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Conserved domains on  [gi|1370466424|ref|XP_024305654|]
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GA-binding protein subunit beta-1 isoform X4 [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];
10-179 7.43e-45

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 156.65  E-value: 7.43e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVE 88
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  89 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQNQINTNP 168
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         170
                  ....*....|.
gi 1370466424 169 ESPDTVTIHAA 179
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 ...
 334-381 7.29e-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: 34.87  E-value: 7.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370466424 334 IENRVESA--EIEERE----ALQKQLDEAN---REAQKYRQQLLKKEQE-AEAYRQKL 381
Cdd:cd21742     5 IENHYTNLlqQLKERRerrkQLEEKLENLNlseEEKEQLRKELLKKESEyLRLQRQKL 62
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-179 7.43e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 156.65  E-value: 7.43e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVE 88
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  89 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQNQINTNP 168
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         170
                  ....*....|.
gi 1370466424 169 ESPDTVTIHAA 179
Cdd:COG0666   251 DGLTALLLAAA 261
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-133 1.92e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 98.65  E-value: 1.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  42 LHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHgADVNAKDMlKMTALHWATEHNHQEVVE 121
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 1370466424 122 LLIKYGADVHTQ 133
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA03095 PHA03095
ankyrin-like protein; Provisional
 20-143 1.32e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.31  E-value: 1.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  20 DEVRILMANGAPF-TTDWLGTSPLHLaaqYGHYSTTE----VLLRAGVSRDARTKVDRTPLHMAAS--EGHASIVEVLLK 92
Cdd:PHA03095   64 DIVRLLLEAGADVnAPERCGFTPLHL---YLYNATTLdvikLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLR 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370466424  93 HGADVNAKDMLKMTALHWATEhNHQ---EVVELLIKYGADVHTQSKFCKTAFDI 143
Cdd:PHA03095  141 KGADVNALDLYGMTPLAVLLK-SRNanvELLRLLIDAGADVYAVDDRFRSLLHH 193
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 10-181 7.73e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 63.49  E-value: 7.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  10 LLEAARAGQDDEVRILMANGA--PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAgvsrdARTKVD----------RTPLHM 77
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCPScdLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  78 AASEGHASIVEVLLKHGADVNAKD------MLKMTALHWATEH--------NHQEVVELLIKYGADVHTQSKFCKTAFDI 143
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVVSPRatgtffRPGPKNLIYYGEHplsfaacvGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1370466424 144 SIDNGNEDLA-EILQIAMQNQINTNPESPDTVTIHAA-TP 181
Cdd:cd22192   176 LVLQPNKTFAcQMYDLILSYDKEDDLQPLDLVPNNQGlTP 215
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 71-99 1.37e-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: 1.37e-07
                           10        20
                   ....*....|....*....|....*....
gi 1370466424   71 DRTPLHMAASEGHASIVEVLLKHGADVNA 99
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 3-158 2.66e-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: 2.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424   3 LVDLGKKLLEAARAGQDDEV----RILMANGAPFTTDWL-----------GTSPLHLAAQYGHYSTTEVLLRAGVSRDAR 67
Cdd:TIGR00870  78 RGAVGDTLLHAISLEYVDAVeailLHLLAAFRKSGPLELandqytseftpGITALHLAAHRQNYEIVKLLLERGASVPAR 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  68 TKVD--------------RTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNH---------QEVVELLI 124
Cdd:TIGR00870 158 ACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEfkaeyeelsCQMYNFAL 237

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1370466424 125 KYGADVHTQSKF-------CKTAFDISIDNGNEDLAE-ILQI 158
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 ...
 334-381 7.29e-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: 34.87  E-value: 7.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370466424 334 IENRVESA--EIEERE----ALQKQLDEAN---REAQKYRQQLLKKEQE-AEAYRQKL 381
Cdd:cd21742     5 IENHYTNLlqQLKERRerrkQLEEKLENLNlseEEKEQLRKELLKKESEyLRLQRQKL 62
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 340-386 8.93e-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: 8.93e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1370466424 340 SAEIEEREALQKQLDEANREAQKYRQQLLKKEQEAEAYRQKLEAMTR 386
Cdd:pfam20492  72 EMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEARE 118
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-179 7.43e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 156.65  E-value: 7.43e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVE 88
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGAdVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  89 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQNQINTNP 168
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                         170
                  ....*....|.
gi 1370466424 169 ESPDTVTIHAA 179
Cdd:COG0666   251 DGLTALLLAAA 261
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-156 4.40e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.54  E-value: 4.40e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  10 LLEAARAGQDDEVRILMANGAP-FTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVE 88
Cdd:COG0666    58 LLAAALAGDLLVALLLLAAGADiNAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVK 137

