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Conserved domains on  [gi|795277808|ref|XP_011813263|]
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PREDICTED: ankyrin repeat and SOCS box protein 9 isoform X1 [Colobus angolensis palliatus]

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];
22-253 2.23e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 2.23e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  22 IRLLSNPLMSDAVSDWSPMHEAAIYGRQLSLRNLISQGWLVNVITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTD 101
Cdd:COG0666   40 LLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 102 WHTPLFNACVSGSQDCVNLLLQHGASV-QPESDLASPIHEAARRGHVECVDFLIAYGGNIDHKISHLGTPLYLACENQQR 180
Cdd:COG0666  120 GETPLHLAAYNGNLEIVKLLLEAGADVnAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL 199

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 795277808 181 ACVKKLLESGADVN-QGKGQDSPLHAAARTASEELACLLMDFGADTQAKNAEGKRPVELVPPDSPLARLFLERE 253
Cdd:COG0666  200 EIVKLLLEAGADVNaKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
SOCS_ASB_9_11 cd03728
SOCS (suppressors of cytokine signaling) box of ASB9 and 11 proteins. ASB family members have ...
 253-294 3.22e-19

SOCS (suppressors of cytokine signaling) box of ASB9 and 11 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: 239698  Cd Length: 42  Bit Score: 79.06  E-value: 3.22e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 795277808 253 EGPPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLHL 294
Cdd:cd03728    1 EGPPSLMQLCRLCIRKCFGRKQHHKIHKLHLPEPLKHFLLYR 42
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-253 2.23e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 2.23e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  22 IRLLSNPLMSDAVSDWSPMHEAAIYGRQLSLRNLISQGWLVNVITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTD 101
Cdd:COG0666   40 LLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 102 WHTPLFNACVSGSQDCVNLLLQHGASV-QPESDLASPIHEAARRGHVECVDFLIAYGGNIDHKISHLGTPLYLACENQQR 180
Cdd:COG0666  120 GETPLHLAAYNGNLEIVKLLLEAGADVnAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL 199

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 795277808 181 ACVKKLLESGADVN-QGKGQDSPLHAAARTASEELACLLMDFGADTQAKNAEGKRPVELVPPDSPLARLFLERE 253
Cdd:COG0666  200 EIVKLLLEAGADVNaKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
Ank_2 pfam12796
Ankyrin repeats (3 copies);
73-163 3.14e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.24  E-value: 3.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808   73 LHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSQDCVNLLLQHgASVQPESDLASPIHEAARRGHVECVDF 152
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|.
gi 795277808  153 LIAYGGNIDHK 163
Cdd:pfam12796  80 LLEKGADINVK 90
SOCS_ASB_9_11 cd03728
SOCS (suppressors of cytokine signaling) box of ASB9 and 11 proteins. ASB family members have ...
 253-294 3.22e-19

SOCS (suppressors of cytokine signaling) box of ASB9 and 11 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: 239698  Cd Length: 42  Bit Score: 79.06  E-value: 3.22e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 795277808 253 EGPPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLHL 294
Cdd:cd03728    1 EGPPSLMQLCRLCIRKCFGRKQHHKIHKLHLPEPLKHFLLYR 42
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 45-236 8.00e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 83.09  E-value: 8.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  45 IYGRQLSL-RNLI-SQGWLVNVITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSQDCVNLLL 122
Cdd:PHA02874   9 IYSGDIEAiEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 123 QHG--ASVQPESDLASpiheaarrghvECVDFLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN-QGKGQ 199
Cdd:PHA02874  89 DNGvdTSILPIPCIEK-----------DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNiEDDNG 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 795277808 200 DSPLHAAARTASEELACLLMDFGADTQAKNAEGKRPV 236
Cdd:PHA02874 158 CYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 254-292 2.76e-10

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: 54.48  E-value: 2.76e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 795277808  254 GPPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLL 292
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
 256-293 5.11e-07

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: 45.09  E-value: 5.11e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 795277808   256 PSLMQLCRLRIRKCFGiqqhhKITKLVLPEDLKQFLLH 293
Cdd:smart00969   1 RSLQHLCRLAIRRSLG-----GIDKLPLPPRLKDYLLY 33
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 94-227 2.20e-06

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: 48.92  E-value: 2.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808   94 QVNGVTTDWHTPLFNACVSGS-QDCVNLLLQHGASVQPESDLaspIHeAARRGHVECVDFLIAYGGNIDHKISHLG---- 168
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAVGDTL---LH-AISLEYVDAVEAILLHLLAAFRKSGPLEland 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  169 ----------TPLYLACENQQRACVKKLLESGADVN---------QGKGQD------SPLHAAARTASEELACLLMDFGA 223
Cdd:TIGR00870 120 qytseftpgiTALHLAAHRQNYEIVKLLLERGASVParacgdffvKSQGVDsfyhgeSPLNAAACLGSPSIVALLSEDPA 199


