NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|2416804683|ref|XP_052665346|]
View 

ankyrin repeat and SOCS box protein 8 isoform X1 [Harpia harpyja]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-184 1.96e-42

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.02  E-value: 1.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  22 IAAIRSFPRDNVEDLIGRGADVNCM-HGTLKPLHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEKDET-CVEI 99
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKdDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLeIVKL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683 100 LLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGALVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLK 179
Cdd:COG0666   139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218


                  ....*
gi 2416804683 180 GQTPI 184
Cdd:COG0666   219 GKTAL 223
SOCS_ASB8 cd03727
SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a ...
 241-283 5.11e-21

SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. Human ASB8 is highly transcribed in skeletal muscle and in lung carcinoma cell lines. 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: 239697  Cd Length: 43  Bit Score: 83.73  E-value: 5.11e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2416804683 241 SAPGTLQTLSRYAVRRSLGVRFLPEAVKQLPLPTCLKEYVLLL 283
Cdd:cd03727     1 SAPGTLKALARYAVRRSLGVQYLPEAVKQLPLPRSVKEYLLLL 43
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-184 1.96e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.02  E-value: 1.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  22 IAAIRSFPRDNVEDLIGRGADVNCM-HGTLKPLHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEKDET-CVEI 99
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKdDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLeIVKL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683 100 LLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGALVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLK 179
Cdd:COG0666   139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218


                  ....*
gi 2416804683 180 GQTPI 184
Cdd:COG0666   219 GKTAL 223
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 22-211 4.35e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 101.68  E-value: 4.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  22 IAAIRSFPRDNVEDLIGRGADVNC---MHGTlkPLHCACMV-ADADCVELLLQKGAEVNALDGYNRTALHYAAEKDETCV 97
Cdd:PHA02876  313 LMAKNGYDTENIRTLIMLGADVNAadrLYIT--PLHQASTLdRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  98 -EILLEYGANPNALDGNKDTPLHWAAFKNNA-ECVRSLLENGALVNARDYNNDTPLSWAAMKG-NLESVSILLDFGAEVR 174
Cdd:PHA02876  391 iNTLLDYGADIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2416804683 175 VVNLKGQTPIsrLVALLVRGL-------GTEREDScfDLLHRAI 211
Cdd:PHA02876  471 AINIQNQYPL--LIALEYHGIvnillhyGAELRDS--RVLHKSL 510
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-144 1.52e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 1.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  53 LHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEKDET-CVEILLEYgANPNaLDGNKDTPLHWAAFKNNAECVR 131
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLeIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2416804683 132 SLLENGALVNARD 144
Cdd:pfam12796  79 LLLEKGADINVKD 91
SOCS_ASB8 cd03727
SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a ...
 241-283 5.11e-21

SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. Human ASB8 is highly transcribed in skeletal muscle and in lung carcinoma cell lines. 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: 239697  Cd Length: 43  Bit Score: 83.73  E-value: 5.11e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2416804683 241 SAPGTLQTLSRYAVRRSLGVRFLPEAVKQLPLPTCLKEYVLLL 283
Cdd:cd03727     1 SAPGTLKALARYAVRRSLGVQYLPEAVKQLPLPRSVKEYLLLL 43
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 47-207 5.42e-08

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: 53.48  E-value: 5.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  47 HGTLKPLHCACMVADADCVE-LLLQKGAEVNALDGYNRTALHYAA--EKDETCVeILLEygANPNALD---------Gnk 114
Cdd:cd22192    15 RISESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAAlyDNLEAAV-VLME--AAPELVNepmtsdlyqG-- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683 115 DTPLHWAAFKNNAECVRSLLENGA-LVNARD-------------YNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKG 180
Cdd:cd22192    90 ETALHIAVVNQNLNLVRELIARGAdVVSPRAtgtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169

                         170       180
                  ....*....|....*....|....*....
gi 2416804683 181 QTPISRLVallvrgLGTEREDSC--FDLL 207
Cdd:cd22192   170 NTVLHILV------LQPNKTFACqmYDLI 192
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 243-281 9.92e-08

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: 47.16  E-value: 9.92e-08
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2416804683 243 PGTLQTLSRYAVRRSLGvRFLPEAVKQLPLPTCLKEYVL 281
Cdd:pfam07525   2 PRSLQHLCRLAIRRALG-KRRLGAIDKLPLPPLLKDYLL 39
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 63-174 1.35e-07

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: 52.39  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  63 DCVELLLQKGAEVNALDgynrTALHYAAEKDETCVEILL--------EYGANPNALDGNKD------TPLHWAAFKNNAE 128
Cdd:TIGR00870  67 ELTELLLNLSCRGAVGD----TLLHAISLEYVDAVEAILlhllaafrKSGPLELANDQYTSeftpgiTALHLAAHRQNYE 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683 129 CVRSLLENGALVNARD--------------YNNDTPLSWAAMKGNLESVSILLDFGAEVR 174
Cdd:TIGR00870 143 IVKLLLERGASVPARAcgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADIL 202
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
 245-282 3.32e-05

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: 198037  Cd Length: 34  Bit Score: 40.08  E-value: 3.32e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2416804683  245 TLQTLSRYAVRRSLGvrflpeAVKQLPLPTCLKEYVLL 282
Cdd:smart00969   2 SLQHLCRLAIRRSLG------GIDKLPLPPRLKDYLLY 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 113-142 9.11e-05