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370466424  89 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL 156
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLL 205
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-167 1.24e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.39  E-value: 1.24e-35
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVE 88
Cdd:COG0666   124 LHLAAYNGNLEIVKLLLEAGAdVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVK 203

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370466424  89 VLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQNQINTN 167
Cdd:COG0666   204 LLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAAL 282
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-156 2.63e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.66  E-value: 2.63e-27
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  10 LLEAARAGQDDEVRILMANGAPFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEV 89
Cdd:COG0666    26 LAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKL 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370466424  90 LLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL 156
Cdd:COG0666   106 LLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
42-133 1.92e-25

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 98.65  E-value: 1.92e-25
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  42 LHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHgADVNAKDMlKMTALHWATEHNHQEVVE 121
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 1370466424 122 LLIKYGADVHTQ 133
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-101 1.23e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 1.23e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDarTKVDRTPLHMAASEGHASIVE 88
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAdANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1370466424  89 VLLKHGADVNAKD 101
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 20-143 1.32e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.31  E-value: 1.32e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  20 DEVRILMANGAPF-TTDWLGTSPLHLaaqYGHYSTTE----VLLRAGVSRDARTKVDRTPLHMAAS--EGHASIVEVLLK 92
Cdd:PHA03095   64 DIVRLLLEAGADVnAPERCGFTPLHL---YLYNATTLdvikLLIKAGADVNAKDKVGRTPLHVYLSgfNINPKVIRLLLR 140

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370466424  93 HGADVNAKDMLKMTALHWATEhNHQ---EVVELLIKYGADVHTQSKFCKTAFDI 143
Cdd:PHA03095  141 KGADVNALDLYGMTPLAVLLK-SRNanvELLRLLIDAGADVYAVDDRFRSLLHH 193
Ank_2 pfam12796
Ankyrin repeats (3 copies);
75-156 4.94e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 4.94e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  75 LHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYgADVHTQSKFcKTAFDISIDNGNEDLAE 154
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG-RTALHYAARSGHLEIVK 78


                  ..
gi 1370466424 155 IL 156
Cdd:pfam12796  79 LL 80
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 22-168 6.93e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.55  E-value: 6.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  22 VRILMANGAPFT-TDWLGTSPLHLAAQY--GHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHA--SIVEVLLKHGAD 96
Cdd:PHA03100   89 VKLLLEYGANVNaPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVD 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  97 ----------------VNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEdlaEILQIAM 160
Cdd:PHA03100  169 inaknrvnyllsygvpINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNK---EIFKLLL 245


                  ....*...
gi 1370466424 161 QNQINTNP 168
Cdd:PHA03100  246 NNGPSIKT 253
PHA03095 PHA03095
ankyrin-like protein; Provisional
 20-153 1.17e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.14  E-value: 1.17e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  20 DEVRILMANGAPFT-TDWLGTSPLHLAAQYGHYSTTEV---LLRAGVSRDARTKVDRTPLH---MAASEghASIVEVLLK 92
Cdd:PHA03095   28 EEVRRLLAAGADVNfRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHlylYNATT--LDVIKLLIK 105

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1370466424  93 HGADVNAKDMLKMTALH--WATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLA 153
Cdd:PHA03095  106 AGADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVE 168
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
24-156 1.29e-14

