKLKLLLEYgADINSLNSYKLTPLSSAV 308
Ank_4 pfam13637
Ankyrin repeats (many copies);
77-129 2.52e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.14  E-value: 2.52e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370466417  77 RTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLI 129
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 28-172 2.78e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.77  E-value: 2.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  28 RILMANGAPFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHAS-----IVEVLLKHGADV 102
Cdd:PHA03100   20 YIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANV 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370466417 103 NAKDMLKMTALHWA--TEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLaEILQIAMQNQINTN 172
Cdd:PHA03100  100 NAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDL-KILKLLIDKGVDIN 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 39-167 7.28e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.20  E-value: 7.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  39 TDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATE 118
Cdd:PLN03192  521 DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAIS 600

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370466417 119 HNHQEVVELLIKYGA--DVHTQSK-FCKTA-------------FDISIDNGNEDLAEILQIAMQN 167
Cdd:PLN03192  601 AKHHKIFRILYHFASisDPHAAGDlLCTAAkrndltamkellkQGLNVDSEDHQGATALQVAMAE 665
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 15-186 8.05e-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: 8.05e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  15 LLEAARAGQDDEVRILMANGA--PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAgvsrdARTKVD----------RTPLHM 82
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCPScdLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  83 AASEGHASIVEVLLKHGADVNAKD------MLKMTALHWATEH--------NHQEVVELLIKYGADVHTQSKFCKTAFDI 148
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVVSPRatgtffRPGPKNLIYYGEHplsfaacvGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1370466417 149 SIDNGNEDLA-EILQIAMQNQINTNPESPDTVTIHAA-TP 186
Cdd:cd22192   176 LVLQPNKTFAcQMYDLILSYDKEDDLQPLDLVPNNQGlTP 215
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 48-136 3.40e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.84  E-value: 3.40e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  48 HLAAQyGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVEL 127
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ....*....
gi 1370466417 128 LIKYGADVH 136
Cdd:PTZ00322  167 LSRHSQCHF 175
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 15-154 9.30e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.98  E-value: 9.30e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  15 LLEAARAGQDDEVRILMANGapfttdwLGTSPLHLAAQygHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEV 94
Cdd:PHA02874   72 LLTAIKIGAHDIIKLLIDNG-------VDTSILPIPCI--EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKM 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  95 LLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGN 154
Cdd:PHA02874  143 LFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGD 202
Ank_5 pfam13857
Ankyrin repeats (many copies);
95-148 1.63e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.50  E-value: 1.63e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370466417  95 LLKHG-ADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDI 148
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
15-113 3.25e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 57.66  E-value: 3.25e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  15 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVE 93
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGAdVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269

                          90       100
                  ....*....|....*....|
gi 1370466417  94 VLLKHGADVNAKDMLKMTAL 113
Cdd:COG0666   270 LLLLALLLLAAALLDLLTLL 289
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 75-161 3.65e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.37  E-value: 3.65e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  75 VDRTPLHMAASE-------GHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFD 147
Cdd:PTZ00322   74 IDPVVAHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153

                          90
                  ....*....|....
gi 1370466417 148 ISIDNGNEDLAEIL 161
Cdd:PTZ00322  154 LAEENGFREVVQLL 167
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 91-172 3.72e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.54  E-value: 3.72e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  91 IVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILqIAMQNQIN 170
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAI-IDNRSNIN 238


                  ..
gi 1370466417 171 TN 172
Cdd:PHA02876  239 KN 240
Ank_4 pfam13637
Ankyrin repeats (many copies);
43-96 4.95e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 4.95e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370466417  43 GTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLL 96
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 10-161 7.35e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.31  E-value: 7.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  10 DLGKKLLEAARAGQDDEVRILMANGApFTTDWL---GTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASE 86
Cdd:PHA02875   67 DIESELHDAVEEGDVKAVEELLDLGK-FADDVFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMM 145

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370466417  87 GHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKF-CKTAFDISIDNGNEDLAEIL 161
Cdd:PHA02875  146 GDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLF 221
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 78-185 7.74e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.98  E-value: 7.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  78 TPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNH-----QEVVELLIKYGADVHTQSKFCKTAFDISIDN 152
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISK 116