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: 38.72  E-value: 9.11e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 2416804683  113 NKDTPLHWAAFKNNAECVRSLLENGALVNA 142
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-184 1.96e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.02  E-value: 1.96e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  22 IAAIRSFPRDNVEDLIGRGADVNCM-HGTLKPLHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEKDET-CVEI 99
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKdDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLeIVKL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683 100 LLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGALVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLK 179
Cdd:COG0666   139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218


                  ....*
gi 2416804683 180 GQTPI 184
Cdd:COG0666   219 GKTAL 223
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-191 7.04e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.48  E-value: 7.04e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  22 IAAIRSFPRDNVEDLIGRGADVN-CMHGTLKPLHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEK-DETCVEI 99
Cdd:COG0666    92 HAAARNGDLEIVKLLLEAGADVNaRDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANgNLEIVKL 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683 100 LLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGALVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLK 179
Cdd:COG0666   172 LLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251

                         170
                  ....*....|..
gi 2416804683 180 GQTPISRLVALL 191
Cdd:COG0666   252 GLTALLLAAAAG 263
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
18-183 1.03e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.30  E-value: 1.03e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  18 LIRTIAAIRSFPRDNVEDLIGRGADVNCMHGTLKPLHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEK-DETC 96
Cdd:COG0666    23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNgDLEI 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  97 VEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGALVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVV 176
Cdd:COG0666   103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182


                  ....*..
gi 2416804683 177 NLKGQTP 183
Cdd:COG0666   183 DNDGETP 189
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
33-184 6.80e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.98  E-value: 6.80e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  33 VEDLIGRGADVNCMHGTLK-PLHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEK-DETCVEILLEYGANPNAL 110
Cdd:COG0666   136 VKLLLEAGADVNAQDNDGNtPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENgHLEIVKLLLEAGADVNAK 215

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2416804683 111 DGNKDTPLHWAAFKNNAECVRSLLENGALVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQTPI 184
Cdd:COG0666   216 DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 22-211 4.35e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 101.68  E-value: 4.35e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  22 IAAIRSFPRDNVEDLIGRGADVNC---MHGTlkPLHCACMV-ADADCVELLLQKGAEVNALDGYNRTALHYAAEKDETCV 97
Cdd:PHA02876  313 LMAKNGYDTENIRTLIMLGADVNAadrLYIT--PLHQASTLdRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  98 -EILLEYGANPNALDGNKDTPLHWAAFKNNA-ECVRSLLENGALVNARDYNNDTPLSWAAMKG-NLESVSILLDFGAEVR 174
Cdd:PHA02876  391 iNTLLDYGADIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 2416804683 175 VVNLKGQTPIsrLVALLVRGL-------GTEREDScfDLLHRAI 211
Cdd:PHA02876  471 AINIQNQYPL--LIALEYHGIvnillhyGAELRDS--RVLHKSL 510
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 33-177 3.19e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 95.12  E-value: 3.19e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  33 VEDLIGRGADVN-CMHGTLKPLHCACM--VADADCVELLLQKGAEVNALDGYNRTALHYAAE------------------ 91
Cdd:PHA03100   89 VKLLLEYGANVNaPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnkidlkilkllidkgvd 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  92 ---KDEtcVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGALVNARDYNNDTPLSWAAMKGNLESVSILLD 168
Cdd:PHA03100  169 inaKNR--VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246


                  ....*....
gi 2416804683 169 FGAEVRVVN 177
Cdd:PHA03100  247 NGPSIKTII 255
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 13-184 4.78e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 95.03  E-value: 4.78e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  13 SLSERLIRTIAAIRSFPRDNVEDLIGRGADVNCMHGTL-KPLHCACMVADADCVELL----------------------- 68
Cdd:PHA02874   31 SVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIpHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmikti 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  69 LQKGAEVNALDGYNRTALHYAAEK-DETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGALVNARDYNN 147
Cdd:PHA02874  111 LDCGIDVNIKDAELKTFLHYAIKKgDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG 190

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 2416804683 148 DTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQTPI 184
Cdd:PHA02874  191 ESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-144 1.52e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 1.52e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  53 LHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEKDET-CVEILLEYgANPNaLDGNKDTPLHWAAFKNNAECVR 131
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLeIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2416804683 132 SLLENGALVNARD 144
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 3-218 3.47e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 92.64  E-value: 3.47e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683   3 YIMQSIQSKYSLSERLIrTIAAIRSFPRDNVED------LIGRGADVNCM--HGTLKPLHCACMVADADCVELLLQKGAE 74
Cdd:PHA02878  115 EIFKIILTNRYKNIQTI-DLVYIDKKSKDDIIEaeitklLLSYGADINMKdrHKGNTALHYATENKDQRLTELLLSYGAN 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  75 VNALDGYNRTALHYAAEK-DETCVEILLEYGANPNALDGNKDTPLHWA-AFKNNAECVRSLLENGALVNARDY-NNDTPL 151
Cdd:PHA02878  194 VNIPDKTNNSPLHHAVKHyNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTAL 273