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 73.83  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  24 ILMANGAPFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDML 103
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370466424 104 KMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL 156
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLL 139
PHA03095 PHA03095
ankyrin-like protein; Provisional
 22-174 3.66e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.52  E-value: 3.66e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  22 VRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTT--EVLLRAGVSRDARTKVDRTPLHMAA--SEGHASIVEVLLKHGAD 96
Cdd:PHA03095  170 LRLLIDAGAdVYAVDDRFRSLLHHHLQSFKPRARivRELIRAGCDPAATDMLGNTPLHSMAtgSSCKRSLVLPLLIAGIS 249

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1370466424  97 VNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDlaeilqiAMQNQINTNPeSPDTV 174
Cdd:PHA03095  250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGR-------AVRAALAKNP-SAETV 319
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 14-193 4.49e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.86  E-value: 4.49e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  14 ARAGQDDE-VRILMANGAPFT-TDWLGTSPLHLAAQYGHYSTTEV-LLRAGVSRDARTKVDRTPLHMAASEGHASIVEVL 90
Cdd:PHA02876  315 AKNGYDTEnIRTLIMLGADVNaADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  91 LKHGADVNAKDMLKMTALHWA-TEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEdlAEILQIAMQNQINTNpe 169
Cdd:PHA02876  395 LDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCK--LDVIEMLLDNGADVN-- 470

                         170       180
                  ....*....|....*....|....*
gi 1370466424 170 spdTVTIHAATPQFI-IGPGGVVNL 193
Cdd:PHA02876  471 ---AINIQNQYPLLIaLEYHGIVNI 492
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 22-176 2.19e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.37  E-value: 2.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  22 VRILMANGAPFT--TDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNA 99
Cdd:PHA02878  150 TKLLLSYGADINmkDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424 100 KDMLKMTALHWATEH-NHQEVVELLIKYGADVHTQSKFCK-TAFDISIDNgNEDLAEILQI-AMQNQINTNPESPDTVTI 176
Cdd:PHA02878  230 RDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGlTALHSSIKS-ERKLKLLLEYgADINSLNSYKLTPLSSAV 308
Ank_4 pfam13637
Ankyrin repeats (many copies);
72-124 2.47e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 61.14  E-value: 2.47e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1370466424  72 RTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLI 124
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 23-167 2.67e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.77  E-value: 2.67e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  23 RILMANGAPFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHAS-----IVEVLLKHGADV 97
Cdd:PHA03100   20 YIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANV 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1370466424  98 NAKDMLKMTALHWA--TEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLaEILQIAMQNQINTN 167
Cdd:PHA03100  100 NAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDL-KILKLLIDKGVDIN 170
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 34-162 6.96e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.20  E-value: 6.96e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  34 TDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATE 113
Cdd:PLN03192  521 DDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAIS 600

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1370466424 114 HNHQEVVELLIKYGA--DVHTQSK-FCKTA-------------FDISIDNGNEDLAEILQIAMQN 162
Cdd:PLN03192  601 AKHHKIFRILYHFASisDPHAAGDlLCTAAkrndltamkellkQGLNVDSEDHQGATALQVAMAE 665
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 10-181 7.73e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 63.49  E-value: 7.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  10 LLEAARAGQDDEVRILMANGA--PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAgvsrdARTKVD----------RTPLHM 77
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCPScdLFQRGALGETALHVAALYDNLEAAVVLMEA-----APELVNepmtsdlyqgETALHI 95

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  78 AASEGHASIVEVLLKHGADVNAKD------MLKMTALHWATEH--------NHQEVVELLIKYGADVHTQSKFCKTAFDI 143
Cdd:cd22192    96 AVVNQNLNLVRELIARGADVVSPRatgtffRPGPKNLIYYGEHplsfaacvGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1370466424 144 SIDNGNEDLA-EILQIAMQNQINTNPESPDTVTIHAA-TP 181
Cdd:cd22192   176 LVLQPNKTFAcQMYDLILSYDKEDDLQPLDLVPNNQGlTP 215
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 43-131 3.39e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.84  E-value: 3.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  43 HLAAQyGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVEL 122
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQL 166


