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Conserved domains on  [gi|157743292|ref|NP_997721|]
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ankyrin repeat and SOCS box protein 18 [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];
119-327 3.73e-31

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.60  E-value: 3.73e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 119 ELTTPLCIAAAHGHTACVRHLLGRGADPDA-SPGGRGALHEACLGGHTACVRLLLQHRADPDLLSAEGLAPLHLCRTAAS 197
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNArDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 198 LGCAQALLEHGASVQRVGGTGRdTPLHVAAQRGLDEHARLYLGRGAHVDARNGRGETALSAACGAARRpdehgrclRLCA 277
Cdd:COG0666  166 LEIVKLLLEAGADVNARDNDGE-TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNL--------EIVK 236

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 157743292 278 LLLRRGAEADARDEDERSPLHKACGHASHSLARLLLRHGADAGALDYGGA 327
Cdd:COG0666  237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
 420-466 9.04e-15

SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. Asb4 was identified as imprinted gene in mice. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


:

Pssm-ID: 239693  Cd Length: 48  Bit Score: 68.24  E-value: 9.04e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 157743292 420 TPRCLQHLCRCALRRLFGKRCFDLIPLLPLPKPLQNYLLLEPQGVLH 466
Cdd:cd03723    2 TPRSLQHLCRCAIRKLLGSRCHKLVPQLSLPTSLKNYLLLEPEGVLY 48
PTZ00322 super family cl31426
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 283-388 1.14e-07

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


The actual alignment was detected with superfamily member PTZ00322:

Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 283 GAEADARDEDERSPLHKACGHASHSLARLLLRHGADAGALDYGGASPLgrvlqtaSCALQASPQRTVQALLNH------G 356
Cdd:PTZ00322 105 GADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL-------ELAEENGFREVVQLLSRHsqchfeL 177

                         90       100       110
                 ....*....|....*....|....*....|...
gi 157743292 357 SPTVWPDAFPKVLKTCASVPAVIEVL-FNSYPQ 388
Cdd:PTZ00322 178 GANAKPDSFTGKPPSLEDSPISSHHPdFSAVPQ 210
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
119-327 3.73e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.60  E-value: 3.73e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 119 ELTTPLCIAAAHGHTACVRHLLGRGADPDA-SPGGRGALHEACLGGHTACVRLLLQHRADPDLLSAEGLAPLHLCRTAAS 197
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNArDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 198 LGCAQALLEHGASVQRVGGTGRdTPLHVAAQRGLDEHARLYLGRGAHVDARNGRGETALSAACGAARRpdehgrclRLCA 277
Cdd:COG0666  166 LEIVKLLLEAGADVNARDNDGE-TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNL--------EIVK 236

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 157743292 278 LLLRRGAEADARDEDERSPLHKACGHASHSLARLLLRHGADAGALDYGGA 327
Cdd:COG0666  237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
Ank_2 pfam12796
Ankyrin repeats (3 copies);
124-213 3.98e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.53  E-value: 3.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292  124 LCIAAAHGHTACVRHLLGRGADPDA-SPGGRGALHEACLGGHTACVRLLLQHrADPDlLSAEGLAPLHLCRTAASLGCAQ 202
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLqDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 157743292  203 ALLEHGASVQR 213
Cdd:pfam12796  79 LLLEKGADINV 89
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
 420-466 9.04e-15

SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. Asb4 was identified as imprinted gene in mice. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239693  Cd Length: 48  Bit Score: 68.24  E-value: 9.04e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 157743292 420 TPRCLQHLCRCALRRLFGKRCFDLIPLLPLPKPLQNYLLLEPQGVLH 466
Cdd:cd03723    2 TPRSLQHLCRCAIRKLLGSRCHKLVPQLSLPTSLKNYLLLEPEGVLY 48
PHA03095 PHA03095
ankyrin-like protein; Provisional
 136-410 2.00e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.82  E-value: 2.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 136 VRHLLGRGADPDASPG-GRGALHeACLGG---HTACVRLLLQHRADPDLLSAEGLAPLH--LCRTAASLGCAQALLEHGA 209
Cdd:PHA03095 100 IKLLIKAGADVNAKDKvGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 210 SVQRVGGTGRdTPLHVAAQ--RGLDEHARLYLGRGAHVDARNGRGETALS--AACGAARRPDehgrclrlCALLLRRGAE 285
Cdd:PHA03095 179 DVYAVDDRFR-SLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHsmATGSSCKRSL--------VLPLLIAGIS 249

