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Conserved domains on  [gi|1411183443|ref|XP_025228166|]
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ankyrin repeat and SOCS box protein 9 isoform X1 [Theropithecus gelada]

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 9.98e-40

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.47  E-value: 9.98e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  22 IRLLSNPLMSDAVSDWSPMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTD 101
Cdd:COG0666    40 LLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 102 WHTPLFNACVSGSRDCVNLLLQHGASV-QPESDLASPIHEAARRGHVECVDSLIAYGSNIDHKISHLGTPLYLACENQQR 180
Cdd:COG0666   120 GETPLHLAAYNGNLEIVKLLLEAGADVnAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL 199

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411183443 181 ACVKKLLESGADVN-QGKGQDSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPVELVPPDSPLARLFLERE 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 3.26e-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: 3.26e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1411183443 253 EGPPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLHL 294
Cdd:cd03728     1 EGPPSLMQLCRLCIRKCFGRKQHHKIHKLHLPEPLKHFLLYR 42
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-253 9.98e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.47  E-value: 9.98e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  22 IRLLSNPLMSDAVSDWSPMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTD 101
Cdd:COG0666    40 LLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 102 WHTPLFNACVSGSRDCVNLLLQHGASV-QPESDLASPIHEAARRGHVECVDSLIAYGSNIDHKISHLGTPLYLACENQQR 180
Cdd:COG0666   120 GETPLHLAAYNGNLEIVKLLLEAGADVnAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL 199

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411183443 181 ACVKKLLESGADVN-QGKGQDSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPVELVPPDSPLARLFLERE 253
Cdd:COG0666   200 EIVKLLLEAGADVNaKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
Ank_2 pfam12796
Ankyrin repeats (3 copies);
73-163 1.66e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  73 LHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSRDCVNLLLQHgASVQPESDLASPIHEAARRGHVECVDS 152
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|.
gi 1411183443 153 LIAYGSNIDHK 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 3.26e-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: 3.26e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1411183443 253 EGPPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLHL 294
Cdd:cd03728     1 EGPPSLMQLCRLCIRKCFGRKQHHKIHKLHLPEPLKHFLLYR 42
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 45-236 9.49e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 82.70  E-value: 9.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  45 IYGHQLSL-RNLI-SQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSRDCVNLLL 122
Cdd:PHA02874    9 IYSGDIEAiEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 123 QHG--ASVQPESDLASpiheaarrghvECVDSLIAYGSNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN-QGKGQ 199
Cdd:PHA02874   89 DNGvdTSILPIPCIEK-----------DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNiEDDNG 157

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1411183443 200 DSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPV 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 3.47e-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: 54.09  E-value: 3.47e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1411183443 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 5.87e-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: 5.87e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1411183443  256 PSLMQLCRLRIRKCFGiqqhhKITKLVLPEDLKQFLLH 293
Cdd:smart00969   1 RSLQHLCRLAIRRSLG-----GIDKLPLPPRLKDYLLY 33
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 94-227 2.77e-05

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: 45.46  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  94 QVNGVTTDWHTPLFNACVSGS-RDCVNLLLQHGASVQPESDLaspIHeAARRGHVECVDSLIAYGSNIDHKISHLG---- 168
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAVGDTL---LH-AISLEYVDAVEAILLHLLAAFRKSGPLEland 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 169 ----------TPLYLACENQQRACVKKLLESGADVN---------QGKGQD------SPLHAVARTASEELACLLMDFGA 223
Cdd:TIGR00870 120 qytseftpgiTALHLAAHRQNYEIVKLLLERGASVParacgdffvKSQGVDsfyhgeSPLNAAACLGSPSIVALLSEDPA 199


                  ....
gi 1411183443 224 DTQA 227
Cdd:TIGR00870 200 DILT 203
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 68-96 1.24e-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: 38.34  E-value: 1.24e-04
                           10        20
                   ....*....|....*....|....*....
gi 1411183443   68 DHVSPLHEACLGGHPSCVKILLKHGAQVN 96
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 73-221 2.62e-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: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  73 LHEACLGGHPSCVKILLKHGAQ-VN-GVTTDWH---TPLFNACVSGSRDCVNLLLQHGASVQpeSDLASPIheAARRGhv 147
Cdd:cd22192    55 LHVAALYDNLEAAVVLMEAAPElVNePMTSDLYqgeTALHIAVVNQNLNLVRELIARGADVV--SPRATGT--FFRPG-- 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411183443 148 ecVDSLIAYGsniDHKIShlgtplYLACENQQRAcVKKLLESGADVnqgKGQDS----PLHAVARTASEELACLLMDF 221
Cdd:cd22192   129 --PKNLIYYG---EHPLS------FAACVGNEEI-VRLLIEHGADI---RAQDSlgntVLHILVLQPNKTFACQMYDL 191
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
22-253 9.98e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.47  E-value: 9.98e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  22 IRLLSNPLMSDAVSDWSPMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTD 101
Cdd:COG0666    40 LLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKD 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 102 WHTPLFNACVSGSRDCVNLLLQHGASV-QPESDLASPIHEAARRGHVECVDSLIAYGSNIDHKISHLGTPLYLACENQQR 180
Cdd:COG0666   120 GETPLHLAAYNGNLEIVKLLLEAGADVnAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL 199

