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Conserved domains on  [gi|676824466|gb|KFP18458|]
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Ankyrin repeat and SOCS box protein 8, partial [Egretta garzetta]

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];
17-149 3.86e-42

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.10  E-value: 3.86e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  17 PLHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEKDET-CVEILLEYGANPNALDGNKDTPLHWAAFKNNAECV 95
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLeIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 676824466  96 RSLLENGAWVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQTPI 149
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
SOCS_ASB8 cd03727
SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a ...
 206-248 2.71e-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: 2.71e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 676824466 206 SAPGTLQTLSRYAVRRSLGVRFLPEAVKQLPLPTCLKEYVLLL 248
Cdd:cd03727    1 SAPGTLKALARYAVRRSLGVQYLPEAVKQLPLPRSVKEYLLLL 43
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
17-149 3.86e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.10  E-value: 3.86e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  17 PLHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEKDET-CVEILLEYGANPNALDGNKDTPLHWAAFKNNAECV 95
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLeIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 676824466  96 RSLLENGAWVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQTPI 149
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1-176 6.02e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 97.44  E-value: 6.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466   1 VISQGADVNC---MHGTlkPLHCACMV-ADADCVELLLQKGAEVNALDGYNRTALHYAAEKDETCV-EILLEYGANPNAL 75
Cdd:PHA02876 327 LIMLGADVNAadrLYIT--PLHQASTLdRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIiNTLLDYGADIEAL 404

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  76 DGNKDTPLHWAAFKNNA-ECVRSLLENGAWVNARDYNNDTPLSWAAMKG-NLESVSILLDFGAEVRVVNLKGQTPIsrLV 153
Cdd:PHA02876 405 SQKIGTALHFALCGTNPyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPL--LI 482

                        170       180       190
                 ....*....|....*....|....*....|
gi 676824466 154 ALLVRGL-------GTEREDScfDLLHRAI 176
Cdd:PHA02876 483 ALEYHGIvnillhyGAELRDS--RVLHKSL 510
SOCS_ASB8 cd03727
SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a ...
 206-248 2.71e-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: 2.71e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 676824466 206 SAPGTLQTLSRYAVRRSLGVRFLPEAVKQLPLPTCLKEYVLLL 248
Cdd:cd03727    1 SAPGTLKALARYAVRRSLGVQYLPEAVKQLPLPRSVKEYLLLL 43
Ank_2 pfam12796
Ankyrin repeats (3 copies);
18-109 4.68e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 4.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466   18 LHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEKDET-CVEILLEYgANPNaLDGNKDTPLHWAAFKNNAECVR 96
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLeIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 676824466   97 SLLENGAWVNARD 109
Cdd:pfam12796  79 LLLEKGADINVKD 91
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 208-246 5.52e-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: 47.93  E-value: 5.52e-08
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 676824466  208 PGTLQTLSRYAVRRSLGvRFLPEAVKQLPLPTCLKEYVL 246
Cdd:pfam07525   2 PRSLQHLCRLAIRRALG-KRRLGAIDKLPLPPLLKDYLL 39
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 12-172 5.79e-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: 53.09  E-value: 5.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  12 HGTLKPLHCACMVADADCVE-LLLQKGAEVNALDGYNRTALHYAA--EKDETCVeILLEygANPNALD---------Gnk 79
Cdd:cd22192   15 RISESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAAlyDNLEAAV-VLME--AAPELVNepmtsdlyqG-- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  80 DTPLHWAAFKNNAECVRSLLENGAWV-NARD-------------YNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKG 145
Cdd:cd22192   90 ETALHIAVVNQNLNLVRELIARGADVvSPRAtgtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169

                        170       180
                 ....*....|....*....|....*....
gi 676824466 146 QTPISRLVallvrgLGTEREDSC--FDLL 172
Cdd:cd22192  170 NTVLHILV------LQPNKTFACqmYDLI 192
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 28-139 5.94e-08

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: 53.16  E-value: 5.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466   28 DCVELLLQKGAEVNALDgynrTALHYAAEKDETCVEILL--------EYGANPNALDGNKD------TPLHWAAFKNNAE 93
Cdd:TIGR00870  67 ELTELLLNLSCRGAVGD----TLLHAISLEYVDAVEAILlhllaafrKSGPLELANDQYTSeftpgiTALHLAAHRQNYE 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466   94 CVRSLLENGAWVNARD--------------YNNDTPLSWAAMKGNLESVSILLDFGAEVR 139
Cdd:TIGR00870 143 IVKLLLERGASVPARAcgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADIL 202
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 78-107 1.66e-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: 40.65  E-value: 1.66e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 676824466    78 NKDTPLHWAAFKNNAECVRSLLENGAWVNA 107
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
 210-247 2.00e-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: 40.47  E-value: 2.00e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 676824466   210 TLQTLSRYAVRRSLGvrflpeAVKQLPLPTCLKEYVLL 247
Cdd:smart00969   2 SLQHLCRLAIRRSLG------GIDKLPLPPRLKDYLLY 33
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
17-149 3.86e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.10  E-value: 3.86e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  17 PLHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEKDET-CVEILLEYGANPNALDGNKDTPLHWAAFKNNAECV 95
Cdd:COG0666   90 LLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLeIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIV 169