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 286 ADARDEDERSPLHKACGHASHSLARLLLRHGADAGALDYGGASPL--------GRVLQTascALQASPQ-RTVQALLNHG 356
Cdd:PHA03095 250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLslmvrnnnGRAVRA---ALAKNPSaETVAATLNTA 326

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157743292 357 SPTVWPDAfpkvlkTCASVPAVIEVLfnsypqLCLSESwkeVIPEEVFQMHKPF 410
Cdd:PHA03095 327 SVAGGDIP------SDATRLCVAKVV------LRGAFS---LLPEPIRAYHADF 365
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 283-388 1.14e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 283 GAEADARDEDERSPLHKACGHASHSLARLLLRHGADAGALDYGGASPLgrvlqtaSCALQASPQRTVQALLNH------G 356
Cdd:PTZ00322 105 GADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL-------ELAEENGFREVVQLLSRHsqchfeL 177

                         90       100       110
                 ....*....|....*....|....*....|...
gi 157743292 357 SPTVWPDAFPKVLKTCASVPAVIEVL-FNSYPQ 388
Cdd:PTZ00322 178 GANAKPDSFTGKPPSLEDSPISSHHPdFSAVPQ 210
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 108-256 3.13e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.71  E-value: 3.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 108 LSGLWTLEYKRELTTPLCIAAAHGHTACVRHLLGrgaDPDASPGGRG-----ALHEACLGGHTACVRLLLqhRADPDLLS 182
Cdd:cd22192    5 LDELHLLQQKRISESPLLLAAKENDVQAIKKLLK---CPSCDLFQRGalgetALHVAALYDNLEAAVVLM--EAAPELVN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 183 A-------EGLAPLHLCRTAASLGCAQALLEHGASVQ--RVGGT----GRDT-------PLHVAAQRGLDEHARLYLGRG 242
Cdd:cd22192   80 EpmtsdlyQGETALHIAVVNQNLNLVRELIARGADVVspRATGTffrpGPKNliyygehPLSFAACVGNEEIVRLLIEHG 159

                        170
                 ....*....|....
gi 157743292 243 AHVDARNGRGETAL 256
Cdd:cd22192  160 ADIRAQDSLGNTVL 173
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 420-442 1.80e-04

SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more generic proteins that comprise a large family of E3 ubiquitin protein ligases.


Pssm-ID: 462192  Cd Length: 39  Bit Score: 38.69  E-value: 1.80e-04
                          10        20
                  ....*....|....*....|...
gi 157743292  420 TPRCLQHLCRCALRRLFGKRCFD 442
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLG 23
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 122-148 5.52e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 5.52e-04
                           10        20
                   ....*....|....*....|....*..
gi 157743292   122 TPLCIAAAHGHTACVRHLLGRGADPDA 148
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
119-327 3.73e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.60  E-value: 3.73e-31
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 119 ELTTPLCIAAAHGHTACVRHLLGRGADPDA-SPGGRGALHEACLGGHTACVRLLLQHRADPDLLSAEGLAPLHLCRTAAS 197
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNArDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 198 LGCAQALLEHGASVQRVGGTGRdTPLHVAAQRGLDEHARLYLGRGAHVDARNGRGETALSAACGAARRpdehgrclRLCA 277
Cdd:COG0666  166 LEIVKLLLEAGADVNARDNDGE-TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNL--------EIVK 236

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 157743292 278 LLLRRGAEADARDEDERSPLHKACGHASHSLARLLLRHGADAGALDYGGA 327
Cdd:COG0666  237 LLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLL 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
120-330 5.64e-28

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 112.74  E-value: 5.64e-28
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 120 LTTPLCIAAAHGHTACVRHLLGRGADPDA-SPGGRGALHEACLGGHTACVRLLLQHRADPDLLSAEGLAPLHLCRTAASL 198
Cdd:COG0666   54 GALLLLAAALAGDLLVALLLLAAGADINAkDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 199 GCAQALLEHGASVQRVGGTGRdTPLHVAAQRGLDEHARLYLGRGAHVDARNGRGETALSAACgAARRPD------EHgrc 272
Cdd:COG0666  134 EIVKLLLEAGADVNAQDNDGN-TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA-ENGHLEivklllEA--- 208

