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Conserved domains on  [gi|1621995554|ref|XP_028565552|]
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ankyrin repeat and SOCS box protein 8 [Podarcis muralis]

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];
22-184 9.44e-43

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.79  E-value: 9.44e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  22 IAAIRSFPHDNVEDLIRRGADVNCM-HGTLKPLHCACMVADADCIELLLEKGAEVNALDGYNRTALHYAAEKDET-CVEI 99
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKdDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLeIVKL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554 100 LLEYGANPNALDGNKDTPLHWAAFKNNAECVRTLLESGAFVNALDYNNDTPLSWAAMKGNLESVSILLEYGAEVRVVNMK 179
Cdd:COG0666   139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218


                  ....*
gi 1621995554 180 GQTPI 184
Cdd:COG0666   219 GKTAL 223
SOCS_ASB8 cd03727
SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a ...
 241-283 3.56e-21

SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. Human ASB8 is highly transcribed in skeletal muscle and in lung carcinoma cell lines. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


:

Pssm-ID: 239697  Cd Length: 43  Bit Score: 84.12  E-value: 3.56e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1621995554 241 SAPGTLKTLSRYAVRRSLGVQFLPDAVKELPLPESLKEYVLLK 283
Cdd:cd03727     1 SAPGTLKALARYAVRRSLGVQYLPEAVKQLPLPRSVKEYLLLL 43
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-184 9.44e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.79  E-value: 9.44e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  22 IAAIRSFPHDNVEDLIRRGADVNCM-HGTLKPLHCACMVADADCIELLLEKGAEVNALDGYNRTALHYAAEKDET-CVEI 99
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKdDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLeIVKL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554 100 LLEYGANPNALDGNKDTPLHWAAFKNNAECVRTLLESGAFVNALDYNNDTPLSWAAMKGNLESVSILLEYGAEVRVVNMK 179
Cdd:COG0666   139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218


                  ....*
gi 1621995554 180 GQTPI 184
Cdd:COG0666   219 GKTAL 223
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 22-211 3.11e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 98.98  E-value: 3.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  22 IAAIRSFPHDNVEDLIRRGADVNC---MHGTlkPLHCACMV-ADADCIELLLEKGAEVNALDGYNRTALHYAAEKDETCV 97
Cdd:PHA02876  313 LMAKNGYDTENIRTLIMLGADVNAadrLYIT--PLHQASTLdRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  98 -EILLEYGANPNALDGNKDTPLHWAAFKNNA-ECVRTLLESGAFVNALDYNNDTPLSWAAMKG-NLESVSILLEYGAEVR 174
Cdd:PHA02876  391 iNTLLDYGADIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1621995554 175 VVNMKGQTPIsrLVALLVRGL-------GTEREDScfDLLHRAV 211
Cdd:PHA02876  471 AINIQNQYPL--LIALEYHGIvnillhyGAELRDS--RVLHKSL 510
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-144 2.22e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 2.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  53 LHCACMVADADCIELLLEKGAEVNALDGYNRTALHYAAEKDET-CVEILLEYgANPNaLDGNKDTPLHWAAFKNNAECVR 131
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLeIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1621995554 132 TLLESGAFVNALD 144
Cdd:pfam12796  79 LLLEKGADINVKD 91
SOCS_ASB8 cd03727
SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a ...
 241-283 3.56e-21

SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. Human ASB8 is highly transcribed in skeletal muscle and in lung carcinoma cell lines. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239697  Cd Length: 43  Bit Score: 84.12  E-value: 3.56e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1621995554 241 SAPGTLKTLSRYAVRRSLGVQFLPDAVKELPLPESLKEYVLLK 283
Cdd:cd03727     1 SAPGTLKALARYAVRRSLGVQYLPEAVKQLPLPRSVKEYLLLL 43
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 47-207 2.50e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 54.63  E-value: 2.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  47 HGTLKPLHCACMVADADCIE-LLLEKGAEVNALDGYNRTALHYAA--EKDETCVeILLEygANPNALD---------Gnk 114
Cdd:cd22192    15 RISESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAAlyDNLEAAV-VLME--AAPELVNepmtsdlyqG-- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554 115 DTPLHWAAFKNNAECVRTLLESGAFVN--------------ALDYNNDTPLSWAAMKGNLESVSILLEYGAEVRVVNMKG 180
Cdd:cd22192    90 ETALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpkNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169

                         170       180
                  ....*....|....*....|....*....
gi 1621995554 181 QTPISRLVallvrgLGTEREDSC--FDLL 207
Cdd:cd22192   170 NTVLHILV------LQPNKTFACqmYDLI 192
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 63-174 1.51e-07

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 52.39  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  63 DCIELLLEKGAEVNALDgynrTALHYAAEKDETCVEILL--------EYGANPNALDGNKD------TPLHWAAFKNNAE 128
Cdd:TIGR00870  67 ELTELLLNLSCRGAVGD----TLLHAISLEYVDAVEAILlhllaafrKSGPLELANDQYTSeftpgiTALHLAAHRQNYE 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554 129 CVRTLLESGAFVNA--------------LDYNNDTPLSWAAMKGNLESVSILLEYGAEVR 174
Cdd:TIGR00870 143 IVKLLLERGASVPAracgdffvksqgvdSFYHGESPLNAAACLGSPSIVALLSEDPADIL 202
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 243-281 2.01e-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: 46.39  E-value: 2.01e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1621995554 243 PGTLKTLSRYAVRRSLGvQFLPDAVKELPLPESLKEYVL 281
Cdd:pfam07525   2 PRSLQHLCRLAIRRALG-KRRLGAIDKLPLPPLLKDYLL 39
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 113-142 2.88e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 2.88e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1621995554  113 NKDTPLHWAAFKNNAECVRTLLESGAFVNA 142
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
 245-283 8.59e-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: 38.93  E-value: 8.59e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1621995554  245 TLKTLSRYAVRRSLGvqflpdAVKELPLPESLKEYVLLK 283
Cdd:smart00969   2 SLQHLCRLAIRRSLG------GIDKLPLPPRLKDYLLYY 34
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-184 9.44e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.79  E-value: 9.44e-43
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  22 IAAIRSFPHDNVEDLIRRGADVNCM-HGTLKPLHCACMVADADCIELLLEKGAEVNALDGYNRTALHYAAEKDET-CVEI 99
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKdDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLeIVKL 138