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1411183443 181 ACVKKLLESGADVN-QGKGQDSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPVELVPPDSPLARLFLERE 253
Cdd:COG0666   200 EIVKLLLEAGADVNaKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLL 273
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
36-234 2.58e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.93  E-value: 2.58e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  36 DWSPMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSR 115
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 116 DCVNLLLQHGASV-QPESDLASPIHEAARRGHVECVDSLIAYGSNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN 194
Cdd:COG0666   167 EIVKLLLEAGADVnARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLN 246

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1411183443 195 -QGKGQDSPLHAVARTASEELACLLMDFGADTQAKNAEGKR 234
Cdd:COG0666   247 aKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
21-294 8.54e-33

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.98  E-value: 8.54e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  21 DIRLLSNPLMSDAVSDWSPMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTT 100
Cdd:COG0666     6 LLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDD 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 101 DWHTPLFNACVSGSRDCVNLLLQHGASV-QPESDLASPIHEAARRGHVECVDSLIAYGSNIDHKISHLGTPLYLACENQQ 179
Cdd:COG0666    86 GGNTLLHAAARNGDLEIVKLLLEAGADVnARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGN 165

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 180 RACVKKLLESGADVN-QGKGQDSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPVEL--VPPDSPLARLFLEREGPP 256
Cdd:COG0666   166 LEIVKLLLEAGADVNaRDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLaaENGNLEIVKLLLEAGADL 245

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1411183443 257 SLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLHL 294
Cdd:COG0666   246 NAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
Ank_2 pfam12796
Ankyrin repeats (3 copies);
73-163 1.66e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 1.66e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  73 LHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSRDCVNLLLQHgASVQPESDLASPIHEAARRGHVECVDS 152
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|.
gi 1411183443 153 LIAYGSNIDHK 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 3.26e-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: 3.26e-19
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1411183443 253 EGPPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLHL 294
Cdd:cd03728     1 EGPPSLMQLCRLCIRKCFGRKQHHKIHKLHLPEPLKHFLLYR 42
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 45-236 9.49e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 82.70  E-value: 9.49e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  45 IYGHQLSL-RNLI-SQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSRDCVNLLL 122
Cdd:PHA02874    9 IYSGDIEAiEKIIkNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 123 QHG--ASVQPESDLASpiheaarrghvECVDSLIAYGSNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN-QGKGQ 199
Cdd:PHA02874   89 DNGvdTSILPIPCIEK-----------DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNiEDDNG 157

                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1411183443 200 DSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPV 236
Cdd:PHA02874  158 CYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPL 194
Ank_2 pfam12796
Ankyrin repeats (3 copies);
40-128 2.48e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 2.48e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  40 MHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHgAQVNGVTTDWhTPLFNACVSGSRDCVN 119
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78


                  ....*....
gi 1411183443 120 LLLQHGASV 128
Cdd:pfam12796  79 LLLEKGADI 87
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 85-239 1.89e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 79.15  E-value: 1.89e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  85 VKILLKHGAQVNGVTTDW-HTPLFNACVSGSRDCVNLLLQHGASVQ-PESDLASPIHEAARRGHVECVDSLIAYGSNIDH 162
Cdd:PHA02878  150 TKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNiPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 163 KISHLGTPLYLA---CENQQraCVKKLLESGADVNQGKG--QDSPLHAVARtaSEELACLLMDFGADTQAKNAEGKRPVE 237
Cdd:PHA02878  230 RDKCGNTPLHISvgyCKDYD--ILKLLLEHGVDVNAKSYilGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLS 305


                  ..
gi 1411183443 238 LV 239
Cdd:PHA02878  306 SA 307
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 38-236 3.47e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 78.57  E-value: 3.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  38 SPMHEAaIYGHQLS--LRNLISQGWLVNIITADHVSPLHEACLGGHPS-CVKILLKHGAQVNGVTTDWHTPLFNA-CVSG 113
Cdd:PHA02876  275 TPLHHA-SQAPSLSrlVPKLLERGADVNAKNIKGETPLYLMAKNGYDTeNIRTLIMLGADVNAADRLYITPLHQAsTLDR 353