                  ....
gi 795277808  224 DTQA 227
Cdd:TIGR00870 200 DILT 203
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 102-236 4.52e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 44.62  E-value: 4.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 102 WHTPLFNACVSGSQDCVN-LLLQHGASVQPESDLA-SPIHEAARRGHVECVDFLI-AYGGNIDHKIS---HLG-TPLYLA 174
Cdd:cd22192   17 SESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGeTALHVAALYDNLEAAVVLMeAAPELVNEPMTsdlYQGeTALHIA 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 795277808 175 CENQQRACVKKLLESGADVNQG--------KGQDS-------PLHAAARTASEELACLLMDFGADTQAKNAEGKRPV 236
Cdd:cd22192   97 VVNQNLNLVRELIARGADVVSPratgtffrPGPKNliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 68-96 1.00e-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: 38.72  E-value: 1.00e-04
                           10        20
                   ....*....|....*....|....*....
gi 795277808    68 DHVSPLHEACLGGHPSCVKILLKHGAQVN 96
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-253 2.23e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 2.23e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  22 IRLLSNPLMSDAVSDWSPMHEAAIYGRQLSLRNLISQGWLVNVITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTD 101
Cdd:COG0666   40 LLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 102 WHTPLFNACVSGSQDCVNLLLQHGASV-QPESDLASPIHEAARRGHVECVDFLIAYGGNIDHKISHLGTPLYLACENQQR 180
Cdd:COG0666  120 GETPLHLAAYNGNLEIVKLLLEAGADVnAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL 199

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 795277808 181 ACVKKLLESGADVN-QGKGQDSPLHAAARTASEELACLLMDFGADTQAKNAEGKRPVELVPPDSPLARLFLERE 253
Cdd:COG0666  200 EIVKLLLEAGADVNaKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-234 5.29e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.85  E-value: 5.29e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  36 DWSPMHEAAIYGRQLSLRNLISQGWLVNVITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSQ 115
Cdd:COG0666   87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 116 DCVNLLLQHGASV-QPESDLASPIHEAARRGHVECVDFLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN 194
Cdd:COG0666  167 EIVKLLLEAGADVnARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 795277808 195 -QGKGQDSPLHAAARTASEELACLLMDFGADTQAKNAEGKR 234
Cdd:COG0666  247 aKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
21-294 5.47e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 127.76  E-value: 5.47e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  21 DIRLLSNPLMSDAVSDWSPMHEAAIYGRQLSLRNLISQGWLVNVITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTT 100
Cdd:COG0666    6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 101 DWHTPLFNACVSGSQDCVNLLLQHGASV-QPESDLASPIHEAARRGHVECVDFLIAYGGNIDHKISHLGTPLYLACENQQ 179
Cdd:COG0666   86 GGNTLLHAAARNGDLEIVKLLLEAGADVnARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 180 RACVKKLLESGADVN-QGKGQDSPLHAAARTASEELACLLMDFGADTQAKNAEGKRPVEL--VPPDSPLARLFLEREGPP 256
Cdd:COG0666  166 LEIVKLLLEAGADVNaRDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLaaENGNLEIVKLLLEAGADL 245

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 795277808 257 SLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLHL 294
Cdd:COG0666  246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
Ank_2 pfam12796
Ankyrin repeats (3 copies);
73-163 3.14e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.24  E-value: 3.14e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808   73 LHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSQDCVNLLLQHgASVQPESDLASPIHEAARRGHVECVDF 152
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|.
gi 795277808  153 LIAYGGNIDHK 163
Cdd:pfam12796  80 LLEKGADINVK 90
SOCS_ASB_9_11 cd03728
SOCS (suppressors of cytokine signaling) box of ASB9 and 11 proteins. ASB family members have ...
 253-294 3.22e-19

SOCS (suppressors of cytokine signaling) box of ASB9 and 11 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: 239698  Cd Length: 42  Bit Score: 79.06  E-value: 3.22e-19
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 795277808 253 EGPPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLHL 294
Cdd:cd03728    1 EGPPSLMQLCRLCIRKCFGRKQHHKIHKLHLPEPLKHFLLYR 42
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 45-236 8.00e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 83.09  E-value: 8.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  45 IYGRQLSL-RNLI-SQGWLVNVITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSQDCVNLLL 122
Cdd:PHA02874   9 IYSGDIEAiEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 123 QHG--ASVQPESDLASpiheaarrghvECVDFLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN-QGKGQ 199
Cdd:PHA02874  89 DNGvdTSILPIPCIEK-----------DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNiEDDNG 157

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 795277808 200 DSPLHAAARTASEELACLLMDFGADTQAKNAEGKRPV 236
Cdd:PHA02874 158 CYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 85-239 3.21e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 81.46  E-value: 3.21e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  85 VKILLKHGAQVNGVTTDW-HTPLFNACVSGSQDCVNLLLQHGASVQ-PESDLASPIHEAARRGHVECVDFLIAYGGNIDH 162
Cdd:PHA02878 150 TKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNiPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 163 KISHLGTPLYLA---CENQQraCVKKLLESGADVNQGKG--QDSPLHAAARtaSEELACLLMDFGADTQAKNAEGKRPVE 237
Cdd:PHA02878 230 RDKCGNTPLHISvgyCKDYD--ILKLLLEHGVDVNAKSYilGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLS 305


                 ..
gi 795277808 238 LV 239
Cdd:PHA02878 306 SA 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
40-128 7.87e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.00  E-value: 7.87e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808   40 MHEAAIYGRQLSLRNLISQGWLVNVITADHVSPLHEACLGGHPSCVKILLKHgAQVNGVTTDWhTPLFNACVSGSQDCVN 119
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78