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157743292 273 lrlcalllrrGAEADARDEDERSPLHKACGHASHSLARLLLRHGADAGALDYGGASPL 330
Cdd:COG0666  209 ----------GADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTAL 256
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
126-330 1.58e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.33  E-value: 1.58e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 126 IAAAHGHTACVRHLLGRGADPDASPGGRGALHEACLGGHTACVRLLLQHRADPDLLSAEGLAPLHLCRTAASLGCAQALL 205
Cdd:COG0666   28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLL 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 206 EHGASVQRVGGTGRdTPLHVAAQRGLDEHARLYLGRGAHVDARNGRGETALSAACgAARRPD------EHgrclrlcall 279
Cdd:COG0666  108 EAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAA-ANGNLEivklllEA---------- 175

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 157743292 280 lrrGAEADARDEDERSPLHKACGHASHSLARLLLRHGADAGALDYGGASPL 330
Cdd:COG0666  176 ---GADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
155-356 3.70e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.84  E-value: 3.70e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 155 ALHEACLGGHTACVRLLLQHRADPDLLSAEGLAPLHLCRTAASLGCAQALLEHGASVQRVGGTGrDTPLHVAAQRGLDEH 234
Cdd:COG0666   24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG-NTLLHAAARNGDLEI 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 235 ARLYLGRGAHVDARNGRGETALSAACgAARRPD------EHgrclrlcalllrrGAEADARDEDERSPLHKACGHASHSL 308
Cdd:COG0666  103 VKLLLEAGADVNARDKDGETPLHLAA-YNGNLEivklllEA-------------GADVNAQDNDGNTPLHLAAANGNLEI 168

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 157743292 309 ARLLLRHGADAGALDYGGASPLgrvlqtaSCALQASPQRTVQALLNHG 356
Cdd:COG0666  169 VKLLLEAGADVNARDNDGETPL-------HLAAENGHLEIVKLLLEAG 209
Ank_2 pfam12796
Ankyrin repeats (3 copies);
124-213 3.98e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.53  E-value: 3.98e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292  124 LCIAAAHGHTACVRHLLGRGADPDA-SPGGRGALHEACLGGHTACVRLLLQHrADPDlLSAEGLAPLHLCRTAASLGCAQ 202
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLqDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|.
gi 157743292  203 ALLEHGASVQR 213
Cdd:pfam12796  79 LLLEKGADINV 89
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
 420-466 9.04e-15

SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. Asb4 was identified as imprinted gene in mice. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239693  Cd Length: 48  Bit Score: 68.24  E-value: 9.04e-15
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 157743292 420 TPRCLQHLCRCALRRLFGKRCFDLIPLLPLPKPLQNYLLLEPQGVLH 466
Cdd:cd03723    2 TPRSLQHLCRCAIRKLLGSRCHKLVPQLSLPTSLKNYLLLEPEGVLY 48
Ank_2 pfam12796
Ankyrin repeats (3 copies);
156-249 1.81e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 1.81e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292  156 LHEACLGGHTACVRLLLQHRADPDLLSAEGLAPLHLcrtAASLG---CAQALLEHGASVQRVGGTgrdTPLHVAAQRGLD 232
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHL---AAKNGhleIVKLLLEHADVNLKDNGR---TALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 157743292  233 EHARLYLGRGAHVDARN 249
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 136-410 2.00e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.82  E-value: 2.00e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 136 VRHLLGRGADPDASPG-GRGALHeACLGG---HTACVRLLLQHRADPDLLSAEGLAPLH--LCRTAASLGCAQALLEHGA 209
Cdd:PHA03095 100 IKLLIKAGADVNAKDKvGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 210 SVQRVGGTGRdTPLHVAAQ--RGLDEHARLYLGRGAHVDARNGRGETALS--AACGAARRPDehgrclrlCALLLRRGAE 285
Cdd:PHA03095 179 DVYAVDDRFR-SLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHsmATGSSCKRSL--------VLPLLIAGIS 249

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 286 ADARDEDERSPLHKACGHASHSLARLLLRHGADAGALDYGGASPL--------GRVLQTascALQASPQ-RTVQALLNHG 356
Cdd:PHA03095 250 INARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLslmvrnnnGRAVRA---ALAKNPSaETVAATLNTA 326