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 114 SRDCVNLLLQHGASVQPESDL-ASPIHEAARRGHVECVDSLIAYGSNIDHKISHLGTPLYLA-CENQQRACVKKLLESGA 191
Cdd:PHA02876  354 NKDIVITLLELGANVNARDYCdKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFAlCGTNPYMSVKTLIDRGA 433

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1411183443 192 DVN-QGKGQDSPLH-AVARTASEELACLLMDFGADTQAKNAEGKRPV 236
Cdd:PHA02876  434 NVNsKNKDLSTPLHyACKKNCKLDVIEMLLDNGADVNAINIQNQYPL 480
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 17-230 2.03e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.86  E-value: 2.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  17 RDSPDIRLLSNPLMSDaVSDWS---PMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGH-----PSCVKIL 88
Cdd:PHA03100   14 KVKNIKYIIMEDDLND-YSYKKpvlPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  89 LKHGAQVNGVTTDWHTPLFNACV--SGSRDCVNLLLQHGASVQP-ESDLASPIHEAARRGHVEC---------------- 149
Cdd:PHA03100   93 LEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIkNSDGENLLHLYLESNKIDLkilkllidkgvdinak 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 150 --VDSLIAYGSNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN--QGKGqDSPLHAVARTASEELACLLMDFGADT 225
Cdd:PHA03100  173 nrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNlvNKYG-DTPLHIAILNNNKEIFKLLLNNGPSI 251


                  ....*
gi 1411183443 226 QAKNA 230
Cdd:PHA03100  252 KTIIE 256
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
 253-293 2.54e-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: 65.59  E-value: 2.54e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1411183443 253 EGPPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLH 293
Cdd:cd03716     1 STPRSLQHLCRLAIRRCLGRRRLELIKKLPLPPRLKDYLLY 41
Ank_2 pfam12796
Ankyrin repeats (3 copies);
138-229 3.74e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 3.74e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 138 IHEAARRGHVECVDSLIAYGSNIDHKISHLGTPLYLACENQQRACVKKLLESgADVNQGKGQDSPLHAVARTASEELACL 217
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 1411183443 218 LMDFGADTQAKN 229
Cdd:pfam12796  80 LLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 51-239 5.28e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.62  E-value: 5.28e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  51 SLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPL--FNACVSGSRDCVN---LLLQHG 125
Cdd:PHA03100   17 NIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhyLSNIKYNLTDVKEivkLLLEYG 96

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 126 ASVQPESDLA-SPIHEAA--RRGHVECVDSLIAYGSNIDHKISHLGTPL--YLACENQQRACVKKLLESGADVNQ----- 195
Cdd:PHA03100   97 ANVNAPDNNGiTPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLhlYLESNKIDLKILKLLIDKGVDINAknrvn 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1411183443 196 ---GKGQD---------SPLHAVARTASEELACLLMDFGADTQAKNAEGKRPVELV 239
Cdd:PHA03100  177 yllSYGVPinikdvygfTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
 255-293 6.50e-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: 61.72  E-value: 6.50e-13
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1411183443 255 PPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLH 293
Cdd:cd03587     2 PRSLQHLCRLAIRRCLGKRRLDLIDKLPLPPRLKDYLLY 40
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 43-193 3.10e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.82  E-value: 3.10e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  43 AAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSRDCVNLLL 122
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1411183443 123 QHGASVQPES--DLaspIHEAARRGHVECVDSLIAYGSNIDHKISHLGTPLYLACENQQRACVKKLLESGADV 193
Cdd:PLN03192  612 HFASISDPHAagDL---LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 17-194 5.99e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.40  E-value: 5.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  17 RDSPDIRLLsnpLMSDAVSDW------SPMHEAAIYGHQLSLRNLISQGWLVN-IITADHVSPLHEACLGGHPSCVKILL 89
Cdd:PHA02875   46 RDSEAIKLL---MKHGAIPDVkypdieSELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLI 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  90 KHGAQVNGVTTDWHTPLFNACVSGSRDCVNLLLQHGASVQPESDLA-SPIHEAARRGHVECVDSLIAYGSNIDHkISHLG 168
Cdd:PHA02875  123 ARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGcTPLIIAMAKGDIAICKMLLDSGANIDY-FGKNG 201