                  ....*....
gi 795277808  120 LLLQHGASV 128
Cdd:pfam12796  79 LLLEKGADI 87
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
37-171 1.07e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 78.46  E-value: 1.07e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  37 WSPMHEAAIYGRQLSLRNLISQGWLVNVITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSQD 116
Cdd:COG0666  154 NTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 795277808 117 CVNLLLQHGASVQPE-SDLASPIHEAARRGHVECVDFLIAYGGNIDHKISHLGTPL 171
Cdd:COG0666  234 IVKLLLEAGADLNAKdKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
138-229 4.37e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 4.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  138 IHEAARRGHVECVDFLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESgADVNQGKGQDSPLHAAARTASEELACL 217
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 795277808  218 LMDFGADTQAKN 229
Cdd:pfam12796  80 LLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 38-236 9.91e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.41  E-value: 9.91e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  38 SPMHEAaIYGRQLS--LRNLISQGWLVNVITADHVSPLHEACLGGHPS-CVKILLKHGAQVNGVTTDWHTPLFNA-CVSG 113
Cdd:PHA02876 275 TPLHHA-SQAPSLSrlVPKLLERGADVNAKNIKGETPLYLMAKNGYDTeNIRTLIMLGADVNAADRLYITPLHQAsTLDR 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 114 SQDCVNLLLQHGASVQPESDL-ASPIHEAARRGHVECVDFLIAYGGNIDHKISHLGTPLYLA-CENQQRACVKKLLESGA 191
Cdd:PHA02876 354 NKDIVITLLELGANVNARDYCdKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGA 433

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 795277808 192 DVN-QGKGQDSPLHAAARTASE-ELACLLMDFGADTQAKNAEGKRPV 236
Cdd:PHA02876 434 NVNsKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPL 480
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 51-239 6.09e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 74.32  E-value: 6.09e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  51 SLRNLISQGWLVNVITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPL--FNACVSGSQDCVN---LLLQHG 125
Cdd:PHA03100  17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhyLSNIKYNLTDVKEivkLLLEYG 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 126 ASVQPESDLA-SPIHEAA--RRGHVECVDFLIAYGGNIDHKISHLGTPL--YLACENQQRACVKKLLESGADVNQ----- 195
Cdd:PHA03100  97 ANVNAPDNNGiTPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLhlYLESNKIDLKILKLLIDKGVDINAknrvn 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 795277808 196 ---GKGQD---------SPLHAAARTASEELACLLMDFGADTQAKNAEGKRPVELV 239
Cdd:PHA03100 177 yllSYGVPinikdvygfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
 253-293 2.11e-14

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: 65.98  E-value: 2.11e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 795277808 253 EGPPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLH 293
Cdd:cd03716    1 STPRSLQHLCRLAIRRCLGRRRLELIKKLPLPPRLKDYLLY 41
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
 255-293 5.48e-13

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: 62.10  E-value: 5.48e-13
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 795277808 255 PPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLH 293
Cdd:cd03587    2 PRSLQHLCRLAIRRCLGKRRLDLIDKLPLPPRLKDYLLY 40
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 17-194 1.40e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 67.32  E-value: 1.40e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  17 RDSPDIRLLsnpLMSDAVSDW------SPMHEAAIYGRQLSLRNLISQGWLVN-VITADHVSPLHEACLGGHPSCVKILL 89
Cdd:PHA02875  46 RDSEAIKLL---MKHGAIPDVkypdieSELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLI 122

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  90 KHGAQVNGVTTDWHTPLFNACVSGSQDCVNLLLQHGASVQPESDLA-SPIHEAARRGHVECVDFLIAYGGNIDHkISHLG 168
Cdd:PHA02875 123 ARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGcTPLIIAMAKGDIAICKMLLDSGANIDY-FGKNG 201

                        170       180
                 ....*....|....*....|....*...
gi 795277808 169 --TPLYLACENQQRACVKKLLESGADVN 194
Cdd:PHA02875 202 cvAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 37-225 2.27e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.94  E-value: 2.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  37 WSPMHEAAIYGRQLSLRNLISQGWLVNVITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVT-TDWHTPLFNACVSGSQ 115
Cdd:PHA02875  36 ISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFyKDGMTPLHLATILKKL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 116 DCVNLLLQHGASVQ-PESDLASPIHEAARRGHVECVDFLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN 194
Cdd:PHA02875 116 DIMKLLIARGADPDiPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195

                        170       180       190
                 ....*....|....*....|....*....|...
gi 795277808 195 Q-GKGQD-SPLHAAARTASEELACLLMDFGADT 225
Cdd:PHA02875 196 YfGKNGCvAALCYAIENNKIDIVRLFIKRGADC 228
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 71-193 7.27e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 65.66  E-value: 7.27e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  71 SPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSQDCVNLLLQHGASVQPES--DLaspIHEAARRGHVE 148
Cdd:PLN03192 560 TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAagDL---LCTAAKRNDLT 636

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*
gi 795277808 149 CVDFLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESGADV 193
Cdd:PLN03192 637 AMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PHA03095 PHA03095
ankyrin-like protein; Provisional
 52-259 2.26e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.81  E-value: 2.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  52 LRNLISQGWLVNVITADHVSPLHeACLGG---HPSCVKILLKHGAQVNGVTTDWHTPLfnACVSGSQDC----VNLLLQH 124
Cdd:PHA03095 100 IKLLIKAGADVNAKDKVGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSRNAnvelLRLLIDA 176

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 125 GASV-QPESDLASPIHEAAR--RGHVECVDFLIAYGGNIDHKISHLGTPL-YLACENQQRAC-VKKLLESGADVN--QGK 197
Cdd:PHA03095 177 GADVyAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLhSMATGSSCKRSlVLPLLIAGISINarNRY 256

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 795277808 198 GQdSPLHAAARTASEELACLLMDFGADTQAKNAEGKRPVE--LVPPDSPLARLFLEREGPPSLM 259
Cdd:PHA03095 257 GQ-TPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSlmVRNNNGRAVRAALAKNPSAETV 319
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 39-236 2.27e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.66  E-value: 2.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  39 PMHEAaIYGRQLSL-RNLISQGWLVNVITADHVSPLHEACLGGHPSCVKILLKHGAQVNgvttdwhtpLFNACVSGSQDC 117
Cdd:PHA02878  40 PLHQA-VEARNLDVvKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCS---------VFYTLVAIKDAF 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 118 VN--------LLLQHGASVQpESDLASpIHEAARRGHVEC--VDFLIAYGGNIDHKISHLG-TPLYLACENQQRACVKKL 186
Cdd:PHA02878 110 NNrnveifkiILTNRYKNIQ-TIDLVY-IDKKSKDDIIEAeiTKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELL 187

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 795277808 187 LESGADVNQ-GKGQDSPLHAAARTASEELACLLMDFGADTQAKNAEGKRPV 236
Cdd:PHA02878 188 LSYGANVNIpDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 254-292 2.76e-10

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: 54.48  E-value: 2.76e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 795277808  254 GPPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLL 292
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 55-167 1.91e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.75  E-value: 1.91e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  55 LISQGWLVNVITADHVSPLHEACLGGHP--SCVKILLKHGAQVN-----------GVTTDW-----HTPLFNACVSGSQD 116
Cdd:PHA03100 127 LLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINaknrvnyllsyGVPINIkdvygFTPLHYAVYNNNPE 206

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 795277808 117 CVNLLLQHGASVQPESDLA-SPIHEAARRGHVECVDFLIAYGGNIDHKISHL 167
Cdd:PHA03100 207 FVKYLLDLGANPNLVNKYGdTPLHIAILNNNKEIFKLLLNNGPSIKTIIETL 258
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 40-259 2.26e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.69  E-value: 2.26e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  40 MHEAAIYGRQLSLRNLISQGWLVNVITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSQDCVN 119
Cdd:PHA02875   6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 120 LLLQHGASVQP--ESDLASPIHEAARRGHVECVDFLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESGA--DVNQ 195
Cdd:PHA02875  86 ELLDLGKFADDvfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAclDIED 165

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 795277808 196 GKGQdSPLHAAARTASEELACLLMDFGADTqakNAEGKRP--------VELVPPDspLARLFLEREGPPSLM 259
Cdd:PHA02875 166 CCGC-TPLIIAMAKGDIAICKMLLDSGANI---DYFGKNGcvaalcyaIENNKID--IVRLFIKRGADCNIM 231
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 30-183 3.83e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.20  E-value: 3.83e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  30 MSDAVSDWSPMHEAAIYGRQLSLRNLISQGWLVNVITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNA 109
Cdd:PHA02878 162 MKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 795277808 110 CVS-GSQDCVNLLLQHGASVQPESDLA--SPIHEAARRGHVecVDFLIAYGGNIDHKISHLGTPLYLACenQQRACV 183
Cdd:PHA02878 242 VGYcKDYDILKLLLEHGVDVNAKSYILglTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAV--KQYLCI 314
Ank_4 pfam13637
Ankyrin repeats (many copies);
102-154 1.38e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 1.38e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 795277808  102 WHTPLFNACVSGSQDCVNLLLQHGASV--QPESDLaSPIHEAARRGHVECVDFLI 154
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADInaVDGNGE-TALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 55-229 7.32e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.53  E-value: 7.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  55 LISQGWLVNVITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSQDCVNLLLQHGASVQpESDL 134
Cdd:PHA02876 164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN-KNDL 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 135 AspIHEAARRGHVECVDFLIAYGGNIDHKISHLGTPLYLACENQQRA-CVKKLLESGADVNQG--KGQdSPLHAAARTA- 210
Cdd:PHA02876 243 S--LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKniKGE-TPLYLMAKNGy 319

                        170       180
                 ....*....|....*....|
gi 795277808 211 -SEELACLLMdFGADTQAKN 229
Cdd:PHA02876 320 dTENIRTLIM-LGADVNAAD 338
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 86-239 9.25e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 53.14  E-value: 9.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  86 KILLKHGAQVNGVTTDWHTPLFNACVSGSQDCVNLLLQHGASVQPES-DLASPIHEAARRGHVECVDFLIAYGGNIDHKi 164
Cdd:PHA02876 162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIAlDDLSVLECAVDSKNIDTIKAIIDNRSNINKN- 240

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 795277808 165 shlGTPLYLACENQQRACVKKLLESGADVNQ-GKGQDSPLHAAARTAS-EELACLLMDFGADTQAKNAEGKRPVELV 239
Cdd:PHA02876 241 ---DLSLLKAIRNEDLETSLLLYDAGFSVNSiDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLM 314
PHA03095 PHA03095
ankyrin-like protein; Provisional
 118-236 3.17e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.18  E-value: 3.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 118 VNLLLQHGASVQPESDLAS-PIHEAARRGHVEC---VDFLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLL-ESGAD 192
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKtPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLiKAGAD 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*..
gi 795277808 193 VN-QGKGQDSPLHAAARTAS--EELACLLMDFGADTQAKNAEGKRPV 236
Cdd:PHA03095 110 VNaKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPL 156
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 42-132 4.53e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 4.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  42 EAAIYGRQLSLRNLISQGWLVNVITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSQDCVNLL 121
Cdd:PTZ00322  88 QLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167

                         90
                 ....*....|....*...
gi 795277808 122 LQH-------GASVQPES 132
Cdd:PTZ00322 168 SRHsqchfelGANAKPDS 185
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
 256-293 5.11e-07

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: 45.09  E-value: 5.11e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 795277808   256 PSLMQLCRLRIRKCFGiqqhhKITKLVLPEDLKQFLLH 293
Cdd:smart00969   1 RSLQHLCRLAIRRSLG-----GIDKLPLPPRLKDYLLY 33
Ank_4 pfam13637
Ankyrin repeats (many copies);
37-89 7.64e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.34  E-value: 7.64e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 795277808   37 WSPMHEAAIYGRQLSLRNLISQGWLVNVITADHVSPLHEACLGGHPSCVKILL 89
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
 41-232 8.02e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.02  E-value: 8.02e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  41 HEAAIYGRQLS--------LRNLISQGWLVNVITADHVSPLHEACLGGHPSCVKI---LLKHGAQVNGVTTDWHTPLFna 109
Cdd:PHA03095  11 MEAALYDYLLNasnvtveeVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLH-- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 110 cvsgsqdcvnLLLQHGASvqpesdlaspiheaarrghVECVDFLIAYGGNIDHKISHLGTPL--YLACENQQRACVKKLL 187
Cdd:PHA03095  89 ----------LYLYNATT-------------------LDVIKLLIKAGADVNAKDKVGRTPLhvYLSGFNINPKVIRLLL 139

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*...
gi 795277808 188 ESGADVNQGKGQD-SPLHAAART--ASEELACLLMDFGADTQAKNAEG 232
Cdd:PHA03095 140 RKGADVNALDLYGmTPLAVLLKSrnANVELLRLLIDAGADVYAVDDRF 187
Ank_2 pfam12796
Ankyrin repeats (3 copies);
37-96 8.72e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 46.26  E-value: 8.72e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808   37 WSPMHEAAIYGRQLSLRNLISQGWLVNviTADHVSPLHEACLGGHPSCVKILLKHGAQVN 96
Cdd:pfam12796  31 RTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVKLLLEKGADIN 88
SOCS_ASB1 cd03720
SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a ...
 255-293 1.03e-06

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: 44.72  E-value: 1.03e-06
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 795277808 255 PPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLH 293
Cdd:cd03720    3 PRSLLSLCRIAVRRALGKQRLSLICSLPLPDPIKKFLLH 41
SOCS_ASB5 cd03724
SOCS (suppressors of cytokine signaling) box of ASB5-like proteins. ASB family members have a ...
 255-291 1.30e-06

SOCS (suppressors of cytokine signaling) box of ASB5-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ASB5 has been implicated in the initiation of arteriogenesis. 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: 239694  Cd Length: 42  Bit Score: 44.48  E-value: 1.30e-06
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 795277808 255 PPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFL 291
Cdd:cd03724    3 PSSLCQLCRLCIRNYIGRSRLHLIPQLQLPTLLKNFL 39
Ank_4 pfam13637
Ankyrin repeats (many copies);
136-187 1.62e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 1.62e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 795277808  136 SPIHEAARRGHVECVDFLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLL 187
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 94-227 2.20e-06

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: 48.92  E-value: 2.20e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808   94 QVNGVTTDWHTPLFNACVSGS-QDCVNLLLQHGASVQPESDLaspIHeAARRGHVECVDFLIAYGGNIDHKISHLG---- 168
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAVGDTL---LH-AISLEYVDAVEAILLHLLAAFRKSGPLEland 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  169 ----------TPLYLACENQQRACVKKLLESGADVN---------QGKGQD------SPLHAAARTASEELACLLMDFGA 223
Cdd:TIGR00870 120 qytseftpgiTALHLAAHRQNYEIVKLLLERGASVParacgdffvKSQGVDsfyhgeSPLNAAACLGSPSIVALLSEDPA 199


                  ....
gi 795277808  224 DTQA 227
Cdd:TIGR00870 200 DILT 203
Ank_4 pfam13637
Ankyrin repeats (many copies);
69-122 2.44e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 2.44e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 795277808   69 HVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSQDCVNLLL 122
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 44-129 2.92e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 2.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  44 AIYGRQ--LSLRNLISQGWLVNVITADHVSPLHEACLGG-HPSCVKILLKHGAQVNGVTTDWHTPLFNACvsGSQDCVNL 120
Cdd:PHA02876 415 ALCGTNpyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNI 492


                 ....*....
gi 795277808 121 LLQHGASVQ 129
Cdd:PHA02876 493 LLHYGAELR 501
SOCS_ASB13 cd03729
SOCS (suppressors of cytokine signaling) box of ASB13-like proteins. ASB family members have a ...
 255-294 5.35e-06

SOCS (suppressors of cytokine signaling) box of ASB13-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: 239699  Cd Length: 42  Bit Score: 42.46  E-value: 5.35e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 795277808 255 PPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLHL 294
Cdd:cd03729    3 PLSLQQLCRINLRKALGTRALEKIAKLNIPNRIIDYLSYN 42
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
 253-293 8.16e-06

SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ASB2 targets specific proteins to destruction by the proteasome in leukemia cells that have been induced to differentiate. 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: 239691  Cd Length: 45  Bit Score: 42.16  E-value: 8.16e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 795277808 253 EGPPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLH 293
Cdd:cd03721    1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNH 41
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 36-128 8.38e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 8.38e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  36 DWSPMHEAAIYGRQLSLRNLISQGWLVNVITADHVSPLHEACLGGHP-SCVKILLKHGAQVNGVTTDWHTPLFNACVSGS 114
Cdd:PHA02876 375 DKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNC 454

                         90
                 ....*....|....*
gi 795277808 115 Q-DCVNLLLQHGASV 128
Cdd:PHA02876 455 KlDVIEMLLDNGADV 469
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
 253-292 1.02e-05

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: 41.81  E-value: 1.02e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 795277808 253 EGPPSLMQLCRLRIRKCFGIqqhHKITKLVLPEDLKQFLL 292
Cdd:cd03717    1 TSVRSLQHLCRFVIRQCTRR---DLIDQLPLPRRLKDYLK 37
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
 255-292 1.92e-05

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


Pssm-ID: 239693  Cd Length: 48  Bit Score: 41.27  E-value: 1.92e-05
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 795277808 255 PPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLL 292
Cdd:cd03723    3 PRSLQHLCRCAIRKLLGSRCHKLVPQLSLPTSLKNYLL 40
SOCS_SSB1_4 cd03718
SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box ...
 255-293 1.95e-05

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: 41.13  E-value: 1.95e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 795277808 255 PPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLH 293
Cdd:cd03718    3 PLPLMDLCRRRVRVALGRDRLEEIEQLPLPPSLKNYLLY 41
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 102-236 4.52e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 44.62  E-value: 4.52e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 102 WHTPLFNACVSGSQDCVN-LLLQHGASVQPESDLA-SPIHEAARRGHVECVDFLI-AYGGNIDHKIS---HLG-TPLYLA 174
Cdd:cd22192   17 SESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGeTALHVAALYDNLEAAVVLMeAAPELVNEPMTsdlYQGeTALHIA 96

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 795277808 175 CENQQRACVKKLLESGADVNQG--------KGQDS-------PLHAAARTASEELACLLMDFGADTQAKNAEGKRPV 236
Cdd:cd22192   97 VVNQNLNLVRELIARGADVVSPratgtffrPGPKNliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 68-96 1.00e-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: 38.72  E-value: 1.00e-04
                           10        20
                   ....*....|....*....|....*....
gi 795277808    68 DHVSPLHEACLGGHPSCVKILLKHGAQVN 96
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02798 PHA02798
ankyrin-like protein; Provisional
 85-195 1.55e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 42.90  E-value: 1.55e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  85 VKILLKHGAQVNGVTTDWHTPLfnaCVSGSQ--------DCVNLLLQHGASV-QPESDLASPIHEAARRGHV---ECVDF 152
Cdd:PHA02798  54 VKLFINLGANVNGLDNEYSTPL---CTILSNikdykhmlDIVKILIENGADInKKNSDGETPLYCLLSNGYInnlEILLF 130

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 795277808 153 LIAYGGNI--DHKISHLGTPLYLACENQ-QRACVKKLLESGADVNQ 195
Cdd:PHA02798 131 MIENGADTtlLDKDGFTMLQVYLQSNHHiDIEIIKLLLEKGVDINT 176
PHA03095 PHA03095
ankyrin-like protein; Provisional
 16-158 1.86e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 42.70  E-value: 1.86e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  16 PRDSPDI-----RLLSNPLMSDaVSDWSPMHEAAIYG--RQLSLRNLISQGWLVNVITADHVSPLHEA-CLGGHPSCVKi 87
Cdd:PHA03095 198 FKPRARIvreliRAGCDPAATD-MLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAaVFNNPRACRR- 275

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 795277808  88 LLKHGAQVNGVTTDWHTPLFNACVSGSQDCVNLLLqhgaSVQPESDL-ASPIHEAARRGHV-------ECVDFLIAYGG 158
Cdd:PHA03095 276 LIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL----AKNPSAETvAATLNTASVAGGDipsdatrLCVAKVVLRGA 350
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 104-184 1.90e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 42.28  E-value: 1.90e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 104 TPLFNACVSGSQDCVNLLLQHGASVQPESDLA--SPIHEAARRGHVECVDFLIAYGGNIDHKISHLGTPLYLA---CENQ 178
Cdd:PHA02884  72 NPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkiTPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELAlmiCNNF 151


                 ....*.
gi 795277808 179 QRACVK 184
Cdd:PHA02884 152 LAFMIC 157
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 38-128 1.92e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.64  E-value: 1.92e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  38 SPMHEAAIYGRQLSLRNLISQGWLVNVITADHVSPLHEACLggHPSCVKILLKHGAQVNGVTTDWHTPLFNA----Cvsg 113
Cdd:PHA02874 192 SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAinppC--- 266

                         90
                 ....*....|....*
gi 795277808 114 SQDCVNLLLQHGASV 128
Cdd:PHA02874 267 DIDIIDILLYHKADI 281
SOCS_SSB4 cd03743
SOCS (suppressors of cytokine signaling) box of SSB4 (SPRY domain-containing SOCS box ...
 255-291 2.71e-04

SOCS (suppressors of cytokine signaling) box of SSB4 (SPRY domain-containing SOCS box proteins)-like proteins. SSB proteins contain a central SPRY domain and a C-terminal SOCS. SSB4 has been shown to bind to MET, the receptor protein-tyrosine kinase for hepatocyte growth factor (HGF). SSB4, like SSB2 and SSB1, also interacts with prostate apoptosis response protein-4. Both types of interactions are mediated through the SPRY domain. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239712  Cd Length: 42  Bit Score: 38.01  E-value: 2.71e-04
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 795277808 255 PPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFL 291
Cdd:cd03743    3 PLPLMDLCRRSARQALGRHRLHHIQSLPLPQTLKNYL 39
SOCS smart00253
suppressors of cytokine signalling; suppressors of cytokine signalling
 252-292 4.14e-04

suppressors of cytokine signalling; suppressors of cytokine signalling


Pssm-ID: 128549  Cd Length: 43  Bit Score: 37.28  E-value: 4.14e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 795277808   252 REGPPSLMQLCRLRIRKCFGIQQhhkITKLVLPEDLKQFLL 292
Cdd:smart00253   4 PSNVPSLQHLCRFTIRRCTRTDQ---IKTLPLPPKLKDYLS 41
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 136-161 5.06e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 5.06e-04
                           10        20
                   ....*....|....*....|....*.
gi 795277808   136 SPIHEAARRGHVECVDFLIAYGGNID 161
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 34-106 6.02e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.74  E-value: 6.02e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 795277808  34 VSDWSPMHEAAIYGRQLSLRNLISQGWLVNVITADHV-SPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPL 106
Cdd:PHA02884  68 NSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPI 141
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 169-194 6.93e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 6.93e-04
                           10        20
                   ....*....|....*....|....*.
gi 795277808   169 TPLYLACENQQRACVKKLLESGADVN 194
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 40-237 8.34e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.72  E-value: 8.34e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  40 MHEAAIYGRQLSLRNLISQGWLVNVITADHVSPLHEACLGGHPSCVKILLKHGAQVNgvttdwhtplfnacvsgsqdcVN 119
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN---------------------VK 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 120 lllqhgasvqpESDLASPIHEAARRGHVECVDFLIAYGGNIDHKISHLGTPLYLACENQQRACvkKLLESGADVN-QGKG 198
Cdd:PHA02874 187 -----------DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINdQDID 253

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 795277808 199 QDSPLHAAAR-TASEELACLLMDFGADTQAKNAEGKRPVE 237
Cdd:PHA02874 254 GSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPID 293
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 183-238 9.77e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 9.77e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 795277808 183 VKKLLESGADVN-QGKGQDSPLHAAARTASEELACLLMDFGADTQAKNAEGKRPVEL 238
Cdd:PTZ00322  98 ARILLTGGADPNcRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 39-199 1.10e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 1.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  39 PMHEAAIYGRQLSLRNLISQGWLVNVITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSgSQDCV 118
Cdd:PHA02874 160 PIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAI 238

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 119 NLLLQHGASVQPESDLASPIHEAARRG-HVECVDFLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESGADVNQGK 197
Cdd:PHA02874 239 ELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDIIANAVLIKEA 318


                 ..
gi 795277808 198 GQ 199
Cdd:PHA02874 319 DK 320
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 153-245 1.31e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 1.31e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 153 LIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN-QGKGQDSPLHAAARTASEELACLLM-------DFGAD 224
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTlLDKDGKTPLELAEENGFREVVQLLSrhsqchfELGAN 180

                         90       100
                 ....*....|....*....|.
gi 795277808 225 TQAKNAEGKRPVELvppDSPL 245
Cdd:PTZ00322 181 AKPDSFTGKPPSLE---DSPI 198
PHA02946 PHA02946
ankyin-like protein; Provisional
 52-239 1.32e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.04  E-value: 1.32e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  52 LRNLISQGWLVNVITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNacVSGSQDCVnlllqhgasvqpe 131
Cdd:PHA02946  55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYY--LSGTDDEV------------- 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 132 sdlaspiheaarrghVECVDFLIAYGGNIDHKISHLGTPLYLACENQQRACVKKLLESGAD---VNQGKGQDSPLHAAAR 208
Cdd:PHA02946 120 ---------------IERINLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEariVDKFGKNHIHRHLMSD 184

                        170       180       190
                 ....*....|....*....|....*....|.
gi 795277808 209 TASEELACLLMDFGADTQAKNAEGKRPVELV 239
Cdd:PHA02946 185 NPKASTISWMMKLGISPSKPDHDGNTPLHIV 215
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 71-96 1.35e-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: 1.35e-03
                          10        20
                  ....*....|....*....|....*..
gi 795277808   71 SPLHEACL-GGHPSCVKILLKHGAQVN 96
Cdd:pfam00023   4 TPLHLAAGrRGNLEIVKLLLSKGADVN 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 40-174 1.70e-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: 39.61  E-value: 1.70e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  40 MHEAAIYGR-QLSLRNLISQGWLVNV-ITAD---HVSPLHEACLGGHPSCVKILLKHGAQVNG--VTTDW---------- 102
Cdd:cd22192   55 LHVAALYDNlEAAVVLMEAAPELVNEpMTSDlyqGETALHIAVVNQNLNLVRELIARGADVVSprATGTFfrpgpknliy 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 103 ---HTPLFNACVsGSQDCVNLLLQHGASVQPESDLA-SPIH----EAARRGHVECVDFLIAYGGN-----IDHKISHLG- 168
Cdd:cd22192  135 ygeHPLSFAACV-GNEEIVRLLIEHGADIRAQDSLGnTVLHilvlQPNKTFACQMYDLILSYDKEddlqpLDLVPNNQGl 213


                 ....*.
gi 795277808 169 TPLYLA 174
Cdd:cd22192  214 TPFKLA 219
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
 253-293 2.30e-03

SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. Human ASB15 is expressed predominantly in skeletal muscle and participates in the regulation of protein turnover and muscle cell development by stimulating protein synthesis and regulating differentiation of muscle cells. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239701  Cd Length: 56  Bit Score: 35.58  E-value: 2.30e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 795277808 253 EGPPSLMQLCRLRIRKCFGIQQHHK---ITKLVLPEDLKQFLLH 293
Cdd:cd03731    1 ENPRPLKHLCRLKIRKLMGLQKLQQpssMKKLPLPPALKRYILY 44
Ank_4 pfam13637
Ankyrin repeats (many copies);
169-218 2.34e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 2.34e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 795277808  169 TPLYLACENQQRACVKKLLESGADVN-QGKGQDSPLHAAARTASEELACLL 218
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINaVDGNGETALHFAASNGNVEVLKLL 53
SOCS_SSB1 cd03744
SOCS (suppressors of cytokine signaling) box of SSB1 (SPRY domain-containing SOCS box proteins) ...
 255-293 2.49e-03

SOCS (suppressors of cytokine signaling) box of SSB1 (SPRY domain-containing SOCS box proteins)-like proteins. SSB proteins contain a central SPRY domain and a C-terminal SOCS. SSB1 has been shown to bind to MET, the receptor protein-tyrosine kinase for hepatocyte growth factor (HGF), both the absence and the presence of HGF and enhances the HGF-MET-induced mitogen-activated protein kinases Erk-transcription factor Elk-1-serum response elements (SRE) pathway. SSB1, like SSB2 and SSB4, also interacts with prostate apoptosis response protein-4. Both types of interactions are mediated through the SPRY domain. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239713  Cd Length: 42  Bit Score: 35.34  E-value: 2.49e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 795277808 255 PPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLH 293
Cdd:cd03744    3 PLPLMDLCRRSVRLALGRERLSEIHTLPLPASLKNYLLY 41
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 68-96 2.72e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.54  E-value: 2.72e-03
                          10        20
                  ....*....|....*....|....*....
gi 795277808   68 DHVSPLHEACLGGHPSCVKILLKHGAQVN 96
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADIN 29
SOCS_ASB7 cd03726
SOCS (suppressors of cytokine signaling) box of ASB7-like proteins. ASB family members have a ...
 255-293 3.22e-03

SOCS (suppressors of cytokine signaling) box of ASB7-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: 239696  Cd Length: 45  Bit Score: 34.82  E-value: 3.22e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 795277808 255 PPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLH 293
Cdd:cd03726    3 PRTLQDLCRIKIRHCIGLQNLKLLDELPIAKVMKDYLKH 41
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 78-231 3.29e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 38.71  E-value: 3.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808  78 LGGHPSCVKILLKHGAQVNGVTTDwhTPLFNACV---SGSQDCVNLLLQhgasVQPESDLASPIHEAarrghvECVDFLi 154
Cdd:cd21882    4 LLGLLECLRWYLTDSAYQRGATGK--TCLHKAALnlnDGVNEAIMLLLE----AAPDSGNPKELVNA------PCTDEF- 70

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 155 aYGGNidhkishlgTPLYLACENQQRACVKKLLESGADV-----------NQGKG---QDSPLHAAARTASEELACLLMD 220
Cdd:cd21882   71 -YQGQ---------TALHIAIENRNLNLVRLLVENGADVsaratgrffrkSPGNLfyfGELPLSLAACTNQEEIVRLLLE 140

                        170
                 ....*....|.
gi 795277808 221 FGADTQAKNAE 231
Cdd:cd21882  141 NGAQPAALEAQ 151
Ank_5 pfam13857
Ankyrin repeats (many copies);
60-106 3.56e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 3.56e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 795277808   60 WLVNVITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPL 106
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
SOCS_ASB14 cd03730
SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a ...
 253-293 3.73e-03

SOCS (suppressors of cytokine signaling) box of ASB14-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: 239700  Cd Length: 57  Bit Score: 35.21  E-value: 3.73e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 795277808 253 EGPPSLMQLCRLRIRKCFG---IQQHHKITKLVLPEDLKQFLLH 293
Cdd:cd03730    1 TNPRSLKHLCRLKIRACMGrlrLRCPVFMSFLPLPNRLKAYILY 44
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 136-162 3.84e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.16  E-value: 3.84e-03
                          10        20
                  ....*....|....*....|....*..
gi 795277808  136 SPIHEAARRGHVECVDFLIAYGGNIDH 162
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 115-194 4.79e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 38.18  E-value: 4.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 795277808 115 QDCVNLLLQHGASVQPESDLASPIHEAARRGHV--ECVDFLIAYGGNIDHKiSHLGTPL------YLACENQQRACVKKL 186
Cdd:PHA02989  16 KNALEFLLRTGFDVNEEYRGNSILLLYLKRKDVkiKIVKLLIDNGADVNYK-GYIETPLcavlrnREITSNKIKKIVKLL 94


                 ....*...
gi 795277808 187 LESGADVN 194
Cdd:PHA02989  95 LKFGADIN 102
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 136-163 6.85e-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: 33.80  E-value: 6.85e-03
                          10        20
                  ....*....|....*....|....*....
gi 795277808  136 SPIHEAA-RRGHVECVDFLIAYGGNIDHK 163
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
Ank_5 pfam13857
Ankyrin repeats (many copies);
121-174 8.40e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 33.86  E-value: 8.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 795277808  121 LLQHG--ASVQPESDLASPIHEAARRGHVECVDFLIAYGGNIDHKISHLGTPLYLA 174
Cdd:pfam13857   1 LLEHGpiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
 
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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