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2416804683 152 SwAAMKGNlESVSILLDFGAEVRVVNLKGQTPISRLVallvrglgteREDSCFDLLHRAIGHFELRK 218
Cdd:PHA02878  274 H-SSIKSE-RKLKLLLEYGADINSLNSYKLTPLSSAV----------KQYLCINIGRILISNICLLK 328
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-184 4.49e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.40  E-value: 4.49e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  53 LHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEKDETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRS 132
Cdd:COG0666    26 LAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKL 105

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2416804683 133 LLENGALVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQTPI 184
Cdd:COG0666   106 LLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
SOCS_ASB8 cd03727
SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a ...
 241-283 5.11e-21

SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. Human ASB8 is highly transcribed in skeletal muscle and in lung carcinoma cell lines. 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: 239697  Cd Length: 43  Bit Score: 83.73  E-value: 5.11e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 2416804683 241 SAPGTLQTLSRYAVRRSLGVRFLPEAVKQLPLPTCLKEYVLLL 283
Cdd:cd03727     1 SAPGTLKALARYAVRRSLGVQYLPEAVKQLPLPRSVKEYLLLL 43
Ank_2 pfam12796
Ankyrin repeats (3 copies);
86-177 1.12e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.01  E-value: 1.12e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  86 LHYAAE-KDETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENgALVNARDYNNdTPLSWAAMKGNLESVS 164
Cdd:pfam12796   1 LHLAAKnGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 2416804683 165 ILLDFGAEVRVVN 177
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 33-189 1.27e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.08  E-value: 1.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  33 VEDLIGRGADVNCM--HGtLKPLHCAcMV---ADADCVELLLQKGAEVNALDGYNRTALHYAAE---KDETCVEILLEYG 104
Cdd:PHA03095  135 IRLLLRKGADVNALdlYG-MTPLAVL-LKsrnANVELLRLLIDAGADVYAVDDRFRSLLHHHLQsfkPRARIVRELIRAG 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683 105 ANPNALDGNKDTPLHWAAfkNNAECVRS----LLENGALVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKG 180
Cdd:PHA03095  213 CDPAATDMLGNTPLHSMA--TGSSCKRSlvlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDG 290


                  ....*....
gi 2416804683 181 QTPISRLVA 189
Cdd:PHA03095  291 NTPLSLMVR 299
PHA03095 PHA03095
ankyrin-like protein; Provisional
 31-183 2.69e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.31  E-value: 2.69e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  31 DNVEDLIGRGADVNCMHGTLKPLHCACM----VADADCVELLLQKGAEVNALDGYNRTALHYAAEKDET--CVEILLEYG 104
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLhyssEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTldVIKLLIKAG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683 105 ANPNALDGNKDTPLH--WAAFKNNAECVRSLLENGALVNARDYNNDTPLSwAAMKG---NLESVSILLDFGAEVRVVNLK 179
Cdd:PHA03095  108 ADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLA-VLLKSrnaNVELLRLLIDAGADVYAVDDR 186


                  ....
gi 2416804683 180 GQTP 183
Cdd:PHA03095  187 FRSL 190
PHA03095 PHA03095
ankyrin-like protein; Provisional
 60-208 3.61e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.92  E-value: 3.61e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  60 ADADCVELLLQKGAEVNALDGYNRTALH----YAAEKDETCVEILLEYGANPNALDGNKDTPLH-WAAFKNNAECVRSLL 134
Cdd:PHA03095   25 VTVEEVRRLLAAGADVNFRGEYGKTPLHlylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLI 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683 135 ENGALVNARDYNNDTPLSwAAMKG---NLESVSILLDFGAEVRVVNLKGQTPIS----------RLVALLVRGLG--TER 199
Cdd:PHA03095  105 KAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAvllksrnanvELLRLLIDAGAdvYAV 183


                  ....*....
gi 2416804683 200 EDSCFDLLH 208
Cdd:PHA03095  184 DDRFRSLLH 192
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 52-194 1.40e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 82.42  E-value: 1.40e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  52 PLHCACMVAD-ADCVELLLQKGAEVNALDGYNRTALHYAAEK--DETCVEILLEYGANPNALDGNKDTPLHWAA-FKNNA 127
Cdd:PHA02876  276 PLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNgyDTENIRTLIMLGADVNAADRLYITPLHQAStLDRNK 355

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2416804683 128 ECVRSLLENGALVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLK----------GQTPISRLVALLVRG 194
Cdd:PHA02876  356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKigtalhfalcGTNPYMSVKTLIDRG 432
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 42-189 3.30e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.78  E-value: 3.30e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  42 DVNCMHGTLkPLHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAA------EKDETCVEILLEYGANPNALDGNKD 115
Cdd:PHA03100   29 DYSYKKPVL-PLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynlTDVKEIVKLLLEYGANVNAPDNNGI 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683 116 TPLHWAAFKN----------------------------------------------------NAEC-VRSLLENGALVNA 142
Cdd:PHA03100  108 TPLLYAISKKsnsysiveylldnganvniknsdgenllhlylesnkidlkilkllidkgvdiNAKNrVNYLLSYGVPINI 187