                  ....*....
gi 1370466424 123 LIKYGADVH 131
Cdd:PTZ00322  167 LSRHSQCHF 175
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 10-149 8.99e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 59.98  E-value: 8.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  10 LLEAARAGQDDEVRILMANGapfttdwLGTSPLHLAAQygHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEV 89
Cdd:PHA02874   72 LLTAIKIGAHDIIKLLIDNG-------VDTSILPIPCI--EKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKM 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  90 LLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGN 149
Cdd:PHA02874  143 LFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGD 202
Ank_5 pfam13857
Ankyrin repeats (many copies);
90-143 1.64e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 53.50  E-value: 1.64e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1370466424  90 LLKHG-ADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDI 143
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 84-167 2.26e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.74  E-value: 2.26e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  84 ASIVEVLLKHGADVNAKDMLKM-TALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILqiaMQN 162
Cdd:PHA02878  147 AEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHIL---LEN 223


                  ....*
gi 1370466424 163 QINTN 167
Cdd:PHA02878  224 GASTD 228
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
10-108 3.17e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 57.66  E-value: 3.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  10 LLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVE 88
Cdd:COG0666   190 LHLAAENGHLEIVKLLLEAGAdVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVK 269

                          90       100
                  ....*....|....*....|
gi 1370466424  89 VLLKHGADVNAKDMLKMTAL 108
Cdd:COG0666   270 LLLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 86-167 3.56e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.54  E-value: 3.56e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  86 IVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILqIAMQNQIN 165
Cdd:PHA02876  160 IAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAI-IDNRSNIN 238


                  ..
gi 1370466424 166 TN 167
Cdd:PHA02876  239 KN 240
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 70-156 3.58e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.37  E-value: 3.58e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  70 VDRTPLHMAASE-------GHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFD 142
Cdd:PTZ00322   74 IDPVVAHMLTVElcqlaasGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153

                          90
                  ....*....|....
gi 1370466424 143 ISIDNGNEDLAEIL 156
Cdd:PTZ00322  154 LAEENGFREVVQLL 167
Ank_4 pfam13637
Ankyrin repeats (many copies);
38-91 4.87e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 4.87e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1370466424  38 GTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLL 91
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 5-156 5.91e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.31  E-value: 5.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424   5 DLGKKLLEAARAGQDDEVRILMANGApFTTDWL---GTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASE 81
Cdd:PHA02875   67 DIESELHDAVEEGDVKAVEELLDLGK-FADDVFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMM 145

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370466424  82 GHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKF-CKTAFDISIDNGNEDLAEIL 156
Cdd:PHA02875  146 GDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLF 221
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 73-180 7.50e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.98  E-value: 7.50e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  73 TPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNH-----QEVVELLIKYGADVHTQSKFCKTAFDISIDN 147
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAISK 116

                          90       100       110
                  ....*....|....*....|....*....|....
gi 1370466424 148 GNEDLaEILQIAMQNQINTNPESPDTVT-IHAAT 180
Cdd:PHA03100  117 KSNSY-SIVEYLLDNGANVNIKNSDGENlLHLYL 149
Ank_4 pfam13637
Ankyrin repeats (many copies);
105-156 7.87e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 7.87e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1370466424 105 MTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL 156
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 20-129 2.05e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 55.77  E-value: 2.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  20 DEVRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVN 98
Cdd:PHA02875  116 DIMKLLIARGAdPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1370466424  99 -AKDMLKMTALHWATEHNHQEVVELLIKYGAD 129
Cdd:PHA02875  196 yFGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 72-101 2.43e-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: 2.43e-08
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1370466424  72 RTPLHMAA-SEGHASIVEVLLKHGADVNAKD 101
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 24-130 2.60e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 2.60e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  24 ILMANGAPFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVL------------- 90
Cdd:PLN03192  544 LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhfasisdphaag 623

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370466424  91 ------------------LKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADV 130
Cdd:PLN03192  624 dllctaakrndltamkelLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 6-93 3.12e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 3.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424   6 LGKKLLEAARAGQDDEVRILMANGA-PFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHA 84
Cdd:PTZ00322   82 LTVELCQLAASGDAVGARILLTGGAdPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161