                         170       180
                  ....*....|....*....|....*...
gi 1411183443 169 --TPLYLACENQQRACVKKLLESGADVN 194
Cdd:PHA02875  202 cvAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 37-225 1.10e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 64.63  E-value: 1.10e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  37 WSPMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVT-TDWHTPLFNACVSGSR 115
Cdd:PHA02875   36 ISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFyKDGMTPLHLATILKKL 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 116 DCVNLLLQHGASVQ-PESDLASPIHEAARRGHVECVDSLIAYGSNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN 194
Cdd:PHA02875  116 DIMKLLIARGADPDiPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195

                         170       180       190
                  ....*....|....*....|....*....|...
gi 1411183443 195 Q-GKGQDSPLHAVA-RTASEELACLLMDFGADT 225
Cdd:PHA02875  196 YfGKNGCVAALCYAiENNKIDIVRLFIKRGADC 228
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 51-237 1.79e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.21  E-value: 1.79e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  51 SLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSRDCVNLLLQHGASVQ- 129
Cdd:PHA02874  106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANv 185

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 130 PESDLASPIHEAARRGHVECVDSLIAYGSNIDHKISHLGTPLYLACENQQRACvkKLLESGADVN-QGKGQDSPLH-AVA 207
Cdd:PHA02874  186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAI--ELLINNASINdQDIDGSTPLHhAIN 263

                         170       180       190
                  ....*....|....*....|....*....|
gi 1411183443 208 RTASEELACLLMDFGADTQAKNAEGKRPVE 237
Cdd:PHA02874  264 PPCDIDIIDILLYHKADISIKDNKGENPID 293
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 254-292 3.47e-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: 54.09  E-value: 3.47e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1411183443 254 GPPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLL 292
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
PHA03095 PHA03095
ankyrin-like protein; Provisional
 72-259 7.21e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.27  E-value: 7.21e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  72 PLHeACLGG---HPSCVKILLKHGAQVNGVTTDWHTPLfnACVSGSRDC----VNLLLQHGASV-QPESDLASPIHEAAR 143
Cdd:PHA03095  120 PLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSRNAnvelLRLLIDAGADVyAVDDRFRSLLHHHLQ 196

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 144 --RGHVECVDSLIAYGSNIDHKISHLGTPL-YLACENQQRAC-VKKLLESGADVN--QGKGQdSPLHAVARTASEELACL 217
Cdd:PHA03095  197 sfKPRARIVRELIRAGCDPAATDMLGNTPLhSMATGSSCKRSlVLPLLIAGISINarNRYGQ-TPLHYAAVFNNPRACRR 275

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....
gi 1411183443 218 LMDFGADTQAKNAEGKRPVE--LVPPDSPLARLFLEREGPPSLM 259
Cdd:PHA03095  276 LIALGADINAVSSDGNTPLSlmVRNNNGRAVRAALAKNPSAETV 319
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 40-259 9.77e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.85  E-value: 9.77e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  40 MHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSRDCVN 119
Cdd:PHA02875    6 LCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVE 85

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 120 LLLQHGASVQP--ESDLASPIHEAARRGHVECVDSLIAYGSNIDHKISHLGTPLYLACENQQRACVKKLLESGA--DVNQ 195
Cdd:PHA02875   86 ELLDLGKFADDvfYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAclDIED 165

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1411183443 196 GKGQDSPLHAVARtASEELACLLMDFGADTqakNAEGKRP--------VELVPPDspLARLFLEREGPPSLM 259
Cdd:PHA02875  166 CCGCTPLIIAMAK-GDIAICKMLLDSGANI---DYFGKNGcvaalcyaIENNKID--IVRLFIKRGADCNIM 231
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 55-167 1.84e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 1.84e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  55 LISQGWLVNIITADHVSPLHEACLGGHP--SCVKILLKHGAQVN-----------GVTTDW-----HTPLFNACVSGSRD 116
Cdd:PHA03100  127 LLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINaknrvnyllsyGVPINIkdvygFTPLHYAVYNNNPE 206

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1411183443 117 CVNLLLQHGASVQPESDLA-SPIHEAARRGHVECVDSLIAYGSNIDHKISHL 167
Cdd:PHA03100  207 FVKYLLDLGANPNLVNKYGdTPLHIAILNNNKEIFKLLLNNGPSIKTIIETL 258
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 30-183 5.36e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 56.81  E-value: 5.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  30 MSDAVSDWSPMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNA 109
Cdd:PHA02878  162 MKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411183443 110 CVS-GSRDCVNLLLQHGASVQPESDLA--SPIHEAARRGHVecVDSLIAYGSNIDHKISHLGTPLYLACenQQRACV 183
Cdd:PHA02878  242 VGYcKDYDILKLLLEHGVDVNAKSYILglTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSAV--KQYLCI 314
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 39-236 3.17e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.50  E-value: 3.17e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  39 PMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNgvttdwhtpLFNACVSGSRDCV 118
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCS---------VFYTLVAIKDAFN 110