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2416804683 143 RDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQTPISRLVA 189
Cdd:PHA03100  188 KDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 24-184 7.44e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.84  E-value: 7.44e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  24 AIRSFPRDNVEDLIGRGADVNC--MHGTLkPLHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAE-KDETCVEIL 100
Cdd:PHA02874  131 AIKKGDLESIKMLFEYGADVNIedDNGCY-PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEyGDYACIKLL 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683 101 LEYGANPNALDGNKDTPLHWAAFKNNAecVRSLLENGALVNARDYNNDTPLSWAAM-KGNLESVSILLDFGAEVRVVNLK 179
Cdd:PHA02874  210 IDHGNHIMNKCKNGFTPLHNAIIHNRS--AIELLINNASINDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNK 287


                  ....*
gi 2416804683 180 GQTPI 184
Cdd:PHA02874  288 GENPI 292
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 66-210 1.62e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 73.56  E-value: 1.62e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  66 ELLLQKGAEVNALDGYNRTALHYAAEKDET-CVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLEN-------- 136
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAkMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNrsninknd 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683 137 ---------------------GALVNARDYNNDTPLSWAAMKGNLES-VSILLDFGAEVRVVNLKGQTPI---------- 184
Cdd:PHA02876  242 lsllkairnedletslllydaGFSVNSIDDCKNTPLHHASQAPSLSRlVPKLLERGADVNAKNIKGETPLylmakngydt 321

                         170       180
                  ....*....|....*....|....*..
gi 2416804683 185 SRLVALLVRGLGTEREDSCFDL-LHRA 210
Cdd:PHA02876  322 ENIRTLIMLGADVNAADRLYITpLHQA 348
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 31-184 1.53e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 67.21  E-value: 1.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  31 DNVEDLIGRGADVNCM-HGTLKPLHCACMVADADCVELLLQ--------------------------KGAEVNALDGYNR 83
Cdd:PHA02878   51 DVVKSLLTRGHNVNQPdHRDLTPLHIICKEPNKLGMKEMIRsinkcsvfytlvaikdafnnrnveifKIILTNRYKNIQT 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  84 TALHYAAEKDE------TCVEILLEYGANPNALDGNKD-TPLHWAAFKNNAECVRSLLENGALVNARDYNNDTPLSWAAM 156
Cdd:PHA02878  131 IDLVYIDKKSKddiieaEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVK 210

                         170       180
                  ....*....|....*....|....*...
gi 2416804683 157 KGNLESVSILLDFGAEVRVVNLKGQTPI 184
Cdd:PHA02878  211 HYNKPIVHILLENGASTDARDKCGNTPL 238
Ank_2 pfam12796
Ankyrin repeats (3 copies);
24-111 2.18e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.67  E-value: 2.18e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  24 AIRSFPRDNVEDLIGRGADVNCMHGT-LKPLHCACMVADADCVELLLQKgAEVNaLDGYNRTALHYAAEKD-ETCVEILL 101
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNgRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGhLEIVKLLL 81

                          90
                  ....*....|
gi 2416804683 102 EYGANPNALD 111
Cdd:pfam12796  82 EKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 21-184 3.50e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.14  E-value: 3.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  21 TIAAIRSFPRDNVEDLIGRGADVNCMHGTLKP-LHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEKDE-TCVE 98
Cdd:PHA02874   95 SILPIPCIEKDMIKTILDCGIDVNIKDAELKTfLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFfDIIK 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  99 ILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGALVNARDYNNDTPLSWAAMKgNLESVSILLDfGAEVRVVNL 178
Cdd:PHA02874  175 LLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLIN-NASINDQDI 252


                  ....*.
gi 2416804683 179 KGQTPI 184
Cdd:PHA02874  253 DGSTPL 258
Ank_2 pfam12796
Ankyrin repeats (3 copies);
118-184 2.55e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 2.55e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2416804683 118 LHWAAFKNNAECVRSLLENGALVNARDYNNDTPLSWAAMKGNLESVSILLDFgAEVRVVNlKGQTPI 184
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTAL 65
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 48-209 1.02e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.55  E-value: 1.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  48 GTLKPLHCACMVADADCVELLLQKGAEVNAL---DGynRTALHYAAE-KDETCVEILLEYGANPNALDGNKDTPLHWAAF 123
Cdd:PHA02875   67 DIESELHDAVEEGDVKAVEELLDLGKFADDVfykDG--MTPLHLATIlKKLDIMKLLIARGADPDIPNTDKFSPLHLAVM 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683 124 KNNAECVRSLLENGALVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQtpisrlVALLVRGLGTEREDSC 203
Cdd:PHA02875  145 MGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGC------VAALCYAIENNKIDIV 218


                  ....*.
gi 2416804683 204 FDLLHR 209
Cdd:PHA02875  219 RLFIKR 224
Ank_4 pfam13637
Ankyrin repeats (many copies);
116-167 2.31e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 2.31e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2416804683 116 TPLHWAAFKNNAECVRSLLENGALVNARDYNNDTPLSWAAMKGNLESVSILL 167
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
66-184 7.02e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 58.43  E-value: 7.02e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  66 ELLLQKGAEVNALDGYNRTALHYAAEKDETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGALVNARDY 145
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2416804683 146 NNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQTPI 184
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL 124
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
 241-282 8.47e-10