                  ....*....
gi 1370466424  85 SIVEVLLKH 93
Cdd:PTZ00322  162 EVVQLLSRH 170
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 38-156 7.25e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.84  E-value: 7.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  38 GTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLL---KHGADVNAKDmlKMTALHWATEH 114
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLdlgKFADDVFYKD--GMTPLHLATIL 112

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1370466424 115 NHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL 156
Cdd:PHA02875  113 KKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELL 154
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 71-99 1.37e-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: 1.37e-07
                           10        20
                   ....*....|....*....|....*....
gi 1370466424   71 DRTPLHMAASEGHASIVEVLLKHGADVNA 99
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 55-152 2.10e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.14  E-value: 2.10e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  55 EVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQs 134
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKN- 240

                          90       100
                  ....*....|....*....|
gi 1370466424 135 kfcktafDISIDNG--NEDL 152
Cdd:PHA02876  241 -------DLSLLKAirNEDL 253
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 13-124 2.76e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.27  E-value: 2.76e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  13 AARAGQDDEVRILMANGAPFTT-DWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLL 91
Cdd:PHA02874  131 AIKKGDLESIKMLFEYGADVNIeDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI 210

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1370466424  92 KHGADVNAKDMLKMTALHWATEHNhQEVVELLI 124
Cdd:PHA02874  211 DHGNHIMNKCKNGFTPLHNAIIHN-RSAIELLI 242
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 72-99 2.09e-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: 2.09e-06
                          10        20
                  ....*....|....*....|....*...
gi 1370466424  72 RTPLHMAASEGHASIVEVLLKHGADVNA 99
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 3-158 2.66e-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: 2.66e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424   3 LVDLGKKLLEAARAGQDDEV----RILMANGAPFTTDWL-----------GTSPLHLAAQYGHYSTTEVLLRAGVSRDAR 67
Cdd:TIGR00870  78 RGAVGDTLLHAISLEYVDAVeailLHLLAAFRKSGPLELandqytseftpGITALHLAAHRQNYEIVKLLLERGASVPAR 157

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  68 TKVD--------------RTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNH---------QEVVELLI 124
Cdd:TIGR00870 158 ACGDffvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLVMENEfkaeyeelsCQMYNFAL 237

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1370466424 125 KYGADVHTQSKF-------CKTAFDISIDNGNEDLAE-ILQI 158
Cdd:TIGR00870 238 SLLDKLRDSKELevilnhqGLTPLKLAAKEGRIVLFRlKLAI 279
Ank_5 pfam13857
Ankyrin repeats (many copies);
57-111 2.79e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 2.79e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1370466424  57 LLRAG-VSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWA 111
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 105-131 4.57e-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: 4.57e-06
                           10        20
                   ....*....|....*....|....*..
gi 1370466424  105 MTALHWATEHNHQEVVELLIKYGADVH 131
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 105-135 1.29e-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: 1.29e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1370466424 105 MTALHWATEH-NHQEVVELLIKYGADVHTQSK 135
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 6-109 2.52e-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: 2.52e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424   6 LGKKLLEAARAGQDDEVRILMANGAP------FTTD-WLGTSPLHLAAQYGHYSTTEVLLRAGV--------------SR 64
Cdd:cd22192    50 LGETALHVAALYDNLEAAVVLMEAAPelvnepMTSDlYQGETALHIAVVNQNLNLVRELIARGAdvvspratgtffrpGP 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*
gi 1370466424  65 DARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALH 109
Cdd:cd22192   130 KNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLH 174
PHA02946 PHA02946
ankyin-like protein; Provisional
 55-131 2.87e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.82  E-value: 2.87e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1370466424  55 EVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHW--ATEHNHQEVVELLIKYGADVH 131
Cdd:PHA02946   56 EELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKIN 134
PHA02741 PHA02741
hypothetical protein; Provisional
 75-157 3.68e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 43.88  E-value: 3.68e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  75 LHMAAsEGH-----ASIVEVLLKHGADVNAKDMLK-MTALHWAT-EHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDN 147
Cdd:PHA02741   64 IHIAA-EKHeaqlaAEIIDHLIELGADINAQEMLEgDTALHLAAhRRDHDLAEWLCCQPGIDLHFCNADNKSPFELAIDN 142