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 676824466  96 RSLLENGAWVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQTPI 149
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTAL 223
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-156 4.56e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.70  E-value: 4.56e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466   2 ISQGADVN-CMHGTLKPLHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEK-DETCVEILLEYGANPNALDGNK 79
Cdd:COG0666  107 LEAGADVNaRDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANgNLEIVKLLLEAGADVNARDNDG 186

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 676824466  80 DTPLHWAAFKNNAECVRSLLENGAWVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQTPISRLVALL 156
Cdd:COG0666  187 ETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
17-148 2.13e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.37  E-value: 2.13e-33
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  17 PLHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEK-DETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECV 95
Cdd:COG0666   57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNgDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIV 136

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 676824466  96 RSLLENGAWVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQTP 148
Cdd:COG0666  137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP 189
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-149 5.36e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.81  E-value: 5.36e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466   2 ISQGADVNCMHGTLK-PLHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEK-DETCVEILLEYGANPNALDGNK 79
Cdd:COG0666  140 LEAGADVNAQDNDGNtPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENgHLEIVKLLLEAGADVNAKDNDG 219

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  80 DTPLHWAAFKNNAECVRSLLENGAWVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQTPI 149
Cdd:COG0666  220 KTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 1-176 6.02e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 97.44  E-value: 6.02e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466   1 VISQGADVNC---MHGTlkPLHCACMV-ADADCVELLLQKGAEVNALDGYNRTALHYAAEKDETCV-EILLEYGANPNAL 75
Cdd:PHA02876 327 LIMLGADVNAadrLYIT--PLHQASTLdRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIiNTLLDYGADIEAL 404

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  76 DGNKDTPLHWAAFKNNA-ECVRSLLENGAWVNARDYNNDTPLSWAAMKG-NLESVSILLDFGAEVRVVNLKGQTPIsrLV 153
Cdd:PHA02876 405 SQKIGTALHFALCGTNPyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPL--LI 482

                        170       180       190
                 ....*....|....*....|....*....|
gi 676824466 154 ALLVRGL-------GTEREDScfDLLHRAI 176
Cdd:PHA02876 483 ALEYHGIvnillhyGAELRDS--RVLHKSL 510
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 2-142 7.22e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 93.19  E-value: 7.22e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466   2 ISQGADVN-CMHGTLKPLHCACM--VADADCVELLLQKGAEVNALDGYNRTALHYAAE---------------------K 57
Cdd:PHA03100  93 LEYGANVNaPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnkidlkilkllidkgvdinaK 172

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  58 DEtcVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGAWVNARDYNNDTPLSWAAMKGNLESVSILLDFGAE 137
Cdd:PHA03100 173 NR--VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250


                 ....*
gi 676824466 138 VRVVN 142
Cdd:PHA03100 251 IKTII 255
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1-183 2.46e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 92.25  E-value: 2.46e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466   1 VISQGADVNCM--HGTLKPLHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEK-DETCVEILLEYGANPNALDG 77
Cdd:PHA02878 153 LLSYGADINMKdrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHyNKPIVHILLENGASTDARDK 232

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  78 NKDTPLHWA-AFKNNAECVRSLLENGAWVNARDY-NNDTPLSwAAMKGNlESVSILLDFGAEVRVVNLKGQTPISRLVal 155
Cdd:PHA02878 233 CGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALH-SSIKSE-RKLKLLLEYGADINSLNSYKLTPLSSAV-- 308

                        170       180
                 ....*....|....*....|....*...
gi 676824466 156 lvrglgteREDSCFDLLHRAIGHFELRK 183
Cdd:PHA02878 309 --------KQYLCINIGRILISNICLLK 328
SOCS_ASB8 cd03727
SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a ...
 206-248 2.71e-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: 2.71e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 676824466 206 SAPGTLQTLSRYAVRRSLGVRFLPEAVKQLPLPTCLKEYVLLL 248
Cdd:cd03727    1 SAPGTLKALARYAVRRSLGVQYLPEAVKQLPLPRSVKEYLLLL 43
Ank_2 pfam12796
Ankyrin repeats (3 copies);
18-109 4.68e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 4.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466   18 LHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEKDET-CVEILLEYgANPNaLDGNKDTPLHWAAFKNNAECVR 96
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLeIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 676824466   97 SLLENGAWVNARD 109
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
18-149 6.81e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.86  E-value: 6.81e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  18 LHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEKDETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRS 97
Cdd:COG0666   26 LAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKL 105