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: 53.27  E-value: 8.47e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2416804683 241 SAPGTLQTLSRYAVRRSLGVRfLPEAVKQLPLPTCLKEYVLL 282
Cdd:cd03716     1 STPRSLQHLCRLAIRRCLGRR-RLELIKKLPLPPRLKDYLLY 41
Ank_4 pfam13637
Ankyrin repeats (many copies);
82-134 1.17e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.05  E-value: 1.17e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2416804683  82 NRTALHYAAEK-DETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLL 134
Cdd:pfam13637   1 ELTALHAAAASgHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
 243-282 5.73e-09

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: 50.93  E-value: 5.73e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2416804683 243 PGTLQTLSRYAVRRSLGVRfLPEAVKQLPLPTCLKEYVLL 282
Cdd:cd03587     2 PRSLQHLCRLAIRRCLGKR-RLDLIDKLPLPPRLKDYLLY 40
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 87-183 6.07e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 6.07e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  87 HYAAEKDETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGALVNARDYNNDTPLSWAAMKGNLESVSIL 166
Cdd:PTZ00322   88 QLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167

                          90       100
                  ....*....|....*....|....
gi 2416804683 167 L-------DFGAEVRVVNLKGQTP 183
Cdd:PTZ00322  168 SrhsqchfELGANAKPDSFTGKPP 191
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 130-184 1.42e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 1.42e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2416804683 130 VRSLLENGALVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQTPI 184
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL 152
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 32-178 2.05e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 54.87  E-value: 2.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  32 NVEDLIGRGADVNCMHGTLKPLHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEKD-ETCVEILLEYGANPNAL 110
Cdd:PLN03192  508 NVGDLLGDNGGEHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGyEDCVLVLLKHACNVHIR 587

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683 111 DGNKDTPLhW--------------------------------AAFKNNAECVRSLLENGALVNARDYNNDTPLSWAAMKG 158
Cdd:PLN03192  588 DANGNTAL-WnaisakhhkifrilyhfasisdphaagdllctAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAED 666

                         170       180
                  ....*....|....*....|
gi 2416804683 159 NLESVSILLDFGAEVRVVNL 178
Cdd:PLN03192  667 HVDMVRLLIMNGADVDKANT 686
PHA02946 PHA02946
ankyin-like protein; Provisional
 93-173 3.24e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 54.29  E-value: 3.24e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  93 DETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGALVNARDYNNDTPLSWAAMKGN--LESVSILLDFG 170
Cdd:PHA02946   51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYG 130


                  ...
gi 2416804683 171 AEV 173
Cdd:PHA02946  131 AKI 133
Ank_5 pfam13857
Ankyrin repeats (many copies);
100-151 3.36e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.27  E-value: 3.36e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2416804683 100 LLEYG-ANPNALDGNKDTPLHWAAFKNNAECVRSLLENGALVNARDYNNDTPL 151
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 47-207 5.42e-08

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: 53.48  E-value: 5.42e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  47 HGTLKPLHCACMVADADCVE-LLLQKGAEVNALDGYNRTALHYAA--EKDETCVeILLEygANPNALD---------Gnk 114
Cdd:cd22192    15 RISESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAAlyDNLEAAV-VLME--AAPELVNepmtsdlyqG-- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683 115 DTPLHWAAFKNNAECVRSLLENGA-LVNARD-------------YNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKG 180
Cdd:cd22192    90 ETALHIAVVNQNLNLVRELIARGAdVVSPRAtgtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169

                         170       180
                  ....*....|....*....|....*....
gi 2416804683 181 QTPISRLVallvrgLGTEREDSC--FDLL 207
Cdd:cd22192   170 NTVLHILV------LQPNKTFACqmYDLI 192
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 243-281 9.92e-08

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: 47.16  E-value: 9.92e-08
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2416804683 243 PGTLQTLSRYAVRRSLGvRFLPEAVKQLPLPTCLKEYVL 281
Cdd:pfam07525   2 PRSLQHLCRLAIRRALG-KRRLGAIDKLPLPPLLKDYLL 39
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 63-174 1.35e-07

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: 52.39  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  63 DCVELLLQKGAEVNALDgynrTALHYAAEKDETCVEILL--------EYGANPNALDGNKD------TPLHWAAFKNNAE 128
Cdd:TIGR00870  67 ELTELLLNLSCRGAVGD----TLLHAISLEYVDAVEAILlhllaafrKSGPLELANDQYTSeftpgiTALHLAAHRQNYE 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683 129 CVRSLLENGALVNARD--------------YNNDTPLSWAAMKGNLESVSILLDFGAEVR 174
Cdd:TIGR00870 143 IVKLLLERGASVPARAcgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADIL 202
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 61-171 1.98e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 1.98e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  61 DADCVELLLQKGAEVNALDGYNRTALHYAAEKDE-TCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGAL 139
Cdd:PTZ00322   94 DAVGARILLTGGADPNCRDYDGRTPLHIACANGHvQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 2416804683 140 VNARDYNNdTPLSWAAMKGNLESVSILL---DFGA 171
Cdd:PTZ00322  174 HFELGANA-KPDSFTGKPPSLEDSPISShhpDFSA 207
PHA02798 PHA02798
ankyrin-like protein; Provisional
 97-182 3.28e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 50.99  E-value: 3.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  97 VEILLEYGANPNALDGNKDTPL-----HWAAFKNNAECVRSLLENGALVNARDYNNDTPLSWAAMKG---NLESVSILLD 168
Cdd:PHA02798   54 VKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFMIE 133