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 119 N--------LLLQHGASVQpESDLASpIHEAARRGHVEC--VDSLIAYGSNIDHKISHLG-TPLYLACENQQRACVKKLL 187
Cdd:PHA02878  111 NrnveifkiILTNRYKNIQ-TIDLVY-IDKKSKDDIIEAeiTKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLL 188

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1411183443 188 ESGADVNQ-GKGQDSPLHAVARTASEELACLLMDFGADTQAKNAEGKRPV 236
Cdd:PHA02878  189 SYGANVNIpDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 86-239 3.69e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 54.30  E-value: 3.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  86 KILLKHGAQVNGVTTDWHTPLFNACVSGSRDCVNLLLQHGASVQPES-DLASPIHEAARRGHVECVDSLIAYGSNIDHKi 164
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIAlDDLSVLECAVDSKNIDTIKAIIDNRSNINKN- 240

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411183443 165 shlGTPLYLACENQQRACVKKLLESGADVNQ-GKGQDSPLHAVARTAS-EELACLLMDFGADTQAKNAEGKRPVELV 239
Cdd:PHA02876  241 ---DLSLLKAIRNEDLETSLLLYDAGFSVNSiDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLYLM 314
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 42-132 9.83e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 9.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  42 EAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSRDCVNLL 121
Cdd:PTZ00322   88 QLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167

                          90
                  ....*....|....*...
gi 1411183443 122 LQH-------GASVQPES 132
Cdd:PTZ00322  168 SRHsqchfelGANAKPDS 185
Ank_2 pfam12796
Ankyrin repeats (3 copies);
37-96 1.15e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.57  E-value: 1.15e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  37 WSPMHEAAIYGHQLSLRNLISQgWLVNIITaDHVSPLHEACLGGHPSCVKILLKHGAQVN 96
Cdd:pfam12796  31 RTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADIN 88
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 55-229 1.21e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.76  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  55 LISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSRDCVNLLLQHGASVQpESDL 134
Cdd:PHA02876  164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNIN-KNDL 242

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 135 AspIHEAARRGHVECvdSLIAY--GSNIDHKISHLGTPLYLACENQQRA-CVKKLLESGADVNQG--KGQdSPLHAVART 209
Cdd:PHA02876  243 S--LLKAIRNEDLET--SLLLYdaGFSVNSIDDCKNTPLHHASQAPSLSrLVPKLLERGADVNAKniKGE-TPLYLMAKN 317

                         170       180
                  ....*....|....*....|..
gi 1411183443 210 A--SEELACLLMdFGADTQAKN 229
Cdd:PHA02876  318 GydTENIRTLIM-LGADVNAAD 338
Ank_4 pfam13637
Ankyrin repeats (many copies);
37-89 3.61e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 3.61e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1411183443  37 WSPMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILL 89
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
69-122 5.74e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 5.74e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1411183443  69 HVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNACVSGSRDCVNLLL 122
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
 256-293 5.87e-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: 5.87e-07
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 1411183443  256 PSLMQLCRLRIRKCFGiqqhhKITKLVLPEDLKQFLLH 293
Cdd:smart00969   1 RSLQHLCRLAIRRSLG-----GIDKLPLPPRLKDYLLY 33
PHA03095 PHA03095
ankyrin-like protein; Provisional
 118-236 7.59e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.02  E-value: 7.59e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 118 VNLLLQHGASVQPESDLAS-PIHEAARRGHVEC---VDSLIAYGSNIDHKISHLGTPLYLACENQQRACVKKLL-ESGAD 192
Cdd:PHA03095   30 VRRLLAAGADVNFRGEYGKtPLHLYLHYSSEKVkdiVRLLLEAGADVNAPERCGFTPLHLYLYNATTLDVIKLLiKAGAD 109

