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Conserved domains on  [gi|1654220539|ref|NP_001164219|]
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ankyrin repeat and SOCS box protein 14 isoform 1 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
74-351 4.91e-47

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 166.67  E-value: 4.91e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539  74 AFDEANGNGWLPLHKAAVQLNKNILEITMNASEPSTWERTTHNGETALFLAVSSSLLENAHFLLLKGCNPNAKTSEGNSP 153
Cdd:COG0666    11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 154 LLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLASGAYPDARSSYGFTPLALAAQGGHTGIMQ 233
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 234 LLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGADANIPKSSGHLPIHVAADKGHFLALKVLVPVT-DIAAIKK 312
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGaDLNAKDK 250
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1654220539 313 SGISPVHCAAAGAHPHCLELLIQAGFDVNFMLDQRIRKH 351
Cdd:COG0666   251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
SOCS super family cl02533
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
529-585 6.70e-34

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.


The actual alignment was detected with superfamily member cd03730:

Pssm-ID: 470605  Cd Length: 57  Bit Score: 122.65  E-value: 6.70e-34
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1654220539 529 TNPRSLQHLCRLKIRKCMGRLRLRCPVFMSFLPLPNLLKAYVLYKEYDLFGQERSTG 585
Cdd:cd03730     1 TNPRSLKHLCRLKIRACMGRLRLRCPVFMSFLPLPNRLKAYILYKEYDLYGQGIFTG 57
Ank_2 pfam12796
Ankyrin repeats (3 copies);
319-413 7.84e-11

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.59  E-value: 7.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 319 HCAAAGAHPHCLELLIQAGFDVNFMldqrirkhyDDQRKSALYFAVSNGDLPSVKLLLSAGALPNQDP-VNCLQIALRMG 397
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQ---------DKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNgRTALHYAARSG 72
                          90
                  ....*....|....*.
gi 1654220539 398 NYELISLLLRHGANVN 413
Cdd:pfam12796  73 HLEIVKLLLEKGADIN 88
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
74-351 4.91e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 166.67  E-value: 4.91e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539  74 AFDEANGNGWLPLHKAAVQLNKNILEITMNASEPSTWERTTHNGETALFLAVSSSLLENAHFLLLKGCNPNAKTSEGNSP 153
Cdd:COG0666    11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 154 LLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLASGAYPDARSSYGFTPLALAAQGGHTGIMQ 233
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 234 LLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGADANIPKSSGHLPIHVAADKGHFLALKVLVPVT-DIAAIKK 312
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGaDLNAKDK 250
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1654220539 313 SGISPVHCAAAGAHPHCLELLIQAGFDVNFMLDQRIRKH 351
Cdd:COG0666   251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
SOCS_ASB14 cd03730
SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a ...
529-585 6.70e-34

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: 122.65  E-value: 6.70e-34
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1654220539 529 TNPRSLQHLCRLKIRKCMGRLRLRCPVFMSFLPLPNLLKAYVLYKEYDLFGQERSTG 585
Cdd:cd03730     1 TNPRSLKHLCRLKIRACMGRLRLRCPVFMSFLPLPNRLKAYILYKEYDLYGQGIFTG 57
PHA02875 PHA02875
ankyrin repeat protein; Provisional
116-343 6.96e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 95.44  E-value: 6.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 116 NGETALFLAVSSSLLENAHFLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGR 195
Cdd:PHA02875    1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 196 LDMVKLMLASGAYP-DARSSYGFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGAD 274
Cdd:PHA02875   81 VKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654220539 275 ANIPKSSGHLPIHVAADKGHFLALKVLVPV-TDIAAIKKSGISPVHCAAA-GAHPHCLELLIQAGFDVNFM 343
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSgANIDYFGKNGCVAALCYAIeNNKIDIVRLFIKRGADCNIM 231
Ank_2 pfam12796
Ankyrin repeats (3 copies);
154-245 1.99e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 1.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 154 LLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLasgAYPDARS-SYGFTPLALAAQGGHTGIM 232
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL---EHADVNLkDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|...
gi 1654220539 233 QLLLQKGADVHSQ 245
Cdd:pfam12796  78 KLLLEKGADINVK 90
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
530-571 1.96e-11

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: 58.72  E-value: 1.96e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1654220539 530 NPRSLQHLCRLKIRKCMGRlrlRCPVFMSFLPLPNLLKAYVL 571
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGK---RRLGAIDKLPLPPLLKDYLL 39
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
118-302 5.91e-11

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: 65.03  E-value: 5.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 118 ETALFLAVSSSLLENAHFLLL-KGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGAD-VNLRCANE----RTALHEAA 191
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSDlyqgETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 192 KLGRLDMVKLMLASGA--------------YPDARSSYGFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVL---- 253
Cdd:cd22192    98 VNQNLNLVRELIARGAdvvspratgtffrpGPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhilv 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1654220539 254 LEAVRGGNPEAVSLLLEYGADAN------IPKSSGHLPIHVAADKGHFLALKVLV 302
Cdd:cd22192   178 LQPNKTFACQMYDLILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLV 232
Ank_2 pfam12796
Ankyrin repeats (3 copies);
319-413 7.84e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.59  E-value: 7.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 319 HCAAAGAHPHCLELLIQAGFDVNFMldqrirkhyDDQRKSALYFAVSNGDLPSVKLLLSAGALPNQDP-VNCLQIALRMG 397
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQ---------DKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNgRTALHYAARSG 72
                          90
                  ....*....|....*.
gi 1654220539 398 NYELISLLLRHGANVN 413
Cdd:pfam12796  73 HLEIVKLLLEKGADIN 88
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
532-573 1.13e-08

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: 50.87  E-value: 1.13e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1654220539  532 RSLQHLCRLKIRKCMGrlrlrcpvFMSFLPLPNLLKAYVLYK 573
Cdd:smart00969   1 RSLQHLCRLAIRRSLG--------GIDKLPLPPRLKDYLLYY 34
PHA03100 PHA03100
ankyrin repeat protein; Provisional
340-446 2.23e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.43  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 340 VNFMLDQRIRKH-YDDQRKSALYF-----AVSNGDLPSVKLLLSAGALPN-QDPVNC--LQIAL--RMGNYELISLLLRH 408
Cdd:PHA03100   51 VKILLDNGADINsSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNaPDNNGItpLLYAIskKSNSYSIVEYLLDN 130
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1654220539 409 GANVN--YFCRVNPLHFpsALQYTLKDEVMLRMLLNYGYD 446
Cdd:PHA03100  131 GANVNikNSDGENLLHL--YLESNKIDLKILKLLIDKGVD 168
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
117-253 2.94e-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: 47.00  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 117 GETALFLAVSSS-LLENAHFLLLKGCNPnaktSEGNSpLLTAVLKDAYD-----MATLLISHGADVNLRCANER------ 184
Cdd:TIGR00870  52 GRSALFVAAIENeNLELTELLLNLSCRG----AVGDT-LLHAISLEYVDaveaiLLHLLAAFRKSGPLELANDQytseft 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 185 ---TALHEAAKLGRLDMVKLMLASGAYPDARS--------------SYGFTPLALAAQGGHTGIMQLLLQKGADVHSQAS 247
Cdd:TIGR00870 127 pgiTALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADILTADS 206