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 157743292 357 SPTVWPDAfpkvlkTCASVPAVIEVLfnsypqLCLSESwkeVIPEEVFQMHKPF 410
Cdd:PHA03095 327 SVAGGDIP------SDATRLCVAKVV------LRGAFS---LLPEPIRAYHADF 365
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 120-207 3.13e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 65.69  E-value: 3.13e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 120 LTTPLCIAAAHGHTACVRHLLGRGADPDASP-GGRGALHEACLGGHTACVRLLLQHRADPDLLSAEGLAPLHLCRTAASL 198
Cdd:PTZ00322  82 LTVELCQLAASGDAVGARILLTGGADPNCRDyDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161


                 ....*....
gi 157743292 199 GCAQALLEH 207
Cdd:PTZ00322 162 EVVQLLSRH 170
Ank_2 pfam12796
Ankyrin repeats (3 copies);
122-180 8.93e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 8.93e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 157743292  122 TPLCIAAAHGHTACVRHLLgRGADPDASPGGRGALHEACLGGHTACVRLLLQHRADPDL 180
Cdd:pfam12796  32 TALHLAAKNGHLEIVKLLL-EHADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINV 89
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 122-357 4.77e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.00  E-value: 4.77e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 122 TPLCIAAAHGHTACVRHLLGRGADPDA-SPGGRGALHEACLGGHTACVRLLLQHRA-----DPDLLSA------------ 183
Cdd:PHA02876 180 TPIHYAAERGNAKMVNLLLSYGADVNIiALDDLSVLECAVDSKNIDTIKAIIDNRSninknDLSLLKAirnedletslll 259

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 184 --EGLA----------PLHLCRTAASLG-CAQALLEHGASVQRVGGTGrDTPLHVAAQRGLD-EHARLYLGRGAHVDARN 249
Cdd:PHA02876 260 ydAGFSvnsiddckntPLHHASQAPSLSrLVPKLLERGADVNAKNIKG-ETPLYLMAKNGYDtENIRTLIMLGADVNAAD 338

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 250 GRGETALSAACGAARRPDehgrclrLCALLLRRGAEADARDEDERSPLHKACGHASHSLARLLLRHGADAGALdyggASP 329
Cdd:PHA02876 339 RLYITPLHQASTLDRNKD-------IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEAL----SQK 407

                        250       260
                 ....*....|....*....|....*...
gi 157743292 330 LGRVLQTASCAlqASPQRTVQALLNHGS 357
Cdd:PHA02876 408 IGTALHFALCG--TNPYMSVKTLIDRGA 433
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 122-243 1.68e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.62  E-value: 1.68e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 122 TPLCIAAAHGHTACVRHLLGRGADPDASPGGR-GALHEACLGGHTACVRLLLQHRADPDLLSAEGLAPLHLCRTAASLGC 200
Cdd:PHA02875 104 TPLHLATILKKLDIMKLLIARGADPDIPNTDKfSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 157743292 201 AQALLEHGASVQRVGGTGRDTPLHVAAQRGLDEHARLYLGRGA 243
Cdd:PHA02875 184 CKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGA 226
PHA03095 PHA03095
ankyrin-like protein; Provisional
 136-340 3.49e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.88  E-value: 3.49e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 136 VRHLLGRGADPD-ASPGGRGALHeACLggHTAC------VRLLLQHRADPDLLSAEGLAPLHLC-RTAASLGCAQALLEH 207
Cdd:PHA03095  30 VRRLLAAGADVNfRGEYGKTPLH-LYL--HYSSekvkdiVRLLLEAGADVNAPERCGFTPLHLYlYNATTLDVIKLLIKA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 208 GASVQRVGGTGRdTPLHVAAqRGLDEHA---RLYLGRGAHVDARNGRGETALSAACGAARRPDEhgrclrLCALLLRRGA 284
Cdd:PHA03095 107 GADVNAKDKVGR-TPLHVYL-SGFNINPkviRLLLRKGADVNALDLYGMTPLAVLLKSRNANVE------LLRLLIDAGA 178

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157743292 285 EADARDEDERSPLHKACG--HASHSLARLLLRHGADAGALDYGGASPLGRVLQTASCA 340
Cdd:PHA03095 179 DVYAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCK 236
Ank_4 pfam13637
Ankyrin repeats (many copies);
121-172 1.38e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.74  E-value: 1.38e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157743292  121 TTPLCIAAAHGHTACVRHLLGRGADPDASPG-GRGALHEACLGGHTACVRLLL 172
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGnGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 283-388 1.14e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 1.14e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 283 GAEADARDEDERSPLHKACGHASHSLARLLLRHGADAGALDYGGASPLgrvlqtaSCALQASPQRTVQALLNH------G 356
Cdd:PTZ00322 105 GADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL-------ELAEENGFREVVQLLSRHsqchfeL 177