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1411183443 193 VN-QGKGQDSPLHAVARTAS--EELACLLMDFGADTQAKNAEGKRPV 236
Cdd:PHA03095  110 VNaKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNALDLYGMTPL 156
SOCS_ASB1 cd03720
SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a ...
 255-293 1.25e-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: 44.33  E-value: 1.25e-06
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1411183443 255 PPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLH 293
Cdd:cd03720     3 PRSLLSLCRIAVRRALGKQRLSLICSLPLPDPIKKFLLH 41
Ank_4 pfam13637
Ankyrin repeats (many copies);
136-187 1.35e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 1.35e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1411183443 136 SPIHEAARRGHVECVDSLIAYGSNIDHKISHLGTPLYLACENQQRACVKKLL 187
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SOCS_ASB5 cd03724
SOCS (suppressors of cytokine signaling) box of ASB5-like proteins. ASB family members have a ...
 255-291 1.36e-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: 1.36e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1411183443 255 PPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFL 291
Cdd:cd03724     3 PSSLCQLCRLCIRNYIGRSRLHLIPQLQLPTLLKNFL 39
Ank_4 pfam13637
Ankyrin repeats (many copies);
102-154 3.45e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 3.45e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1411183443 102 WHTPLFNACVSGSRDCVNLLLQHGASV--QPESDLaSPIHEAARRGHVECVDSLI 154
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADInaVDGNGE-TALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 44-129 5.41e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.75  E-value: 5.41e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  44 AIYGHQ--LSLRNLISQGWLVNIITADHVSPLHEACLGG-HPSCVKILLKHGAQVNGVTTDWHTPLFNACvsGSRDCVNL 120
Cdd:PHA02876  415 ALCGTNpyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNI 492


                  ....*....
gi 1411183443 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 5.57e-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: 5.57e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1411183443 255 PPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLHL 294
Cdd:cd03729     3 PLSLQQLCRINLRKALGTRALEKIAKLNIPNRIIDYLSYN 42
PHA03095 PHA03095
ankyrin-like protein; Provisional
 41-235 6.22e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 47.33  E-value: 6.22e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  41 HEAAIYGHQLS--------LRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKI---LLKHGAQVNGVTTDWHTPLF-- 107
Cdd:PHA03095   11 MEAALYDYLLNasnvtveeVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHly 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 108 --NACVsgsRDCVNLLLQHGASVQPESDLA-SPIHEAAR--RGHVECVDSLIAYGSNIDHKISHLGTPL--YLACENQQR 180
Cdd:PHA03095   91 lyNATT---LDVIKLLIKAGADVNAKDKVGrTPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGMTPLavLLKSRNANV 167

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1411183443 181 ACVKKLLESGADV----NQGkgqDSPLHAVARTASEELACL--LMDFGADTQAKNAEGKRP 235
Cdd:PHA03095  168 ELLRLLIDAGADVyavdDRF---RSLLHHHLQSFKPRARIVreLIRAGCDPAATDMLGNTP 225
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 36-128 7.80e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 7.80e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  36 DWSPMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLGGHP-SCVKILLKHGAQVNGVTTDWHTPLFNACVSGS 114
Cdd:PHA02876  375 DKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPyMSVKTLIDRGANVNSKNKDLSTPLHYACKKNC 454

                          90
                  ....*....|....*
gi 1411183443 115 R-DCVNLLLQHGASV 128
Cdd:PHA02876  455 KlDVIEMLLDNGADV 469
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
 253-293 8.57e-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: 8.57e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1411183443 253 EGPPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLH 293
Cdd:cd03721     1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNH 41
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
 253-292 1.16e-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: 41.43  E-value: 1.16e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1411183443 253 EGPPSLMQLCRLRIRKCFGIqqhHKITKLVLPEDLKQFLL 292
Cdd:cd03717     1 TSVRSLQHLCRFVIRQCTRR---DLIDQLPLPRRLKDYLK 37
SOCS_SSB1_4 cd03718
SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box ...
 255-293 1.91e-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: 1.91e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1411183443 255 PPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLH 293
Cdd:cd03718     3 PLPLMDLCRRRVRVALGRDRLEEIEQLPLPPSLKNYLLY 41
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
 255-292 2.32e-05

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


Pssm-ID: 239693  Cd Length: 48  Bit Score: 40.89  E-value: 2.32e-05
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1411183443 255 PPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLL 292
Cdd:cd03723     3 PRSLQHLCRCAIRKLLGSRCHKLVPQLSLPTSLKNYLL 40
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 94-227 2.77e-05

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: 45.46  E-value: 2.77e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  94 QVNGVTTDWHTPLFNACVSGS-RDCVNLLLQHGASVQPESDLaspIHeAARRGHVECVDSLIAYGSNIDHKISHLG---- 168
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIENEnLELTELLLNLSCRGAVGDTL---LH-AISLEYVDAVEAILLHLLAAFRKSGPLEland 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 169 ----------TPLYLACENQQRACVKKLLESGADVN---------QGKGQD------SPLHAVARTASEELACLLMDFGA 223
Cdd:TIGR00870 120 qytseftpgiTALHLAAHRQNYEIVKLLLERGASVParacgdffvKSQGVDsfyhgeSPLNAAACLGSPSIVALLSEDPA 199