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554 100 LLEYGANPNALDGNKDTPLHWAAFKNNAECVRTLLESGAFVNALDYNNDTPLSWAAMKGNLESVSILLEYGAEVRVVNMK 179
Cdd:COG0666   139 LLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND 218


                  ....*
gi 1621995554 180 GQTPI 184
Cdd:COG0666   219 GKTAL 223
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-191 1.08e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.10  E-value: 1.08e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  22 IAAIRSFPHDNVEDLIRRGADVN-CMHGTLKPLHCACMVADADCIELLLEKGAEVNALDGYNRTALHYAAEK-DETCVEI 99
Cdd:COG0666    92 HAAARNGDLEIVKLLLEAGADVNaRDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANgNLEIVKL 171

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554 100 LLEYGANPNALDGNKDTPLHWAAFKNNAECVRTLLESGAFVNALDYNNDTPLSWAAMKGNLESVSILLEYGAEVRVVNMK 179
Cdd:COG0666   172 LLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251

                         170
                  ....*....|..
gi 1621995554 180 GQTPISRLVALL 191
Cdd:COG0666   252 GLTALLLAAAAG 263
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
18-183 1.34e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 123.91  E-value: 1.34e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  18 LIRTIAAIRSFPHDNVEDLIRRGADVNCMHGTLKPLHCACMVADADCIELLLEKGAEVNALDGYNRTALHYAAEK-DETC 96
Cdd:COG0666    23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNgDLEI 102

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  97 VEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRTLLESGAFVNALDYNNDTPLSWAAMKGNLESVSILLEYGAEVRVV 176
Cdd:COG0666   103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182


                  ....*..
gi 1621995554 177 NMKGQTP 183
Cdd:COG0666   183 DNDGETP 189
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
33-184 1.28e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 116.21  E-value: 1.28e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  33 VEDLIRRGADVNCMHGTLK-PLHCACMVADADCIELLLEKGAEVNALDGYNRTALHYAAEK-DETCVEILLEYGANPNAL 110
Cdd:COG0666   136 VKLLLEAGADVNAQDNDGNtPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENgHLEIVKLLLEAGADVNAK 215

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1621995554 111 DGNKDTPLHWAAFKNNAECVRTLLESGAFVNALDYNNDTPLSWAAMKGNLESVSILLEYGAEVRVVNMKGQTPI 184
Cdd:COG0666   216 DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 22-211 3.11e-23

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 98.98  E-value: 3.11e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  22 IAAIRSFPHDNVEDLIRRGADVNC---MHGTlkPLHCACMV-ADADCIELLLEKGAEVNALDGYNRTALHYAAEKDETCV 97
Cdd:PHA02876  313 LMAKNGYDTENIRTLIMLGADVNAadrLYIT--PLHQASTLdRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVI 390

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  98 -EILLEYGANPNALDGNKDTPLHWAAFKNNA-ECVRTLLESGAFVNALDYNNDTPLSWAAMKG-NLESVSILLEYGAEVR 174
Cdd:PHA02876  391 iNTLLDYGADIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1621995554 175 VVNMKGQTPIsrLVALLVRGL-------GTEREDScfDLLHRAV 211
Cdd:PHA02876  471 AINIQNQYPL--LIALEYHGIvnillhyGAELRDS--RVLHKSL 510
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 33-177 6.13e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.43  E-value: 6.13e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  33 VEDLIRRGADVN-CMHGTLKPLHCACM--VADADCIELLLEKGAEVNALDGYNRTALHYAAE------------------ 91
Cdd:PHA03100   89 VKLLLEYGANVNaPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnkidlkilkllidkgvd 168

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  92 ---KDEtcVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRTLLESGAFVNALDYNNDTPLSWAAMKGNLESVSILLE 168
Cdd:PHA03100  169 inaKNR--VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLN 246


                  ....*....
gi 1621995554 169 YGAEVRVVN 177
Cdd:PHA03100  247 NGPSIKTII 255
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 13-184 5.06e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 94.65  E-value: 5.06e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  13 SLSERLIRTIAAIRSFPHDNVEDLIRRGADVNCMHGTL-KPLHCACMVADADCIELL----------------------- 68
Cdd:PHA02874   31 SVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIpHPLLTAIKIGAHDIIKLLidngvdtsilpipciekdmikti 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  69 LEKGAEVNALDGYNRTALHYAAEK-DETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRTLLESGAFVNALDYNN 147
Cdd:PHA02874  111 LDCGIDVNIKDAELKTFLHYAIKKgDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG 190

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1621995554 148 DTPLSWAAMKGNLESVSILLEYGAEVRVVNMKGQTPI 184
Cdd:PHA02874  191 ESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPL 227
Ank_2 pfam12796
Ankyrin repeats (3 copies);
53-144 2.22e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 2.22e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  53 LHCACMVADADCIELLLEKGAEVNALDGYNRTALHYAAEKDET-CVEILLEYgANPNaLDGNKDTPLHWAAFKNNAECVR 131
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLeIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1621995554 132 TLLESGAFVNALD 144
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 3-218 3.06e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 92.64  E-value: 3.06e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554   3 YIMQSIQSKYSLSERLIRTIAAIRSFPHDNVEDLIRR-----GADVNCM--HGTLKPLHCACMVADADCIELLLEKGAEV 75
Cdd:PHA02878  115 EIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKlllsyGADINMKdrHKGNTALHYATENKDQRLTELLLSYGANV 194

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  76 NALDGYNRTALHYAAEK-DETCVEILLEYGANPNALDGNKDTPLHWA-AFKNNAECVRTLLESGAFVNALDY-NNDTPLS 152
Cdd:PHA02878  195 NIPDKTNNSPLHHAVKHyNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALH 274

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1621995554 153 wAAMKGNlESVSILLEYGAEVRVVNMKGQTPISRLVallvrglgteREDSCFDLLHRAVGHFELRK 218
Cdd:PHA02878  275 -SSIKSE-RKLKLLLEYGADINSLNSYKLTPLSSAV----------KQYLCINIGRILISNICLLK 328
SOCS_ASB8 cd03727
SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a ...
 241-283 3.56e-21

SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. Human ASB8 is highly transcribed in skeletal muscle and in lung carcinoma cell lines. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239697  Cd Length: 43  Bit Score: 84.12  E-value: 3.56e-21
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1621995554 241 SAPGTLKTLSRYAVRRSLGVQFLPDAVKELPLPESLKEYVLLK 283
Cdd:cd03727     1 SAPGTLKALARYAVRRSLGVQYLPEAVKQLPLPRSVKEYLLLL 43
Ank_2 pfam12796
Ankyrin repeats (3 copies);
86-177 4.38e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 4.38e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  86 LHYAAE-KDETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRTLLESgAFVNALDYNNdTPLSWAAMKGNLESVS 164
Cdd:pfam12796   1 LHLAAKnGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1621995554 165 ILLEYGAEVRVVN 177
Cdd:pfam12796  79 LLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
56-184 1.47e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.86  E-value: 1.47e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  56 ACMVADADCIELLLEKGAEVNALDGYNRTALHYAAEKDET-CVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRTLL 134
Cdd:COG0666    28 AALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLlVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLL 107

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1621995554 135 ESGAFVNALDYNNDTPLSWAAMKGNLESVSILLEYGAEVRVVNMKGQTPI 184
Cdd:COG0666   108 EAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL 157
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 24-189 2.79e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 86.64  E-value: 2.79e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  24 AIRSFPHDNVEDLIRRGADVNC-MHGTLKPLH---CACMVA--DADCIELLLEKGAEVNALDGYNRTALHYAAEK---DE 94
Cdd:PHA03100   42 AKEARNIDVVKILLDNGADINSsTKNNSTPLHylsNIKYNLtdVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksnSY 121

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  95 TCVEILLEYGANPNALDGNKDTPLHWAA--FKNNAECVRTLLESGAFVNAL----------------DYNNDTPLSWAAM 156
Cdd:PHA03100  122 SIVEYLLDNGANVNIKNSDGENLLHLYLesNKIDLKILKLLIDKGVDINAKnrvnyllsygvpinikDVYGFTPLHYAVY 201

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1621995554 157 KGNLESVSILLEYGAEVRVVNMKGQTPISRLVA 189
Cdd:PHA03100  202 NNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234
PHA03095 PHA03095
ankyrin-like protein; Provisional
 31-183 1.37e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 85.08  E-value: 1.37e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  31 DNVEDLIRRGADVNCMHGTLKPLHCACM----VADADCIELLLEKGAEVNALDGYNRTALHYAAEKDET--CVEILLEYG 104
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLhyssEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTldVIKLLIKAG 107

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554 105 ANPNALDGNKDTPLH--WAAFKNNAECVRTLLESGAFVNALDYNNDTPLSwAAMKG---NLESVSILLEYGAEVRVVNMK 179
Cdd:PHA03095  108 ADVNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLA-VLLKSrnaNVELLRLLIDAGADVYAVDDR 186


                  ....
gi 1621995554 180 GQTP 183
Cdd:PHA03095  187 FRSL 190
PHA03095 PHA03095
ankyrin-like protein; Provisional
 30-184 4.05e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.54  E-value: 4.05e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  30 HDNVED----LIRRGADVNCMHGTLK-PLH-CAC-MVADADCIELLLEKGAEVNALDGYNRTALHYAAEKDETCVEI--- 99
Cdd:PHA03095   93 NATTLDviklLIKAGADVNAKDKVGRtPLHvYLSgFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVELlrl 172

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554 100 LLEYGANPNALDGNKDTPLHWAA--FKNNAECVRTLLESGAFVNALDYNNDTPLSWAAMKGNLES--VSILLEYGAEVRV 175
Cdd:PHA03095  173 LIDAGADVYAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRslVLPLLIAGISINA 252


                  ....*....
gi 1621995554 176 VNMKGQTPI 184
Cdd:PHA03095  253 RNRYGQTPL 261
PHA03095 PHA03095
ankyrin-like protein; Provisional
 33-189 6.75e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 83.15  E-value: 6.75e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  33 VEDLIRRGADVNCM--HGtLKPLHCAcMV---ADADCIELLLEKGAEVNALDGYNRTALHYAAE---KDETCVEILLEYG 104
Cdd:PHA03095  135 IRLLLRKGADVNALdlYG-MTPLAVL-LKsrnANVELLRLLIDAGADVYAVDDRFRSLLHHHLQsfkPRARIVRELIRAG 212

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554 105 ANPNALDGNKDTPLHWAAFKNNAEC--VRTLLESGAFVNALDYNNDTPLSWAAMKGNLESVSILLEYGAEVRVVNMKGQT 182
Cdd:PHA03095  213 CDPAATDMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNT 292


                  ....*..
gi 1621995554 183 PISRLVA 189
Cdd:PHA03095  293 PLSLMVR 299
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 52-194 2.27e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 82.03  E-value: 2.27e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  52 PLHCACMVAD-ADCIELLLEKGAEVNALDGYNRTALHYAAEK--DETCVEILLEYGANPNALDGNKDTPLHWAA-FKNNA 127
Cdd:PHA02876  276 PLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLMAKNgyDTENIRTLIMLGADVNAADRLYITPLHQAStLDRNK 355

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1621995554 128 ECVRTLLESGAFVNALDYNNDTPLSWAAMKGNLESVSILLEYGAEVRVVNMK----------GQTPISRLVALLVRG 194
Cdd:PHA02876  356 DIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKigtalhfalcGTNPYMSVKTLIDRG 432
PHA03095 PHA03095
ankyrin-like protein; Provisional
 60-208 2.21e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.53  E-value: 2.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  60 ADADCIELLLEKGAEVNALDGYNRTALH----YAAEKDETCVEILLEYGANPNALDGNKDTPLH-WAAFKNNAECVRTLL 134
Cdd:PHA03095   25 VTVEEVRRLLAAGADVNFRGEYGKTPLHlylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHlYLYNATTLDVIKLLI 104

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554 135 ESGAFVNALDYNNDTPLSwAAMKG---NLESVSILLEYGAEVRVVNMKGQTPIS----------RLVALLVRGLG--TER 199
Cdd:PHA03095  105 KAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAvllksrnanvELLRLLIDAGAdvYAV 183