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 676824466  98 LLENGAWVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQTPI 149
Cdd:COG0666  106 LLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
Ank_2 pfam12796
Ankyrin repeats (3 copies);
51-142 1.16e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.24  E-value: 1.16e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466   51 LHYAAE-KDETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGAwVNARDYNNdTPLSWAAMKGNLESVS 129
Cdd:pfam12796   1 LHLAAKnGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD-VNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 676824466  130 ILLDFGAEVRVVN 142
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 2-149 3.80e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 88.48  E-value: 3.80e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466   2 ISQGADVNCMHGTL-KPLHCACMVADADCVELL-----------------------LQKGAEVNALDGYNRTALHYAAEK 57
Cdd:PHA02874  55 IKHGADINHINTKIpHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmiktiLDCGIDVNIKDAELKTFLHYAIKK 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  58 -DETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGAWVNARDYNNDTPLSWAAMKGNLESVSILLDFGA 136
Cdd:PHA02874 135 gDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGN 214

                        170
                 ....*....|...
gi 676824466 137 EVRVVNLKGQTPI 149
Cdd:PHA02874 215 HIMNKCKNGFTPL 227
PHA03095 PHA03095
ankyrin-like protein; Provisional
 25-173 1.19e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.31  E-value: 1.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  25 ADADCVELLLQKGAEVNALDGYNRTALH----YAAEKDETCVEILLEYGANPNALDGNKDTPLH-WAAFKNNAECVRSLL 99
Cdd:PHA03095  25 VTVEEVRRLLAAGADVNFRGEYGKTPLHlylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLI 104

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466 100 ENGAWVNARDYNNDTPLSwAAMKG---NLESVSILLDFGAEVRVVNLKGQTPIS----------RLVALLVRGLG--TER 164
Cdd:PHA03095 105 KAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAvllksrnanvELLRLLIDAGAdvYAV 183


                 ....*....
gi 676824466 165 EDSCFDLLH 173
Cdd:PHA03095 184 DDRFRSLLH 192
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 17-159 4.36e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 83.19  E-value: 4.36e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  17 PLHCACMVAD-ADCVELLLQKGAEVNALDGYNRTALHYAAEK--DETCVEILLEYGANPNALDGNKDTPLHWAA-FKNNA 92
Cdd:PHA02876 276 PLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNgyDTENIRTLIMLGADVNAADRLYITPLHQAStLDRNK 355

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 676824466  93 ECVRSLLENGAWVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLK----------GQTPISRLVALLVRG 159
Cdd:PHA02876 356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKigtalhfalcGTNPYMSVKTLIDRG 432
PHA03095 PHA03095
ankyrin-like protein; Provisional
 2-154 1.86e-17

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 80.84  E-value: 1.86e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466   2 ISQGADVNCM--HGtLKPLHCAcMV---ADADCVELLLQKGAEVNALDGYNRTALHYAAE---KDETCVEILLEYGANPN 73
Cdd:PHA03095 139 LRKGADVNALdlYG-MTPLAVL-LKsrnANVELLRLLIDAGADVYAVDDRFRSLLHHHLQsfkPRARIVRELIRAGCDPA 216

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  74 ALDGNKDTPLHWAAfkNNAECVRS----LLENGAWVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQTPI 149
Cdd:PHA03095 217 ATDMLGNTPLHSMA--TGSSCKRSlvlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPL 294


                 ....*
gi 676824466 150 SRLVA 154
Cdd:PHA03095 295 SLMVR 299
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 7-154 4.31e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 76.63  E-value: 4.31e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466   7 DVNCMHGTLkPLHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAA------EKDETCVEILLEYGANPNALDGNKD 80
Cdd:PHA03100  29 DYSYKKPVL-PLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynlTDVKEIVKLLLEYGANVNAPDNNGI 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  81 TPLHWAAFKN----------------------------------------------------NAEC-VRSLLENGAWVNA 107
Cdd:PHA03100 108 TPLLYAISKKsnsysiveylldnganvniknsdgenllhlylesnkidlkilkllidkgvdiNAKNrVNYLLSYGVPINI 187

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 676824466 108 RDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQTPISRLVA 154
Cdd:PHA03100 188 KDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 31-175 5.18e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 73.94  E-value: 5.18e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  31 ELLLQKGAEVNALDGYNRTALHYAAEKDET-CVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLEN-------- 101
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAkMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNrsninknd 241

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466 102 ---------------------GAWVNARDYNNDTPLSWAAMKGNLES-VSILLDFGAEVRVVNLKGQTPI---------- 149
Cdd:PHA02876 242 lsllkairnedletslllydaGFSVNSIDDCKNTPLHHASQAPSLSRlVPKLLERGADVNAKNIKGETPLylmakngydt 321

                        170       180
                 ....*....|....*....|....*..
gi 676824466 150 SRLVALLVRGLGTEREDSCFDL-LHRA 175
Cdd:PHA02876 322 ENIRTLIMLGADVNAADRLYITpLHQA 348
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 5-149 3.01e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 71.53  E-value: 3.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466   5 GADVNC--MHGTLkPLHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAE-KDETCVEILLEYGANPNALDGNKDT 81
Cdd:PHA02874 147 GADVNIedDNGCY-PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEyGDYACIKLLIDHGNHIMNKCKNGFT 225