                  ....
gi 1411183443 224 DTQA 227
Cdd:TIGR00870 200 DILT 203
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 68-96 1.24e-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: 38.34  E-value: 1.24e-04
                           10        20
                   ....*....|....*....|....*....
gi 1411183443   68 DHVSPLHEACLGGHPSCVKILLKHGAQVN 96
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 38-128 2.58e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.26  E-value: 2.58e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  38 SPMHEAAIYGHQLSLRNLISQGWLVNIITADHVSPLHEACLggHPSCVKILLKHGAQVNGVTTDWHTPLFNA----Cvsg 113
Cdd:PHA02874  192 SPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAinppC--- 266

                          90
                  ....*....|....*
gi 1411183443 114 SRDCVNLLLQHGASV 128
Cdd:PHA02874  267 DIDIIDILLYHKADI 281
SOCS_SSB4 cd03743
SOCS (suppressors of cytokine signaling) box of SSB4 (SPRY domain-containing SOCS box ...
 255-291 2.61e-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: 2.61e-04
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1411183443 255 PPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFL 291
Cdd:cd03743     3 PLPLMDLCRRSARQALGRHRLHHIQSLPLPQTLKNYL 39
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 104-184 3.63e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 41.51  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 104 TPLFNACVSGSRDCVNLLLQHGASVQPESDLA--SPIHEAARRGHVECVDSLIAYGSNIDHKISHLGTPLYLA---CENQ 178
Cdd:PHA02884   72 NPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkiTPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELAlmiCNNF 151


                  ....*.
gi 1411183443 179 QRACVK 184
Cdd:PHA02884  152 LAFMIC 157
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 34-121 4.05e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 41.12  E-value: 4.05e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  34 VSDWSPMHEAAIYGHQLSLRNLISQGWLVNIITADHV-SPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNAcvs 112
Cdd:PHA02884   68 NSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELA--- 144


                  ....*....
gi 1411183443 113 gSRDCVNLL 121
Cdd:PHA02884  145 -LMICNNFL 152
SOCS smart00253
suppressors of cytokine signalling; suppressors of cytokine signalling
 252-292 4.53e-04

suppressors of cytokine signalling; suppressors of cytokine signalling


Pssm-ID: 128549  Cd Length: 43  Bit Score: 37.28  E-value: 4.53e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1411183443  252 REGPPSLMQLCRLRIRKCFGIQQhhkITKLVLPEDLKQFLL 292
Cdd:smart00253   4 PSNVPSLQHLCRFTIRRCTRTDQ---IKTLPLPPKLKDYLS 41
PHA03095 PHA03095
ankyrin-like protein; Provisional
 16-122 7.64e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 40.78  E-value: 7.64e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  16 PRDSPDI-----RLLSNPLMSDaVSDWSPMHEAAIYG--HQLSLRNLISQGWLVNIITADHVSPLHEA-CLGGHPSCVKi 87
Cdd:PHA03095  198 FKPRARIvreliRAGCDPAATD-MLGNTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAaVFNNPRACRR- 275

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1411183443  88 LLKHGAQVNGVTTDWHTPLFNACVSGSRDCVNLLL 122
Cdd:PHA03095  276 LIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 169-194 8.35e-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: 36.03  E-value: 8.35e-04
                           10        20
                   ....*....|....*....|....*.
gi 1411183443  169 TPLYLACENQQRACVKKLLESGADVN 194
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 71-96 1.56e-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: 35.34  E-value: 1.56e-03
                          10        20
                  ....*....|....*....|....*..
gi 1411183443  71 SPLHEACL-GGHPSCVKILLKHGAQVN 96
Cdd:pfam00023   4 TPLHLAAGrRGNLEIVKLLLSKGADVN 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 85-195 1.67e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.82  E-value: 1.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  85 VKILLKHGAQVNGVTTDWHTPLfnaCVSGSR--------DCVNLLLQHGASV-QPESDLASPIHEAARRGHV---ECVDS 152
Cdd:PHA02798   54 VKLFINLGANVNGLDNEYSTPL---CTILSNikdykhmlDIVKILIENGADInKKNSDGETPLYCLLSNGYInnlEILLF 130