                          90
                  ....*....|....
gi 2416804683 169 FGAEVRVVNLKGQT 182
Cdd:PHA02798  134 NGADTTLLDKDGFT 147
Ank_4 pfam13637
Ankyrin repeats (many copies);
52-101 3.39e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 3.39e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2416804683  52 PLHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEK-DETCVEILL 101
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNgNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 93-182 4.47e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.83  E-value: 4.47e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  93 DETCVEILLEyganpnALDGNKdtpLHWAAFKNNAECVRS---------------LLENGALVNARDYNNDTPLSWAAMK 157
Cdd:PHA02876  118 DEACIHILKE------AISGND---IHYDKINESIEYMKLikeriqqdelliaemLLEGGADVNAKDIYCITPIHYAAER 188

                          90       100
                  ....*....|....*....|....*
gi 2416804683 158 GNLESVSILLDFGAEVRVVNLKGQT 182
Cdd:PHA02876  189 GNAKMVNLLLSYGADVNIIALDDLS 213
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 97-184 6.09e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 49.98  E-value: 6.09e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  97 VEILLEYGANPNA----LDGNKDTPLHWAAFKNNAECVRSLLENGALVNA-RDYNNDTPLSWAAMKGNLESVSILLDFGA 171
Cdd:PHA02884   49 IDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKITPLYISVLHGCLKCLEILLSYGA 128

                          90
                  ....*....|...
gi 2416804683 172 EVRVVNLKGQTPI 184
Cdd:PHA02884  129 DINIQTNDMVTPI 141
PHA02946 PHA02946
ankyin-like protein; Provisional
 4-108 4.61e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 47.36  E-value: 4.61e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683   4 IMQSIQSkySLSERLIRTIAAIRSFPRDNVEDLIGRGADVNCMHGTLK-PLHCACMVADADCVELLLQKGAEVNALDGYN 82
Cdd:PHA02946   28 MLQAIEP--SGNYHILHAYCGIKGLDERFVEELLHRGYSPNETDDDGNyPLHIASKINNNRIVAMLLTHGADPNACDKQH 105

                          90       100
                  ....*....|....*....|....*....
gi 2416804683  83 RTALHYAAEKDETCVE---ILLEYGANPN 108
Cdd:PHA02946  106 KTPLYYLSGTDDEVIErinLLVQYGAKIN 134
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 60-184 5.38e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 46.35  E-value: 5.38e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  60 ADADCVELLLQKGAEVN-ALDGYNRTALHYAAEKDETC----VEILLEYGANPNALDGNKDTPLH--WAAFKNNAECVRS 132
Cdd:PHA02859   64 VNVEILKFLIENGADVNfKTRDNNLSALHHYLSFNKNVepeiLKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKL 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2416804683 133 LLENG-ALVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQTPI 184
Cdd:PHA02859  144 LIDSGvSFLNKDFDNNNILYSYILFHSDKKIFDFLTSLGIDINETNKSGYNCY 196
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 91-168 8.19e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 8.19e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2416804683  91 EKDETCV-EILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGALVNARDYNNDTPLSWAAMKGNLESVSILLD 168
Cdd:PHA02876  154 QQDELLIaEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIID 232
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 113-144 8.31e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.89  E-value: 8.31e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2416804683 113 NKDTPLHWAAFK-NNAECVRSLLENGALVNARD 144
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 36-118 1.16e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  36 LIGRGADVNCM--HGTlKPLHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEKD-ETCVEILLEY-------GA 105
Cdd:PTZ00322  101 LLTGGADPNCRdyDGR-TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGfREVVQLLSRHsqchfelGA 179

                          90
                  ....*....|....*....
gi 2416804683 106 N--PNALDGN----KDTPL 118
Cdd:PTZ00322  180 NakPDSFTGKppslEDSPI 198
PHA02798 PHA02798
ankyrin-like protein; Provisional
 63-177 1.18e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 46.37  E-value: 1.18e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  63 DCVELLLQKGAEVNALDGYNRTAL--------HYAAEKDetCVEILLEYGANPNALDGNKDTPLHWA---AFKNNAECVR 131
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLctilsnikDYKHMLD--IVKILIENGADINKKNSDGETPLYCLlsnGYINNLEILL 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 2416804683 132 SLLENGALVNARDYNNDTPLSWAAMKGN---LESVSILLDFGAEVRVVN 177
Cdd:PHA02798  130 FMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHN 178
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 61-171 1.51e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.01  E-value: 1.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  61 DADCVELLLQKGAE-VNALDGYNrtALHYAAEKDETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGAL 139
Cdd:PLN03192  506 DLNVGDLLGDNGGEhDDPNMASN--LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN 583

                          90       100       110
                  ....*....|....*....|....*....|..
gi 2416804683 140 VNARDYNNDTPLSWAAMKGNLESVSILLDFGA 171
Cdd:PLN03192  584 VHIRDANGNTALWNAISAKHHKIFRILYHFAS 615
PHA03095 PHA03095
ankyrin-like protein; Provisional
 28-135 1.65e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 45.79  E-value: 1.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  28 FPRDN---VEDLIGRGAD---VNCMHGTlkPLHCACMVADADC--VELLLQKGAEVNALDGYNRTALHYAAEKDETCV-E 98
Cdd:PHA03095  197 SFKPRariVRELIRAGCDpaaTDMLGNT--PLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAVFNNPRAcR 274