                  ....*.
gi 1654220539 248 DSSSVL 253
Cdd:TIGR00870 207 LGNTLL 212
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
215-243 7.57e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 7.57e-04
                           10        20
                   ....*....|....*....|....*....
gi 1654220539  215 YGFTPLALAAQGGHTGIMQLLLQKGADVH 243
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
388-414 7.94e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 7.94e-03
                           10        20
                   ....*....|....*....|....*..
gi 1654220539  388 NCLQIALRMGNYELISLLLRHGANVNY 414
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
74-351 4.91e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 166.67  E-value: 4.91e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539  74 AFDEANGNGWLPLHKAAVQLNKNILEITMNASEPSTWERTTHNGETALFLAVSSSLLENAHFLLLKGCNPNAKTSEGNSP 153
Cdd:COG0666    11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 154 LLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLASGAYPDARSSYGFTPLALAAQGGHTGIMQ 233
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 234 LLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGADANIPKSSGHLPIHVAADKGHFLALKVLVPVT-DIAAIKK 312
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGaDLNAKDK 250
                         250       260       270
                  ....*....|....*....|....*....|....*....
gi 1654220539 313 SGISPVHCAAAGAHPHCLELLIQAGFDVNFMLDQRIRKH 351
Cdd:COG0666   251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
38-301 4.59e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 163.97  E-value: 4.59e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539  38 EAARLHSFPSDDYKKIAEAIETGKEDALAGFAKYHPAFDEANGNGWLPLHKAAVQLNKNILEITMNASEPSTWERTTHNG 117
Cdd:COG0666     8 LLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGG 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 118 ETALFLAVSSSLLENAHFLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLD 197
Cdd:COG0666    88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLE 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 198 MVKLMLASGAYPDARSSYGFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGADANI 277
Cdd:COG0666   168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247
                         250       260
                  ....*....|....*....|....
gi 1654220539 278 PKSSGHLPIHVAADKGHFLALKVL 301
Cdd:COG0666   248 KDKDGLTALLLAAAAGAALIVKLL 271
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
130-442 2.64e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.09  E-value: 2.64e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 130 LENAHFLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLASGAYP 209
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 210 DARSSYGFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGADANIPKSSGHLPIHVA 289
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 290 ADKGHflalkvlvpvTDIAaikksgispvhcaaagahphclELLIQAGFDVNfmldqrirkHYDDQRKSALYFAVSNGDL 369
Cdd:COG0666   161 AANGN----------LEIV----------------------KLLLEAGADVN---------ARDNDGETPLHLAAENGHL 199
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1654220539 370 PSVKLLLSAGALPN---QDPVNCLQIALRMGNYELISLLLRHGANVNYFCRVNPLHFPSALQYTLKDEVMLRMLLN 442
Cdd:COG0666   200 EIVKLLLEAGADVNakdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
SOCS_ASB14 cd03730
SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a ...
529-585 6.70e-34

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: 122.65  E-value: 6.70e-34
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1654220539 529 TNPRSLQHLCRLKIRKCMGRLRLRCPVFMSFLPLPNLLKAYVLYKEYDLFGQERSTG 585
Cdd:cd03730     1 TNPRSLKHLCRLKIRACMGRLRLRCPVFMSFLPLPNRLKAYILYKEYDLYGQGIFTG 57
PHA02875 PHA02875
ankyrin repeat protein; Provisional
116-343 6.96e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 95.44  E-value: 6.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 116 NGETALFLAVSSSLLENAHFLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGR 195
Cdd:PHA02875    1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGD 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 196 LDMVKLMLASGAYP-DARSSYGFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGAD 274
Cdd:PHA02875   81 VKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKAC 160
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654220539 275 ANIPKSSGHLPIHVAADKGHFLALKVLVPV-TDIAAIKKSGISPVHCAAA-GAHPHCLELLIQAGFDVNFM 343
Cdd:PHA02875  161 LDIEDCCGCTPLIIAMAKGDIAICKMLLDSgANIDYFGKNGCVAALCYAIeNNKIDIVRLFIKRGADCNIM 231
PHA03100 PHA03100
ankyrin repeat protein; Provisional
169-417 1.50e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 91.27  E-value: 1.50e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 169 LISHGADVNLRCANERTALHEAAKLGRLDMVKLMLASGAYPDARSSYGFTPLALAAQGGHT-----GIMQLLLQKGADVH 243
Cdd:PHA03100   21 IIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVN 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 244 SQASDSSSVLLEAV--RGGNPEAVSLLLEYGADANIPKSSGHLPIHvaadkghfLALKVLVPVTDIaaikksgispvhca 321
Cdd:PHA03100  101 APDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLH--------LYLESNKIDLKI-------------- 158
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 322 aagahphcLELLIQAGFDVNFM--LDQRIRKHYDDQRK-----SALYFAVSNGDLPSVKLLLSAGALPN---QDPVNCLQ 391
Cdd:PHA03100  159 --------LKLLIDKGVDINAKnrVNYLLSYGVPINIKdvygfTPLHYAVYNNNPEFVKYLLDLGANPNlvnKYGDTPLH 230
                         250       260
                  ....*....|....*....|....*.
gi 1654220539 392 IALRMGNYELISLLLRHGANVNYFCR 417
Cdd:PHA03100  231 IAILNNNKEIFKLLLNNGPSIKTIIE 256
PHA03095 PHA03095
ankyrin-like protein; Provisional
135-377 1.92e-18

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 88.16  E-value: 1.92e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 135 FLLLKGCNPNAKTSEGNSPLLTAVL-KDAYDMATLLISHGADVNLRCANERTALHE--AAKLGRLDMVKLMLASGAYPDA 211
Cdd:PHA03095   68 LLLEAGADVNAPERCGFTPLHLYLYnATTLDVIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNA 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 212 RSSYGFTPLA--LAAQGGHTGIMQLLLQKGADVHSQASDSSSVL---LEAVRgGNPEAVSLLLEYGADANIPKSSGHLPI 286
Cdd:PHA03095  148 LDLYGMTPLAvlLKSRNANVELLRLLIDAGADVYAVDDRFRSLLhhhLQSFK-PRARIVRELIRAGCDPAATDMLGNTPL 226
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 287 HVAADKGHFLALKV---LVPVTDIAAIKKSGISPVHCAAAGAHPHCLELLIQAGFDVNfmldqrirkHYDDQRKSALYFA 363
Cdd:PHA03095  227 HSMATGSSCKRSLVlplLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN---------AVSSDGNTPLSLM 297
                         250
                  ....*....|....
gi 1654220539 364 VSNGDLPSVKLLLS 377
Cdd:PHA03095  298 VRNNNGRAVRAALA 311
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
530-581 2.77e-18

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: 78.72  E-value: 2.77e-18
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1654220539 530 NPRSLQHLCRLKIRKCMGRLRLRCPVFMSFLPLPNLLKAYVLYKEYDLFGQE 581
Cdd:cd03731     2 NPRPLKHLCRLKIRKLMGLQKLQQPSSMKKLPLPPALKRYILYKEYDLYGQE 53
PHA02878 PHA02878
ankyrin repeat protein; Provisional
136-292 1.58e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 85.70  E-value: 1.58e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 136 LLLKGCNPNAKT-SEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLASGAYPDARSS 214
Cdd:PHA02878  153 LLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDK 232
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 215 YGFTPLALAAQG-GHTGIMQLLLQKGADVHSQASDSS-SVLLEAVRggNPEAVSLLLEYGADANIPKSSGHLPIHVAADK 292
Cdd:PHA02878  233 CGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGlTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA03100 PHA03100
ankyrin repeat protein; Provisional
94-292 1.85e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 84.72  E-value: 1.85e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539  94 NKNILEITMNAS--EPSTWERTThngetALFLAVSS---SLLEnahFLLLKGCNPN--AKTSEGNSPLLT---AVLKDAY 163
Cdd:PHA03100   15 VKNIKYIIMEDDlnDYSYKKPVL-----PLYLAKEArniDVVK---ILLDNGADINssTKNNSTPLHYLSnikYNLTDVK 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 164 DMATLLISHGADVNLRCANERTALHEAA--KLGRLDMVKLMLASGAYPDARSSYGFTPLALAAQGGH--TGIMQLLLQKG 239
Cdd:PHA03100   87 EIVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKG 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654220539 240 ADV--------------HSQASD--SSSVLLEAVRGGNPEAVSLLLEYGADANIPKSSGHLPIHVAADK 292
Cdd:PHA03100  167 VDInaknrvnyllsygvPINIKDvyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILN 235
Ank_2 pfam12796
Ankyrin repeats (3 copies);
154-245 1.99e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 1.99e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 154 LLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLasgAYPDARS-SYGFTPLALAAQGGHTGIM 232
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL---EHADVNLkDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|...
gi 1654220539 233 QLLLQKGADVHSQ 245
Cdd:pfam12796  78 KLLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
144-337 5.68e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 83.47  E-value: 5.68e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 144 NAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLASGA------YPDARSSygf 217
Cdd:PHA02874   29 NISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVdtsilpIPCIEKD--- 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 218 tplalaaqgghtgIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGADANIPKSSGHLPIHVAADKGHFLA 297
Cdd:PHA02874  106 -------------MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDI 172
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|.
gi 1654220539 298 LKVLVPVTDIAAIKKSGI-SPVHCAAAGAHPHCLELLIQAG 337
Cdd:PHA02874  173 IKLLLEKGAYANVKDNNGeSPLHNAAEYGDYACIKLLIDHG 213
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
530-573 1.13e-16