                          90
                  ....*....|
gi 1370466424 148 GNEDLAEILQ 157
Cdd:PHA02741  143 EDVAMMQILR 152
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 20-101 5.08e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.04  E-value: 5.08e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  20 DEVRILMANGAPF-TTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVN 98
Cdd:PHA03100  173 NRVNYLLSYGVPInIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252


                  ...
gi 1370466424  99 AKD 101
Cdd:PHA03100  253 TII 255
PHA03095 PHA03095
ankyrin-like protein; Provisional
 77-150 9.81e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 9.81e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370466424  77 MAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQ---EVVELLIKYGADVHTQSKFCKTAFDISIDNGNE 150
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHLYLYNATT 96
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 42-141 1.40e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.80  E-value: 1.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  42 LHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVE 121
Cdd:PHA02874  128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIK 207

                          90       100
                  ....*....|....*....|
gi 1370466424 122 LLIKYGADVHTQskfCKTAF 141
Cdd:PHA02874  208 LLIDHGNHIMNK---CKNGF 224
Ank_4 pfam13637
Ankyrin repeats (many copies);
10-58 2.15e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 2.15e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370466424  10 LLEAARAGQDDEVRILMANGAPF-TTDWLGTSPLHLAAQYGHYSTTEVLL 58
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADInAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 86-156 2.32e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 42.66  E-value: 2.32e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1370466424  86 IVEVLLKHGADVNAK----DMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCK-TAFDISIDNGNEDLAEIL 156
Cdd:PHA02884   48 IIDAILKLGADPEAPfplsENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEIL 123
Ank_5 pfam13857
Ankyrin repeats (many copies);
30-78 3.69e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 3.69e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1370466424  30 APFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTKVDRTPLHMA 78
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 86-167 4.52e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.13  E-value: 4.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  86 IVEVLLKHGADVNAKDMLKMTALHWATEH---NHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEILQIAMQN 162
Cdd:PHA02798   91 IVKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHIDIEIIKLLLEK 170


                  ....*
gi 1370466424 163 QINTN 167
Cdd:PHA02798  171 GVDIN 175
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 73-171 8.10e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 41.49  E-value: 8.10e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  73 TPLHMAASEGHASIVEVLLKHGADVN-----------------AKDMLKM------------------------------ 105
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINhintkiphplltaikigAHDIIKLlidngvdtsilpipciekdmiktildcgid 116

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1370466424 106 ---------TALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGNEDLAEIL--QIAMQNQINTNPESP 171
Cdd:PHA02874  117 vnikdaelkTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLleKGAYANVKDNNGESP 193
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 105-132 9.24e-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: 9.24e-04
                          10        20
                  ....*....|....*....|....*...
gi 1370466424 105 MTALHWATEHNHQEVVELLIKYGADVHT 132
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 38-69 1.32e-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: 1.32e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1370466424  38 GTSPLHLAA-QYGHYSTTEVLLRAGVSRDARTK 69
Cdd:pfam00023   2 GNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 86-177 2.62e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.65  E-value: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  86 IVEVLLKHGADVNAKDMLKMTALHWATEHNHQEVVELLIKYGADVHTQSKFCKTAFDISIDNGN--EDLAEILQIAMQNq 163
Cdd:PHA03100   17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnlTDVKEIVKLLLEY- 95

                          90
                  ....*....|....
gi 1370466424 164 iNTNPESPDTVTIH 177
Cdd:PHA03100   96 -GANVNAPDNNGIT 108
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 46-130 2.98e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 39.90  E-value: 2.98e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  46 AQYGHYSTTEVLLRAGVSRDARTKVDRTPLH--MAASEGHASIVEVLLKHGADVNAKDMLKMTALH-----------WAT 112
Cdd:PHA02716  292 ARNIDISVVYSFLQPGVKLHYKDSAGRTCLHqyILRHNISTDIIKLLHEYGNDLNEPDNIGNTVLHtylsmlsvvniLDP 371

                          90       100
                  ....*....|....*....|.
gi 1370466424 113 EHNHQ---EVVELLIKYGADV 130
Cdd:PHA02716  372 ETDNDirlDVIQCLISLGADI 392
PHA02798 PHA02798
ankyrin-like protein; Provisional
 54-162 3.59e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.43  E-value: 3.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  54 TEVLLRAGVSRDARTKVDRTPLHMAASEGHASIVEVLL---KHGADVNAKDMLKMTALHWATEHNHQ---EVVELLIKYG 127
Cdd:PHA02798   92 VKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKG 171

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1370466424 128 ADVHTQS-KFCKTAFDISID-NGNEDLAEILQIAMQN 162
Cdd:PHA02798  172 VDINTHNnKEKYDTLHCYFKyNIDRIDADILKLFVDN 208
PHA02791 PHA02791
ankyrin-like protein; Provisional
 18-125 4.32e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 38.87  E-value: 4.32e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  18 QDDEVRILMANGAPFTTDWLGTSPLHLAAQYGHYSTTEVLLRAGVSRDARTkvDRTPLHMAASEGHASIVEVLLKHGADV 97
Cdd:PHA02791   10 KSKQLKSFLSSKDAFKADVHGHSALYYAIADNNVRLVCTLLNAGALKNLLE--NEFPLHQAATLEDTKIVKILLFSGMDD 87

                          90       100
                  ....*....|....*....|....*...
gi 1370466424  98 NAKDMLKMTALHWATEHNHQEVVELLIK 125
Cdd:PHA02791   88 SQFDDKGNTALYYAVDSGNMQTVKLFVK 115
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 73-149 6.15e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 37.88  E-value: 6.15e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  73 TPLHMAASEGHAS--IVEVLLKHGADVNAKDM-LKMTALHWATEHN---HQEVVELLIKYGADVHTQSKFCKTAFDISID 146
Cdd:PHA02859   53 TPIFSCLEKDKVNveILKFLIENGADVNFKTRdNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHMYMC 132


                  ...
gi 1370466424 147 NGN 149
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 ...
 334-381 7.29e-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: 34.87  E-value: 7.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1370466424 334 IENRVESA--EIEERE----ALQKQLDEAN---REAQKYRQQLLKKEQE-AEAYRQKL 381
Cdd:cd21742     5 IENHYTNLlqQLKERRerrkQLEEKLENLNlseEEKEQLRKELLKKESEyLRLQRQKL 62
ERM_helical pfam20492
Ezrin/radixin/moesin, alpha-helical domain; The ERM family consists of three closely-related ...
 340-386 8.93e-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: 8.93e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1370466424 340 SAEIEEREALQKQLDEANREAQKYRQQLLKKEQEAEAYRQKLEAMTR 386
Cdd:pfam20492  72 EMEAEEKEQLEAELAEAQEEIARLEEEVERKEEEARRLQEELEEARE 118
PHA02743 PHA02743
Viral ankyrin protein; Provisional
 43-128 9.04e-03

Viral ankyrin protein; Provisional


Pssm-ID: 222925 [Multi-domain]  Cd Length: 166  Bit Score: 36.72  E-value: 9.04e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1370466424  43 HLAAQYGHYSTT---EVLLRAGVSRDAR-TKVDRTPLHMAASEGHASIVEVLLKH-GADVNAKDMLKMTALHWATEHNHQ 117
Cdd:PHA02743   62 HMVAWYDRANAVmkiELLVNMGADINAReLGTGNTLLHIAASTKNYELAEWLCRQlGVNLGAINYQHETAYHIAYKMRDR 141

                          90
                  ....*....|.
gi 1370466424 118 EVVELLIKYGA 128
Cdd:PHA02743  142 RMMEILRANGA 152
CREPT pfam16566
Cell-cycle alteration and expression-elevated protein in tumour; CREPT (Cell-cycle alteration ...
 340-389 9.86e-03

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


Pssm-ID: 465181 [Multi-domain]  Cd Length: 147  Bit Score: 36.44  E-value: 9.86e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1370466424 340 SAEIEEREALQKQLDEAnreAQKYRQQLLKKEQEAEAYRQKLEAMTRLQT 389
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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