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Conserved domains on  [gi|1622854979|ref|XP_028687466|]
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ankyrin repeat and SOCS box protein 3 isoform X5 [Macaca mulatta]

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];
9-230 3.44e-48

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 166.67  E-value: 3.44e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979   9 ALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLKLLLQHGANVNgSHSMCGWNSLHQASFQENAEI 88
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN-ARDKDGETPLHLAAYNGNLEI 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  89 IKLLLKKGANEECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGADPDLY 168
Cdd:COG0666   136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622854979 169 CNEDNWqlPIHAAAQMGHTKILDLLIPLTNRACDTELNKVSPVYSAVFGGHEDCLEILLRNG 230
Cdd:COG0666   216 DNDGKT--ALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
SOCS_ASB3 cd03722
SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a ...
386-436 5.07e-25

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: 96.78  E-value: 5.07e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622854979 386 ATIPSLTHLCRLEIRSSLKSERLRSDSYISELPLPRSLHNYLLYEDVLRMY 436
Cdd:cd03722     1 ASVPSLTHLCRLEIRSSLKSERLRSDSFICQLPLPRSLQDYLLYSDVLRMY 51
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-230 3.44e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 166.67  E-value: 3.44e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979   9 ALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLKLLLQHGANVNgSHSMCGWNSLHQASFQENAEI 88
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN-ARDKDGETPLHLAAYNGNLEI 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  89 IKLLLKKGANEECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGADPDLY 168
Cdd:COG0666   136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622854979 169 CNEDNWqlPIHAAAQMGHTKILDLLIPLTNRACDTELNKVSPVYSAVFGGHEDCLEILLRNG 230
Cdd:COG0666   216 DNDGKT--ALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
SOCS_ASB3 cd03722
SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a ...
386-436 5.07e-25

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: 96.78  E-value: 5.07e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622854979 386 ATIPSLTHLCRLEIRSSLKSERLRSDSYISELPLPRSLHNYLLYEDVLRMY 436
Cdd:cd03722     1 ASVPSLTHLCRLEIRSSLKSERLRSDSFICQLPLPRSLQDYLLYSDVLRMY 51
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-103 7.89e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.71  E-value: 7.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  10 LHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLKLLLQHganVNGSHSMCGWNSLHQASFQENAEII 89
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 1622854979  90 KLLLKKGANEECQD 103
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
6-235 1.05e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 94.32  E-value: 1.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979   6 GFCALHLAASQGHWK---IVQILLEAGADPNATTLEETTPLFLAVENGQ-IDVLKLLLQHGANVNGSHSmCGWNSLHQ-- 79
Cdd:PHA03095   47 GKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDK-VGRTPLHVyl 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  80 ASFQENAEIIKLLLKKGANEECQDDFGITPLFVaaqYGK-----LESLSILISSGANVNCQALDKATPLFIAAQEGHT-- 152
Cdd:PHA03095  126 SGFNINPKVIRLLLRKGADVNALDLYGMTPLAV---LLKsrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPra 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 153 KCVELLLSSGADPDLYCNEDNwqLPIHAAAQMG---HTKILDLL-----IPLTNRACDTELNkvspvYSAVFGGHEDCLE 224
Cdd:PHA03095  203 RIVRELIRAGCDPAATDMLGN--TPLHSMATGSsckRSLVLPLLiagisINARNRYGQTPLH-----YAAVFNNPRACRR 275
                         250
                  ....*....|.
gi 1622854979 225 iLLRNGYSPDA 235
Cdd:PHA03095  276 -LIALGADINA 285
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
9-161 5.84e-12

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: 67.73  E-value: 5.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979   9 ALHLAASQGHWKIVQILLEAgaDPNATTLEET-------TPLFLAVENGQIDVLKLLLQHGANVN-----------GSHS 70
Cdd:cd22192    54 ALHVAALYDNLEAAVVLMEA--APELVNEPMTsdlyqgeTALHIAVVNQNLNLVRELIARGADVVspratgtffrpGPKN 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  71 MC--GWNSLHQASFQENAEIIKLLLKKGANEECQDDFGITPLFV-AAQYGKL---ESLSILISSGANVNCQALDKA---- 140
Cdd:cd22192   132 LIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIlVLQPNKTfacQMYDLILSYDKEDDLQPLDLVpnnq 211
                         170       180
                  ....*....|....*....|...
gi 1622854979 141 --TPLFIAAQEGHTKCVELLLSS 161
Cdd:cd22192   212 glTPFKLAAKEGNIVMFQHLVQK 234
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
389-428 4.86e-10

SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more generic proteins that comprise a large family of E3 ubiquitin protein ligases.


Pssm-ID: 462192  Cd Length: 39  Bit Score: 54.48  E-value: 4.86e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622854979 389 PSLTHLCRLEIRSSLKSERLrsdSYISELPLPRSLHNYLL 428
Cdd:pfam07525   3 RSLQHLCRLAIRRALGKRRL---GAIDKLPLPPLLKDYLL 39
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
389-430 3.06e-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: 49.33  E-value: 3.06e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1622854979  389 PSLTHLCRLEIRSSLKSerlrsdsyISELPLPRSLHNYLLYE 430
Cdd:smart00969   1 RSLQHLCRLAIRRSLGG--------IDKLPLPPRLKDYLLYY 34
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
41-194 1.81e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.46  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  41 TPLF-LAVENGQIDVLKLLLQHGANVNgshsmCGWNSLHQAS--FQENAE-IIKLLLKKG--------ANEECQDDF--G 106
Cdd:TIGR00870  54 SALFvAAIENENLELTELLLNLSCRGA-----VGDTLLHAISleYVDAVEaILLHLLAAFrksgplelANDQYTSEFtpG 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 107 ITPLFVAAQYGKLESLSILISSGANVNCQAldkatplfiaaqeghtKCVELLLSSGADpDLYCNEdnwqLPIHAAAQMGH 186
Cdd:TIGR00870 129 ITALHLAAHRQNYEIVKLLLERGASVPARA----------------CGDFFVKSQGVD-SFYHGE----SPLNAAACLGS 187

                  ....*...
gi 1622854979 187 TKILDLLI 194
Cdd:TIGR00870 188 PSIVALLS 195
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
41-66 4.08e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.35  E-value: 4.08e-06
                           10        20
                   ....*....|....*....|....*.
gi 1622854979   41 TPLFLAVENGQIDVLKLLLQHGANVN 66
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-230 3.44e-48

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 166.67  E-value: 3.44e-48
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979   9 ALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLKLLLQHGANVNgSHSMCGWNSLHQASFQENAEI 88
Cdd:COG0666    57 LLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN-ARDKDGETPLHLAAYNGNLEI 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  89 IKLLLKKGANEECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGADPDLY 168
Cdd:COG0666   136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622854979 169 CNEDNWqlPIHAAAQMGHTKILDLLIPLTNRACDTELNKVSPVYSAVFGGHEDCLEILLRNG 230
Cdd:COG0666   216 DNDGKT--ALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-196 3.68e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 161.66  E-value: 3.68e-46
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979   1 MKTFEGFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLKLLLQHGANVNGSHSMcGWNSLHQA 80
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLA 160
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  81 SFQENAEIIKLLLKKGANEECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLS 160
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622854979 161 SGADPDLYCNEDNwqLPIHAAAQMGHTKILDLLIPL 196
Cdd:COG0666   241 AGADLNAKDKDGL--TALLLAAAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
5-176 2.44e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.17  E-value: 2.44e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979   5 EGFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLKLLLQHGANVNGSHSMcGWNSLHQASFQE 84
Cdd:COG0666   119 DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENG 197
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  85 NAEIIKLLLKKGANEECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGAD 164
Cdd:COG0666   198 HLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLL 277
                         170
                  ....*....|..
gi 1622854979 165 PDLYCNEDNWQL 176
Cdd:COG0666   278 LAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
9-230 2.87e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 135.08  E-value: 2.87e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979   9 ALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLKLLLQHGANVNGSHSMcGWNSLHQASFQENAEI 88
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG-GNTLLHAAARNGDLEI 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  89 IKLLLKKGANEECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGADPDLY 168
Cdd:COG0666   103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622854979 169 CNEDNwqLPIHAAAQMGHTKILDLLIPLTNRACDTELNKVSPVYSAVFGGHEDCLEILLRNG 230
Cdd:COG0666   183 DNDGE--TPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG 242
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
21-274 8.04e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 114.67  E-value: 8.04e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  21 IVQILLEAGADPNATTLEETTPLFLAVENGQIDVLKLLLQHGANVNGSHSMCGWNSLHQASFQENAEIIKLLLKKGANEE 100
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 101 CQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGADPDLYCNEDNwqLPIHA 180
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN--TPLHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 181 AAQMGHTKILDLLIpltNRACDTEL---NKVSPVYSAVFGGHEDCLEILLRNGYSPDAQACLvfgFSSPVCMAFQKEWSc 257
Cdd:COG0666   160 AAANGNLEIVKLLL---EAGADVNArdnDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND---GKTALDLAAENGNL- 232
                         250
                  ....*....|....*..
gi 1622854979 258 effGIVNILLKYGARIN 274
Cdd:COG0666   233 ---EIVKLLLEAGADLN 246
SOCS_ASB3 cd03722
SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a ...
386-436 5.07e-25

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: 96.78  E-value: 5.07e-25
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622854979 386 ATIPSLTHLCRLEIRSSLKSERLRSDSYISELPLPRSLHNYLLYEDVLRMY 436
Cdd:cd03722     1 ASVPSLTHLCRLEIRSSLKSERLRSDSFICQLPLPRSLQDYLLYSDVLRMY 51
Ank_2 pfam12796
Ankyrin repeats (3 copies);
10-103 7.89e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.71  E-value: 7.89e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  10 LHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLKLLLQHganVNGSHSMCGWNSLHQASFQENAEII 89
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 1622854979  90 KLLLKKGANEECQD 103
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
77-167 9.53e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.32  E-value: 9.53e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  77 LHQASFQENAEIIKLLLKKGANEECQDDFGITPLFVAAQYGKLESLSILISSgANVNCQaLDKATPLFIAAQEGHTKCVE 156
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|.
gi 1622854979 157 LLLSSGADPDL 167
Cdd:pfam12796  79 LLLEKGADINV 89
PHA03095 PHA03095
ankyrin-like protein; Provisional
6-235 1.05e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 94.32  E-value: 1.05e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979   6 GFCALHLAASQGHWK---IVQILLEAGADPNATTLEETTPLFLAVENGQ-IDVLKLLLQHGANVNGSHSmCGWNSLHQ-- 79
Cdd:PHA03095   47 GKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDK-VGRTPLHVyl 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  80 ASFQENAEIIKLLLKKGANEECQDDFGITPLFVaaqYGK-----LESLSILISSGANVNCQALDKATPLFIAAQEGHT-- 152
Cdd:PHA03095  126 SGFNINPKVIRLLLRKGADVNALDLYGMTPLAV---LLKsrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPra 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 153 KCVELLLSSGADPDLYCNEDNwqLPIHAAAQMG---HTKILDLL-----IPLTNRACDTELNkvspvYSAVFGGHEDCLE 224
Cdd:PHA03095  203 RIVRELIRAGCDPAATDMLGN--TPLHSMATGSsckRSLVLPLLiagisINARNRYGQTPLH-----YAAVFNNPRACRR 275
                         250
                  ....*....|.
gi 1622854979 225 iLLRNGYSPDA 235
Cdd:PHA03095  276 -LIALGADINA 285
PHA03100 PHA03100
ankyrin repeat protein; Provisional
20-164 4.54e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 92.04  E-value: 4.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  20 KIVQILLEAGADPNATTLEETTPLFLAVEN--GQIDVLKLLLQHGANVNgSHSMCGWNSLHQA--SFQENAEIIKLLLKK 95
Cdd:PHA03100   87 EIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVN-IKNSDGENLLHLYleSNKIDLKILKLLIDK 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  96 GA--NEECQ--------------DDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLL 159
Cdd:PHA03100  166 GVdiNAKNRvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245

                  ....*
gi 1622854979 160 SSGAD 164
Cdd:PHA03100  246 NNGPS 250
PHA03100 PHA03100
ankyrin repeat protein; Provisional
40-290 4.31e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 88.95  E-value: 4.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  40 TTPLFLAVENGQIDVLKLLLQHGANVNgSHSMCGWNSLH-----QASFQENAEIIKLLLKKGANEECQDDFGITPLFVAA 114
Cdd:PHA03100   36 VLPLYLAKEARNIDVVKILLDNGADIN-SSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAI 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 115 QyGKLESLSI---LISSGANVNCQALDKATPLFIAAQEGH--TKCVELLLSSGADPDLYCNEDnwqlpihaaaqmghtKI 189
Cdd:PHA03100  115 S-KKSNSYSIveyLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNRVN---------------YL 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 190 LDLLIPLTNRacdtELNKVSPVYSAVFGGHEDCLEILLRNGYSPDaqACLVFGfSSPVCMAFQKEWSCeffgIVNILLKY 269
Cdd:PHA03100  179 LSYGVPINIK----DVYGFTPLHYAVYNNNPEFVKYLLDLGANPN--LVNKYG-DTPLHIAILNNNKE----IFKLLLNN 247
                         250       260
                  ....*....|....*....|.
gi 1622854979 270 GARINelHLAYCLKYEKFSIF 290
Cdd:PHA03100  248 GPSIK--TIIETLLYFKDKDL 266
PHA02874 PHA02874
ankyrin repeat protein; Provisional
13-229 2.27e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 80.78  E-value: 2.27e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  13 AASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLKLLLQHGANVNGSHSMCGWNS---------------- 76
Cdd:PHA02874   42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPIPCIEKDmiktildcgidvnikd 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  77 ------LHQASFQENAEIIKLLLKKGANEECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEG 150
Cdd:PHA02874  122 aelktfLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYG 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 151 HTKCVELLLSSGADPDLYCNedNWQLPIHAAAqMGHTKILDLLIplTNRAC-DTELNKVSPVYSAV-FGGHEDCLEILLR 228
Cdd:PHA02874  202 DYACIKLLIDHGNHIMNKCK--NGFTPLHNAI-IHNRSAIELLI--NNASInDQDIDGSTPLHHAInPPCDIDIIDILLY 276

                  .
gi 1622854979 229 N 229
Cdd:PHA02874  277 H 277
PHA02876 PHA02876
ankyrin repeat protein; Provisional
10-196 2.58e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 81.26  E-value: 2.58e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  10 LHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLKLLLQHGANVNGSHSmcgwnSLHQASFQENAEII 89
Cdd:PHA02876  182 IHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDL-----SLLKAIRNEDLETS 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  90 KLLLKKGANEECQDDFGITPLFVAAQYGKLESL-SILISSGANVNCQALDKATPLFIAAQEGH-TKCVELLLSSGADPDl 167
Cdd:PHA02876  257 LLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVN- 335
                         170       180
                  ....*....|....*....|....*....
gi 1622854979 168 yCNEDNWQLPIHAAAQMGHTKilDLLIPL 196
Cdd:PHA02876  336 -AADRLYITPLHQASTLDRNK--DIVITL 361
Ank_2 pfam12796
Ankyrin repeats (3 copies);
110-194 7.71e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 7.71e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 110 LFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSgADPDLYCNEDNwqlPIHAAAQMGHTKI 189
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRT---ALHYAARSGHLEI 76

                  ....*
gi 1622854979 190 LDLLI 194
Cdd:pfam12796  77 VKLLL 81
PHA03095 PHA03095
ankyrin-like protein; Provisional
1-173 9.47e-16

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.91  E-value: 9.47e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979   1 MKTFEGFCALH--LAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDV--LKLLLQHGANVNGShSMCGWNS 76
Cdd:PHA03095  112 AKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV-DDRFRSL 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  77 LHQ--ASFQENAEIIKLLLKKGANEECQDDFGITPLFVAAQYGKLESLSI--LISSGANVNCQALDKATPLFIAAQEGHT 152
Cdd:PHA03095  191 LHHhlQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNP 270
                         170       180
                  ....*....|....*....|.
gi 1622854979 153 KCVELLLSSGADPDLYCNEDN 173
Cdd:PHA03095  271 RACRRLIALGADINAVSSDGN 291
PHA03100 PHA03100
ankyrin repeat protein; Provisional
10-232 1.03e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.55  E-value: 1.03e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  10 LHLAASQGHWKIVQILLEAGADPNATTLEETTPLFL-----AVENGQIDVLKLLLQHGANVNgSHSMCGWNSLHQASFQ- 83
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVN-APDNNGITPLLYAISKk 117
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  84 -ENAEIIKLLLKKGANEECQDDFGITPLFVAAQYG--KLESLSILISSGANVNcqALDKatplfiaaqeghtkcVELLLS 160
Cdd:PHA03100  118 sNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNkiDLKILKLLIDKGVDIN--AKNR---------------VNYLLS 180
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622854979 161 SGAD---PDLYCNEdnwqlPIHAAAQMGHTKILDLLIPLTNRACDTELNKVSPVYSAVFGGHEDCLEILLRNGYS 232
Cdd:PHA03100  181 YGVPiniKDVYGFT-----PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA03100 PHA03100
ankyrin repeat protein; Provisional
10-133 1.99e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 77.78  E-value: 1.99e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  10 LHLAASQ--GHWKIVQILLEAGADPNATTLEETTPLFLAVENGQID--VLKLLLQHGANVN-----------GSH----S 70
Cdd:PHA03100  110 LLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINaknrvnyllsyGVPinikD 189
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622854979  71 MCGWNSLHQASFQENAEIIKLLLKKGANEECQDDFGITPLFVAAQYGKLESLSILISSGANVN 133
Cdd:PHA03100  190 VYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
Ank_2 pfam12796
Ankyrin repeats (3 copies);
143-236 3.35e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 3.35e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 143 LFIAAQEGHTKCVELLLSSGADPDlyCNEDNWQLPIHAAAQMGHTKILDLLIPltNRACDTELNKVSPVYSAVFGGHEDC 222
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN--LQDKNGRTALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEI 76
                          90
                  ....*....|....
gi 1622854979 223 LEILLRNGYSPDAQ 236
Cdd:pfam12796  77 VKLLLEKGADINVK 90
PHA02878 PHA02878
ankyrin repeat protein; Provisional
20-166 3.94e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 77.23  E-value: 3.94e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  20 KIVQILLEAGADPNATTLEE-TTPLFLAVENGQIDVLKLLLQHGANVNgSHSMCGWNSLHQASFQENAEIIKLLLKKGAN 98
Cdd:PHA02878  148 EITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVN-IPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  99 EECQDDFGITPLFVAAQYGK-LESLSILISSGANVNCQA-LDKATPLFIAAQEghTKCVELLLSSGADPD 166
Cdd:PHA02878  227 TDARDKCGNTPLHISVGYCKdYDILKLLLEHGVDVNAKSyILGLTALHSSIKS--ERKLKLLLEYGADIN 294
PHA02875 PHA02875
ankyrin repeat protein; Provisional
4-166 9.11e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 75.80  E-value: 9.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979   4 FEGFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLKLLLQHGANVNGSHSMCGWNSLHQASFQ 83
Cdd:PHA02875   33 YDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATIL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  84 ENAEIIKLLLKKGANEECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGA 163
Cdd:PHA02875  113 KKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA 192