                         90       100       110
                 ....*....|....*....|....*....|...
gi 157743292 357 SPTVWPDAFPKVLKTCASVPAVIEVL-FNSYPQ 388
Cdd:PTZ00322 178 GANAKPDSFTGKPPSLEDSPISSHHPdFSAVPQ 210
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 122-267 1.55e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.46  E-value: 1.55e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 122 TPLCIAAAHGHTACVRHLL--GRGADPDASPGGRGALHEACLGGHTACVRLLLQHRADPDLLSAEGLAPLHLCRTAASLG 199
Cdd:PHA02875  70 SELHDAVEEGDVKAVEELLdlGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157743292 200 CAQALLEHGASVQRVGGTGRdTPLHVAAQRGLDEHARLYLGRGAHVDARNGRGETALSAACGAARRPD 267
Cdd:PHA02875 150 GIELLIDHKACLDIEDCCGC-TPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKID 216
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 122-256 2.11e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.07  E-value: 2.11e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 122 TPLCIAAAHGHTACVRHLLGRGADPDAS-PGGRGALHEACLGGHTACVRLLLQ-HRADPDLLSAEGLAPLHLCRTAASLG 199
Cdd:PHA02875  37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKyPDIESELHDAVEEGDVKAVEELLDlGKFADDVFYKDGMTPLHLATILKKLD 116

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 157743292 200 CAQALLEHGASVQrVGGTGRDTPLHVAAQRGLDEHARLYLGRGAHVDARNGRGETAL 256
Cdd:PHA02875 117 IMKLLIARGADPD-IPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 108-256 3.13e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.71  E-value: 3.13e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 108 LSGLWTLEYKRELTTPLCIAAAHGHTACVRHLLGrgaDPDASPGGRG-----ALHEACLGGHTACVRLLLqhRADPDLLS 182
Cdd:cd22192    5 LDELHLLQQKRISESPLLLAAKENDVQAIKKLLK---CPSCDLFQRGalgetALHVAALYDNLEAAVVLM--EAAPELVN 79

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 183 A-------EGLAPLHLCRTAASLGCAQALLEHGASVQ--RVGGT----GRDT-------PLHVAAQRGLDEHARLYLGRG 242
Cdd:cd22192   80 EpmtsdlyQGETALHIAVVNQNLNLVRELIARGADVVspRATGTffrpGPKNliyygehPLSFAACVGNEEIVRLLIEHG 159

                        170
                 ....*....|....
gi 157743292 243 AHVDARNGRGETAL 256
Cdd:cd22192  160 ADIRAQDSLGNTVL 173
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 156-330 7.21e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.50  E-value: 7.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 156 LHEACLGGHTACVRLLLQHRADPDLLSAEGLAPLHLCRTAASLGCAQALLEHGASVQrVGGTGRDTPLHVAAQRGLDEHA 235
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN-VKDNNGESPLHNAAEYGDYACI 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 236 RLYLGRGAHVDARNGRGETALSAACGAARRPDEhgrclrlcalLLRRGAEADARDEDERSPLHKACGH-ASHSLARLLLR 314
Cdd:PHA02874 207 KLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE----------LLINNASINDQDIDGSTPLHHAINPpCDIDIIDILLY 276

                        170
                 ....*....|....*.
gi 157743292 315 HGADAGALDYGGASPL 330
Cdd:PHA02874 277 HKADISIKDNKGENPI 292
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 117-259 1.36e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.65  E-value: 1.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 117 KRELTTPLCIAAAHGHTACVRHLLGRGADPDA-SPGGRGALHEACLGGHTACVRLLLQHRADPDLLSAEGLAPLHLCRTA 195
Cdd:PHA02878 165 RHKGNTALHYATENKDQRLTELLLSYGANVNIpDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY 244

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 157743292 196 A-SLGCAQALLEHGASVQRVGGTGRDTPLHVAAQRglDEHARLYLGRGAHVDARNGRGETALSAA 259
Cdd:PHA02878 245 CkDYDILKLLLEHGVDVNAKSYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 165-339 1.49e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.26  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 165 TACVRLLLQHRADPDLLSAEGL-APLHLCRTAASLGCAQALLEHGASVQrVGGTGRDTPLHVAAQRGLDEHARLYLGRGA 243
Cdd:PHA02878 147 AEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVN-IPDKTNNSPLHHAVKHYNKPIVHILLENGA 225