                  ....*....
gi 1621995554 200 EDSCFDLLH 208
Cdd:PHA03095  184 DDRFRSLLH 192
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 66-210 2.35e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 75.87  E-value: 2.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  66 ELLLEKGAEVNALDGYNRTALHYAAEKDET-CVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRT------------ 132
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAkMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAiidnrsninknd 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554 133 -----------------LLESGAFVNALDYNNDTPLSWAAMKGNLES-VSILLEYGAEVRVVNMKGQTPI---------- 184
Cdd:PHA02876  242 lsllkairnedletsllLYDAGFSVNSIDDCKNTPLHHASQAPSLSRlVPKLLERGADVNAKNIKGETPLylmakngydt 321

                         170       180
                  ....*....|....*....|....*..
gi 1621995554 185 SRLVALLVRGLGTEREDSCFDL-LHRA 210
Cdd:PHA02876  322 ENIRTLIMLGADVNAADRLYITpLHQA 348
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 31-184 3.98e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.83  E-value: 3.98e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  31 DNVEDLIRRGADVNCM-HGTLKPLHCACMVADADCIELLLE--------------------------KGAEVNALDGYNR 83
Cdd:PHA02878   51 DVVKSLLTRGHNVNQPdHRDLTPLHIICKEPNKLGMKEMIRsinkcsvfytlvaikdafnnrnveifKIILTNRYKNIQT 130

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  84 TALHYAAEKDE------TCVEILLEYGANPNALDGNKD-TPLHWAAFKNNAECVRTLLESGAFVNALDYNNDTPLSWAAM 156
Cdd:PHA02878  131 IDLVYIDKKSKddiieaEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVK 210

                         170       180
                  ....*....|....*....|....*...
gi 1621995554 157 KGNLESVSILLEYGAEVRVVNMKGQTPI 184
Cdd:PHA02878  211 HYNKPIVHILLENGASTDARDKCGNTPL 238
Ank_2 pfam12796
Ankyrin repeats (3 copies);
24-111 7.30e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 7.30e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  24 AIRSFPHDNVEDLIRRGADVNCMHGT-LKPLHCACMVADADCIELLLEKgAEVNaLDGYNRTALHYAAEKD-ETCVEILL 101
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNgRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGhLEIVKLLL 81

                          90
                  ....*....|
gi 1621995554 102 EYGANPNALD 111
Cdd:pfam12796  82 EKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 64-184 1.23e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 67.38  E-value: 1.23e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  64 CIELLLEKGAEVNALDG----YNRTALHYAAEKDET--CVEILLEYGANPNALDGNKDTPLHWAA-----FKNNAECVRT 132
Cdd:PHA03100   12 IIKVKNIKYIIMEDDLNdysyKKPVLPLYLAKEARNidVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKL 91

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1621995554 133 LLESGAFVNALDYNNDTPLSWAAMK--GNLESVSILLEYGAEVRVVNMKGQTPI 184
Cdd:PHA03100   92 LLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLL 145
Ank_2 pfam12796
Ankyrin repeats (3 copies);
118-184 1.91e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.36  E-value: 1.91e-11
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1621995554 118 LHWAAFKNNAECVRTLLESGAFVNALDYNNDTPLSWAAMKGNLESVSILLEYgAEVRVVNmKGQTPI 184
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTAL 65
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 21-184 2.61e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.44  E-value: 2.61e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  21 TIAAIRSFPHDNVEDLIRRGADVNCMHGTLKP-LHCACMVADADCIELLLEKGAEVNALDGYNRTALHYAAEKDE-TCVE 98
Cdd:PHA02874   95 SILPIPCIEKDMIKTILDCGIDVNIKDAELKTfLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFfDIIK 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  99 ILLEYGANPNALDGNKDTPLHWAAFKNNAECVRTLLESGAFVNALDYNNDTPLSWAAMKGnlESVSILLEYGAEVRVVNM 178
Cdd:PHA02874  175 LLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHN--RSAIELLINNASINDQDI 252


                  ....*.
gi 1621995554 179 KGQTPI 184
Cdd:PHA02874  253 DGSTPL 258
Ank_4 pfam13637
Ankyrin repeats (many copies);
82-134 1.16e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 1.16e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1621995554  82 NRTALHYAAEK-DETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRTLL 134
Cdd:pfam13637   1 ELTALHAAAASgHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 87-172 1.79e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.07  E-value: 1.79e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  87 HYAAEKDETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRTLLESGAFVNALDYNNDTPLSWAAMKGNLESVSIL 166
Cdd:PTZ00322   88 QLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167


                  ....*.
gi 1621995554 167 LEYGAE 172
Cdd:PTZ00322  168 SRHSQC 173
Ank_4 pfam13637
Ankyrin repeats (many copies);
116-167 3.22e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 3.22e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1621995554 116 TPLHWAAFKNNAECVRTLLESGAFVNALDYNNDTPLSWAAMKGNLESVSILL 167
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
65-184 4.04e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.20  E-value: 4.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  65 IELLLEKGAEVNALDGYNRTALHYAAEKDETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRTLLESGAFVNALD 144
Cdd:COG0666     5 LLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKD 84

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1621995554 145 YNNDTPLSWAAMKGNLESVSILLEYGAEVRVVNMKGQTPI 184
Cdd:COG0666    85 DGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPL 124
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 48-209 3.03e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.31  E-value: 3.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  48 GTLKPLHCACMVADADCIELLLEKGAEVNAL---DGynRTALHYAAE-KDETCVEILLEYGANPNALDGNKDTPLHWAAF 123
Cdd:PHA02875   67 DIESELHDAVEEGDVKAVEELLDLGKFADDVfykDG--MTPLHLATIlKKLDIMKLLIARGADPDIPNTDKFSPLHLAVM 144

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554 124 KNNAECVRTLLESGAFVNALDYNNDTPLSWAAMKGNLESVSILLEYGAEVRVVNMKGQtpisrlVALLVRGLGTEREDSC 203
Cdd:PHA02875  145 MGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGC------VAALCYAIENNKIDIV 218


                  ....*.
gi 1621995554 204 FDLLHR 209
Cdd:PHA02875  219 RLFIKR 224
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
 241-283 3.27e-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: 51.34  E-value: 3.27e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1621995554 241 SAPGTLKTLSRYAVRRSLGVQfLPDAVKELPLPESLKEYVLLK 283
Cdd:cd03716     1 STPRSLQHLCRLAIRRCLGRR-RLELIKKLPLPPRLKDYLLYE 42
PHA02946 PHA02946
ankyin-like protein; Provisional
 93-184 3.38e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 56.99  E-value: 3.38e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  93 DETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRTLLESGAFVNALDYNNDTPLSWAAMKGN--LESVSILLEYG 170
Cdd:PHA02946   51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYG 130