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1370466417 153 GNEDLaEILQIAMQNQINTNPESPDTVT-IHAAT 185
Cdd:PHA03100  117 KSNSY-SIVEYLLDNGANVNIKNSDGENlLHLYL 149
Ank_4 pfam13637
Ankyrin repeats (many copies);
110-161 8.00e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 8.00e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370466417 110 MTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL 161
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 25-134 2.44e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.38  E-value: 2.44e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  25 DEVRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVN 103
Cdd:PHA02875  116 DIMKLLIARGAdPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1370466417 104 -AKDMLKMTALHWATEHNHQEVVELLIKYGAD 134
Cdd:PHA02875  196 yFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 77-106 2.47e-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: 49.60  E-value: 2.47e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1370466417  77 RTPLHMAA-SEGHASIVEVLLKHGADVNAKD 106
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 29-135 2.72e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 2.72e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  29 ILMANGAPFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVL------------- 95
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhfasisdphaag 623

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370466417  96 ------------------LKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADV 135
Cdd:PLN03192  624 dllctaakrndltamkelLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 11-98 3.14e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 3.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  11 LGKKLLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHA 89
Cdd:PTZ00322   82 LTVELCQLAASGDAVGARILLTGGAdPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161


                  ....*....
gi 1370466417  90 SIVEVLLKH 98
Cdd:PTZ00322  162 EVVQLLSRH 170
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 43-161 8.77e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.84  E-value: 8.77e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  43 GTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLL---KHGADVNAKDmlKMTALHWATEH 119
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLdlgKFADDVFYKD--GMTPLHLATIL 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1370466417 120 NHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL 161
Cdd:PHA02875  113 KKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 76-104 1.56e-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: 1.56e-07
                           10        20
                   ....*....|....*....|....*....
gi 1370466417   76 DRTPLHMAASEGHASIVEVLLKHGADVNA 104
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 60-157 2.18e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.14  E-value: 2.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  60 EVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQs 139
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKN- 240

                          90       100
                  ....*....|....*....|
gi 1370466417 140 kfcktafDISIDNG--NEDL 157
Cdd:PHA02876  241 -------DLSLLKAirNEDL 253
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 18-129 2.84e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.27  E-value: 2.84e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  18 AARAGQDDEVRILMANGAPFTT-DWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLL 96
Cdd:PHA02874  131 AIKKGDLESIKMLFEYGADVNIeDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1370466417  97 KHGADVNAKDMLKMTALHWATEHNhQEVVELLI 129
Cdd:PHA02874  211 DHGNHIMNKCKNGFTPLHNAIIHN-RSAIELLI 242
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 77-104 2.12e-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: 2.12e-06
                          10        20
                  ....*....|....*....|....*...
gi 1370466417  77 RTPLHMAASEGHASIVEVLLKHGADVNA 104
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
62-116 2.70e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 2.70e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370466417  62 LLRAG-VSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWA 116
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 8-163 2.74e-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: 2.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417   8 LVDLGKKLLEAARAGQDDEV----RILMANGAPFTTDWL-----------GTSPLHLAAQYGHYSTTEVLLRAGVSRDAR 72
Cdd:TIGR00870  78 RGAVGDTLLHAISLEYVDAVeailLHLLAAFRKSGPLELandqytseftpGITALHLAAHRQNYEIVKLLLERGASVPAR 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  73 TKVD--------------RTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNH---------QEVVELLI 129
Cdd:TIGR00870 158 ACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEfkaeyeelsCQMYNFAL 237

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1370466417 130 KYGADVHTQSKF-------CKTAFDISIDNGNEDLAE-ILQI 163
Cdd:TIGR00870 238 SLLDKLRDSKELevilnhqGLTPLKLAAKEGRIVLFRlKLAI 279
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 110-136 5.06e-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: 5.06e-06
                           10        20
                   ....*....|....*....|....*..
gi 1370466417  110 MTALHWATEHNHQEVVELLIKYGADVH 136
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 110-140 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: 41.89  E-value: 1.31e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1370466417 110 MTALHWATEH-NHQEVVELLIKYGADVHTQSK 140
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 11-114 2.59e-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: 2.59e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  11 LGKKLLEAARAGQDDEVRILMANGAP------FTTD-WLGTSPLHLAAQYGHYSTTEVLLRAGV--------------SR 69
Cdd:cd22192    50 LGETALHVAALYDNLEAAVVLMEAAPelvnepMTSDlYQGETALHIAVVNQNLNLVRELIARGAdvvspratgtffrpGP 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1370466417  70 DARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALH 114
Cdd:cd22192   130 KNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
PHA02946 PHA02946
ankyin-like protein; Provisional
 60-136 2.95e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.82  E-value: 2.95e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370466417  60 EVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHW--ATEHNHQEVVELLIKYGADVH 136
Cdd:PHA02946   56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKIN 134
PHA02741 PHA02741
hypothetical protein; Provisional
 80-162 3.55e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 43.88  E-value: 3.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  80 LHMAAsEGH-----ASIVEVLLKHGADVNAKDMLK-MTALHWAT-EHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDN 152
Cdd:PHA02741   64 IHIAA-EKHeaqlaAEIIDHLIELGADINAQEMLEgDTALHLAAhRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAIDN 142