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: 73.68  E-value: 1.13e-16
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1654220539 530 NPRSLQHLCRLKIRKCMGRlrlRCPVFMSFLPLPNLLKAYVLYK 573
Cdd:cd03716     2 TPRSLQHLCRLAIRRCLGR---RRLELIKKLPLPPRLKDYLLYE 42
PHA02875 PHA02875
ankyrin repeat protein; Provisional
53-277 3.14e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 81.19  E-value: 3.14e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539  53 IAEAIETGKEDALAGF--AKYHPAFDEANGngWLPLhKAAVQLnKNILEITMNASEPSTWERTTHNGETALFLAVSSSLL 130
Cdd:PHA02875    6 LCDAILFGELDIARRLldIGINPNFEIYDG--ISPI-KLAMKF-RDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDV 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 131 ENAHFLLLKGCNPN-AKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLASGAYP 209
Cdd:PHA02875   82 KAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654220539 210 DARSSYGFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLL-EAVRGGNPEAVSLLLEYGADANI 277
Cdd:PHA02875  162 DIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAALcYAIENNKIDIVRLFIKRGADCNI 230
Ank_2 pfam12796
Ankyrin repeats (3 copies);
187-277 1.64e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 1.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 187 LHEAAKLGRLDMVKLMLASGAYPDARSSYGFTPLALAAQGGHTGIMQLLLQKgADVHSQaSDSSSVLLEAVRGGNPEAVS 266
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|.
gi 1654220539 267 LLLEYGADANI 277
Cdd:pfam12796  79 LLLEKGADINV 89
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
530-573 5.54e-15

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: 69.04  E-value: 5.54e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1654220539 530 NPRSLQHLCRLKIRKCMGRlrlRCPVFMSFLPLPNLLKAYVLYK 573
Cdd:cd03587     1 NPRSLQHLCRLAIRRCLGK---RRLDLIDKLPLPPRLKDYLLYK 41
Ank_2 pfam12796
Ankyrin repeats (3 copies);
121-212 6.09e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.53  E-value: 6.09e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 121 LFLAVSSSLLENAHFLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHgADVNLRCaNERTALHEAAKLGRLDMVK 200
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|..
gi 1654220539 201 LMLASGAYPDAR 212
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA02875 PHA02875
ankyrin repeat protein; Provisional
182-447 6.77e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.95  E-value: 6.77e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 182 NERTALHEAAKLGRLDMVKLMLASGAYPDARSSYGFTPLALAaqgghtgimqlllqkgadvhsqasdsssvlleaVRGGN 261
Cdd:PHA02875    1 MDQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLA---------------------------------MKFRD 47
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 262 PEAVSLLLEYGADANIPKSSGHLPIHVAADKGHFLALKVLVPVTDIA--AIKKSGISPVHCAAAGAHPHCLELLIQAGFD 339
Cdd:PHA02875   48 SEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAddVFYKDGMTPLHLATILKKLDIMKLLIARGAD 127
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 340 VNFMldqrirkhyDDQRKSALYFAVSNGDLPSVKLLLSAGALPN-QDPVNC--LQIALRMGNYELISLLLRHGANVNYFC 416
Cdd:PHA02875  128 PDIP---------NTDKFSPLHLAVMMGDIKGIELLIDHKACLDiEDCCGCtpLIIAMAKGDIAICKMLLDSGANIDYFG 198
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1654220539 417 RvNPLhfPSALQYTLKDEV--MLRMLLNYGYDT 447
Cdd:PHA02875  199 K-NGC--VAALCYAIENNKidIVRLFIKRGADC 228
PHA03100 PHA03100
ankyrin repeat protein; Provisional
124-277 1.09e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 76.24  E-value: 1.09e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 124 AVSSSLLENAHFLLLKGCNPNAKTSEGNSPLLTAVLK--DAYDMATLLISHGADVNLRCANERTALHEAAKLGR--LDMV 199
Cdd:PHA03100   80 YNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKIL 159
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 200 KLMLASGAYPDARSS----------------YGFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPE 263
Cdd:PHA03100  160 KLLIDKGVDINAKNRvnyllsygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKE 239
                         170
                  ....*....|....
gi 1654220539 264 AVSLLLEYGADANI 277
Cdd:PHA03100  240 IFKLLLNNGPSIKT 253
PHA03095 PHA03095
ankyrin-like protein; Provisional
168-407 6.03e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 74.29  E-value: 6.03e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 168 LLISHGADVNLRCANERTALHEAAKLG---RLDMVKLMLASGAYPDARSSYGFTPLALAAQGGHT-GIMQLLLQKGADVH 243
Cdd:PHA03095   32 RLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAGADVN 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 244 SQaSDSSSVLLEAVRGG---NPEAVSLLLEYGADANIPKSSGHLPIHV-----------------------AADKGHFLA 297
Cdd:PHA03095  112 AK-DKVGRTPLHVYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAVllksrnanvellrllidagadvyAVDDRFRSL 190
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 298 L---------------KVLVPVTDIAAIKKSGISPVHCAAagAHPHCLELLIQ----AGFDVNfmldqrIRKHYDdqrKS 358
Cdd:PHA03095  191 LhhhlqsfkprarivrELIRAGCDPAATDMLGNTPLHSMA--TGSSCKRSLVLplliAGISIN------ARNRYG---QT 259
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1654220539 359 ALYFAVSNGDLPSVKLLLSAGALPN---QDPVNCLQIALRMGNYELISLLLR 407
Cdd:PHA03095  260 PLHYAAVFNNPRACRRLIALGADINavsSDGNTPLSLMVRNNNGRAVRAALA 311
PHA02876 PHA02876
ankyrin repeat protein; Provisional
133-444 1.74e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 73.56  E-value: 1.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 133 AHFLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVK------------ 200
Cdd:PHA02876  161 AEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKaiidnrsninkn 240
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 201 -----------------LMLASGAYPDARSSYGFTPLALAAQGGH-TGIMQLLLQKGADVHSQASDSSSVL-LEAVRGGN 261
Cdd:PHA02876  241 dlsllkairnedletslLLYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGETPLyLMAKNGYD 320
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 262 PEAVSLLLEYGADANIPKSSGHLPIHVAA--DKGHFLALKVLVPVTDIAAIKKSGISPVHCAAAGAHPHCLELLIQAGFD 339
Cdd:PHA02876  321 TENIRTLIMLGADVNAADRLYITPLHQAStlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 340 VNfMLDQRIrkhyddqrKSALYFAVSnGDLP--SVKLLLSAGA---LPNQDPVNCLQIALRMG-NYELISLLLRHGANVN 413
Cdd:PHA02876  401 IE-ALSQKI--------GTALHFALC-GTNPymSVKTLIDRGAnvnSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVN 470
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1654220539 414 YFCRVNPLHFPSALQYtlkdEVMLRMLLNYG 444
Cdd:PHA02876  471 AINIQNQYPLLIALEY----HGIVNILLHYG 497
Ank_2 pfam12796
Ankyrin repeats (3 copies);
253-341 3.12e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 3.12e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 253 LLEAVRGGNPEAVSLLLEYGADANIPKSSGHLPIHVAADKGHFLALKVLVPVTDIaAIKKSGISPVHCAAAGAHPHCLEL 332
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV-NLKDNGRTALHYAARSGHLEIVKL 79