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 244 HVDARNGRGETALSAACGAARRPD------EHGRCLrlcalllrrGAEADARDedeRSPLHKACghASHSLARLLLRHGA 317
Cdd:PHA02878 226 STDARDKCGNTPLHISVGYCKDYDilklllEHGVDV---------NAKSYILG---LTALHSSI--KSERKLKLLLEYGA 291

                        170       180
                 ....*....|....*....|..
gi 157743292 318 DAGALDYGGASPLGRVLQTASC 339
Cdd:PHA02878 292 DINSLNSYKLTPLSSAVKQYLC 313
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
 420-460 3.26e-06

SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB (SPRY domain-containing SOCS box proteins) protein families. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence of a variable number of repeats. SSB proteins contain a central SPRY domain and a C-terminal SOCS. Recently, it has been shown that all four SSB proteins interact with the MET, the receptor protein-tyrosine kinase for hepatocyte growth factor (HGF), and that SSB-1, SSB-2, and SSB-4 interact with prostate apoptosis response protein-4. Both types of interactions are mediated through the SPRY domain.


Pssm-ID: 239686  Cd Length: 42  Bit Score: 43.64  E-value: 3.26e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 157743292 420 TPRCLQHLCRCALRRLFGKRCFDLIPLLPLPKPLQNYLLLE 460
Cdd:cd03716    2 TPRSLQHLCRLAIRRCLGRRRLELIKKLPLPPRLKDYLLYE 42
PHA03095 PHA03095
ankyrin-like protein; Provisional
 203-357 3.62e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.25  E-value: 3.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 203 ALLEHGASVQRVGGTGRdTPLHVAAQRGLDEHA---RLYLGRGAHVDARNGRGETALSA-ACGAARRPdehgrclrLCAL 278
Cdd:PHA03095  32 RLLAAGADVNFRGEYGK-TPLHLYLHYSSEKVKdivRLLLEAGADVNAPERCGFTPLHLyLYNATTLD--------VIKL 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 279 LLRRGAEADARDEDERSPLHK-ACGHASH-SLARLLLRHGADAGALDYGGASPLGRVLQTASCALqaspqRTVQALLNHG 356
Cdd:PHA03095 103 LIKAGADVNAKDKVGRTPLHVyLSGFNINpKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANV-----ELLRLLIDAG 177


                 .
gi 157743292 357 S 357
Cdd:PHA03095 178 A 178
Ank_2 pfam12796
Ankyrin repeats (3 copies);
223-323 4.94e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.72  E-value: 4.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292  223 LHVAAQRGLDEHARLYLGRGAHVDARNGRGETALSAACgaarrpdEHGRCLRLCALLlrrgAEADARDEDE-RSPLHKAC 301
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAA-------KNGHLEIVKLLL----EHADVNLKDNgRTALHYAA 69

                          90       100
                  ....*....|....*....|..
gi 157743292  302 GHASHSLARLLLRHGADAGALD 323
Cdd:pfam12796  70 RSGHLEIVKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 122-330 1.89e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 1.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 122 TPLCIAA-AHGHTACVRHLLGRGADPDA-SPGGRGALHEACLGGH-TACVRLLLQHRADPDLLSAEGLAPLHLCRTA-AS 197
Cdd:PHA02876 275 TPLHHASqAPSLSRLVPKLLERGADVNAkNIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLdRN 354

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 198 LGCAQALLEHGASVQrvggtGRD----TPLHVAAQRGLDEHARLYLGRGAHVDARNGRGETALS-AACGAarrpdehgRC 272
Cdd:PHA02876 355 KDIVITLLELGANVN-----ARDycdkTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHfALCGT--------NP 421

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 157743292 273 LRLCALLLRRGAEADARDEDERSPLHKAC-GHASHSLARLLLRHGADAGALDYGGASPL 330
Cdd:PHA02876 422 YMSVKTLIDRGANVNSKNKDLSTPLHYACkKNCKLDVIEMLLDNGADVNAINIQNQYPL 480
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 122-249 3.45e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.40  E-value: 3.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 122 TPLCIAAAHGHTACVRHLLGRGAD---PDASpgGRGALHEACLGGHTACVRLLLQHRADPDLLSAEGLaplhLCRTA--A 196
Cdd:PLN03192 560 TPLHIAASKGYEDCVLVLLKHACNvhiRDAN--GNTALWNAISAKHHKIFRILYHFASISDPHAAGDL----LCTAAkrN 633