                          90
                  ....*....|
gi 1370466417 153 GNEDLAEILQ 162
Cdd:PHA02741  143 EDVAMMQILR 152
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 25-106 5.21e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.04  E-value: 5.21e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  25 DEVRILMANGAPF-TTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVN 103
Cdd:PHA03100  173 NRVNYLLSYGVPInIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252


                  ...
gi 1370466417 104 AKD 106
Cdd:PHA03100  253 TII 255
PHA03095 PHA03095
ankyrin-like protein; Provisional
 82-155 1.01e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 1.01e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370466417  82 MAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQ---EVVELLIKYGADVHTQSKFCKTAFDISIDNGNE 155
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATT 96
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 47-146 1.44e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.80  E-value: 1.44e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  47 LHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVE 126
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                          90       100
                  ....*....|....*....|
gi 1370466417 127 LLIKYGADVHTQskfCKTAF 146
Cdd:PHA02874  208 LLIDHGNHIMNK---CKNGF 224
Ank_4 pfam13637
Ankyrin repeats (many copies);
15-63 2.19e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 2.19e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370466417  15 LLEAARAGQDDEVRILMANGAPF-TTDWLGTSPLHLAAQYGHYSTTEVLL 63
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADInAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 91-161 2.37e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 42.66  E-value: 2.37e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370466417  91 IVEVLLKHGADVNAK----DMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCK-TAFDISIDNGNEDLAEIL 161
Cdd:PHA02884   48 IIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEIL 123
Ank_5 pfam13857
Ankyrin repeats (many copies);
35-83 3.68e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 3.68e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1370466417  35 APFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMA 83
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 91-172 4.64e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.13  E-value: 4.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  91 IVEVLLKHGADVNAKDMLKMTALHWATEH---NHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQN 167
Cdd:PHA02798   91 IVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHIDIEIIKLLLEK 170


                  ....*
gi 1370466417 168 QINTN 172
Cdd:PHA02798  171 GVDIN 175
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 78-176 8.30e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.49  E-value: 8.30e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  78 TPLHMAASEGHASIVEVLLKHGADVN-----------------AKDMLKM------------------------------ 110
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINhintkiphplltaikigAHDIIKLlidngvdtsilpipciekdmiktildcgid 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370466417 111 ---------TALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL--QIAMQNQINTNPESP 176
Cdd:PHA02874  117 vnikdaelkTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLleKGAYANVKDNNGESP 193
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 110-137 9.38e-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: 9.38e-04
                          10        20
                  ....*....|....*....|....*...
gi 1370466417 110 MTALHWATEHNHQEVVELLIKYGADVHT 137
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 43-74 1.34e-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: 36.11  E-value: 1.34e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1370466417  43 GTSPLHLAA-QYGHYSTTEVLLRAGVSRDARTK 74
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 91-182 2.69e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.65  E-value: 2.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  91 IVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGN--EDLAEILQIAMQNq 168
Cdd:PHA03100   17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnlTDVKEIVKLLLEY- 95

                          90
                  ....*....|....
gi 1370466417 169 iNTNPESPDTVTIH 182
Cdd:PHA03100   96 -GANVNAPDNNGIT 108
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 51-135 3.05e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 39.90  E-value: 3.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  51 AQYGHYSTTEVLLRAGVSRDARTKVDRTPLH--MAASEGHASIVEVLLKHGADVNAKDMLKMTALH-----------WAT 117
Cdd:PHA02716  292 ARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvvniLDP 371