                  ....*....
gi 1654220539 333 LIQAGFDVN 341
Cdd:pfam12796  80 LLEKGADIN 88
PHA02874 PHA02874
ankyrin repeat protein; Provisional
231-444 5.92e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 71.15  E-value: 5.92e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 231 IMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGADANIPKSSGHLPIHVAADKGHFLALKVLVpvtdIAAI 310
Cdd:PHA02874   17 IEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI----DNGV 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 311 KKSgISPVHCaaagAHPHCLELLIQAGFDVNfmldqrIRkhyDDQRKSALYFAVSNGDLPSVKLLLSAGALPNQDPVNC- 389
Cdd:PHA02874   93 DTS-ILPIPC----IEKDMIKTILDCGIDVN------IK---DAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGc 158
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1654220539 390 --LQIALRMGNYELISLLLRHGA--NVNYFCRVNPLHFpsALQYtlKDEVMLRMLLNYG 444
Cdd:PHA02874  159 ypIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGESPLHN--AAEY--GDYACIKLLIDHG 213
PHA02874 PHA02874
ankyrin repeat protein; Provisional
119-321 1.84e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 69.61  E-value: 1.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 119 TALFLAVSSSLLENAHFLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVN---LRCANErtalheaaklgr 195
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSilpIPCIEK------------ 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 196 lDMVKLMLASGAYPDARSSYGFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGADA 275
Cdd:PHA02874  105 -DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYA 183
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1654220539 276 NIPKSSGHLPIHVAADKGHFLALKVLVPVTDIAAIK-KSGISPVHCA 321
Cdd:PHA02874  184 NVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKcKNGFTPLHNA 230
PHA02874 PHA02874
ankyrin repeat protein; Provisional
118-289 2.74e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.84  E-value: 2.74e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 118 ETALFLAVSSSLLENAHFLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLD 197
Cdd:PHA02874  125 KTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYA 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 198 MVKLMLASGAYPDARSSYGFTPLalaaqggHTGIMQ-----LLLQKGADVHSQASDSSSVLLEAVrggNP----EAVSLL 268
Cdd:PHA02874  205 CIKLLIDHGNHIMNKCKNGFTPL-------HNAIIHnrsaiELLINNASINDQDIDGSTPLHHAI---NPpcdiDIIDIL 274
                         170       180
                  ....*....|....*....|.
gi 1654220539 269 LEYGADANIPKSSGHLPIHVA 289
Cdd:PHA02874  275 LYHKADISIKDNKGENPIDTA 295
PHA03095 PHA03095
ankyrin-like protein; Provisional
116-290 5.00e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.13  E-value: 5.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 116 NGETALFLAVSSSLLEN-AHFLLLKGCNPNAKTSEGNSPL---LTAVLKDaYDMATLLISHGADVNLRCANERTALHEAA 191
Cdd:PHA03095   82 CGFTPLHLYLYNATTLDvIKLLIKAGADVNAKDKVGRTPLhvyLSGFNIN-PKVIRLLLRKGADVNALDLYGMTPLAVLL 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 192 KLGR--LDMVKLMLASGAYPDARSSYGFTPLALAAQGGHT--GIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEA--V 265
Cdd:PHA03095  161 KSRNanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRslV 240
                         170       180
                  ....*....|....*....|....*
gi 1654220539 266 SLLLEYGADANIPKSSGHLPIHVAA 290
Cdd:PHA03095  241 LPLLIAGISINARNRYGQTPLHYAA 265
PHA02876 PHA02876
ankyrin repeat protein; Provisional
117-289 5.22e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 68.55  E-value: 5.22e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 117 GETALFLAVSSSL-LENAHFLLLKGCNPNAKTSEGNSPLLTAVLKDAY-DMATLLISHGADVNLRCANERTALHEAAKLG 194
Cdd:PHA02876  307 GETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLDRNkDIVITLLELGANVNARDYCDKTPIHYAAVRN 386
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 195 RLDMVKLMLASGAYPDARSSYGFTPLALAAQGGHTGI-MQLLLQKGADVHSQASDSSSVLLEAVRGG-NPEAVSLLLEYG 272
Cdd:PHA02876  387 NVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMsVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNG 466
                         170
                  ....*....|....*..
gi 1654220539 273 ADANIPKSSGHLPIHVA 289
Cdd:PHA02876  467 ADVNAINIQNQYPLLIA 483
PHA03100 PHA03100
ankyrin repeat protein; Provisional
85-242 1.42e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.61  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539  85 PLHKAAVQL-----NKNILEITMNASepSTWERTTHNGETALFLAVSSSL--LENAHFLLLKGCNPNAKTSEGNSpLLTA 157
Cdd:PHA03100   71 PLHYLSNIKynltdVKEIVKLLLEYG--ANVNAPDNNGITPLLYAISKKSnsYSIVEYLLDNGANVNIKNSDGEN-LLHL 147
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 158 VLK-------------------DAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLASGAYPDARSSYGFT 218
Cdd:PHA03100  148 YLEsnkidlkilkllidkgvdiNAKNRVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDT 227
                         170       180
                  ....*....|....*....|....
gi 1654220539 219 PLALAAQGGHTGIMQLLLQKGADV 242
Cdd:PHA03100  228 PLHIAILNNNKEIFKLLLNNGPSI 251
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
530-571 1.96e-11

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: 58.72  E-value: 1.96e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1654220539 530 NPRSLQHLCRLKIRKCMGRlrlRCPVFMSFLPLPNLLKAYVL 571
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGK---RRLGAIDKLPLPPLLKDYLL 39
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
118-302 5.91e-11

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: 65.03  E-value: 5.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 118 ETALFLAVSSSLLENAHFLLL-KGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGAD-VNLRCANE----RTALHEAA 191
Cdd:cd22192    18 ESPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMTSDlyqgETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 192 KLGRLDMVKLMLASGA--------------YPDARSSYGFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVL---- 253
Cdd:cd22192    98 VNQNLNLVRELIARGAdvvspratgtffrpGPKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLhilv 177
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1654220539 254 LEAVRGGNPEAVSLLLEYGADAN------IPKSSGHLPIHVAADKGHFLALKVLV 302
Cdd:cd22192   178 LQPNKTFACQMYDLILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLV 232
Ank_2 pfam12796
Ankyrin repeats (3 copies);
319-413 7.84e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.59  E-value: 7.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 319 HCAAAGAHPHCLELLIQAGFDVNFMldqrirkhyDDQRKSALYFAVSNGDLPSVKLLLSAGALPNQDP-VNCLQIALRMG 397
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQ---------DKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNgRTALHYAARSG 72
                          90
                  ....*....|....*.
gi 1654220539 398 NYELISLLLRHGANVN 413
Cdd:pfam12796  73 HLEIVKLLLEKGADIN 88
PHA02876 PHA02876
ankyrin repeat protein; Provisional
158-446 8.42e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 64.70  E-value: 8.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 158 VLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLASGAYPDARSSYGFTPLALAAQGGHTGIMQLLLq 237
Cdd:PHA02876  153 IQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII- 231
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 238 kgaDVHSQASDSSSVLLEAVRGGNPEA----------------------------------VSLLLEYGADANIPKSSGH 283
Cdd:PHA02876  232 ---DNRSNINKNDLSLLKAIRNEDLETslllydagfsvnsiddckntplhhasqapslsrlVPKLLERGADVNAKNIKGE 308
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 284 LPIHVAADKGHFLA-LKVLVPV-TDIAAIKKSGISPVHCAAA-GAHPHCLELLIQAGFDVNfmldqrIRKHYDdqrKSAL 360
Cdd:PHA02876  309 TPLYLMAKNGYDTEnIRTLIMLgADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVN------ARDYCD---KTPI 379
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 361 YFAVSNGDLPSVKLLLSAGA---LPNQDPVNCLQIALRMGN-YELISLLLRHGANVNYFCR--VNPLHFpsALQYTLKDE 434
Cdd:PHA02876  380 HYAAVRNNVVIINTLLDYGAdieALSQKIGTALHFALCGTNpYMSVKTLIDRGANVNSKNKdlSTPLHY--ACKKNCKLD 457
                         330
                  ....*....|..
gi 1654220539 435 VmLRMLLNYGYD 446
Cdd:PHA02876  458 V-IEMLLDNGAD 468
PHA02874 PHA02874
ankyrin repeat protein; Provisional
136-289 1.78e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.44  E-value: 1.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 136 LLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLASGAYPDARSSY 215
Cdd:PHA02874  110 ILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNN 189
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654220539 216 GFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRgGNPEAVSLLLEyGADANIPKSSGHLPIHVA 289
Cdd:PHA02874  190 GESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII-HNRSAIELLIN-NASINDQDIDGSTPLHHA 261
PHA02876 PHA02876
ankyrin repeat protein; Provisional
196-448 4.62e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.39  E-value: 4.62e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 196 LDMVKLMLASGAYPDARSSYGFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGADA 275
Cdd:PHA02876  158 LLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNI 237
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 276 NIPKSSGHLPIHVAADKGHFLALKVLVPVTDIAAIKKsgiSPVHCAA-AGAHPHCLELLIQAGFDVNfmlDQRIRKhydd 354
Cdd:PHA02876  238 NKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKN---TPLHHASqAPSLSRLVPKLLERGADVN---AKNIKG---- 307
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 355 qrKSALYFAVSNG-DLPSVKLLLSAGALPNQ------DPVNclQIALRMGNYELISLLLRHGANVNY--FCRVNPLHFpS 425
Cdd:PHA02876  308 --ETPLYLMAKNGyDTENIRTLIMLGADVNAadrlyiTPLH--QASTLDRNKDIVITLLELGANVNArdYCDKTPIHY-A 382
                         250       260
                  ....*....|....*....|...
gi 1654220539 426 ALQYTLkdeVMLRMLLNYGYDTE 448
Cdd:PHA02876  383 AVRNNV---VIINTLLDYGADIE 402
PHA02878 PHA02878
ankyrin repeat protein; Provisional
153-446 1.01e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.05  E-value: 1.01e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 153 PLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLASgaYPDARSSYGFTPLALAAQGGHTGIM 232
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS--INKCSVFYTLVAIKDAFNNRNVEIF 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 233 QLLLqkgADVHSQASDSSSVLLEAVRGGN---PEAVSLLLEYGADANI-PKSSGHLPIHVAADKghflalkvlvPVTDIA 308
Cdd:PHA02878  118 KIIL---TNRYKNIQTIDLVYIDKKSKDDiieAEITKLLLSYGADINMkDRHKGNTALHYATEN----------KDQRLT 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 309 aikksgispvhcaaagahphclELLIQAGFDVNFMldqrirkhyDDQRKSALYFAVSNGDLPSVKLLLSAGAlpNQDPVN 388
Cdd:PHA02878  185 ----------------------ELLLSYGANVNIP---------DKTNNSPLHHAVKHYNKPIVHILLENGA--STDARD 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654220539 389 C-----LQIAL-RMGNYELISLLLRHGANVNYFCRVNPLhfpSALQYTLKDEVMLRMLLNYGYD 446
Cdd:PHA02878  232 KcgntpLHISVgYCKDYDILKLLLEHGVDVNAKSYILGL---TALHSSIKSERKLKLLLEYGAD 292
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
126-274 8.66e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.34  E-value: 8.66e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 126 SSSLLENahfLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLM--L 203
Cdd:PLN03192  537 NAALLEE---LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILyhF 613
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654220539 204 ASGAYPDArssyGFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGAD 274
Cdd:PLN03192  614 ASISDPHA----AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
Ank_4 pfam13637
Ankyrin repeats (many copies);
183-236 9.08e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 9.08e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1654220539 183 ERTALHEAAKLGRLDMVKLMLASGAYPDARSSYGFTPLALAAQGGHTGIMQLLL 236
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
117-258 1.12e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.96  E-value: 1.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 117 GETALFLAVSSSLLENAHFLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANErtALHEAAKLGRL 196
Cdd:PLN03192  558 GRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAGD--LLCTAAKRNDL 635
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1654220539 197 DMVKLMLASGAYPDARSSYGFTPLALAAQGGHTGIMQLLLQKGADVHSQASD---SSSVLLEAVR 258
Cdd:PLN03192  636 TAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDddfSPTELRELLQ 700
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
532-573 1.13e-08

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: 50.87  E-value: 1.13e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1654220539  532 RSLQHLCRLKIRKCMGrlrlrcpvFMSFLPLPNLLKAYVLYK 573
Cdd:smart00969   1 RSLQHLCRLAIRRSLG--------GIDKLPLPPRLKDYLLYY 34
Ank_2 pfam12796
Ankyrin repeats (3 copies);
360-446 1.23e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 52.43  E-value: 1.23e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 360 LYFAVSNGDLPSVKLLLSAGA---LPNQDPVNCLQIALRMGNYELISLLLRHGANVNYFCRVNPLHFpsALQYTLKDevM 436
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAdanLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDNGRTALHY--AARSGHLE--I 76
                          90
                  ....*....|
gi 1654220539 437 LRMLLNYGYD 446
Cdd:pfam12796  77 VKLLLEKGAD 86
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
166-244 3.52e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 3.52e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654220539 166 ATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLMLASGAYPDARSSYGFTPLALAAQGGHTGIMQLLLQKGADVHS 244
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFE 176
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
530-571 4.45e-08

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: 49.36  E-value: 4.45e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1654220539 530 NPRSLQHLCRLKIRKCMGRlrlRCPVFMSFLPLPNLLKAYVL 571
Cdd:cd03723     2 TPRSLQHLCRCAIRKLLGS---RCHKLVPQLSLPTSLKNYLL 40
PHA02798 PHA02798
ankyrin-like protein; Provisional
140-243 5.30e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 55.61  E-value: 5.30e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 140 GCNPNAKTSEGNSPLLTAV-----LKDAYDMATLLISHGADVNLRCANERTALH---EAAKLGRLDMVKLMLASGAYPDA 211
Cdd:PHA02798   61 GANVNGLDNEYSTPLCTILsnikdYKHMLDIVKILIENGADINKKNSDGETPLYcllSNGYINNLEILLFMIENGADTTL 140
                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1654220539 212 RSSYGFTPLALAAQGGHT---GIMQLLLQKGADVH 243
Cdd:PHA02798  141 LDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDIN 175
SOCS_ASB3 cd03722
SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a ...
533-574 1.17e-07

SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ABS3 has been shown to be negative regulator of TNF-R2-mediated cellular responses to TNF-alpha by direct targeting of tumor necrosis factor receptor II (TNF-R2) for ubiquitination and proteasome-mediated degradation. 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: 239692  Cd Length: 51  Bit Score: 48.63  E-value: 1.17e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1654220539 533 SLQHLCRLKIRKCMGRLRLRCPVFMSFLPLPNLLKAYVLYKE 574
Cdd:cd03722     5 SLTHLCRLEIRSSLKSERLRSDSFICQLPLPRSLQDYLLYSD 46
PHA03095 PHA03095
ankyrin-like protein; Provisional
230-446 1.21e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 54.26  E-value: 1.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 230 GIMQLLLQKGADVHSQASDSSSVLLEAVRGGNP---EAVSLLLEYGADANIPKSSGHLPIHVaadkghFLALKVLVPVtd 306
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEAGADVNAPERCGFTPLHL------YLYNATTLDV-- 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 307 iaaikksgispvhcaaagahphcLELLIQAGFDVNFMldqrirkhyDDQRKSAL--YFAVSNGDLPSVKLLLSAGALPN- 383
Cdd:PHA03095  100 -----------------------IKLLIKAGADVNAK---------DKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNa 147
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1654220539 384 --QDPVNCLQIALRMGN--YELISLLLRHGANVNY--FCRVNPLHfpSALQYTLKDEVMLRMLLNYGYD 446
Cdd:PHA03095  148 ldLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAvdDRFRSLLH--HHLQSFKPRARIVRELIRAGCD 214
SOCS smart00253
suppressors of cytokine signalling; suppressors of cytokine signalling
529-573 1.73e-07

suppressors of cytokine signalling; suppressors of cytokine signalling


Pssm-ID: 128549  Cd Length: 43  Bit Score: 47.68  E-value: 1.73e-07
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1654220539  529 TNPRSLQHLCRLKIRKCMGRLRLRCpvfmsfLPLPNLLKAYVLYK 573
Cdd:smart00253   5 SNVPSLQHLCRFTIRRCTRTDQIKT------LPLPPKLKDYLSYY 43
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
199-281 2.79e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 2.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 199 VKLMLASGAYPDARSSYGFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYG-----A 273
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSqchfeL 177

                  ....*...
gi 1654220539 274 DANIPKSS 281
Cdd:PTZ00322  178 GANAKPDS 185
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
529-573 2.88e-07

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: 46.82  E-value: 2.88e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1654220539 529 TNPRSLQHLCRLKIRKCMGRLRLRCpvfmsfLPLPNLLKAYVLYK 573
Cdd:cd03717     1 TSVRSLQHLCRFVIRQCTRRDLIDQ------LPLPRRLKDYLKEY 39
PHA02874 PHA02874
ankyrin repeat protein; Provisional
116-285 3.15e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.04  E-value: 3.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 116 NGETALFLAVSSSLLENAHFLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGR 195
Cdd:PHA02874  156 NGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR 235
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 196 lDMVKLMLASGAYPDARSSyGFTPLALAAQ-GGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVslLLEYGAD 274
Cdd:PHA02874  236 -SAIELLINNASINDQDID-GSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPV--IKDIIAN 311
                         170
                  ....*....|.
gi 1654220539 275 ANIPKSSGHLP 285
Cdd:PHA02874  312 AVLIKEADKLK 322
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
190-340 4.18e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.95  E-value: 4.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 190 AAKLGRLDMVKLMLASGAYPDARSSYGFTPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLL 269
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654220539 270 EYGADANiPKSSGHLpIHVAADKGHFLALKVLVPV-TDIAAIKKSGISPVHCAAAGAHPHCLELLIQAGFDV 340
Cdd:PLN03192  612 HFASISD-PHAAGDL-LCTAAKRNDLTAMKELLKQgLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
SOCS_ASB7 cd03726
SOCS (suppressors of cytokine signaling) box of ASB7-like proteins. ASB family members have a ...
531-576 4.72e-07

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: 46.38  E-value: 4.72e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1654220539 531 PRSLQHLCRLKIRKCMGRLRLRcpvFMSFLPLPNLLKAYVLYKEYD 576
Cdd:cd03726     3 PRTLQDLCRIKIRHCIGLQNLK---LLDELPIAKVMKDYLKHKFDD 45
Ank_2 pfam12796
Ankyrin repeats (3 copies);
56-146 7.11e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.42  E-value: 7.11e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539  56 AIETGKEDALAGFAKYHPAFDEANGNGWLPLHKAAVQLNKNILEITMNASEPstweRTTHNGETALFLAVSSSLLENAHF 135
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV----NLKDNGRTALHYAARSGHLEIVKL 79
                          90
                  ....*....|.
gi 1654220539 136 LLLKGCNPNAK 146
Cdd:pfam12796  80 LLEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
85-223 7.75e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.80  E-value: 7.75e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539  85 PLHKAAVQLNKNILEItmnasepstwertthngetalflavsssLLENahflllkGCNPNAKTSEGNSPLLTAV--LKDa 162
Cdd:PHA02878  204 PLHHAVKHYNKPIVHI----------------------------LLEN-------GASTDARDKCGNTPLHISVgyCKD- 247
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654220539 163 YDMATLLISHGADVNLRCA-NERTALHEAAKlgRLDMVKLMLASGAYPDARSSYGFTPLALA 223
Cdd:PHA02878  248 YDILKLLLEHGVDVNAKSYiLGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSA 307
SOCS_ASB5 cd03724
SOCS (suppressors of cytokine signaling) box of ASB5-like proteins. ASB family members have a ...
531-573 9.94e-07

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: 45.64  E-value: 9.94e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1654220539 531 PRSLQHLCRLKIRKCMGRLRLRcpvFMSFLPLPNLLKAYVLYK 573
Cdd:cd03724     3 PSSLCQLCRLCIRNYIGRSRLH---LIPQLQLPTLLKNFLQYR 42
Ank_4 pfam13637
Ankyrin repeats (many copies);
150-203 1.26e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 1.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1654220539 150 GNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGRLDMVKLML 203
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SOCS_SSB1_4 cd03718
SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box ...
531-573 1.26e-06

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: 45.37  E-value: 1.26e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1654220539 531 PRSLQHLCRLKIRKCMGRLRLRcpvFMSFLPLPNLLKAYVLYK 573
Cdd:cd03718     3 PLPLMDLCRRRVRVALGRDRLE---EIEQLPLPPSLKNYLLYQ 42
PHA03100 PHA03100
ankyrin repeat protein; Provisional
340-446 2.23e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.43  E-value: 2.23e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 340 VNFMLDQRIRKH-YDDQRKSALYF-----AVSNGDLPSVKLLLSAGALPN-QDPVNC--LQIAL--RMGNYELISLLLRH 408
Cdd:PHA03100   51 VKILLDNGADINsSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNaPDNNGItpLLYAIskKSNSYSIVEYLLDN 130
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1654220539 409 GANVN--YFCRVNPLHFpsALQYTLKDEVMLRMLLNYGYD 446
Cdd:PHA03100  131 GANVNikNSDGENLLHL--YLESNKIDLKILKLLIDKGVD 168
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
531-574 3.77e-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: 44.09  E-value: 3.77e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1654220539 531 PRSLQHLCRLKIRKCMGRLRLRcpvFMSFLPLPNLLKAYVLYKE 574
Cdd:cd03721     3 PRPLAHLCRLKVRTLIGINRIK---LIDTLPLPPRLIRYLNHQE 43
PHA03100 PHA03100
ankyrin repeat protein; Provisional
116-177 5.98e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 48.89  E-value: 5.98e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654220539 116 NGETALFLAVSSSLLENAHFLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVN 177
Cdd:PHA03100  191 YGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02946 PHA02946
ankyin-like protein; Provisional
136-318 1.19e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 48.13  E-value: 1.19e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 136 LLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEAAKLGR--LDMVKLMLASGA-YPDAR 212
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAkINNSV 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 213 SSYGFTPLaLAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEA--VSLLLEYGADANIPKSSGHLPIHVAA 290
Cdd:PHA02946  138 DEEGCGPL-LACTDPSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKAstISWMMKLGISPSKPDHDGNTPLHIVC 216
                         170       180       190
                  ....*....|....*....|....*....|
gi 1654220539 291 DK--GHFLALKVLVPVTDIAAIKKSGISPV 318
Cdd:PHA02946  217 SKtvKNVDIINLLLPSTDVNKQNKFGDSPL 246
Ank_5 pfam13857
Ankyrin repeats (many copies);
169-223 1.27e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 42.72  E-value: 1.27e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1654220539 169 LISHG-ADVNLRCANERTALHEAAKLGRLDMVKLMLASGAYPDARSSYGFTPLALA 223
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
229-383 1.31e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.95  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 229 TGIMQLLLQKGADVHSQASDS-SSVLLEAVRGGNPEAVSLLLEYGADANIPKSSGHLPIHVAADKGHFLALKVLVPV-TD 306
Cdd:PHA02878  147 AEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENgAS 226
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1654220539 307 IAAIKKSGISPVHCAAAGAHPH-CLELLIQAGFDVNfmLDQRIRKHyddqrkSALYFAVSNGDlpSVKLLLSAGALPN 383
Cdd:PHA02878  227 TDARDKCGNTPLHISVGYCKDYdILKLLLEHGVDVN--AKSYILGL------TALHSSIKSER--KLKLLLEYGADIN 294
Ank_4 pfam13637
Ankyrin repeats (many copies);
218-269 1.57e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 1.57e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1654220539 218 TPLALAAQGGHTGIMQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLL 269
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
117-253 2.94e-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: 47.00  E-value: 2.94e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 117 GETALFLAVSSS-LLENAHFLLLKGCNPnaktSEGNSpLLTAVLKDAYD-----MATLLISHGADVNLRCANER------ 184
Cdd:TIGR00870  52 GRSALFVAAIENeNLELTELLLNLSCRG----AVGDT-LLHAISLEYVDaveaiLLHLLAAFRKSGPLELANDQytseft 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 185 ---TALHEAAKLGRLDMVKLMLASGAYPDARS--------------SYGFTPLALAAQGGHTGIMQLLLQKGADVHSQAS 247
Cdd:TIGR00870 127 pgiTALHLAAHRQNYEIVKLLLERGASVPARAcgdffvksqgvdsfYHGESPLNAAACLGSPSIVALLSEDPADILTADS 206

                  ....*.
gi 1654220539 248 DSSSVL 253
Cdd:TIGR00870 207 LGNTLL 212
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
86-238 3.75e-05

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 46.80  E-value: 3.75e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539  86 LHKAAVQLNKNILEITMN--------------ASEPSTWErtTHNGETALFLAVS-------SSLLENAHFLLLKGCNPN 144
Cdd:cd21882    30 LHKAALNLNDGVNEAIMLlleaapdsgnpkelVNAPCTDE--FYQGQTALHIAIEnrnlnlvRLLVENGADVSARATGRF 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 145 AKTSEGNS------PLLTAVLKDAYDMATLLISHGADVNLRCANE---RTALH----------EAAKLGrLDMVKLMLAS 205
Cdd:cd21882   108 FRKSPGNLfyfgelPLSLAACTNQEEIVRLLLENGAQPAALEAQDslgNTVLHalvlqadntpENSAFV-CQMYNLLLSY 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1654220539 206 GAYPDARSSY-------GFTPLALAAQGGHTGIMQLLLQK 238
Cdd:cd21882   187 GAHLDPTQQLeeipnhqGLTPLKLAAVEGKIVMFQHILQR 226
PHA02798 PHA02798
ankyrin-like protein; Provisional
122-277 4.25e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 46.37  E-value: 4.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 122 FLAVSSSLLENAHFLLLKGCNPNaKTSEGNSPLLTAVLKD--AYDMATLLISHGADVNLRCANERTAL-----HEAAKLG 194
Cdd:PHA02798    9 YITFSDNVKLSTVKLLIKSCNPN-EIVNEYSIFQKYLQRDspSTDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKH 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 195 RLDMVKLMLASGAYPDARSSYGFTPLALAAQGGHTG---IMQLLLQKGADVHSQASDSSSVLLEAVRGGNP---EAVSLL 268
Cdd:PHA02798   88 MLDIVKILIENGADINKKNSDGETPLYCLLSNGYINnleILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLL 167

                  ....*....
gi 1654220539 269 LEYGADANI 277
Cdd:PHA02798  168 LEKGVDINT 176
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
222-293 6.39e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 6.39e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1654220539 222 LAAQGGHTGImQLLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGADANIPKSSGHLPIHVAADKG 293
Cdd:PTZ00322   89 LAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENG 159
SOCS_SSB2 cd03719
SOCS (suppressors of cytokine signaling) box of SSB2 (SPRY domain-containing SOCS box proteins) ...
531-573 9.56e-05

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


Pssm-ID: 239689  Cd Length: 42  Bit Score: 40.00  E-value: 9.56e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1654220539 531 PRSLQHLCRLKIRKCMGRLRLRcpvFMSFLPLPNLLKAYVLYK 573
Cdd:cd03719     3 PHSLLHLSRLCVRHALGDTRLG---QVSALPLPPAMKRYLLYQ 42
SOCS_SOCS2 cd03736
SOCS (suppressors of cytokine signaling) box of SOCS2-like proteins. Together with CIS1, the ...
529-575 9.64e-05

SOCS (suppressors of cytokine signaling) box of SOCS2-like proteins. Together with CIS1, the CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 domain. SOCS2 has recently been shown to regulate neuronal differentiation by controlling expression of a neurogenic transcription factor, Neurogenin-1. SOCS2 binds to GH receptors and inhibits the activation of STAT5b induced by GH. 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: 239705  Cd Length: 41  Bit Score: 39.83  E-value: 9.64e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1654220539 529 TNPRSLQHLCRLKIRKCMGRLRLrcpvfmsfLPLPNLLKAYVlyKEY 575
Cdd:cd03736     1 TSTPSLQHLCRITINKCTRQIQE--------LPLPTRLKDYL--TEY 37
Ank_4 pfam13637
Ankyrin repeats (many copies);
285-334 1.32e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 1.32e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1654220539 285 PIHVAADKGHFLALKVLVPVT-DIAAIKKSGISPVHCAAAGAHPHCLELLI 334
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGaDINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
316-376 1.53e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 1.53e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1654220539 316 SPVHCAAAGAHPHCLELLIQAGFDVNfmldqrirkHYDDQRKSALYFAVSNGDLPSVKLLL 376
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADIN---------AVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
111-238 1.89e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 44.23  E-value: 1.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 111 ERTTHnGETALFLAVSSSLLENAHFLLlkGCNP----NAKTSE---GNSPLLTAVLKDAYDMATLLISHGADVnlrcANE 183
Cdd:cd22192    46 QRGAL-GETALHVAALYDNLEAAVVLM--EAAPelvnEPMTSDlyqGETALHIAVVNQNLNLVRELIARGADV----VSP 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 184 RTA------------------LHEAAKLGRLDMVKLMLASGAYPDARSSYG----------------------------- 216
Cdd:cd22192   119 RATgtffrpgpknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGntvlhilvlqpnktfacqmydlilsydke 198
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1654220539 217 --------------FTPLALAAQGGHTGIMQLLLQK 238
Cdd:cd22192   199 ddlqpldlvpnnqgLTPFKLAAKEGNIVMFQHLVQK 234
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
148-293 2.27e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 44.10  E-value: 2.27e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 148 SEGNSPLLTAVLKD---AYDMATLLISHGAD-------VNLRCANE----RTALHEAAKLGRLDMVKLMLASGAYPDARS 213
Cdd:cd21882    24 ATGKTCLHKAALNLndgVNEAIMLLLEAAPDsgnpkelVNAPCTDEfyqgQTALHIAIENRNLNLVRLLVENGADVSARA 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 214 S-------------YGFTPLALAAQGGHTGIMQLLLQKGADVHS-QASDS--SSVL--LEAVRGGNPEAVS-------LL 268
Cdd:cd21882   104 TgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQPAAlEAQDSlgNTVLhaLVLQADNTPENSAfvcqmynLL 183
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1654220539 269 LEYGADAN-------IPKSSGHLPIHVAADKG 293
Cdd:cd21882   184 LSYGAHLDptqqleeIPNHQGLTPLKLAAVEG 215
Ank_4 pfam13637
Ankyrin repeats (many copies);
119-170 2.88e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 2.88e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1654220539 119 TALFLAVSSSLLENAHFLLLKGCNPNAKTSEGNSPLLTAVLKDAYDMATLLI 170
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SOCS_ASB1 cd03720
SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a ...
530-572 3.67e-04

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: 38.17  E-value: 3.67e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1654220539 530 NPRSLQHLCRLKIRKCMGRLRLRcpvFMSFLPLPNLLKAYVLY 572
Cdd:cd03720     2 NPRSLLSLCRIAVRRALGKQRLS---LICSLPLPDPIKKFLLH 41
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
184-253 4.78e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all 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.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 43.21  E-value: 4.78e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 184 RTALHEAAKLGRLDMVKLMLASGAYPDARSS--------------YGFTPLALAAQGGHTGIMQLLLQKGAD-VHSQASD 248
Cdd:cd22194   142 QTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPEIVQLLMEKESTdITSQDSR 221

                  ....*
gi 1654220539 249 SSSVL 253
Cdd:cd22194   222 GNTVL 226
SOCS_SSB1 cd03744
SOCS (suppressors of cytokine signaling) box of SSB1 (SPRY domain-containing SOCS box proteins) ...
531-573 5.50e-04

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: 38.04  E-value: 5.50e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1654220539 531 PRSLQHLCRLKIRKCMGRLRLRcpvFMSFLPLPNLLKAYVLYK 573
Cdd:cd03744     3 PLPLMDLCRRSVRLALGRERLS---EIHTLPLPASLKNYLLYQ 42
Ank_4 pfam13637
Ankyrin repeats (many copies);
250-302 5.96e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 5.96e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1654220539 250 SSVLLEAVRGGNPEAVSLLLEYGADANIPKSSGHLPIHVAADKGHFLALKVLV 302
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SOCS_SSB4 cd03743
SOCS (suppressors of cytokine signaling) box of SSB4 (SPRY domain-containing SOCS box ...
531-573 6.36e-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: 37.63  E-value: 6.36e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1654220539 531 PRSLQHLCRLKIRKCMGRLRLRcpvFMSFLPLPNLLKAYVLYK 573
Cdd:cd03743     3 PLPLMDLCRRSARQALGRHRLH---HIQSLPLPQTLKNYLQYQ 42
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
215-245 7.22e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 7.22e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1654220539 215 YGFTPLALAA-QGGHTGIMQLLLQKGADVHSQ 245
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
215-243 7.57e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 7.57e-04
                           10        20
                   ....*....|....*....|....*....
gi 1654220539  215 YGFTPLALAAQGGHTGIMQLLLQKGADVH 243
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
SOCS_SOCS7 cd03741
SOCS (suppressors of cytokine signaling) box of SOCS7-like proteins. Together with CIS1, the ...
530-575 7.73e-04

SOCS (suppressors of cytokine signaling) box of SOCS7-like proteins. Together with CIS1, the CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 domain. SOCS7 is important in the functioning of neuronal 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: 239710  Cd Length: 49  Bit Score: 37.77  E-value: 7.73e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1654220539 530 NPRSLQHLCRLKIRKcMGRLRLrcpvfMSFLPLPNLLKAYVLYKEY 575
Cdd:cd03741     2 NVQSLQHLCRFVIRK-LVRRDH-----IPALPLPRRLIDYLREKHY 41
Ank_5 pfam13857
Ankyrin repeats (many copies);
141-190 8.08e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 8.08e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1654220539 141 CNPNAKTSEGNSPLLTAVLKDAYDMATLLISHGADVNLRCANERTALHEA 190
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
358-406 8.92e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.64  E-value: 8.92e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1654220539 358 SALYFAVSNGDLPSVKLLLSAGALPNQDPVN---CLQIALRMGNYELISLLL 406
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNgetALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
142-274 1.11e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.99  E-value: 1.11e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 142 NPNAKTSEGNSPLLTAVLK-DAYDMATLLISHGADVnlrcANERTALHeAAKLGRLDMVKLMLA--------SGAYPDAR 212
Cdd:TIGR00870  44 NINCPDRLGRSALFVAAIEnENLELTELLLNLSCRG----AVGDTLLH-AISLEYVDAVEAILLhllaafrkSGPLELAN 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 213 SSY------GFTPLALAAQGGHTGIMQLLLQKGADVH----------SQASDS---SSVLLEAVRG-GNPEAVSLLLEYG 272
Cdd:TIGR00870 119 DQYtseftpGITALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDSfyhGESPLNAAAClGSPSIVALLSEDP 198

                  ..
gi 1654220539 273 AD 274
Cdd:TIGR00870 199 AD 200
PHA02884 PHA02884
ankyrin repeat protein; Provisional
187-289 1.27e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 41.12  E-value: 1.27e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 187 LHEAAKLGRLDMVKLMLASGAYPDARSSYGF----TPLALAAQGGHTGIMQLLLQKGADVHSQASDSS-SVLLEAVRGGN 261
Cdd:PHA02884   37 LYSSIKFHYTDIIDAILKLGADPEAPFPLSEnsktNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKiTPLYISVLHGC 116
                          90       100
                  ....*....|....*....|....*...
gi 1654220539 262 PEAVSLLLEYGADANIPKSSGHLPIHVA 289
Cdd:PHA02884  117 LKCLEILLSYGADINIQTNDMVTPIELA 144
SOCS_ASB13 cd03729
SOCS (suppressors of cytokine signaling) box of ASB13-like proteins. ASB family members have a ...
530-573 1.47e-03

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: 36.69  E-value: 1.47e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1654220539 530 NPRSLQHLCRLKIRKCMGRlrlRCPVFMSFLPLPNLLKAYVLYK 573
Cdd:cd03729     2 TPLSLQQLCRINLRKALGT---RALEKIAKLNIPNRIIDYLSYN 42
SOCS_SOCS6 cd03740
SOCS (suppressors of cytokine signaling) box of SOCS6-like proteins. Together with CIS1, the ...
532-575 1.50e-03

SOCS (suppressors of cytokine signaling) box of SOCS6-like proteins. Together with CIS1, the CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 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: 239709  Cd Length: 41  Bit Score: 36.63  E-value: 1.50e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1654220539 532 RSLQHLCRLKIRKCMGRLRLRcpvfmsFLPLPNLLKAYVLYKEY 575
Cdd:cd03740     4 RSLQYLCRFVIRQYTRIDLIQ------KLPLPNKMKGYLLEKHY 41
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
182-212 2.22e-03

Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the membrane-associated, spectrin- actin cytoskeleton. This repeat-domain is a 'membrane-binding' domain of up to 24 repeated units, and it mediates most of the protein's binding activities. 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: 2.22e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1654220539 182 NERTALHEAA-KLGRLDMVKLMLASGAYPDAR 212
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNAR 32
SOCS_ASB_9_11 cd03728
SOCS (suppressors of cytokine signaling) box of ASB9 and 11 proteins. ASB family members have ...
531-573 2.64e-03

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: 35.92  E-value: 2.64e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1654220539 531 PRSLQHLCRLKIRKCMGRlrlRCPVFMSFLPLPNLLKAYVLYK 573
Cdd:cd03728     3 PPSLMQLCRLCIRKCFGR---KQHHKIHKLHLPEPLKHFLLYR 42
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
314-341 6.45e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 6.45e-03
                           10        20
                   ....*....|....*....|....*...
gi 1654220539  314 GISPVHCAAAGAHPHCLELLIQAGFDVN 341
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_5 pfam13857
Ankyrin repeats (many copies);
234-289 7.20e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 7.20e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1654220539 234 LLLQKGADVHSQASDSSSVLLEAVRGGNPEAVSLLLEYGADANIPKSSGHLPIHVA 289
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
388-414 7.94e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 7.94e-03
                           10        20
                   ....*....|....*....|....*..
gi 1654220539  388 NCLQIALRMGNYELISLLLRHGANVNY 414
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
176-293 9.35e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). 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.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 39.07  E-value: 9.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539 176 VNLRCANE----RTALHEAAKLGRLDMVKLMLASGAYPDARSS-------------YGFTPLALAAQGGHTGIMQLLLQK 238
Cdd:cd22197    83 VNAQCTDEyyrgHSALHIAIEKRSLQCVKLLVENGADVHARACgrffqkkqgtcfyFGELPLSLAACTKQWDVVNYLLEN 162
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1654220539 239 GADVHS-QASDS--SSVL--LEAVRGGNPEAVSL-------LLEYGADAN-------IPKSSGHLPIHVAADKG 293
Cdd:cd22197   163 PHQPASlQAQDSlgNTVLhaLVMIADNSPENSALvikmydgLLQAGARLCptvqleeISNHEGLTPLKLAAKEG 236
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
86-224 9.70e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 38.91  E-value: 9.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1654220539  86 LHKAAVQLnKNILEITMNasepstWERTTHNGETALFLAVSSSLLEnahflllkgcnpnakTSEGNSPLLTAVLKDAYDM 165
Cdd:TIGR00870  86 LHAISLEY-VDAVEAILL------HLLAAFRKSGPLELANDQYTSE---------------FTPGITALHLAAHRQNYEI 143
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1654220539 166 ATLLISHGADVNLRC-ANE-------------RTALHEAAKLGRLDMVKLMLASGAYPDARSSYGFTPLALAA 224
Cdd:TIGR00870 144 VKLLLERGASVPARAcGDFfvksqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLLV 216
 
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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