                          90
                  ....*....|....*
gi 1621995554 171 AEV-RVVNMKGQTPI 184
Cdd:PHA02946  131 AKInNSVDEEGCGPL 145
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 24-185 3.91e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.90  E-value: 3.91e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  24 AIRSFPHDNVEDLIRRGADVNC--MHGTLkPLHCACMVADADCIELLLEKGAEVNALDGYNRTALHYAAE-KDETCVEIL 100
Cdd:PHA02874  131 AIKKGDLESIKMLFEYGADVNIedDNGCY-PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEyGDYACIKLL 209

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554 101 LEYGAN----------P---------------------NALDGNKDTPLHWA-AFKNNAECVRTLLESGAFVNALDYNND 148
Cdd:PHA02874  210 IDHGNHimnkckngftPlhnaiihnrsaiellinnasiNDQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKDNKGE 289

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1621995554 149 TPLSwAAMKgNLESVSILLEYGAEVRVVNMKGQTPIS 185
Cdd:PHA02874  290 NPID-TAFK-YINKDPVIKDIIANAVLIKEADKLKDS 324
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
 243-283 1.90e-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: 1.90e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1621995554 243 PGTLKTLSRYAVRRSLGVQfLPDAVKELPLPESLKEYVLLK 283
Cdd:cd03587     2 PRSLQHLCRLAIRRCLGKR-RLDLIDKLPLPPRLKDYLLYK 41
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 130-184 2.36e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.90  E-value: 2.36e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1621995554 130 VRTLLESGAFVNALDYNNDTPLSWAAMKGNLESVSILLEYGAEVRVVNMKGQTPI 184
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPL 152
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 47-207 2.50e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 54.63  E-value: 2.50e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  47 HGTLKPLHCACMVADADCIE-LLLEKGAEVNALDGYNRTALHYAA--EKDETCVeILLEygANPNALD---------Gnk 114
Cdd:cd22192    15 RISESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAAlyDNLEAAV-VLME--AAPELVNepmtsdlyqG-- 89

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554 115 DTPLHWAAFKNNAECVRTLLESGAFVN--------------ALDYNNDTPLSWAAMKGNLESVSILLEYGAEVRVVNMKG 180
Cdd:cd22192    90 ETALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpkNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169

                         170       180
                  ....*....|....*....|....*....
gi 1621995554 181 QTPISRLVallvrgLGTEREDSC--FDLL 207
Cdd:cd22192   170 NTVLHILV------LQPNKTFACqmYDLI 192
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 61-162 5.34e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.75  E-value: 5.34e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  61 DADCIELLLEKGAEVNALDGYNRTALHYAAEKDE-TCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRTLLESGAF 139
Cdd:PTZ00322   94 DAVGARILLTGGADPNCRDYDGRTPLHIACANGHvQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQC 173

                          90       100
                  ....*....|....*....|...
gi 1621995554 140 VNALDYNNdTPLSWAAMKGNLES 162
Cdd:PTZ00322  174 HFELGANA-KPDSFTGKPPSLED 195
PHA03095 PHA03095
ankyrin-like protein; Provisional
 33-145 1.08e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.33  E-value: 1.08e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  33 VEDLIRRGAD---VNCMHGTlkPLHCACMVADADCIEL--LLEKGAEVNALDGYNRTALHYAAEKDETCV-EILLEYGAN 106
Cdd:PHA03095  205 VRELIRAGCDpaaTDMLGNT--PLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRAcRRLIALGAD 282

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1621995554 107 PNALDGNKDTPLHWAAFKNNAECVRTLLES----GAFVNALDY 145
Cdd:PHA03095  283 INAVSSDGNTPLSLMVRNNNGRAVRAALAKnpsaETVAATLNT 325
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 63-174 1.51e-07

transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ Channel (TRP-CC) Family (TC. 1.A.4)The TRP-CC family has also been called the store-operated calcium channel (SOC) family. The prototypical members include the Drosophila retinal proteinsTRP and TRPL (Montell and Rubin, 1989; Hardie and Minke, 1993). SOC members of the family mediate the entry of extracellular Ca2+ into cells in responseto depletion of intracellular Ca2+ stores (Clapham, 1996) and agonist stimulated production of inositol-1,4,5 trisphosphate (IP3). One member of the TRP-CCfamily, mammalian Htrp3, has been shown to form a tight complex with the IP3 receptor (TC #1.A.3.2.1). This interaction is apparently required for IP3 tostimulate Ca2+ release via Htrp3. The vanilloid receptor subtype 1 (VR1), which is the receptor for capsaicin (the ?hot? ingredient in chili peppers) and servesas a heat-activated ion channel in the pain pathway (Caterina et al., 1997), is also a member of this family. The stretch-inhibitable non-selective cation channel(SIC) is identical to the vanilloid receptor throughout all of its first 700 residues, but it exhibits a different sequence in its last 100 residues. VR1 and SICtransport monovalent cations as well as Ca2+. VR1 is about 10x more permeable to Ca2+ than to monovalent ions. Ca2+ overload probably causes cell deathafter chronic exposure to capsaicin. (McCleskey and Gold, 1999). [Transport and binding proteins, Cations and iron carrying compounds]


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 52.39  E-value: 1.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  63 DCIELLLEKGAEVNALDgynrTALHYAAEKDETCVEILL--------EYGANPNALDGNKD------TPLHWAAFKNNAE 128
Cdd:TIGR00870  67 ELTELLLNLSCRGAVGD----TLLHAISLEYVDAVEAILlhllaafrKSGPLELANDQYTSeftpgiTALHLAAHRQNYE 142