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1411183443 153 LIAYGSNI--DHKISHLGTPLYLACENQ-QRACVKKLLESGADVNQ 195
Cdd:PHA02798  131 MIENGADTtlLDKDGFTMLQVYLQSNHHiDIEIIKLLLEKGVDINT 176
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 1411183443 253 EGPPSLMQLCRLRIRKCFGIQQHHK---ITKLVLPEDLKQFLLH 293
Cdd:cd03731     1 ENPRPLKHLCRLKIRKLMGLQKLQQpssMKKLPLPPALKRYILY 44
Ank_5 pfam13857
Ankyrin repeats (many copies);
60-106 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 1411183443  60 WLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPL 106
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
SOCS_SSB1 cd03744
SOCS (suppressors of cytokine signaling) box of SSB1 (SPRY domain-containing SOCS box proteins) ...
 255-293 2.47e-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: 2.47e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1411183443 255 PPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLH 293
Cdd:cd03744     3 PLPLMDLCRRSVRLALGRERLSEIHTLPLPASLKNYLLY 41
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 73-221 2.62e-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: 2.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  73 LHEACLGGHPSCVKILLKHGAQ-VN-GVTTDWH---TPLFNACVSGSRDCVNLLLQHGASVQpeSDLASPIheAARRGhv 147
Cdd:cd22192    55 LHVAALYDNLEAAVVLMEAAPElVNePMTSDLYqgeTALHIAVVNQNLNLVRELIARGADVV--SPRATGT--FFRPG-- 128

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1411183443 148 ecVDSLIAYGsniDHKIShlgtplYLACENQQRAcVKKLLESGADVnqgKGQDS----PLHAVARTASEELACLLMDF 221
Cdd:cd22192   129 --PKNLIYYG---EHPLS------FAACVGNEEI-VRLLIEHGADI---RAQDSlgntVLHILVLQPNKTFACQMYDL 191
PHA02946 PHA02946
ankyin-like protein; Provisional
 52-239 3.06e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.88  E-value: 3.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443  52 LRNLISQGWLVNIITADHVSPLHEACLGGHPSCVKILLKHGAQVNGVTTDWHTPLFNacVSGSRDCVnlllqhgasvqpe 131
Cdd:PHA02946   55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYY--LSGTDDEV------------- 119

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 132 sdlaspiheaarrghVECVDSLIAYGSNIDHKISHLGTPLYLACENQQRACVKKLLESGAD---VNQGKGQDSPLHAVAR 208
Cdd:PHA02946  120 ---------------IERINLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEariVDKFGKNHIHRHLMSD 184

                         170       180       190
                  ....*....|....*....|....*....|.
gi 1411183443 209 TASEELACLLMDFGADTQAKNAEGKRPVELV 239
Cdd:PHA02946  185 NPKASTISWMMKLGISPSKPDHDGNTPLHIV 215
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 68-96 3.18e-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: 3.18e-03
                          10        20
                  ....*....|....*....|....*....
gi 1411183443  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 3.35e-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: 3.35e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1411183443 255 PPSLMQLCRLRIRKCFGIQQHHKITKLVLPEDLKQFLLH 293
Cdd:cd03726     3 PRTLQDLCRIKIRHCIGLQNLKLLDELPIAKVMKDYLKH 41
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 1411183443 253 EGPPSLMQLCRLRIRKCFG---IQQHHKITKLVLPEDLKQFLLH 293
Cdd:cd03730     1 TNPRSLKHLCRLKIRACMGrlrLRCPVFMSFLPLPNRLKAYILY 44
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 102-236 4.19e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 38.46  E-value: 4.19e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 102 WHTPLFNACVSGSRDCVN-LLLQHGASVQPESDLA-SPIHEAARRGHVECVDSLI-AYGSNIDHKIS---HLG-TPLYLA 174
Cdd:cd22192    17 SESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGeTALHVAALYDNLEAAVVLMeAAPELVNEPMTsdlYQGeTALHIA 96

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1411183443 175 CENQQRACVKKLLESGADVNQG--------KGQDS-------PLHAVARTASEELACLLMDFGADTQAKNAEGKRPV 236
Cdd:cd22192    97 VVNQNLNLVRELIARGADVVSPratgtffrPGPKNliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 153-245 5.46e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 38.34  E-value: 5.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1411183443 153 LIAYGSNIDHKISHLGTPLYLACENQQRACVKKLLESGADVN-QGKGQDSPLHAVARTASEELACLLM-------DFGAD 224
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTlLDKDGKTPLELAEENGFREVVQLLSrhsqchfELGAN 180

                          90       100
                  ....*....|....*....|.
gi 1411183443 225 TQAKNAEGKRPVELvppDSPL 245
Cdd:PTZ00322  181 AKPDSFTGKPPSLE---DSPI 198
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 101-128 5.74e-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: 33.72  E-value: 5.74e-03
                           10        20
                   ....*....|....*....|....*...
gi 1411183443  101 DWHTPLFNACVSGSRDCVNLLLQHGASV 128
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADI 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 136-161 7.12e-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: 33.33  E-value: 7.12e-03
                           10        20
                   ....*....|....*....|....*.
gi 1411183443  136 SPIHEAARRGHVECVDSLIAYGSNID 161
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
 
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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