                          90       100
                  ....*....|....*....|.
gi 1370466417 118 EHNHQ---EVVELLIKYGADV 135
Cdd:PHA02716  372 ETDNDirlDVIQCLISLGADI 392
PHA02798 PHA02798
ankyrin-like protein; Provisional
 59-167 3.67e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.43  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  59 TEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLL---KHGADVNAKDMLKMTALHWATEHNHQ---EVVELLIKYG 132
Cdd:PHA02798   92 VKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKG 171

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1370466417 133 ADVHTQS-KFCKTAFDISID-NGNEDLAEILQIAMQN 167
Cdd:PHA02798  172 VDINTHNnKEKYDTLHCYFKyNIDRIDADILKLFVDN 208
PHA02791 PHA02791
ankyrin-like protein; Provisional
 23-130 4.69e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 38.48  E-value: 4.69e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  23 QDDEVRILMANGAPFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTkvDRTPLHMAASEGHASIVEVLLKHGADV 102
Cdd:PHA02791   10 KSKQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLE--NEFPLHQAATLEDTKIVKILLFSGMDD 87

                          90       100
                  ....*....|....*....|....*...
gi 1370466417 103 NAKDMLKMTALHWATEHNHQEVVELLIK 130
Cdd:PHA02791   88 SQFDDKGNTALYYAVDSGNMQTVKLFVK 115
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 78-154 6.27e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 37.88  E-value: 6.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  78 TPLHMAASEGHAS--IVEVLLKHGADVNAKDM-LKMTALHWATEHN---HQEVVELLIKYGADVHTQSKFCKTAFDISID 151
Cdd:PHA02859   53 TPIFSCLEKDKVNveILKFLIENGADVNFKTRdNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHMYMC 132


                  ...
gi 1370466417 152 NGN 154
Cdd:PHA02859  133 NFN 135
MobB_NDR_LATS-like cd21742
Mob-binding domain found in the NDR/LATS family serine/threonine protein kinases; The nuclear ...
 340-387 8.67e-03

Mob-binding domain found in the NDR/LATS family serine/threonine protein kinases; The nuclear Dbf2-related (NDR)/large tumor suppressor (LATS) family includes NDR, LATS, CBK1, and Sid2p. They are involved in regulating many cellular functions including contraction, motility, division, proliferation, apoptosis, morphogenesis, and cytokinesis. NDR/LATS kinases bind to highly conserved Mob (Mps One binder) coactivators, forming regulatory complexes that control a diverse set of in vivo effector proteins, and are essential and evolutionarily conserved components of "Hippo" signaling pathways. Mob association creates a novel binding pocket that participates in the formation of the active state of NDR/LATS kinases. These kinases contain a regulatory domain located N-terminal to the serine/threonine kinase domain (called the N-terminal regulatory (NTR) domain) and an insert within the catalytic domain that contains an auto-inhibitory sequence. This model corresponds to the NTR or Mob-binding domain of NDR/LATS family serine/threonine protein kinases.


Pssm-ID: 439267  Cd Length: 62  Bit Score: 34.48  E-value: 8.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370466417 340 IENRVESA--EIEERE----ALQKQLDEAN---REAQKYRQQLLKKEQE-AEAYRQKL 387
Cdd:cd21742     5 IENHYTNLlqQLKERRerrkQLEEKLENLNlseEEKEQLRKELLKKESEyLRLQRQKL 62
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 48-133 8.79e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 36.72  E-value: 8.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466417  48 HLAAQYGHYSTT---EVLLRAGVSRDAR-TKVDRTPLHMAASEGHASIVEVLLKH-GADVNAKDMLKMTALHWATEHNHQ 122
Cdd:PHA02743   62 HMVAWYDRANAVmkiELLVNMGADINAReLGTGNTLLHIAASTKNYELAEWLCRQlGVNLGAINYQHETAYHIAYKMRDR 141

                          90
                  ....*....|.
gi 1370466417 123 EVVELLIKYGA 133
Cdd:PHA02743  142 RMMEILRANGA 152
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 346-392 9.09e-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: 36.05  E-value: 9.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1370466417 346 SAEIEEREALQKQLDEANREAQKYRQQLLKKEQEAEAYRQKLEAMTR 392
Cdd:pfam20492  72 EMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEARE 118
 
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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