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554 129 CVRTLLESGAFVNA--------------LDYNNDTPLSWAAMKGNLESVSILLEYGAEVR 174
Cdd:TIGR00870 143 IVKLLLERGASVPAracgdffvksqgvdSFYHGESPLNAAACLGSPSIVALLSEDPADIL 202
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 243-281 2.01e-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: 46.39  E-value: 2.01e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1621995554 243 PGTLKTLSRYAVRRSLGvQFLPDAVKELPLPESLKEYVL 281
Cdd:pfam07525   2 PRSLQHLCRLAIRRALG-KRRLGAIDKLPLPPLLKDYLL 39
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 60-184 2.02e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 50.59  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  60 ADADCIELLLEKGAEVN-ALDGYNRTALHYAAEKDETC----VEILLEYGANPNALDGNKDTPLH--WAAFKNNAECVRT 132
Cdd:PHA02859   64 VNVEILKFLIENGADVNfKTRDNNLSALHHYLSFNKNVepeiLKILIDSGSSITEEDEDGKNLLHmyMCNFNVRINVIKL 143

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1621995554 133 LLESG-AFVNALDYNNDTPLSWAAMKGNLESVSILLEYGAEVRVVNMKGQTPI 184
Cdd:PHA02859  144 LIDSGvSFLNKDFDNNNILYSYILFHSDKKIFDFLTSLGIDINETNKSGYNCY 196
Ank_4 pfam13637
Ankyrin repeats (many copies);
52-101 2.58e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 2.58e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1621995554  52 PLHCACMVADADCIELLLEKGAEVNALDGYNRTALHYAAEK-DETCVEILL 101
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNgNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 92-184 2.61e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.15  E-value: 2.61e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  92 KDETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRTLLESGAFVNALDYNN-DTPLSWAAMKGNLESVSILLEYG 170
Cdd:PHA02875   46 RDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARG 125

                          90
                  ....*....|....
gi 1621995554 171 AEVRVVNMKGQTPI 184
Cdd:PHA02875  126 ADPDIPNTDKFSPL 139
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 97-184 2.67e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 50.75  E-value: 2.67e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  97 VEILLEYGANPNA----LDGNKDTPLHWAAFKNNAECVRTLLESGAFVNAL-DYNNDTPLSWAAMKGNLESVSILLEYGA 171
Cdd:PHA02884   49 IDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYaEEAKITPLYISVLHGCLKCLEILLSYGA 128

                          90
                  ....*....|...
gi 1621995554 172 EVRVVNMKGQTPI 184
Cdd:PHA02884  129 DINIQTNDMVTPI 141
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 56-178 3.19e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.41  E-value: 3.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  56 ACMVADADCIELLLEKGAEVNALDGYNRTALHYAAEKD-ETCVEILLEYGANPNALDGNKDTPLhW-------------- 120
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGyEDCVLVLLKHACNVHIRDANGNTAL-Wnaisakhhkifril 610

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1621995554 121 ------------------AAFKNNAECVRTLLESGAFVNALDYNNDTPLSWAAMKGNLESVSILLEYGAEVRVVNM 178
Cdd:PLN03192  611 yhfasisdphaagdllctAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANT 686
Ank_5 pfam13857
Ankyrin repeats (many copies);
100-151 2.24e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 2.24e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1621995554 100 LLEYG-ANPNALDGNKDTPLHWAAFKNNAECVRTLLESGAFVNALDYNNDTPL 151
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 93-182 2.34e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 2.34e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  93 DETCVEILLEyganpnALDGNKdtpLHWAAFKNNAECVRT---------------LLESGAFVNALDYNNDTPLSWAAMK 157
Cdd:PHA02876  118 DEACIHILKE------AISGND---IHYDKINESIEYMKLikeriqqdelliaemLLEGGADVNAKDIYCITPIHYAAER 188

                          90       100
                  ....*....|....*....|....*
gi 1621995554 158 GNLESVSILLEYGAEVRVVNMKGQT 182
Cdd:PHA02876  189 GNAKMVNLLLSYGADVNIIALDDLS 213
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 91-168 5.67e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.37  E-value: 5.67e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1621995554  91 EKDETCV-EILLEYGANPNALDGNKDTPLHWAAFKNNAECVRTLLESGAFVNALDYNNDTPLSWAAMKGNLESVSILLE 168
Cdd:PHA02876  154 QQDELLIaEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIID 232
PHA02946 PHA02946
ankyin-like protein; Provisional
 4-108 5.73e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 47.36  E-value: 5.73e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554   4 IMQSIQSkySLSERLIRTIAAIRSFPHDNVEDLIRRGADVNCMHGTLK-PLHCACMVADADCIELLLEKGAEVNALDGYN 82
Cdd:PHA02946   28 MLQAIEP--SGNYHILHAYCGIKGLDERFVEELLHRGYSPNETDDDGNyPLHIASKINNNRIVAMLLTHGADPNACDKQH 105

                          90       100
                  ....*....|....*....|....*....
gi 1621995554  83 RTALHYAAEKDETCVE---ILLEYGANPN 108
Cdd:PHA02946  106 KTPLYYLSGTDDEVIErinLLVQYGAKIN 134
PHA02798 PHA02798
ankyrin-like protein; Provisional
 97-182 5.76e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.14  E-value: 5.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  97 VEILLEYGANPNALDGNKDTPL-----HWAAFKNNAECVRTLLESGAFVNALDYNNDTPLSWAAMKG---NLESVSILLE 168
Cdd:PHA02798   54 VKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGyinNLEILLFMIE 133

                          90
                  ....*....|....
gi 1621995554 169 YGAEVRVVNMKGQT 182
Cdd:PHA02798  134 NGADTTLLDKDGFT 147
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 36-118 7.03e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 7.03e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  36 LIRRGADVNCM--HGTlKPLHCACMVADADCIELLLEKGAEVNALDGYNRTALHYAAEKD-ETCVEILLEY-------GA 105
Cdd:PTZ00322  101 LLTGGADPNCRdyDGR-TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGfREVVQLLSRHsqchfelGA 179

                          90
                  ....*....|....*....
gi 1621995554 106 N--PNALDGN----KDTPL 118
Cdd:PTZ00322  180 NakPDSFTGKppslEDSPI 198
PHA02798 PHA02798
ankyrin-like protein; Provisional
 63-179 1.16e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 46.37  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  63 DCIELLLEKGAEVNALDGYNRTAL--------HYAAEKDetCVEILLEYGANPNALDGNKDTPLHWA---AFKNNAECVR 131
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLctilsnikDYKHMLD--IVKILIENGADINKKNSDGETPLYCLlsnGYINNLEILL 129

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1621995554 132 TLLESGAFVNALDYNNDTPLSWAAMKGN---LESVSILLEYGAEVRVVNMK 179
Cdd:PHA02798  130 FMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNNK 180
PHA02741 PHA02741
hypothetical protein; Provisional
 63-174 1.16e-05

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 44.65  E-value: 1.16e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  63 DCIELLLekgaevNALDGYNRTALHYAAEKDET-----CVEILLEYGANPNALDG-NKDTPLHWAAFKNNAECVRTLL-E 135
Cdd:PHA02741   47 DCHAAAL------NATDDAGQMCIHIAAEKHEAqlaaeIIDHLIELGADINAQEMlEGDTALHLAAHRRDHDLAEWLCcQ 120

                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 1621995554 136 SGAFVNALDYNNDTPLSWAAMKGNLESVSILLEYGAEVR 174
Cdd:PHA02741  121 PGIDLHFCNADNKSPFELAIDNEDVAMMQILREIVATSR 159
Ank_5 pfam13857
Ankyrin repeats (many copies);
67-121 1.56e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 1.56e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1621995554  67 LLLEKGAEVNALDGYNRTALHYAAEKDE-TCVEILLEYGANPNALDGNKDTPLHWA 121
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGAlEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 113-142 2.88e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 40.26  E-value: 2.88e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 1621995554  113 NKDTPLHWAAFKNNAECVRTLLESGAFVNA 142
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 81-111 3.66e-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: 3.66e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1621995554  81 YNRTALHYAAEK--DETCVEILLEYGANPNALD 111
Cdd:pfam00023   1 DGNTPLHLAAGRrgNLEIVKLLLSKGADVNARD 33
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 83-174 4.36e-05

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 44.49  E-value: 4.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  83 RTALHYAAEKDET----CVEILLEYG---------ANPNALDG--NKDTPLHWAAFKNNAECVRTLLESGAFVNA----- 142
Cdd:cd21882    27 KTCLHKAALNLNDgvneAIMLLLEAApdsgnpkelVNAPCTDEfyQGQTALHIAIENRNLNLVRLLVENGADVSAratgr 106

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1621995554 143 --------LDYNNDTPLSWAAMKGNLESVSILLEYGAEVR 174
Cdd:cd21882   107 ffrkspgnLFYFGELPLSLAACTNQEEIVRLLLENGAQPA 146
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 113-144 4.41e-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: 4.41e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1621995554 113 NKDTPLHWAAFK-NNAECVRTLLESGAFVNALD 144
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
 245-283 8.59e-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: 38.93  E-value: 8.59e-05
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1621995554  245 TLKTLSRYAVRRSLGvqflpdAVKELPLPESLKEYVLLK 283
Cdd:smart00969   2 SLQHLCRLAIRRSLG------GIDKLPLPPRLKDYLLYY 34
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
 243-283 9.24e-05

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: 39.43  E-value: 9.24e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1621995554 243 PGTLKTLSRYAVRRSLGVQFL--PDAVKELPLPESLKEYVLLK 283
Cdd:cd03731     3 PRPLKHLCRLKIRKLMGLQKLqqPSSMKKLPLPPALKRYILYK 45
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 52-161 1.38e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.08  E-value: 1.38e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  52 PLHCACMVADADCIELLLEKGAEVN--------------ALDGYNRTALHYAA-EKDETCVEILLEYGANPNALDGNKDT 116
Cdd:cd22192    92 ALHIAVVNQNLNLVRELIARGADVVspratgtffrpgpkNLIYYGEHPLSFAAcVGNEEIVRLLIEHGADIRAQDSLGNT 171

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1621995554 117 PLHWAAFKNNAECVRTLLEsgaFVNALDYNND-------------TPLSWAAMKGNLE 161
Cdd:cd22192   172 VLHILVLQPNKTFACQMYD---LILSYDKEDDlqpldlvpnnqglTPFKLAAKEGNIV 226
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 53-175 1.49e-04

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 41.40  E-value: 1.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  53 LHCACMvaDADCIELLLEKGAEVNA----LDGYNRTA---LHYAAEKD-----ETCvEILLEYGANPNALDG-NKDTPLH 119
Cdd:PHA02736   21 LHYLCR--NGGVTDLLAFKNAISDEnrylVLEYNRHGkqcVHIVSNPDkadpqEKL-KLLMEWGADINGKERvFGNTPLH 97

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1621995554 120 WAAFKNNAECVRTLL-ESGAFVNALDYNNDTPLSWAAMKGNLESVSILLEYGAEVRV 175
Cdd:PHA02736   98 IAVYTQNYELATWLCnQPGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQCKV 154
SOCS_SSB1_4 cd03718
SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box ...
 242-281 1.70e-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: 38.44  E-value: 1.70e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1621995554 242 APGTLKTLSRYAVRRSLGVQFLPDaVKELPLPESLKEYVL 281
Cdd:cd03718     2 EPLPLMDLCRRRVRVALGRDRLEE-IEQLPLPPSLKNYLL 40
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 63-156 2.32e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 41.89  E-value: 2.32e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  63 DCIELLLEKGAEVNA-----LDGYNrTALHYAAEKD-ETCVEILLEYGANPNALDGN-KDTPLHWAAFKNNAECVRTLLE 135
Cdd:PHA02884   47 DIIDAILKLGADPEApfplsENSKT-NPLIYAIDCDnDDAAKLLIRYGADVNRYAEEaKITPLYISVLHGCLKCLEILLS 125

                          90       100
                  ....*....|....*....|.
gi 1621995554 136 SGAFVNALDYNNDTPLSWAAM 156
Cdd:PHA02884  126 YGADINIQTNDMVTPIELALM 146
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 66-171 2.65e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 2.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  66 ELLLEKGAE-VNALDGYNrtALHYAAEKDETCVEILLEYGANPNALDGNKDTPLHWAAFKNNAECVRTLLESGAFVNALD 144
Cdd:PLN03192  511 DLLGDNGGEhDDPNMASN--LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRD 588

                          90       100
                  ....*....|....*....|....*..
gi 1621995554 145 YNNDTPLSWAAMKGNLESVSILLEYGA 171
Cdd:PLN03192  589 ANGNTALWNAISAKHHKIFRILYHFAS 615
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 81-109 2.95e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 2.95e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1621995554   81 YNRTALHYAAEK-DETCVEILLEYGANPNA 109
Cdd:smart00248   1 DGRTPLHLAAENgNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 52-77 3.70e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 3.70e-04
                           10        20
                   ....*....|....*....|....*.
gi 1621995554   52 PLHCACMVADADCIELLLEKGAEVNA 77
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank_4 pfam13637
Ankyrin repeats (many copies);
147-184 6.06e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 6.06e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1621995554 147 NDTPLSWAAMKGNLESVSILLEYGAEVRVVNMKGQTPI 184
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETAL 38
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 61-185 7.88e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 40.67  E-value: 7.88e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  61 DADCIELLLEKGAEVNALDGYNRTALHYAAEK---DETCVEILLEYGANPNALDGNKDTPLHwaafknnaecvrTLLESG 137
Cdd:PHA02716  296 DISVVYSFLQPGVKLHYKDSAGRTCLHQYILRhniSTDIIKLLHEYGNDLNEPDNIGNTVLH------------TYLSML 363

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*...
gi 1621995554 138 AFVNALDYNNDTPLswaamkgNLESVSILLEYGAEVRVVNMKGQTPIS 185
Cdd:PHA02716  364 SVVNILDPETDNDI-------RLDVIQCLISLGADITAVNCLGYTPLT 404
Ank_2 pfam12796
Ankyrin repeats (3 copies);
22-79 8.97e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 37.79  E-value: 8.97e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1621995554  22 IAAIRSFPHDNVEDLIRRgADVNCMHGTLKPLHCACMVADADCIELLLEKGAEVNALD 79
Cdd:pfam12796  35 HLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 52-79 1.09e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 35.73  E-value: 1.09e-03
                          10        20
                  ....*....|....*....|....*....
gi 1621995554  52 PLHCAC-MVADADCIELLLEKGAEVNALD 79
Cdd:pfam00023   5 PLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02791 PHA02791
ankyrin-like protein; Provisional
 79-168 1.20e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 39.64  E-value: 1.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  79 DGYNRTALHYA-AEKDETCVEILLEYGANPNALDgnKDTPLHWAAFKNNAECVRTLLESGAFVNALDYNNDTPLSWAAMK 157
Cdd:PHA02791   27 DVHGHSALYYAiADNNVRLVCTLLNAGALKNLLE--NEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDS 104

                          90
                  ....*....|.
gi 1621995554 158 GNLESVSILLE 168
Cdd:PHA02791  105 GNMQTVKLFVK 115
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 75-151 1.73e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 38.65  E-value: 1.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  75 VNALDGYNRTALHYAAEKDETCVEI---LLEYGANPN-ALDGNKDTPLHWAAFKN---NAECVRTLLESGAFVNALDYNN 147
Cdd:PHA02859   44 VNDCNDLYETPIFSCLEKDKVNVEIlkfLIENGADVNfKTRDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDG 123


                  ....
gi 1621995554 148 DTPL 151
Cdd:PHA02859  124 KNLL 127
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 146-173 2.33e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 2.33e-03
                           10        20
                   ....*....|....*....|....*...
gi 1621995554  146 NNDTPLSWAAMKGNLESVSILLEYGAEV 173
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
Ank_5 pfam13857
Ankyrin repeats (many copies);
140-184 2.38e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 2.38e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1621995554 140 VNALDYNNDTPLSWAAMKGNLESVSILLEYGAEVRVVNMKGQTPI 184
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 33-128 2.64e-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: 39.23  E-value: 2.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1621995554  33 VEDLIRRGADVN----------------CMHGTlKPLHCACMVADADCIELLLEKGAEVNALDGYNRTALHY---AAEKD 93
Cdd:cd22192   105 VRELIARGADVVspratgtffrpgpknlIYYGE-HPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIlvlQPNKT 183

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|...
gi 1621995554  94 ETC--VEILLEYGA--NPNALD--GNKD--TPLHWAAFKNNAE 128
Cdd:cd22192   184 FACqmYDLILSYDKedDLQPLDlvPNNQglTPFKLAAKEGNIV 226
SOCS_ASB1 cd03720
SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a ...
 241-281 4.08e-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: 34.32  E-value: 4.08e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1621995554 241 SAPGTLKTLSRYAVRRSLGVQFLpDAVKELPLPESLKEYVL 281
Cdd:cd03720     1 GNPRSLLSLCRIAVRRALGKQRL-SLICSLPLPDPIKKFLL 40
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
 245-279 4.60e-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: 34.11  E-value: 4.60e-03
                          10        20        30
                  ....*....|....*....|....*....|....*
gi 1621995554 245 TLKTLSRYAVRRSLGVqflpDAVKELPLPESLKEY 279
Cdd:cd03717     5 SLQHLCRFVIRQCTRR----DLIDQLPLPRRLKDY 35
SOCS_SSB2 cd03719
SOCS (suppressors of cytokine signaling) box of SSB2 (SPRY domain-containing SOCS box proteins) ...
 243-283 4.84e-03

SOCS (suppressors of cytokine signaling) box of SSB2 (SPRY domain-containing SOCS box proteins)-like proteins. SSB proteins contain a central SPRY domain and a C-terminal SOCS. SSB2 has been shown to bind to MET, the receptor protein-tyrosine kinase for hepatocyte growth factor (HGF). SSB2, like SSB4 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: 239689  Cd Length: 42  Bit Score: 34.23  E-value: 4.84e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1621995554 243 PGTLKTLSRYAVRRSLGVQFLpDAVKELPLPESLKEYVLLK 283
Cdd:cd03719     3 PHSLLHLSRLCVRHALGDTRL-GQVSALPLPPAMKRYLLYQ 42
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 52-77 5.22e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 33.77  E-value: 5.22e-03
                          10        20
                  ....*....|....*....|....*.
gi 1621995554  52 PLHCACMVADADCIELLLEKGAEVNA 77
Cdd:pfam13606   5 PLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 146-177 8.78e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 33.42  E-value: 8.78e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1621995554 146 NNDTPLSWAAMK-GNLESVSILLEYGAEVRVVN 177
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 8-76 9.73e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 36.88  E-value: 9.73e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1621995554   8 IQSKYSLSERLIRTIAAIRSFPHDNVEDLIRRGADVNCMHGTLK--PLHCACMVADADCIELLLEKGAEVN 76
Cdd:PHA02884   61 APFPLSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKitPLYISVLHGCLKCLEILLSYGADIN 131
 
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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