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 2416804683  99 ILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLE 135
Cdd:PHA03095  275 RLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 83-174 1.75e-05

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: 46.03  E-value: 1.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  83 RTALHYAAEKDET----CVEILLEYG---------ANPNALDG--NKDTPLHWAAFKNNAECVRSLLENGALVNARD--- 144
Cdd:cd21882    27 KTCLHKAALNLNDgvneAIMLLLEAApdsgnpkelVNAPCTDEfyQGQTALHIAIENRNLNLVRLLVENGADVSARAtgr 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 2416804683 145 ----------YNNDTPLSWAAMKGNLESVSILLDFGAEVR 174
Cdd:cd21882   107 ffrkspgnlfYFGELPLSLAACTNQEEIVRLLLENGAQPA 146
Ank_5 pfam13857
Ankyrin repeats (many copies);
67-121 2.44e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.18  E-value: 2.44e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2416804683  67 LLLQKGAEVNALDGYNRTALHYAAEKDE-TCVEILLEYGANPNALDGNKDTPLHWA 121
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGAlEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
 243-282 3.24e-05

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: 40.50  E-value: 3.24e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2416804683 243 PGTLQTLSRYAVRRSLGVRfLPEAVKQLPLPTCLKEYVLL 282
Cdd:cd03723     3 PRSLQHLCRCAIRKLLGSR-CHKLVPQLSLPTSLKNYLLL 41
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
 245-282 3.32e-05

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: 198037  Cd Length: 34  Bit Score: 40.08  E-value: 3.32e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 2416804683  245 TLQTLSRYAVRRSLGvrflpeAVKQLPLPTCLKEYVLL 282
Cdd:smart00969   2 SLQHLCRLAIRRSLG------GIDKLPLPPRLKDYLLY 33
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 81-111 4.13e-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: 39.97  E-value: 4.13e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2416804683  81 YNRTALHYAAEK--DETCVEILLEYGANPNALD 111
Cdd:pfam00023   1 DGNTPLHLAAGRrgNLEIVKLLLSKGADVNARD 33
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 52-161 4.86e-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: 44.62  E-value: 4.86e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  52 PLHCACMVADADCVELLLQKGAEVN--------------ALDGYNRTALHYAA-EKDETCVEILLEYGANPNALDGNKDT 116
Cdd:cd22192    92 ALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpkNLIYYGEHPLSFAAcVGNEEIVRLLIEHGADIRAQDSLGNT 171

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2416804683 117 PLHWAAFKNNAECVRSLLEngaLVNARDYNND-------------TPLSWAAMKGNLE 161
Cdd:cd22192   172 VLHILVLQPNKTFACQMYD---LILSYDKEDDlqpldlvpnnqglTPFKLAAKEGNIV 226
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 92-184 6.45e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.83  E-value: 6.45e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  92 KDETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGALVNARDYNN-DTPLSWAAMKGNLESVSILLDFG 170
Cdd:PHA02875   46 RDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARG 125

                          90
                  ....*....|....
gi 2416804683 171 AEVRVVNLKGQTPI 184
Cdd:PHA02875  126 ADPDIPNTDKFSPL 139
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 113-142 9.11e-05

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: 38.72  E-value: 9.11e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 2416804683  113 NKDTPLHWAAFKNNAECVRSLLENGALVNA 142
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 52-77 1.90e-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: 37.95  E-value: 1.90e-04
                           10        20
                   ....*....|....*....|....*.
gi 2416804683   52 PLHCACMVADADCVELLLQKGAEVNA 77
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 81-109 2.69e-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: 37.57  E-value: 2.69e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 2416804683   81 YNRTALHYAAEK-DETCVEILLEYGANPNA 109
Cdd:smart00248   1 DGRTPLHLAAENgNLEVVKLLLDKGADINA 30
SOCS_SSB1_4 cd03718
SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box ...
 242-281 3.11e-04

SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box proteins)-like proteins. SSB proteins contain a central SPRY domain and a C-terminal SOCS. SSB1 and SSB4 has been shown to bind to MET, the receptor protein-tyrosine kinase for hepatocyte growth factor (HGF) and also interacts with prostate apoptosis response protein-4. Both types of interactions are mediated through the SPRY domain. 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: 239688  Cd Length: 42  Bit Score: 37.67  E-value: 3.11e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2416804683 242 APGTLQTLSRYAVRRSLGVRFLpEAVKQLPLPTCLKEYVL 281
Cdd:cd03718     2 EPLPLMDLCRRRVRVALGRDRL-EEIEQLPLPPSLKNYLL 40
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 52-79 3.78e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 3.78e-04
                          10        20
                  ....*....|....*....|....*....
gi 2416804683  52 PLHCAC-MVADADCVELLLQKGAEVNALD 79
Cdd:pfam00023   5 PLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
147-184 4.35e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 4.35e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 2416804683 147 NDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQTPI 184
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETAL 38
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 63-156 5.70e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.74  E-value: 5.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  63 DCVELLLQKGAEVNA-----LDGYNrTALHYAAEKD-ETCVEILLEYGANPNALDGN-KDTPLHWAAFKNNAECVRSLLE 135
Cdd:PHA02884   47 DIIDAILKLGADPEApfplsENSKT-NPLIYAIDCDnDDAAKLLIRYGADVNRYAEEaKITPLYISVLHGCLKCLEILLS 125