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 676824466  82 PLHWAAFKNNAecVRSLLENGAWVNARDYNNDTPLSWAAM-KGNLESVSILLDFGAEVRVVNLKGQTPI 149
Cdd:PHA02874 226 PLHNAIIHNRS--AIELLINNASINDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPI 292
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 1-149 7.98e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.21  E-value: 7.98e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466   1 VISQGADVNCMHGTLKP-LHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEKDE-TCVEILLEYGANPNALDGN 78
Cdd:PHA02874 110 ILDCGIDVNIKDAELKTfLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFfDIIKLLLEKGAYANVKDNN 189

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 676824466  79 KDTPLHWAAFKNNAECVRSLLENGAWVNARDYNNDTPLSWAAMKgNLESVSILLDfGAEVRVVNLKGQTPI 149
Cdd:PHA02874 190 GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLIN-NASINDQDIDGSTPL 258
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 1-149 1.55e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.36  E-value: 1.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466   1 VISQGADVNCM-HGTLKPLHCACMVADADCVELLLQ--------------------------KGAEVNALDGYNRTALHY 53
Cdd:PHA02878  56 LLTRGHNVNQPdHRDLTPLHIICKEPNKLGMKEMIRsinkcsvfytlvaikdafnnrnveifKIILTNRYKNIQTIDLVY 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  54 AAEKDE------TCVEILLEYGANPNALDGNKD-TPLHWAAFKNNAECVRSLLENGAWVNARDYNNDTPLSWAAMKGNLE 126
Cdd:PHA02878 136 IDKKSKddiieaEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKP 215

                        170       180
                 ....*....|....*....|...
gi 676824466 127 SVSILLDFGAEVRVVNLKGQTPI 149
Cdd:PHA02878 216 IVHILLENGASTDARDKCGNTPL 238
PHA03095 PHA03095
ankyrin-like protein; Provisional
 25-132 1.74e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.51  E-value: 1.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  25 ADADCVELLLQKGAEVNALDGYNRTALHYAAeKDETCVEI----LLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLE 100
Cdd:PHA03095 200 PRARIVRELIRAGCDPAATDMLGNTPLHSMA-TGSSCKRSlvlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIA 278

                         90       100       110
                 ....*....|....*....|....*....|..
gi 676824466 101 NGAWVNARDYNNDTPLSWAAMKGNLESVSILL 132
Cdd:PHA03095 279 LGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
Ank_2 pfam12796
Ankyrin repeats (3 copies);
2-76 3.36e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.20  E-value: 3.36e-11
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 676824466    2 ISQGADVNCMHGT-LKPLHCACMVADADCVELLLQKgAEVNaLDGYNRTALHYAAEKD-ETCVEILLEYGANPNALD 76
Cdd:pfam12796  17 LENGADANLQDKNgRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGhLEIVKLLLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 13-174 5.74e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.93  E-value: 5.74e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  13 GTLKPLHCACMVADADCVELLLQKGAEVNAL---DGynRTALHYAAE-KDETCVEILLEYGANPNALDGNKDTPLHWAAF 88
Cdd:PHA02875  67 DIESELHDAVEEGDVKAVEELLDLGKFADDVfykDG--MTPLHLATIlKKLDIMKLLIARGADPDIPNTDKFSPLHLAVM 144

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  89 KNNAECVRSLLENGAWVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQtpisrlVALLVRGLGTEREDSC 168
Cdd:PHA02875 145 MGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGC------VAALCYAIENNKIDIV 218


                 ....*.
gi 676824466 169 FDLLHR 174
Cdd:PHA02875 219 RLFIKR 224
Ank_2 pfam12796
Ankyrin repeats (3 copies);
83-149 7.30e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.05  E-value: 7.30e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 676824466   83 LHWAAFKNNAECVRSLLENGAWVNARDYNNDTPLSWAAMKGNLESVSILLDFgAEVRVVNlKGQTPI 149
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTAL 65
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
 206-247 4.20e-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: 53.65  E-value: 4.20e-10
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 676824466 206 SAPGTLQTLSRYAVRRSLGVRfLPEAVKQLPLPTCLKEYVLL 247
Cdd:cd03716    1 STPRSLQHLCRLAIRRCLGRR-RLELIKKLPLPPRLKDYLLY 41
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 14-149 5.28e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.82  E-value: 5.28e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  14 TLKPLHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAE-KDETCVEILLEYGANPNAL---DGNKDTplhwaafk 89
Cdd:PHA02874  35 TTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKiGAHDIIKLLIDNGVDTSILpipCIEKDM-------- 106

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  90 nnaecVRSLLENGAWVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQTPI 149
Cdd:PHA02874 107 -----IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPI 161
Ank_4 pfam13637
Ankyrin repeats (many copies);
81-132 6.81e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 6.81e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 676824466   81 TPLHWAAFKNNAECVRSLLENGAWVNARDYNNDTPLSWAAMKGNLESVSILL 132
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
47-99 1.24e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 52.66  E-value: 1.24e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 676824466   47 NRTALHYAAEK-DETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLL 99
Cdd:pfam13637   1 ELTALHAAAASgHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
31-149 1.38e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 57.27  E-value: 1.38e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  31 ELLLQKGAEVNALDGYNRTALHYAAEKDETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGAWVNARDY 110
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 676824466 111 NNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQTPI 149
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL 124
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
 208-247 2.93e-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: 51.32  E-value: 2.93e-09
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 676824466 208 PGTLQTLSRYAVRRSLGVRfLPEAVKQLPLPTCLKEYVLL 247
Cdd:cd03587    2 PRSLQHLCRLAIRRCLGKR-RLDLIDKLPLPPRLKDYLLY 40
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 52-148 3.81e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 3.81e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  52 HYAAEKDETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGAWVNARDYNNDTPLSWAAMKGNLESVSIL 131
Cdd:PTZ00322  88 QLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167

                         90       100
                 ....*....|....*....|....
gi 676824466 132 L-------DFGAEVRVVNLKGQTP 148
Cdd:PTZ00322 168 SrhsqchfELGANAKPDSFTGKPP 191
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 95-149 9.32e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 9.32e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 676824466  95 VRSLLENGAWVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQTPI 149
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL 152
PHA02946 PHA02946
ankyin-like protein; Provisional
 58-138 2.33e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 53.90  E-value: 2.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  58 DETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGAWVNARDYNNDTPLSWAAMKGN--LESVSILLDFG 135
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYG 130


                 ...
gi 676824466 136 AEV 138
Cdd:PHA02946 131 AKI 133
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 21-143 3.67e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 3.67e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  21 ACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEKD-ETCVEILLEYGANPNALDGNKDTPLhW-------------- 85
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGyEDCVLVLLKHACNVHIRDANGNTAL-Wnaisakhhkifril 610

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 676824466  86 ------------------AAFKNNAECVRSLLENGAWVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNL 143
Cdd:PLN03192 611 yhfasisdphaagdllctAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANT 686
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 208-246 5.52e-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: 47.93  E-value: 5.52e-08
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 676824466  208 PGTLQTLSRYAVRRSLGvRFLPEAVKQLPLPTCLKEYVL 246
Cdd:pfam07525   2 PRSLQHLCRLAIRRALG-KRRLGAIDKLPLPPLLKDYLL 39
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 12-172 5.79e-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: 53.09  E-value: 5.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  12 HGTLKPLHCACMVADADCVE-LLLQKGAEVNALDGYNRTALHYAA--EKDETCVeILLEygANPNALD---------Gnk 79
Cdd:cd22192   15 RISESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAAlyDNLEAAV-VLME--AAPELVNepmtsdlyqG-- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  80 DTPLHWAAFKNNAECVRSLLENGAWV-NARD-------------YNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKG 145
Cdd:cd22192   90 ETALHIAVVNQNLNLVRELIARGADVvSPRAtgtffrpgpknliYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169

                        170       180
                 ....*....|....*....|....*....
gi 676824466 146 QTPISRLVallvrgLGTEREDSC--FDLL 172
Cdd:cd22192  170 NTVLHILV------LQPNKTFACqmYDLI 192
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 28-139 5.94e-08

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: 53.16  E-value: 5.94e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466   28 DCVELLLQKGAEVNALDgynrTALHYAAEKDETCVEILL--------EYGANPNALDGNKD------TPLHWAAFKNNAE 93
Cdd:TIGR00870  67 ELTELLLNLSCRGAVGD----TLLHAISLEYVDAVEAILlhllaafrKSGPLELANDQYTSeftpgiTALHLAAHRQNYE 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466   94 CVRSLLENGAWVNARD--------------YNNDTPLSWAAMKGNLESVSILLDFGAEVR 139
Cdd:TIGR00870 143 IVKLLLERGASVPARAcgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADIL 202
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 26-136 1.07e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  26 DADCVELLLQKGAEVNALDGYNRTALHYAAEKDE-TCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGAW 104
Cdd:PTZ00322  94 DAVGARILLTGGADPNCRDYDGRTPLHIACANGHvQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173

                         90       100       110
                 ....*....|....*....|....*....|....*
gi 676824466 105 VNARDYNNdTPLSWAAMKGNLESVSILL---DFGA 136
Cdd:PTZ00322 174 HFELGANA-KPDSFTGKPPSLEDSPISShhpDFSA 207
Ank_5 pfam13857
Ankyrin repeats (many copies);
65-116 1.40e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 1.40e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 676824466   65 LLEYG-ANPNALDGNKDTPLHWAAFKNNAECVRSLLENGAWVNARDYNNDTPL 116
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 58-147 2.52e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.22  E-value: 2.52e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  58 DETCVEILLEyganpnALDGNKdtpLHWAAFKNNAECVRS---------------LLENGAWVNARDYNNDTPLSWAAMK 122
Cdd:PHA02876 118 DEACIHILKE------AISGND---IHYDKINESIEYMKLikeriqqdelliaemLLEGGADVNAKDIYCITPIHYAAER 188

                         90       100
                 ....*....|....*....|....*
gi 676824466 123 GNLESVSILLDFGAEVRVVNLKGQT 147
Cdd:PHA02876 189 GNAKMVNLLLSYGADVNIIALDDLS 213
PHA02798 PHA02798
ankyrin-like protein; Provisional
 62-147 2.62e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 50.99  E-value: 2.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  62 VEILLEYGANPNALDGNKDTPL-----HWAAFKNNAECVRSLLENGAWVNARDYNNDTPLSWAAMKG---NLESVSILLD 133
Cdd:PHA02798  54 VKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFMIE 133

                         90
                 ....*....|....
gi 676824466 134 FGAEVRVVNLKGQT 147
Cdd:PHA02798 134 NGADTTLLDKDGFT 147
Ank_4 pfam13637
Ankyrin repeats (many copies);
17-66 3.87e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 3.87e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 676824466   17 PLHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEK-DETCVEILL 66
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNgNVEVLKLLL 54
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 62-149 4.76e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 49.60  E-value: 4.76e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  62 VEILLEYGANPNA----LDGNKDTPLHWAAFKNNAECVRSLLENGAWVNA-RDYNNDTPLSWAAMKGNLESVSILLDFGA 136
Cdd:PHA02884  49 IDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKITPLYISVLHGCLKCLEILLSYGA 128

                         90
                 ....*....|...
gi 676824466 137 EVRVVNLKGQTPI 149
Cdd:PHA02884 129 DINIQTNDMVTPI 141
PHA02946 PHA02946
ankyin-like protein; Provisional
 13-151 1.81e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 48.13  E-value: 1.81e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  13 GTLKPLHCACMVA--DADCVELLLQKGAEVNALDGYNRTALHYAAE-KDETCVEILLEYGANPNALDGNKDTPLHWAAFK 89
Cdd:PHA02946  36 GNYHILHAYCGIKglDERFVEELLHRGYSPNETDDDGNYPLHIASKiNNNRIVAMLLTHGADPNACDKQHKTPLYYLSGT 115

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 676824466  90 NNA--ECVRSLLENGAWV-NARDYNNDTPLsWAAMKGNLESVSILLDFGAEVRVVNLKGQTPISR 151
Cdd:PHA02946 116 DDEviERINLLVQYGAKInNSVDEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHR 179
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 25-149 5.06e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.97  E-value: 5.06e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  25 ADADCVELLLQKGAEVN-ALDGYNRTALHYAAEKDETC----VEILLEYGANPNALDGNKDTPLH--WAAFKNNAECVRS 97
Cdd:PHA02859  64 VNVEILKFLIENGADVNfKTRDNNLSALHHYLSFNKNVepeiLKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKL 143

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 676824466  98 LLENGAWVNARDYNNDTPL-SWAAMKGNLESVSILLDFGAEVRVVNLKGQTPI 149
Cdd:PHA02859 144 LIDSGVSFLNKDFDNNNILySYILFHSDKKIFDFLTSLGIDINETNKSGYNCY 196
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 56-133 5.30e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 5.30e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 676824466  56 EKDETCV-EILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGAWVNARDYNNDTPLSWAAMKGNLESVSILLD 133
Cdd:PHA02876 154 QQDELLIaEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIID 232
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 1-83 5.43e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 5.43e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466   1 VISQGADVNCM--HGTlKPLHCACMVADADCVELLLQKGAEVNALDGYNRTALHYAAEKD-ETCVEILLEY-------GA 70
Cdd:PTZ00322 101 LLTGGADPNCRdyDGR-TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGfREVVQLLSRHsqchfelGA 179

                         90
                 ....*....|....*....
gi 676824466  71 N--PNALDGN----KDTPL 83
Cdd:PTZ00322 180 NakPDSFTGKppslEDSPI 198
PHA02798 PHA02798
ankyrin-like protein; Provisional
 28-142 9.66e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.98  E-value: 9.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  28 DCVELLLQKGAEVNALDGYNRTAL--------HYAAEKDetCVEILLEYGANPNALDGNKDTPLHWA---AFKNNAECVR 96
Cdd:PHA02798  52 DIVKLFINLGANVNGLDNEYSTPLctilsnikDYKHMLD--IVKILIENGADINKKNSDGETPLYCLlsnGYINNLEILL 129

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 676824466  97 SLLENGAWVNARDYNNDTPLSWAAMKGN---LESVSILLDFGAEVRVVN 142
Cdd:PHA02798 130 FMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHN 178
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 78-109 9.67e-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: 41.51  E-value: 9.67e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 676824466   78 NKDTPLHWAAFK-NNAECVRSLLENGAWVNARD 109
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 26-136 9.68e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.40  E-value: 9.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  26 DADCVELLLQKGAE-VNALDGYNrtALHYAAEKDETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGAW 104
Cdd:PLN03192 506 DLNVGDLLGDNGGEhDDPNMASN--LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN 583

                         90       100       110
                 ....*....|....*....|....*....|..
gi 676824466 105 VNARDYNNDTPLSWAAMKGNLESVSILLDFGA 136
Cdd:PLN03192 584 VHIRDANGNTALWNAISAKHHKIFRILYHFAS 615
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 48-139 1.28e-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: 1.28e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  48 RTALHYAAEKDET----CVEILLEYG---------ANPNALDG--NKDTPLHWAAFKNNAECVRSLLENGAWVNARD--- 109
Cdd:cd21882   27 KTCLHKAALNLNDgvneAIMLLLEAApdsgnpkelVNAPCTDEfyQGQTALHIAIENRNLNLVRLLVENGADVSARAtgr 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 676824466 110 ----------YNNDTPLSWAAMKGNLESVSILLDFGAEVR 139
Cdd:cd21882  107 ffrkspgnlfYFGELPLSLAACTNQEEIVRLLLENGAQPA 146
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 78-107 1.66e-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: 40.65  E-value: 1.66e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 676824466    78 NKDTPLHWAAFKNNAECVRSLLENGAWVNA 107
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 57-149 2.00e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.98  E-value: 2.00e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  57 KDETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGAWVNARDYNN-DTPLSWAAMKGNLESVSILLDFG 135
Cdd:PHA02875  46 RDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARG 125

                         90
                 ....*....|....
gi 676824466 136 AEVRVVNLKGQTPI 149
Cdd:PHA02875 126 ADPDIPNTDKFSPL 139
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
 210-247 2.00e-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: 40.47  E-value: 2.00e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 676824466   210 TLQTLSRYAVRRSLGvrflpeAVKQLPLPTCLKEYVLL 247
Cdd:smart00969   2 SLQHLCRLAIRRSLG------GIDKLPLPPRLKDYLLY 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
32-86 2.67e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.79  E-value: 2.67e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 676824466   32 LLLQKGAEVNALDGYNRTALHYAAEKDE-TCVEILLEYGANPNALDGNKDTPLHWA 86
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGAlEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
 208-247 2.78e-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: 2.78e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 676824466 208 PGTLQTLSRYAVRRSLGVRfLPEAVKQLPLPTCLKEYVLL 247
Cdd:cd03723    3 PRSLQHLCRCAIRKLLGSR-CHKLVPQLSLPTSLKNYLLL 41
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 46-76 5.80e-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: 39.19  E-value: 5.80e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 676824466   46 YNRTALHYAAEK--DETCVEILLEYGANPNALD 76
Cdd:pfam00023   1 DGNTPLHLAAGRrgNLEIVKLLLSKGADVNARD 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 17-100 9.36e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 43.09  E-value: 9.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  17 PLHCACMVADADC--VELLLQKGAEVNALDGYNRTALHYAAEKDETCV-EILLEYGANPNALDGNKDTPLHWAAFKNNAE 93
Cdd:PHA03095 225 PLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAVFNNPRAcRRLIALGADINAVSSDGNTPLSLMVRNNNGR 304


                 ....*..
gi 676824466  94 CVRSLLE 100
Cdd:PHA03095 305 AVRAALA 311
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 17-126 1.68e-04

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: 42.31  E-value: 1.68e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  17 PLHCACMVADADCVELLLQKGAEVN--------------ALDGYNRTALHYAA-EKDETCVEILLEYGANPNALDGNKDT 81
Cdd:cd22192   92 ALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpkNLIYYGEHPLSFAAcVGNEEIVRLLIEHGADIRAQDSLGNT 171

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 676824466  82 PLHWAAFKNNAECVRSLLEngaWVNARDYNND-------------TPLSWAAMKGNLE 126
Cdd:cd22192  172 VLHILVLQPNKTFACQMYD---LILSYDKEDDlqpldlvpnnqglTPFKLAAKEGNIV 226
SOCS_SSB1_4 cd03718
SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box ...
 207-246 1.78e-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: 38.05  E-value: 1.78e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 676824466 207 APGTLQTLSRYAVRRSLGVRFLpEAVKQLPLPTCLKEYVL 246
Cdd:cd03718    2 EPLPLMDLCRRRVRVALGRDRL-EEIEQLPLPPSLKNYLL 40
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 17-42 1.80e-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: 1.80e-04
                           10        20
                   ....*....|....*....|....*.
gi 676824466    17 PLHCACMVADADCVELLLQKGAEVNA 42
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 46-74 2.59e-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: 2.59e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 676824466    46 YNRTALHYAAEK-DETCVEILLEYGANPNA 74
Cdd:smart00248   1 DGRTPLHLAAENgNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
112-149 4.58e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 4.58e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 676824466  112 NDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQTPI 149
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETAL 38
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 28-121 4.72e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.74  E-value: 4.72e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  28 DCVELLLQKGAEVNA-----LDGYNrTALHYAAEKD-ETCVEILLEYGANPNALDGN-KDTPLHWAAFKNNAECVRSLLE 100
Cdd:PHA02884  47 DIIDAILKLGADPEApfplsENSKT-NPLIYAIDCDnDDAAKLLIRYGADVNRYAEEaKITPLYISVLHGCLKCLEILLS 125

                         90       100
                 ....*....|....*....|.
gi 676824466 101 NGAWVNARDYNNDTPLSWAAM 121
Cdd:PHA02884 126 YGADINIQTNDMVTPIELALM 146
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 17-44 5.19e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 5.19e-04
                          10        20
                  ....*....|....*....|....*....
gi 676824466   17 PLHCAC-MVADADCVELLLQKGAEVNALD 44
Cdd:pfam00023   5 PLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 65-149 7.93e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 40.36  E-value: 7.93e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  65 LLEYGANPNALDGNKDTPLHWAAFKNNAECVRSLLENGAWVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVR-VVNL 143
Cdd:PHA02875  21 LLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYK 100


                 ....*.
gi 676824466 144 KGQTPI 149
Cdd:PHA02875 101 DGMTPL 106
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
 210-244 8.58e-04

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: 36.04  E-value: 8.58e-04
                         10        20        30
                 ....*....|....*....|....*....|....*
gi 676824466 210 TLQTLSRYAVRRSLGVrflpEAVKQLPLPTCLKEY 244
Cdd:cd03717    5 SLQHLCRFVIRQCTRR----DLIDQLPLPRRLKDY 35
Ank_5 pfam13857
Ankyrin repeats (many copies);
98-149 1.46e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 1.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 676824466   98 LLENGAW-VNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRVVNLKGQTPI 149
Cdd:pfam13857   1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 81-107 1.77e-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: 34.93  E-value: 1.77e-03
                          10        20
                  ....*....|....*....|....*..
gi 676824466   81 TPLHWAAFKNNAECVRSLLENGAWVNA 107
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 26-150 1.90e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 39.12  E-value: 1.90e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  26 DADCVELLLQKGAEVNALDGYNRTALHYAAEK---DETCVEILLEYGANPNALDGNKDTPLHwaafknnaecvrSLLENG 102
Cdd:PHA02716 296 DISVVYSFLQPGVKLHYKDSAGRTCLHQYILRhniSTDIIKLLHEYGNDLNEPDNIGNTVLH------------TYLSML 363

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*...
gi 676824466 103 AWVNARDYNNDTPLswaamkgNLESVSILLDFGAEVRVVNLKGQTPIS 150
Cdd:PHA02716 364 SVVNILDPETDNDI-------RLDVIQCLISLGADITAVNCLGYTPLT 404
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 111-138 3.22e-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: 34.10  E-value: 3.22e-03
                           10        20
                   ....*....|....*....|....*...
gi 676824466   111 NNDTPLSWAAMKGNLESVSILLDFGAEV 138
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
 208-246 4.23e-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: 34.81  E-value: 4.23e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 676824466 208 PGTLQTLSRYAVRRSLGVRFL--PEAVKQLPLPTCLKEYVL 246
Cdd:cd03731    3 PRPLKHLCRLKIRKLMGLQKLqqPSSMKKLPLPPALKRYIL 43
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 18-140 4.52e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 36.78  E-value: 4.52e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  18 LHCACMvaDADCVELLLQKGAEVNA----LDGYNRTA---LHYAAEKD-----ETCvEILLEYGANPNALDG-NKDTPLH 84
Cdd:PHA02736  21 LHYLCR--NGGVTDLLAFKNAISDEnrylVLEYNRHGkqcVHIVSNPDkadpqEKL-KLLMEWGADINGKERvFGNTPLH 97

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 676824466  85 WAAFKNNAECVRSLLEN-GAWVNARDYNNDTPLSWAAMKGNLESVSILLDFGAEVRV 140
Cdd:PHA02736  98 IAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCKV 154
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 40-116 5.98e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 36.72  E-value: 5.98e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466  40 VNALDGYNRTALHYAAEKDETCVEI---LLEYGANPN-ALDGNKDTPLHWAAFKN---NAECVRSLLENGAWVNARDYNN 112
Cdd:PHA02859  44 VNDCNDLYETPIFSCLEKDKVNVEIlkfLIENGADVNfKTRDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDG 123


                 ....
gi 676824466 113 DTPL 116
Cdd:PHA02859 124 KNLL 127
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 17-42 6.43e-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: 6.43e-03
                          10        20
                  ....*....|....*....|....*.
gi 676824466   17 PLHCACMVADADCVELLLQKGAEVNA 42
Cdd:pfam13606   5 PLHLAARNGRLEIVKLLLENGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 17-124 7.94e-03

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: 37.37  E-value: 7.94e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 676824466   17 PLHCACMVADADCVELLLQKGAEVNA--------------LDGYNRTALH-YAAEKDETCVEILLEYGANPNALDGNKDT 81
Cdd:TIGR00870 131 ALHLAAHRQNYEIVKLLLERGASVPAracgdffvksqgvdSFYHGESPLNaAACLGSPSIVALLSEDPADILTADSLGNT 210

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 676824466   82 PLHWAA----FKNNAECVRSLLENGA---WVNARD---------YNNDTPLSWAAMKGN 124
Cdd:TIGR00870 211 LLHLLVmeneFKAEYEELSCQMYNFAlslLDKLRDskelevilnHQGLTPLKLAAKEGR 269
 
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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