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 157743292 197 SLGCAQALLEHGASVQRVGGTGRdTPLHVAAQRGLDEHARLYLGRGAHVDARN 249
Cdd:PLN03192 634 DLTAMKELLKQGLNVDSEDHQGA-TALQVAMAEDHVDMVRLLIMNGADVDKAN 685
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 163-240 4.33e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 4.33e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 157743292 163 GHTACVRLLLQHRADPDLLSAEGLAPLHLCRTAASLGCAQALLEHGASVQRVGGTGRdTPLHVAAQRGLDEHARLYLG 240
Cdd:PTZ00322  93 GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK-TPLELAEENGFREVVQLLSR 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
152-205 5.20e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 5.20e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 157743292  152 GRGALHEACLGGHTACVRLLLQHRADPDLLSAEGLAPLHLCRTAASLGCAQALL 205
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
 420-440 6.68e-05

SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region of CIS/SOCS family proteins (in combination with a SH2 domain), ASBs (ankyrin repeat-containing proteins with a SOCS box), SSBs (SPRY domain-containing proteins with a SOCS box), and WSBs (WD40 repeat-containing proteins with a SOCS box), as well as, other miscellaneous proteins. The function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239641  Cd Length: 41  Bit Score: 40.15  E-value: 6.68e-05
                         10        20
                 ....*....|....*....|.
gi 157743292 420 TPRCLQHLCRCALRRLFGKRC 440
Cdd:cd03587    1 NPRSLQHLCRLAIRRCLGKRR 21
Ank_5 pfam13857
Ankyrin repeats (many copies);
204-256 1.02e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 1.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 157743292  204 LLEHGASVQRVGGTGRDTPLHVAAQRGLDEHARLYLGRGAHVDARNGRGETAL 256
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 420-442 1.80e-04

SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more generic proteins that comprise a large family of E3 ubiquitin protein ligases.


Pssm-ID: 462192  Cd Length: 39  Bit Score: 38.69  E-value: 1.80e-04
                          10        20
                  ....*....|....*....|...
gi 157743292  420 TPRCLQHLCRCALRRLFGKRCFD 442
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLG 23
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 136-318 3.90e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.93  E-value: 3.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 136 VRHLLGRGADPDASPGGRGALHEACLGGHTACVRLLLQHRADPDLLSAEGLAPLHLcrtAASLG---CAQALLEHGASVQ 212
Cdd:PLN03192 509 VGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHI---AASKGyedCVLVLLKHACNVH 585

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 213 RVGGTGrDTPLHVAAQRGldeHARLYlgRGAHVDARNGRGETALSAACGAARRPDehgrcLRLCALLLRRGAEADARDED 292
Cdd:PLN03192 586 IRDANG-NTALWNAISAK---HHKIF--RILYHFASISDPHAAGDLLCTAAKRND-----LTAMKELLKQGLNVDSEDHQ 654

                        170       180
                 ....*....|....*....|....*.
gi 157743292 293 ERSPLHKACGHASHSLARLLLRHGAD 318
Cdd:PLN03192 655 GATALQVAMAEDHVDMVRLLIMNGAD 680
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 122-148 5.52e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 5.52e-04
                           10        20
                   ....*....|....*....|....*..
gi 157743292   122 TPLCIAAAHGHTACVRHLLGRGADPDA 148
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_2 pfam12796
Ankyrin repeats (3 copies);
283-356 8.17e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 38.56  E-value: 8.17e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 157743292  283 GAEADARDEDERSPLHKACGHASHSLARLLLRHgADAGALDYGGaSPLgrvlqtaSCALQASPQRTVQALLNHG 356
Cdd:pfam12796  20 GADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TAL-------HYAARSGHLEIVKLLLEKG 84
Ank_5 pfam13857
Ankyrin repeats (many copies);
155-192 1.49e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 1.49e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 157743292  155 ALHEACLGGHTACVRLLLQHRADPDLLSAEGLAPLHLC 192
Cdd:pfam13857  19 PLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 122-191 1.80e-03