                          90       100
                  ....*....|....*....|.
gi 2416804683 136 NGALVNARDYNNDTPLSWAAM 156
Cdd:PHA02884  126 YGADINIQTNDMVTPIELALM 146
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 100-184 1.29e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.97  E-value: 1.29e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683 100 LLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGALVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVR-VVNL 178
Cdd:PHA02875   21 LLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYK 100


                  ....*.
gi 2416804683 179 KGQTPI 184
Cdd:PHA02875  101 DGMTPL 106
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 61-185 1.30e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 40.28  E-value: 1.30e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  61 DADCVELLLQKGAEVNALDGYNRTALHYAAEK---DETCVEILLEYGANPNALDGNKDTPLHwaafknnaecvrSLLENG 137
Cdd:PHA02716  296 DISVVYSFLQPGVKLHYKDSAGRTCLHQYILRhniSTDIIKLLHEYGNDLNEPDNIGNTVLH------------TYLSML 363

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 2416804683 138 ALVNARDYNNDTPLswaamkgNLESVSILLDFGAEVRVVNLKGQTPIS 185
Cdd:PHA02716  364 SVVNILDPETDNDI-------RLDVIQCLISLGADITAVNCLGYTPLT 404
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
 245-279 1.33e-03

SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 domain. These intracellular proteins regulate the responses of immune cells to cytokines. Identified as negative regulators of the cytokine-JAK-STAT pathway, they seem to play a role in many immunological and pathological processes. The function of the SOCS box is the recruitment of the ubiquitin-transferase system. Related SOCS boxes are also present in Rab40-like proteins and insect proteins of unknown function that also contain a NEUZ (domain in neuralized proteins) domain.


Pssm-ID: 239687  Cd Length: 39  Bit Score: 35.65  E-value: 1.33e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 2416804683 245 TLQTLSRYAVRRSLGVrflpEAVKQLPLPTCLKEY 279
Cdd:cd03717     5 SLQHLCRFVIRQCTRR----DLIDQLPLPRRLKDY 35
Ank_5 pfam13857
Ankyrin repeats (many copies);
133-184 1.37e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 1.37e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2416804683 133 LLENG-ALVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQTPI 184
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 146-173 3.39e-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: 34.49  E-value: 3.39e-03
                           10        20
                   ....*....|....*....|....*...
gi 2416804683  146 NNDTPLSWAAMKGNLESVSILLDFGAEV 173
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 33-128 3.85e-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: 38.46  E-value: 3.85e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  33 VEDLIGRGADVN----------------CMHGTlKPLHCACMVADADCVELLLQKGAEVNALDGYNRTALHY---AAEKD 93
Cdd:cd22192   105 VRELIARGADVVspratgtffrpgpknlIYYGE-HPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIlvlQPNKT 183

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 2416804683  94 ETC--VEILLEYGA--NPNALD--GNKD--TPLHWAAFKNNAE 128
Cdd:cd22192   184 FACqmYDLILSYDKedDLQPLDlvPNNQglTPFKLAAKEGNIV 226
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 53-175 4.39e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 36.78  E-value: 4.39e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  53 LHCACMvaDADCVELLLQKGAEVNA----LDGYNRTA---LHYAAEKD-----ETCvEILLEYGANPNALDG-NKDTPLH 119
Cdd:PHA02736   21 LHYLCR--NGGVTDLLAFKNAISDEnrylVLEYNRHGkqcVHIVSNPDkadpqEKL-KLLMEWGADINGKERvFGNTPLH 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2416804683 120 WAAFKNNAECVRSLLEN-GALVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRV 175
Cdd:PHA02736   98 IAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCKV 154
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
 243-281 6.49e-03

SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. Human ASB15 is expressed predominantly in skeletal muscle and participates in the regulation of protein turnover and muscle cell development by stimulating protein synthesis and regulating differentiation of muscle cells. 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: 239701  Cd Length: 56  Bit Score: 34.42  E-value: 6.49e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2416804683 243 PGTLQTLSRYAVRRSLGVRFL--PEAVKQLPLPTCLKEYVL 281
Cdd:cd03731     3 PRPLKHLCRLKIRKLMGLQKLqqPSSMKKLPLPPALKRYIL 43
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 75-151 6.63e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 37.11  E-value: 6.63e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2416804683  75 VNALDGYNRTALHYAAEKDETCVEI---LLEYGANPN-ALDGNKDTPLHWAAFKN---NAECVRSLLENGALVNARDYNN 147
Cdd:PHA02859   44 VNDCNDLYETPIFSCLEKDKVNVEIlkfLIENGADVNfKTRDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDG 123


                  ....
gi 2416804683 148 DTPL 151
Cdd:PHA02859  124 KNLL 127
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 52-77 7.17e-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: 33.38  E-value: 7.17e-03
                          10        20
                  ....*....|....*....|....*.
gi 2416804683  52 PLHCACMVADADCVELLLQKGAEVNA 77
Cdd:pfam13606   5 PLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 116-142 7.84e-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: 33.38  E-value: 7.84e-03
                          10        20
                  ....*....|....*....|....*..
gi 2416804683 116 TPLHWAAFKNNAECVRSLLENGALVNA 142
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH