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Conserved domains on  [gi|1720385305|ref|XP_030104679|]
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ankyrin repeat and SOCS box protein 8 isoform X1 [Mus musculus]

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];
26-188 5.06e-43

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.95  E-value: 5.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  26 IAAIRSFPHDNVEDLIRGGADVNCT-HGTLKPLHCACMVSDADCVELLLEKGAEVNALDGYNRTALHYAAEK-DEACVEV 103
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKdDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNgNLEIVKL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305 104 LLEYGANPNALDGNRDTPLHWAAFKNNAECVRALLESGASVNALDYNNDTPLSWAAMKGNLESVSILLDYGAEVRVINLK 183
Cdd:COG0666   139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218


                  ....*
gi 1720385305 184 GQTPI 188
Cdd:COG0666   219 GKTAL 223
SOCS_ASB8 cd03727
SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a ...
 245-287 6.78e-20

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: 80.65  E-value: 6.78e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1720385305 245 SAPGTLKTLARYAVRRSLGLQYLPDAVKGLPLPVSLKDYLLLL 287
Cdd:cd03727     1 SAPGTLKALARYAVRRSLGVQYLPEAVKQLPLPRSVKEYLLLL 43
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
26-188 5.06e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.95  E-value: 5.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  26 IAAIRSFPHDNVEDLIRGGADVNCT-HGTLKPLHCACMVSDADCVELLLEKGAEVNALDGYNRTALHYAAEK-DEACVEV 103
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKdDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNgNLEIVKL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305 104 LLEYGANPNALDGNRDTPLHWAAFKNNAECVRALLESGASVNALDYNNDTPLSWAAMKGNLESVSILLDYGAEVRVINLK 183
Cdd:COG0666   139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218


                  ....*
gi 1720385305 184 GQTPI 188
Cdd:COG0666   219 GKTAL 223
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 26-215 8.73e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 100.91  E-value: 8.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  26 IAAIRSFPHDNVEDLIRGGADVNCTHGT-LKPLHCACMVS-DADCVELLLEKGAEVNALDGYNRTALHYAAEKDEACV-E 102
Cdd:PHA02876  313 LMAKNGYDTENIRTLIMLGADVNAADRLyITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIiN 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305 103 VLLEYGANPNALDGNRDTPLHWAAFKNNA-ECVRALLESGASVNALDYNNDTPLSWAAMKG-NLESVSILLDYGAEVRVI 180
Cdd:PHA02876  393 TLLDYGADIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAI 472

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1720385305 181 NLKGQTPIsrLVALLVRGL-------GTEKEDScfELLHRAV 215
Cdd:PHA02876  473 NIQNQYPL--LIALEYHGIvnillhyGAELRDS--RVLHKSL 510
Ank_2 pfam12796
Ankyrin repeats (3 copies);
57-148 3.68e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 3.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  57 LHCACMVSDADCVELLLEKGAEVNALDGYNRTALHYAAEKDEA-CVEVLLEYgANPNALDGNRdTPLHWAAFKNNAECVR 135
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLeIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1720385305 136 ALLESGASVNALD 148
Cdd:pfam12796  79 LLLEKGADINVKD 91
SOCS_ASB8 cd03727
SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a ...
 245-287 6.78e-20

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: 80.65  E-value: 6.78e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1720385305 245 SAPGTLKTLARYAVRRSLGLQYLPDAVKGLPLPVSLKDYLLLL 287
Cdd:cd03727     1 SAPGTLKALARYAVRRSLGVQYLPEAVKQLPLPRSVKEYLLLL 43
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 51-192 3.99e-10

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: 60.03  E-value: 3.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  51 HGTLKPLHCACMVSDADCVE-LLLEKGAEVNALDGYNRTALHYAA--EKDEACVeVLLEygANPNALD---------Gnr 118
Cdd:cd22192    15 RISESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAAlyDNLEAAV-VLME--AAPELVNepmtsdlyqG-- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305 119 DTPLHWAAFKNNAECVRALLESGASVN--------------ALDYNNDTPLSWAAMKGNLESVSILLDYGAEVRVINLKG 184
Cdd:cd22192    90 ETALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpkNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169


                  ....*...
gi 1720385305 185 QTPISRLV 192
Cdd:cd22192   170 NTVLHILV 177
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 247-285 1.39e-07

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: 46.77  E-value: 1.39e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1720385305 247 PGTLKTLARYAVRRSLGlQYLPDAVKGLPLPVSLKDYLL 285
Cdd:pfam07525   2 PRSLQHLCRLAIRRALG-KRRLGAIDKLPLPPLLKDYLL 39
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 67-178 1.74e-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: 52.01  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  67 DCVELLLEKGAEVNALDgynrTALHYAAEKDEACVEVLL--------EYGANPNALDGNRD------TPLHWAAFKNNAE 132
Cdd:TIGR00870  67 ELTELLLNLSCRGAVGD----TLLHAISLEYVDAVEAILlhllaafrKSGPLELANDQYTSeftpgiTALHLAAHRQNYE 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305 133 CVRALLESGASVNA--------------LDYNNDTPLSWAAMKGNLESVSILLDYGAEVR 178
Cdd:TIGR00870 143 IVKLLLERGASVPAracgdffvksqgvdSFYHGESPLNAAACLGSPSIVALLSEDPADIL 202
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 117-146 4.80e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 4.80e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1720385305  117 NRDTPLHWAAFKNNAECVRALLESGASVNA 146
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
 249-286 6.02e-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: 39.31  E-value: 6.02e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1720385305  249 TLKTLARYAVRRSLGlqylpdAVKGLPLPVSLKDYLLL 286
Cdd:smart00969   2 SLQHLCRLAIRRSLG------GIDKLPLPPRLKDYLLY 33
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
26-188 5.06e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.95  E-value: 5.06e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  26 IAAIRSFPHDNVEDLIRGGADVNCT-HGTLKPLHCACMVSDADCVELLLEKGAEVNALDGYNRTALHYAAEK-DEACVEV 103
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKdDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNgNLEIVKL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305 104 LLEYGANPNALDGNRDTPLHWAAFKNNAECVRALLESGASVNALDYNNDTPLSWAAMKGNLESVSILLDYGAEVRVINLK 183
Cdd:COG0666   139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218


                  ....*
gi 1720385305 184 GQTPI 188
Cdd:COG0666   219 GKTAL 223
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
26-195 9.16e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.48  E-value: 9.16e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  26 IAAIRSFPHDNVEDLIRGGADVN-CTHGTLKPLHCACMVSDADCVELLLEKGAEVNALDGYNRTALHYAAEK-DEACVEV 103
Cdd:COG0666    92 HAAARNGDLEIVKLLLEAGADVNaRDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANgNLEIVKL 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305 104 LLEYGANPNALDGNRDTPLHWAAFKNNAECVRALLESGASVNALDYNNDTPLSWAAMKGNLESVSILLDYGAEVRVINLK 183
Cdd:COG0666   172 LLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251

                         170
                  ....*....|..
gi 1720385305 184 GQTPISRLVALL 195
Cdd:COG0666   252 GLTALLLAAAAG 263
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-187 1.16e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 124.30  E-value: 1.16e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  22 LIRTIAAIRSFPHDNVEDLIRGGADVNCTHGTLKPLHCACMVSDADCVELLLEKGAEVNALDGYNRTALHYAAEK-DEAC 100
Cdd:COG0666    23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNgDLEI 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305 101 VEVLLEYGANPNALDGNRDTPLHWAAFKNNAECVRALLESGASVNALDYNNDTPLSWAAMKGNLESVSILLDYGAEVRVI 180
Cdd:COG0666   103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182


                  ....*..
gi 1720385305 181 NLKGQTP 187
Cdd:COG0666   183 DNDGETP 189
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
37-188 3.20e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 115.05  E-value: 3.20e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  37 VEDLIRGGADVNCTHGTLK-PLHCACMVSDADCVELLLEKGAEVNALDGYNRTALHYAAEK-DEACVEVLLEYGANPNAL 114
Cdd:COG0666   136 VKLLLEAGADVNAQDNDGNtPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENgHLEIVKLLLEAGADVNAK 215

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1720385305 115 DGNRDTPLHWAAFKNNAECVRALLESGASVNALDYNNDTPLSWAAMKGNLESVSILLDYGAEVRVINLKGQTPI 188
Cdd:COG0666   216 DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 26-215 8.73e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 100.91  E-value: 8.73e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  26 IAAIRSFPHDNVEDLIRGGADVNCTHGT-LKPLHCACMVS-DADCVELLLEKGAEVNALDGYNRTALHYAAEKDEACV-E 102
Cdd:PHA02876  313 LMAKNGYDTENIRTLIMLGADVNAADRLyITPLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIiN 392

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305 103 VLLEYGANPNALDGNRDTPLHWAAFKNNA-ECVRALLESGASVNALDYNNDTPLSWAAMKG-NLESVSILLDYGAEVRVI 180
Cdd:PHA02876  393 TLLDYGADIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAI 472

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1720385305 181 NLKGQTPIsrLVALLVRGL-------GTEKEDScfELLHRAV 215
Cdd:PHA02876  473 NIQNQYPL--LIALEYHGIvnillhyGAELRDS--RVLHKSL 510
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 37-181 3.05e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 95.50  E-value: 3.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  37 VEDLIRGGADVN-CTHGTLKPLHCACM--VSDADCVELLLEKGAEVNALDGYNRTALHYAAE------------------ 95
Cdd:PHA03100   89 VKLLLEYGANVNaPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnkidlkilkllidkgvd 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  96 ---KDEacVEVLLEYGANPNALDGNRDTPLHWAAFKNNAECVRALLESGASVNALDYNNDTPLSWAAMKGNLESVSILLD 172
Cdd:PHA03100  169 inaKNR--VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246


                  ....*....
gi 1720385305 173 YGAEVRVIN 181
Cdd:PHA03100  247 NGPSIKTII 255
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 17-188 2.84e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 92.72  E-value: 2.84e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  17 SLSERLIRTIAAIRSFPHDNVEDLIRGGADVNCTHGTL-KPLHCACMVSDADCVELL----------------------- 72
Cdd:PHA02874   31 SVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIpHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmikti 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  73 LEKGAEVNALDGYNRTALHYAAEK-DEACVEVLLEYGANPNALDGNRDTPLHWAAFKNNAECVRALLESGASVNALDYNN 151
Cdd:PHA02874  111 LDCGIDVNIKDAELKTFLHYAIKKgDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG 190

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1720385305 152 DTPLSWAAMKGNLESVSILLDYGAEVRVINLKGQTPI 188
Cdd:PHA02874  191 ESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
57-148 3.68e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.55  E-value: 3.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  57 LHCACMVSDADCVELLLEKGAEVNALDGYNRTALHYAAEKDEA-CVEVLLEYgANPNALDGNRdTPLHWAAFKNNAECVR 135
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLeIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1720385305 136 ALLESGASVNALD 148
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
34-188 7.86e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 89.63  E-value: 7.86e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  34 HDNVEDLIRGGADVNCTHGTLKPLHCACMVSDADCVELLLEKGAEVNALDGYNRTALHYAAEK--DEACVEVLLEYGANP 111
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALagDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720385305 112 NALDGNRDTPLHWAAFKNNAECVRALLESGASVNALDYNNDTPLSWAAMKGNLESVSILLDYGAEVRVINLKGQTPI 188
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
Ank_2 pfam12796
Ankyrin repeats (3 copies);
90-181 1.05e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 1.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  90 LHYAAE-KDEACVEVLLEYGANPNALDGNRDTPLHWAAFKNNAECVRALLESgASVNALDYNNdTPLSWAAMKGNLESVS 168
Cdd:pfam12796   1 LHLAAKnGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1720385305 169 ILLDYGAEVRVIN 181
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 7-222 2.23e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 90.32  E-value: 2.23e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305   7 YIMQSIQSKYSLSERLIrTIAAIRSFPHDNVED------LIRGGADVNCT--HGTLKPLHCACMVSDADCVELLLEKGAE 78
Cdd:PHA02878  115 EIFKIILTNRYKNIQTI-DLVYIDKKSKDDIIEaeitklLLSYGADINMKdrHKGNTALHYATENKDQRLTELLLSYGAN 193

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  79 VNALDGYNRTALHYAAEK-DEACVEVLLEYGANPNALDGNRDTPLHWA-AFKNNAECVRALLESGASVNALDY-NNDTPL 155
Cdd:PHA02878  194 VNIPDKTNNSPLHHAVKHyNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTAL 273

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720385305 156 SwAAMKGNlESVSILLDYGAEVRVINLKGQTPISRLVallvrglgteKEDSCFELLHRAVGQFELRK 222
Cdd:PHA02878  274 H-SSIKSE-RKLKLLLEYGADINSLNSYKLTPLSSAV----------KQYLCINIGRILISNICLLK 328
PHA03095 PHA03095
ankyrin-like protein; Provisional
 35-187 4.62e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 89.31  E-value: 4.62e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  35 DNVEDLIRGGADVNCTHGTLKPLHCACMVS----DADCVELLLEKGAEVNALDGYNRTALHYAAEKD--EACVEVLLEYG 108
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYssekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNAttLDVIKLLIKAG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305 109 ANPNALDGNRDTPLH--WAAFKNNAECVRALLESGASVNALDYNNDTPLSwAAMKG---NLESVSILLDYGAEVRVINLK 183
Cdd:PHA03095  108 ADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLA-VLLKSrnaNVELLRLLIDAGADVYAVDDR 186


                  ....
gi 1720385305 184 GQTP 187
Cdd:PHA03095  187 FRSL 190
SOCS_ASB8 cd03727
SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a ...
 245-287 6.78e-20

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: 80.65  E-value: 6.78e-20
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1720385305 245 SAPGTLKTLARYAVRRSLGLQYLPDAVKGLPLPVSLKDYLLLL 287
Cdd:cd03727     1 SAPGTLKALARYAVRRSLGVQYLPEAVKQLPLPRSVKEYLLLL 43
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 28-193 7.34e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 85.87  E-value: 7.34e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  28 AIRSFPHDNVEDLIRGGADVNC---THGTLKPLHCACMVS---DADCVELLLEKGAEVNALDGYNRTALHYAAEK---DE 98
Cdd:PHA03100   42 AKEARNIDVVKILLDNGADINSstkNNSTPLHYLSNIKYNltdVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksnSY 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  99 ACVEVLLEYGANPNALDGNRDTPLHWAAFKN-----------------NAEC-VRALLESGASVNALDYNNDTPLSWAAM 160
Cdd:PHA03100  122 SIVEYLLDNGANVNIKNSDGENLLHLYLESNkidlkilkllidkgvdiNAKNrVNYLLSYGVPINIKDVYGFTPLHYAVY 201

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1720385305 161 KGNLESVSILLDYGAEVRVINLKGQTPISRLVA 193
Cdd:PHA03100  202 NNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234
PHA03095 PHA03095
ankyrin-like protein; Provisional
 34-188 1.27e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.46  E-value: 1.27e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  34 HDNVED----LIRGGADVNCTHGTLK-PLH-CACMVS-DADCVELLLEKGAEVNALDGYNRTALHYAAEKDEACVEV--- 103
Cdd:PHA03095   93 NATTLDviklLIKAGADVNAKDKVGRtPLHvYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELlrl 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305 104 LLEYGANPNALDGNRDTPLHWAA--FKNNAECVRALLESGASVNALDYNNDTPLSWAAMKGNLES--VSILLDYGAEVRV 179
Cdd:PHA03095  173 LIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRslVLPLLIAGISINA 252


                  ....*....
gi 1720385305 180 INLKGQTPI 188
Cdd:PHA03095  253 RNRYGQTPL 261
PHA03095 PHA03095
ankyrin-like protein; Provisional
 37-193 1.96e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 84.69  E-value: 1.96e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  37 VEDLIRGGADVNCT--HGtLKPLHCAcMVS---DADCVELLLEKGAEVNALDGYNRTALHYAAE---KDEACVEVLLEYG 108
Cdd:PHA03095  135 IRLLLRKGADVNALdlYG-MTPLAVL-LKSrnaNVELLRLLIDAGADVYAVDDRFRSLLHHHLQsfkPRARIVRELIRAG 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305 109 ANPNALDGNRDTPLHWAAFKNNAEC--VRALLESGASVNALDYNNDTPLSWAAMKGNLESVSILLDYGAEVRVINLKGQT 186
Cdd:PHA03095  213 CDPAATDMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNT 292


                  ....*..
gi 1720385305 187 PISRLVA 193
Cdd:PHA03095  293 PLSLMVR 299
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 56-198 3.34e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 84.34  E-value: 3.34e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  56 PLHCACMV-SDADCVELLLEKGAEVNALDGYNRTALHYAAEK--DEACVEVLLEYGANPNALDGNRDTPLHWAA-FKNNA 131
Cdd:PHA02876  276 PLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNgyDTENIRTLIMLGADVNAADRLYITPLHQAStLDRNK 355

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720385305 132 ECVRALLESGASVNALDYNNDTPLSWAAMKGNLESVSILLDYGAEVRVINLK----------GQTPISRLVALLVRG 198
Cdd:PHA02876  356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKigtalhfalcGTNPYMSVKTLIDRG 432
PHA03095 PHA03095
ankyrin-like protein; Provisional
 65-212 2.65e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.53  E-value: 2.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  65 DADCVELLLEKGAEVNALDGYNRTALH----YAAEKDEACVEVLLEYGANPNALDGNRDTPLH-WAAFKNNAECVRALLE 139
Cdd:PHA03095   26 TVEEVRRLLAAGADVNFRGEYGKTPLHlylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLIK 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305 140 SGASVNALDYNNDTPLSwAAMKG---NLESVSILLDYGAEVRVINLKGQTPIS----------RLVALLVRGLG--TEKE 204
Cdd:PHA03095  106 AGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAvllksrnanvELLRLLIDAGAdvYAVD 184


                  ....*...
gi 1720385305 205 DSCFELLH 212
Cdd:PHA03095  185 DRFRSLLH 192
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 28-243 4.19e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 77.70  E-value: 4.19e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  28 AIRSFPHDNVEDLIRGGADVNCT--HGTLkPLHCACMVSDADCVELLLEKGAEVNALDGYNRTALHYAAE-KDEACVEVL 104
Cdd:PHA02874  131 AIKKGDLESIKMLFEYGADVNIEddNGCY-PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEyGDYACIKLL 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305 105 LEYGANPNALDGNRDTPLHWAAFKNNAecVRALLESGASVNALDYNNDTPLSWAAM-KGNLESVSILLDYGAEVRVINLK 183
Cdd:PHA02874  210 IDHGNHIMNKCKNGFTPLHNAIIHNRS--AIELLINNASINDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNK 287

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1720385305 184 GQTPIsrlvallvrglgtekeDSCFELLHRAVGQFELRKNGIMPREVTK--DQQLCEKLTVL 243
Cdd:PHA02874  288 GENPI----------------DTAFKYINKDPVIKDIIANAVLIKEADKlkDSDFLEHIEIK 333
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 70-214 6.00e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.80  E-value: 6.00e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  70 ELLLEKGAEVNALDGYNRTALHYAAEKDEA-CVEVLLEYGANPNALDGNRDTPLHWAAFKNNAECVRA------------ 136
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAkMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAiidnrsninknd 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305 137 -----------------LLESGASVNALDYNNDTPLSWAAMKGNLES-VSILLDYGAEVRVINLKGQTPI---------- 188
Cdd:PHA02876  242 lsllkairnedletsllLYDAGFSVNSIDDCKNTPLHHASQAPSLSRlVPKLLERGADVNAKNIKGETPLylmakngydt 321

                         170       180
                  ....*....|....*....|....*..
gi 1720385305 189 SRLVALLVRGLGTEKEDSCFEL-LHRA 214
Cdd:PHA02876  322 ENIRTLIMLGADVNAADRLYITpLHQA 348
Ank_2 pfam12796
Ankyrin repeats (3 copies);
28-115 3.38e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.98  E-value: 3.38e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  28 AIRSFPHDNVEDLIRGGADVNCTHGT-LKPLHCACMVSDADCVELLLEKgAEVNaLDGYNRTALHYAAEKD-EACVEVLL 105
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNgRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGhLEIVKLLL 81

                          90
                  ....*....|
gi 1720385305 106 EYGANPNALD 115
Cdd:pfam12796  82 EKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 35-188 4.92e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.75  E-value: 4.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  35 DNVEDLIRGGADVNCT-HGTLKPLHCACMVSDADCVELLLE--------------------------KGAEVNALDGYNR 87
Cdd:PHA02878   51 DVVKSLLTRGHNVNQPdHRDLTPLHIICKEPNKLGMKEMIRsinkcsvfytlvaikdafnnrnveifKIILTNRYKNIQT 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  88 TALHYAAEKDE------ACVEVLLEYGANPNALDGNRD-TPLHWAAFKNNAECVRALLESGASVNALDYNNDTPLSWAAM 160
Cdd:PHA02878  131 IDLVYIDKKSKddiieaEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVK 210

                         170       180
                  ....*....|....*....|....*...
gi 1720385305 161 KGNLESVSILLDYGAEVRVINLKGQTPI 188
Cdd:PHA02878  211 HYNKPIVHILLENGASTDARDKCGNTPL 238
Ank_2 pfam12796
Ankyrin repeats (3 copies);
122-188 7.51e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.51  E-value: 7.51e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1720385305 122 LHWAAFKNNAECVRALLESGASVNALDYNNDTPLSWAAMKGNLESVSILLDYgAEVRVINlKGQTPI 188
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTAL 65
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 25-188 8.63e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.98  E-value: 8.63e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  25 TIAAIRSFPHDNVEDLIRGGADVNCTHGTLKP-LHCACMVSDADCVELLLEKGAEVNALDGYNRTALHYAAEKDE-ACVE 102
Cdd:PHA02874   95 SILPIPCIEKDMIKTILDCGIDVNIKDAELKTfLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFfDIIK 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305 103 VLLEYGANPNALDGNRDTPLHWAAFKNNAECVRALLESGASVNALDYNNDTPLSWAAMKGnlESVSILLDYGAEVRVINL 182
Cdd:PHA02874  175 LLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN--RSAIELLINNASINDQDI 252


                  ....*.
gi 1720385305 183 KGQTPI 188
Cdd:PHA02874  253 DGSTPL 258
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 85-188 1.06e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.69  E-value: 1.06e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  85 YNRTALHYAAEKD--EACVEVLLEYGANPNALDGNRDTPLHWAA-----FKNNAECVRALLESGASVNALDYNNDTPLSW 157
Cdd:PHA03100   33 KKPVLPLYLAKEArnIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNGITPLLY 112

                          90       100       110
                  ....*....|....*....|....*....|...
gi 1720385305 158 AAMK--GNLESVSILLDYGAEVRVINLKGQTPI 188
Cdd:PHA03100  113 AISKksNSYSIVEYLLDNGANVNIKNSDGENLL 145
Ank_4 pfam13637
Ankyrin repeats (many copies);
118-171 1.42e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 1.42e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720385305 118 RDTPLHWAAFKNNAECVRALLESGASVNALDYNNDTPLSWAAMKGNLESVSILL 171
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 91-176 1.49e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.45  E-value: 1.49e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  91 HYAAEKDEACVEVLLEYGANPNALDGNRDTPLHWAAFKNNAECVRALLESGASVNALDYNNDTPLSWAAMKGNLESVSIL 170
Cdd:PTZ00322   88 QLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167


                  ....*.
gi 1720385305 171 LDYGAE 176
Cdd:PTZ00322  168 SRHSQC 173
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 52-213 2.29e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.78  E-value: 2.29e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  52 GTLKPLHCACMVSDADCVELLLEKGAEVNAL---DGynRTALHYAAE-KDEACVEVLLEYGANPNALDGNRDTPLHWAAF 127
Cdd:PHA02875   67 DIESELHDAVEEGDVKAVEELLDLGKFADDVfykDG--MTPLHLATIlKKLDIMKLLIARGADPDIPNTDKFSPLHLAVM 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305 128 KNNAECVRALLESGASVNALDYNNDTPLSWAAMKGNLESVSILLDYGAEvrvINLKGQTPIsrlVALLVRGLGTEKEDSC 207
Cdd:PHA02875  145 MGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN---IDYFGKNGC---VAALCYAIENNKIDIV 218


                  ....*.
gi 1720385305 208 FELLHR 213
Cdd:PHA02875  219 RLFIKR 224
Ank_4 pfam13637
Ankyrin repeats (many copies);
86-138 3.80e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 3.80e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1720385305  86 NRTALHYAAEK-DEACVEVLLEYGANPNALDGNRDTPLHWAAFKNNAECVRALL 138
Cdd:pfam13637   1 ELTALHAAAASgHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 51-192 3.99e-10

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: 60.03  E-value: 3.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  51 HGTLKPLHCACMVSDADCVE-LLLEKGAEVNALDGYNRTALHYAA--EKDEACVeVLLEygANPNALD---------Gnr 118
Cdd:cd22192    15 RISESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAAlyDNLEAAV-VLME--AAPELVNepmtsdlyqG-- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305 119 DTPLHWAAFKNNAECVRALLESGASVN--------------ALDYNNDTPLSWAAMKGNLESVSILLDYGAEVRVINLKG 184
Cdd:cd22192    90 ETALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpkNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169


                  ....*...
gi 1720385305 185 QTPISRLV 192
Cdd:cd22192   170 NTVLHILV 177
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
 245-286 2.68e-09

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: 51.73  E-value: 2.68e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1720385305 245 SAPGTLKTLARYAVRRSLGLQyLPDAVKGLPLPVSLKDYLLL 286
Cdd:cd03716     1 STPRSLQHLCRLAIRRCLGRR-RLELIKKLPLPPRLKDYLLY 41
PHA02946 PHA02946
ankyin-like protein; Provisional
 97-177 3.91e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 56.99  E-value: 3.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  97 DEACVEVLLEYGANPNALDGNRDTPLHWAAFKNNAECVRALLESGASVNALDYNNDTPLSWAAMKGN--LESVSILLDYG 174
Cdd:PHA02946   51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYG 130


                  ...
gi 1720385305 175 AEV 177
Cdd:PHA02946  131 AKI 133
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
 247-286 1.68e-08

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: 49.39  E-value: 1.68e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1720385305 247 PGTLKTLARYAVRRSLGLQyLPDAVKGLPLPVSLKDYLLL 286
Cdd:cd03587     2 PRSLQHLCRLAIRRCLGKR-RLDLIDKLPLPPRLKDYLLY 40
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 36-182 1.82e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.26  E-value: 1.82e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  36 NVEDLI--RGGADVNCTHGTlkPLHCACMVSDADCVELLLEKGAEVNALDGYNRTALHYAAEKD-EACVEVLLEYGANPN 112
Cdd:PLN03192  508 NVGDLLgdNGGEHDDPNMAS--NLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGyEDCVLVLLKHACNVH 585

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305 113 ALDGNRDTPLhW--------------------------------AAFKNNAECVRALLESGASVNALDYNNDTPLSWAAM 160
Cdd:PLN03192  586 IRDANGNTAL-WnaisakhhkifrilyhfasisdphaagdllctAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMA 664

                         170       180
                  ....*....|....*....|..
gi 1720385305 161 KGNLESVSILLDYGAEVRVINL 182
Cdd:PLN03192  665 EDHVDMVRLLIMNGADVDKANT 686
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 65-166 2.66e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.52  E-value: 2.66e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  65 DADCVELLLEKGAEVNALDGYNRTALHYAAEKDE-ACVEVLLEYGANPNALDGNRDTPLHWAAFKNNAECVRALLESGAS 143
Cdd:PTZ00322   94 DAVGARILLTGGADPNCRDYDGRTPLHIACANGHvQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173

                          90       100
                  ....*....|....*....|...
gi 1720385305 144 VNALDYNNdTPLSWAAMKGNLES 166
Cdd:PTZ00322  174 HFELGANA-KPDSFTGKPPSLED 195
PHA03095 PHA03095
ankyrin-like protein; Provisional
 37-148 4.13e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.88  E-value: 4.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  37 VEDLIRGGADVNCTH-GTLKPLHCACMVSDADC--VELLLEKGAEVNALDGYNRTALHYAA--EKDEACVEvLLEYGANP 111
Cdd:PHA03095  205 VRELIRAGCDPAATDmLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAvfNNPRACRR-LIALGADI 283

                          90       100       110
                  ....*....|....*....|....*....|....*..
gi 1720385305 112 NALDGNRDTPLHWAAFKNNAECVRALLESGASVNALD 148
Cdd:PHA03095  284 NAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA 320
Ank_4 pfam13637
Ankyrin repeats (many copies);
56-105 4.41e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 4.41e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1720385305  56 PLHCACMVSDADCVELLLEKGAEVNALDGYNRTALHYAAEK-DEACVEVLL 105
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNgNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 134-188 4.79e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 4.79e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720385305 134 VRALLESGASVNALDYNNDTPLSWAAMKGNLESVSILLDYGAEVRVINLKGQTPI 188
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL 152
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 247-285 1.39e-07

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: 46.77  E-value: 1.39e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1720385305 247 PGTLKTLARYAVRRSLGlQYLPDAVKGLPLPVSLKDYLL 285
Cdd:pfam07525   2 PRSLQHLCRLAIRRALG-KRRLGAIDKLPLPPLLKDYLL 39
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 97-186 1.70e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.37  E-value: 1.70e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  97 DEACVEVLLEyganpnALDGNRdtpLHWAAFKNNAECVRA---------------LLESGASVNALDYNNDTPLSWAAMK 161
Cdd:PHA02876  118 DEACIHILKE------AISGND---IHYDKINESIEYMKLikeriqqdelliaemLLEGGADVNAKDIYCITPIHYAAER 188

                          90       100
                  ....*....|....*....|....*
gi 1720385305 162 GNLESVSILLDYGAEVRVINLKGQT 186
Cdd:PHA02876  189 GNAKMVNLLLSYGADVNIIALDDLS 213
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 67-178 1.74e-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: 52.01  E-value: 1.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  67 DCVELLLEKGAEVNALDgynrTALHYAAEKDEACVEVLL--------EYGANPNALDGNRD------TPLHWAAFKNNAE 132
Cdd:TIGR00870  67 ELTELLLNLSCRGAVGD----TLLHAISLEYVDAVEAILlhllaafrKSGPLELANDQYTSeftpgiTALHLAAHRQNYE 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305 133 CVRALLESGASVNA--------------LDYNNDTPLSWAAMKGNLESVSILLDYGAEVR 178
Cdd:TIGR00870 143 IVKLLLERGASVPAracgdffvksqgvdSFYHGESPLNAAACLGSPSIVALLSEDPADIL 202
Ank_5 pfam13857
Ankyrin repeats (many copies);
104-155 1.96e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 1.96e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720385305 104 LLEYG-ANPNALDGNRDTPLHWAAFKNNAECVRALLESGASVNALDYNNDTPL 155
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 40-122 4.60e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 50.67  E-value: 4.60e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  40 LIRGGADVNCT--HGTlKPLHCACMVSDADCVELLLEKGAEVNALDGYNRTALHYAAEKDEACVEVLL--------EYGA 109
Cdd:PTZ00322  101 LLTGGADPNCRdyDGR-TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLsrhsqchfELGA 179

                          90
                  ....*....|....*....
gi 1720385305 110 N--PNALDGN----RDTPL 122
Cdd:PTZ00322  180 NakPDSFTGKppslEDSPI 198
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 101-188 7.83e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 49.60  E-value: 7.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305 101 VEVLLEYGANPNA----LDGNRDTPLHWAAFKNNAECVRALLESGASVNAL-DYNNDTPLSWAAMKGNLESVSILLDYGA 175
Cdd:PHA02884   49 IDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYaEEAKITPLYISVLHGCLKCLEILLSYGA 128

                          90
                  ....*....|...
gi 1720385305 176 EVRVINLKGQTPI 188
Cdd:PHA02884  129 DINIQTNDMVTPI 141
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 95-172 8.49e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.06  E-value: 8.49e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720385305  95 EKDEACV-EVLLEYGANPNALDGNRDTPLHWAAFKNNAECVRALLESGASVNALDYNNDTPLSWAAMKGNLESVSILLD 172
Cdd:PHA02876  154 QQDELLIaEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIID 232
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 69-188 1.49e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 47.89  E-value: 1.49e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  69 VELLLEKGAEVN-ALDGYNRTALH----YAAEKDEACVEVLLEYGANPNALDGNRDTPLH--WAAFKNNAECVRALLESG 141
Cdd:PHA02859   69 LKFLIENGADVNfKTRDNNLSALHhylsFNKNVEPEILKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKLLIDSG 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1720385305 142 ASVNALDYNNDTPL-SWAAMKGNLESVSILLDYGAEVRVINLKGQTPI 188
Cdd:PHA02859  149 VSFLNKDFDNNNILySYILFHSDKKIFDFLTSLGIDINETNKSGYNCY 196
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 87-192 1.95e-06

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: 48.72  E-value: 1.95e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  87 RTALHYAAEKDE----ACVEVLLEYG---------ANPNALDG--NRDTPLHWAAFKNNAECVRALLESGASVNA----- 146
Cdd:cd21882    27 KTCLHKAALNLNdgvnEAIMLLLEAApdsgnpkelVNAPCTDEfyQGQTALHIAIENRNLNLVRLLVENGADVSAratgr 106

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1720385305 147 --------LDYNNDTPLSWAAMKGNLESVSILLDYGAEVRVINLK---GQTPISRLV 192
Cdd:cd21882   107 ffrkspgnLFYFGELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHALV 163
PHA02946 PHA02946
ankyin-like protein; Provisional
 8-195 3.42e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 48.13  E-value: 3.42e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305   8 IMQSIQSkySLSERLIRTIAAIRSFPHDNVEDLIRGGADVNCTHGTLK-PLHCACMVSDADCVELLLEKGAEVNALDGYN 86
Cdd:PHA02946   28 MLQAIEP--SGNYHILHAYCGIKGLDERFVEELLHRGYSPNETDDDGNyPLHIASKINNNRIVAMLLTHGADPNACDKQH 105

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  87 RTALHYAAEKDEACVE---VLLEYGAN-PNALDGNRDTPL----------------------------------HWAAFK 128
Cdd:PHA02946  106 KTPLYYLSGTDDEVIErinLLVQYGAKiNNSVDEEGCGPLlactdpservfkkimsigfearivdkfgknhihrHLMSDN 185

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1720385305 129 NNAECVRALLESGASVNALDYNNDTPLSWAAMK--GNLESVSILLDyGAEVRVINLKGQTPISRLVALL 195
Cdd:PHA02946  186 PKASTISWMMKLGISPSKPDHDGNTPLHIVCSKtvKNVDIINLLLP-STDVNKQNKFGDSPLTLLIKTL 253
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 117-146 4.80e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.57  E-value: 4.80e-06
                           10        20        30
                   ....*....|....*....|....*....|
gi 1720385305  117 NRDTPLHWAAFKNNAECVRALLESGASVNA 146
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02741 PHA02741
hypothetical protein; Provisional
 67-178 4.84e-06

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 45.80  E-value: 4.84e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  67 DCVELLLekgaevNALDGYNRTALHYAAEKDEA-----CVEVLLEYGANPNALDG-NRDTPLHWAAFKNNAECVRALL-E 139
Cdd:PHA02741   47 DCHAAAL------NATDDAGQMCIHIAAEKHEAqlaaeIIDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCcQ 120

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1720385305 140 SGASVNALDYNNDTPLSWAAMKGNLESVSILLDYGAEVR 178
Cdd:PHA02741  121 PGIDLHFCNADNKSPFELAIDNEDVAMMQILREIVATSR 159
PHA02798 PHA02798
ankyrin-like protein; Provisional
 67-181 5.45e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.52  E-value: 5.45e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  67 DCVELLLEKGAEVNALDGYNRTAL--------HYAAEKDeaCVEVLLEYGANPNALDGNRDTPLHWA---AFKNNAECVR 135
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLctilsnikDYKHMLD--IVKILIENGADINKKNSDGETPLYCLlsnGYINNLEILL 129

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1720385305 136 ALLESGASVNALDYNNDTPLSWAAMKGN---LESVSILLDYGAEVRVIN 181
Cdd:PHA02798  130 FMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHN 178
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 96-188 7.63e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 46.91  E-value: 7.63e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  96 KDEACVEVLLEYGANPNALDGNRDTPLHWAAFKNNAECVRALLESGASVNALDYNN-DTPLSWAAMKGNLESVSILLDYG 174
Cdd:PHA02875   46 RDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARG 125

                          90
                  ....*....|....
gi 1720385305 175 AEVRVINLKGQTPI 188
Cdd:PHA02875  126 ADPDIPNTDKFSPL 139
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 117-148 8.03e-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: 8.03e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1720385305 117 NRDTPLHWAAFK-NNAECVRALLESGASVNALD 148
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
71-125 8.15e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.33  E-value: 8.15e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720385305  71 LLLEKGAEVNALDGYNRTALHYAAEKDEA-CVEVLLEYGANPNALDGNRDTPLHWA 125
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALeIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02798 PHA02798
ankyrin-like protein; Provisional
 101-186 1.40e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.98  E-value: 1.40e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305 101 VEVLLEYGANPNALDGNRDTPL-----HWAAFKNNAECVRALLESGASVNALDYNNDTPLSWAAMKG---NLESVSILLD 172
Cdd:PHA02798   54 VKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFMIE 133

                          90
                  ....*....|....
gi 1720385305 173 YGAEVRVINLKGQT 186
Cdd:PHA02798  134 NGADTTLLDKDGFT 147
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 63-160 1.63e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.01  E-value: 1.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  63 VSDADCVELLLEKGAE-VNALDGYNrtALHYAAEKDEACVEVLLEYGANPNALDGNRDTPLHWAAFKNNAECVRALLESG 141
Cdd:PLN03192  504 LHDLNVGDLLGDNGGEhDDPNMASN--LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHA 581

                          90
                  ....*....|....*....
gi 1720385305 142 ASVNALDYNNDTPLsWAAM 160
Cdd:PLN03192  582 CNVHIRDANGNTAL-WNAI 599
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 85-115 4.11e-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: 4.11e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1720385305  85 YNRTALHYAAEK--DEACVEVLLEYGANPNALD 115
Cdd:pfam00023   1 DGNTPLHLAAGRrgNLEIVKLLLSKGADVNARD 33
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
 249-286 6.02e-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: 39.31  E-value: 6.02e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1720385305  249 TLKTLARYAVRRSLGlqylpdAVKGLPLPVSLKDYLLL 286
Cdd:smart00969   2 SLQHLCRLAIRRSLG------GIDKLPLPPRLKDYLLY 33
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 57-179 7.98e-05

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 42.17  E-value: 7.98e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  57 LHCACmvSDADCVELLLEKGAEVNA----LDGYNRTA---LHYAAEKDEA----CVEVLLEYGANPNALDG-NRDTPLHW 124
Cdd:PHA02736   21 LHYLC--RNGGVTDLLAFKNAISDEnrylVLEYNRHGkqcVHIVSNPDKAdpqeKLKLLMEWGADINGKERvFGNTPLHI 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1720385305 125 AAFKNNAECVRALL-ESGASVNALDYNNDTPLSWAAMKGNLESVSILLDYGAEVRV 179
Cdd:PHA02736   99 AVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCKV 154
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 56-165 9.70e-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: 43.46  E-value: 9.70e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  56 PLHCACMVSDADCVELLLEKGAEVN--------------ALDGYNRTALHYAA-EKDEACVEVLLEYGANPNALDGNRDT 120
Cdd:cd22192    92 ALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpkNLIYYGEHPLSFAAcVGNEEIVRLLIEHGADIRAQDSLGNT 171

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1720385305 121 PLHWAAFKNNAECVRALLESGASVNALDY--------NND--TPLSWAAMKGNLE 165
Cdd:cd22192   172 VLHILVLQPNKTFACQMYDLILSYDKEDDlqpldlvpNNQglTPFKLAAKEGNIV 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
26-83 1.53e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 39.71  E-value: 1.53e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1720385305  26 IAAIRSFPHDNVEDLIRGgADVNCTHGTLKPLHCACMVSDADCVELLLEKGAEVNALD 83
Cdd:pfam12796  35 HLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
 247-288 1.62e-04

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: 38.66  E-value: 1.62e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1720385305 247 PGTLKTLARYAVRRSLGLQYL--PDAVKGLPLPVSLKDYLLLLE 288
Cdd:cd03731     3 PRPLKHLCRLKIRKLMGLQKLqqPSSMKKLPLPPALKRYILYKE 46
SOCS_SSB1_4 cd03718
SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box ...
 246-285 2.46e-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: 2.46e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1720385305 246 APGTLKTLARYAVRRSLGLQYLPDaVKGLPLPVSLKDYLL 285
Cdd:cd03718     2 EPLPLMDLCRRRVRVALGRDRLEE-IEQLPLPPSLKNYLL 40
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 79-155 3.74e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.96  E-value: 3.74e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  79 VNALDGYNRTALHYAAEKDEACVEV---LLEYGANPN-ALDGNRDTPLHWAAFKN---NAECVRALLESGASVNALDYNN 151
Cdd:PHA02859   44 VNDCNDLYETPIFSCLEKDKVNVEIlkfLIENGADVNfKTRDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDG 123


                  ....
gi 1720385305 152 DTPL 155
Cdd:PHA02859  124 KNLL 127
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 56-83 3.83e-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: 3.83e-04
                          10        20
                  ....*....|....*....|....*....
gi 1720385305  56 PLHCAC-MVSDADCVELLLEKGAEVNALD 83
Cdd:pfam00023   5 PLHLAAgRRGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 56-81 4.32e-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: 36.80  E-value: 4.32e-04
                           10        20
                   ....*....|....*....|....*.
gi 1720385305   56 PLHCACMVSDADCVELLLEKGAEVNA 81
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
42-93 4.40e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 4.40e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720385305  42 RGGADVNCTHG-TLKPLHCACMVSDADCVELLLEKGAEVNALDGYNRTALHYA 93
Cdd:pfam13857   4 HGPIDLNRLDGeGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 85-113 5.31e-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: 36.80  E-value: 5.31e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1720385305   85 YNRTALHYAAEK-DEACVEVLLEYGANPNA 113
Cdd:smart00248   1 DGRTPLHLAAENgNLEVVKLLLDKGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 37-150 6.52e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.19  E-value: 6.52e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  37 VEDLIRGGADVNCT--HGTLKPLHCACMVS---DADCVELLLEKGAEVNALDGYNRTALHYAAEKDEACVEV---LLEYG 108
Cdd:PHA02859   69 LKFLIENGADVNFKtrDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRINViklLIDSG 148

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720385305 109 ANPNALDGNRDTPLH-WAAFKNNAECVRALLESGasvnaLDYN 150
Cdd:PHA02859  149 VSFLNKDFDNNNILYsYILFHSDKKIFDFLTSLG-----IDIN 186
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 67-160 7.33e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.35  E-value: 7.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  67 DCVELLLEKGAEVNA-----LDGYNrTALHYAAEKD-EACVEVLLEYGANPNALDGN-RDTPLHWAAFKNNAECVRALLE 139
Cdd:PHA02884   47 DIIDAILKLGADPEApfplsENSKT-NPLIYAIDCDnDDAAKLLIRYGADVNRYAEEaKITPLYISVLHGCLKCLEILLS 125

                          90       100
                  ....*....|....*....|.
gi 1720385305 140 SGASVNALDYNNDTPLSWAAM 160
Cdd:PHA02884  126 YGADINIQTNDMVTPIELALM 146
PHA02791 PHA02791
ankyrin-like protein; Provisional
 83-171 8.00e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 40.41  E-value: 8.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  83 DGYNRTALHYA-AEKDEACVEVLLEYGANPNALDGnrDTPLHWAAFKNNAECVRALLESGASVNALDYNNDTPLSWAAMK 161
Cdd:PHA02791   27 DVHGHSALYYAiADNNVRLVCTLLNAGALKNLLEN--EFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDS 104

                          90
                  ....*....|
gi 1720385305 162 GNLESVSILL 171
Cdd:PHA02791  105 GNMQTVKLFV 114
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
 247-286 8.66e-04

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: 36.65  E-value: 8.66e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1720385305 247 PGTLKTLARYAVRRSLGlQYLPDAVKGLPLPVSLKDYLLL 286
Cdd:cd03723     3 PRSLQHLCRCAIRKLLG-SRCHKLVPQLSLPTSLKNYLLL 41
SOCS_ASB6 cd03725
SOCS (suppressors of cytokine signaling) box of ASB6-like proteins. ASB family members have a ...
 245-285 9.62e-04

SOCS (suppressors of cytokine signaling) box of ASB6-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ASB6 interacts with the adaptor protein APS and recruits elongin B/C to the insulin receptor signaling complex. 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: 239695  Cd Length: 44  Bit Score: 36.27  E-value: 9.62e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1720385305 245 SAPGTLKTLARYAVRRSLGLQYLPDAVKGLPLPVSLKDYLL 285
Cdd:cd03725     1 SYPPPLKHLCRVFIRLCLRPWPVDVKVKALPLPDRLKWYLL 41
Ank_4 pfam13637
Ankyrin repeats (many copies);
151-188 1.00e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 1.00e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1720385305 151 NDTPLSWAAMKGNLESVSILLDYGAEVRVINLKGQTPI 188
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETAL 38
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
 249-285 1.01e-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: 36.04  E-value: 1.01e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1720385305 249 TLKTLARYAVRRSLGLqylpDAVKGLPLPVSLKDYLL 285
Cdd:cd03717     5 SLQHLCRFVIRQCTRR----DLIDQLPLPRRLKDYLK 37
SOCS_SSB4 cd03743
SOCS (suppressors of cytokine signaling) box of SSB4 (SPRY domain-containing SOCS box ...
 247-284 1.21e-03

SOCS (suppressors of cytokine signaling) box of SSB4 (SPRY domain-containing SOCS box proteins)-like proteins. SSB proteins contain a central SPRY domain and a C-terminal SOCS. SSB4 has been shown to bind to MET, the receptor protein-tyrosine kinase for hepatocyte growth factor (HGF). SSB4, like SSB2 and SSB1, 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: 239712  Cd Length: 42  Bit Score: 36.09  E-value: 1.21e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1720385305 247 PGTLKTLARYAVRRSLGLQYLPDaVKGLPLPVSLKDYL 284
Cdd:cd03743     3 PLPLMDLCRRSARQALGRHRLHH-IQSLPLPQTLKNYL 39
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 120-146 1.68e-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: 35.31  E-value: 1.68e-03
                          10        20
                  ....*....|....*....|....*..
gi 1720385305 120 TPLHWAAFKNNAECVRALLESGASVNA 146
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 150-177 1.71e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 1.71e-03
                           10        20
                   ....*....|....*....|....*...
gi 1720385305  150 NNDTPLSWAAMKGNLESVSILLDYGAEV 177
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
SOCS_SSB1 cd03744
SOCS (suppressors of cytokine signaling) box of SSB1 (SPRY domain-containing SOCS box proteins) ...
 247-285 3.16e-03

SOCS (suppressors of cytokine signaling) box of SSB1 (SPRY domain-containing SOCS box proteins)-like proteins. SSB proteins contain a central SPRY domain and a C-terminal SOCS. SSB1 has been shown to bind to MET, the receptor protein-tyrosine kinase for hepatocyte growth factor (HGF), both the absence and the presence of HGF and enhances the HGF-MET-induced mitogen-activated protein kinases Erk-transcription factor Elk-1-serum response elements (SRE) pathway. SSB1, like SSB2 and SSB4, 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: 239713  Cd Length: 42  Bit Score: 34.96  E-value: 3.16e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1720385305 247 PGTLKTLARYAVRRSLGLQYLPDaVKGLPLPVSLKDYLL 285
Cdd:cd03744     3 PLPLMDLCRRSVRLALGRERLSE-IHTLPLPASLKNYLL 40
Ank_5 pfam13857
Ankyrin repeats (many copies);
137-188 5.59e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 34.63  E-value: 5.59e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1720385305 137 LLESG-ASVNALDYNNDTPLSWAAMKGNLESVSILLDYGAEVRVINLKGQTPI 188
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 12-80 6.23e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 37.66  E-value: 6.23e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1720385305  12 IQSKYSLSERLIRTIAAIRSFPHDNVEDLIRGGADVNCTHGTLK--PLHCACMVSDADCVELLLEKGAEVN 80
Cdd:PHA02884   61 APFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKitPLYISVLHGCLKCLEILLSYGADIN 131
SOCS_ASB1 cd03720
SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a ...
 245-285 8.53e-03

SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. 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: 239690  Cd Length: 42  Bit Score: 33.55  E-value: 8.53e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1720385305 245 SAPGTLKTLARYAVRRSLGLQYLpDAVKGLPLPVSLKDYLL 285
Cdd:cd03720     1 GNPRSLLSLCRIAVRRALGKQRL-SLICSLPLPDPIKKFLL 40
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 37-132 8.92e-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: 37.30  E-value: 8.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305  37 VEDLIRGGADVN----------------CTHGTlKPLHCACMVSDADCVELLLEKGAEVNALDGYNRTALHY---AAEKD 97
Cdd:cd22192   105 VRELIARGADVVspratgtffrpgpknlIYYGE-HPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIlvlQPNKT 183

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1720385305  98 EAC--VEVLLEYGA--NPNALD--GNRD--TPLHWAAFKNNAE 132
Cdd:cd22192   184 FACqmYDLILSYDKedDLQPLDlvPNNQglTPFKLAAKEGNIV 226
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 104-188 9.47e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 37.28  E-value: 9.47e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1720385305 104 LLEYGANPNALDGNRDTPLHWAAFKNNAECVRALLESGASVNALDYNNDTPLSWAAMKGNLESVSILLDYGAEVR-VINL 182
Cdd:PHA02875   21 LLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYK 100


                  ....*.
gi 1720385305 183 KGQTPI 188
Cdd:PHA02875  101 DGMTPL 106
 
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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