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: 40.77  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 122 TPLCIAAAHGHTACVRHLLGRGAD---PDA-----SPGGRGALH--------EACLgGHTACVRLLLQHRADPDLLSAEG 185
Cdd:cd22192   91 TALHIAVVNQNLNLVRELIARGADvvsPRAtgtffRPGPKNLIYygehplsfAACV-GNEEIVRLLIEHGADIRAQDSLG 169


                 ....*.
gi 157743292 186 LAPLHL 191
Cdd:cd22192  170 NTVLHI 175
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 168-330 2.16e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.42  E-value: 2.16e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 168 VRLLLQHRADPDLLSAEGLAPLHLC--RTAASLGCAQALLEHGASVQRVGGTGrDTPLHVAAQRGLDEH--ARLYLGRGA 243
Cdd:PHA03100  89 VKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDG-ENLLHLYLESNKIDLkiLKLLIDKGV 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 244 HVDARNgRGETALSaacgaarrpdehgrclrlcalllrRGAEADARDEDERSPLHKACGHASHSLARLLLRHGADAGALD 323
Cdd:PHA03100 168 DINAKN-RVNYLLS------------------------YGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVN 222


                 ....*..
gi 157743292 324 YGGASPL 330
Cdd:PHA03100 223 KYGDTPL 229
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 152-180 2.36e-03

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: 35.26  E-value: 2.36e-03
                           10        20
                   ....*....|....*....|....*....
gi 157743292   152 GRGALHEACLGGHTACVRLLLQHRADPDL 180
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03095 PHA03095
ankyrin-like protein; Provisional
 118-209 2.46e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.01  E-value: 2.46e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 118 RELTTPLCIAAAHGHTACVRHLLGRGADPDA-SPGGRGALHEACLGGHTACVRLLLQHRADPDLLsAEGLA----PLHLC 192
Cdd:PHA03095 255 RYGQTPLHYAAVFNNPRACRRLIALGADINAvSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETV-AATLNtasvAGGDI 333

                         90
                 ....*....|....*..
gi 157743292 193 RTAASLGCAQALLEHGA 209
Cdd:PHA03095 334 PSDATRLCVAKVVLRGA 350
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 152-180 3.18e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.34  E-value: 3.18e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 157743292  152 GRGALHEACL-GGHTACVRLLLQHRADPDL 180
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNA 31
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 122-148 4.32e-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: 34.96  E-value: 4.32e-03
                          10        20
                  ....*....|....*....|....*...
gi 157743292  122 TPLCIAAAH-GHTACVRHLLGRGADPDA 148
Cdd:pfam00023   4 TPLHLAAGRrGNLEIVKLLLSKGADVNA 31
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 153-330 5.82e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 38.82  E-value: 5.82e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 153 RGALHEACLGGHTACVRLLLQHRADPDLLSAEGLAPLHLCRTAASLGCAQALLEHGAsVQRVGGTGRDTPLHVAAQRGLD 232
Cdd:PHA02875   3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGA-IPDVKYPDIESELHDAVEEGDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 233 EHARLYLGRGAHV-DARNGRGETALSAACGAARrpdehgrcLRLCALLLRRGAEADARDEDERSPLHKACGHASHSLARL 311
Cdd:PHA02875  82 KAVEELLDLGKFAdDVFYKDGMTPLHLATILKK--------LDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIEL 153

                        170
                 ....*....|....*....
gi 157743292 312 LLRHGADAGALDYGGASPL 330
Cdd:PHA02875 154 LIDHKACLDIEDCCGCTPL 172
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 152-258 8.24e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 38.71  E-value: 8.24e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 157743292 152 GRGALHEACL---GGHTACVRLLLQhrADPDLLSA-------------EGLAPLHLCRTAASLGCAQALLEHGASV---- 211
Cdd:cd21882   26 GKTCLHKAALnlnDGVNEAIMLLLE--AAPDSGNPkelvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADVsara 103

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 157743292 212 -----QRVGGTG---RDTPLHVAAQRGLDEHARLYLGRGAH---VDARNGRGETALSA 258
Cdd:cd21882  104 tgrffRKSPGNLfyfGELPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLHA 161
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 292-318 9.29e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 33.77  E-value: 9.29e-03
                          10        20
                  ....*....|....*....|....*..
gi 157743292  292 DERSPLHKACGHASHSLARLLLRHGAD 318
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
 
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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