                  ...
gi 1622854979 164 DPD 166
Cdd:PHA02875  193 NID 195
PHA02876 PHA02876
ankyrin repeat protein; Provisional
20-194 5.44e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 73.94  E-value: 5.44e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  20 KIVQILLEAGADPNATTLEETTPLFLAVENG-QIDVLKLLLQHGANVNGSHSMcgWNS-LHQAS-FQENAEIIKLLLKKG 96
Cdd:PHA02876  288 RLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRL--YITpLHQAStLDRNKDIVITLLELG 365
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  97 ANEECQDDFGITPLFVAA------------QYG-KLESLS---------------------ILISSGANVNCQALDKATP 142
Cdd:PHA02876  366 ANVNARDYCDKTPIHYAAvrnnvviintllDYGaDIEALSqkigtalhfalcgtnpymsvkTLIDRGANVNSKNKDLSTP 445
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622854979 143 LFIAAQEG-HTKCVELLLSSGADPDLYCNEDNWQLPIhaaaQMGHTKILDLLI 194
Cdd:PHA02876  446 LHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLI----ALEYHGIVNILL 494
PHA02875 PHA02875
ankyrin repeat protein; Provisional
5-133 6.94e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 73.10  E-value: 6.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979   5 EGFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLKLLLQHGANVNgSHSMCGWNSLHQASFQE 84
Cdd:PHA02875  101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD-IEDCCGCTPLIIAMAKG 179
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622854979  85 NAEIIKLLLKKGANeecQDDFG----ITPLFVAAQYGKLESLSILISSGANVN 133
Cdd:PHA02875  180 DIAICKMLLDSGAN---IDYFGkngcVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02878 PHA02878
ankyrin repeat protein; Provisional
9-146 1.21e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.61  E-value: 1.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979   9 ALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLKLLLQHGANVNgSHSMCGWNSLHQA-SFQENAE 87
Cdd:PHA02878  171 ALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTD-ARDKCGNTPLHISvGYCKDYD 249
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  88 IIKLLLKKGANEECQDDF-GITPLFVAAQygKLESLSILISSGANVNCQALDKATPLFIA 146
Cdd:PHA02878  250 ILKLLLEHGVDVNAKSYIlGLTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSA 307
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
386-430 6.89e-13

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: 62.51  E-value: 6.89e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1622854979 386 ATIPSLTHLCRLEIRSSLKSERLrsdSYISELPLPRSLHNYLLYE 430
Cdd:cd03716     1 STPRSLQHLCRLAIRRCLGRRRL---ELIKKLPLPPRLKDYLLYE 42
Ank_2 pfam12796
Ankyrin repeats (3 copies);
5-66 2.18e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 2.18e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622854979   5 EGFCALHLAASQGHWKIVQILLEaGADPNATTlEETTPLFLAVENGQIDVLKLLLQHGANVN 66
Cdd:pfam12796  29 NGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADIN 88
PHA02875 PHA02875
ankyrin repeat protein; Provisional
13-194 2.28e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 68.48  E-value: 2.28e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  13 AASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLKLLLQHGA--NVN--GSHSmcgwnSLHQASFQENAEI 88
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKypDIES-----ELHDAVEEGDVKA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  89 IKLLLKKG--ANEECQDDfGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGADPD 166
Cdd:PHA02875   84 VEELLDLGkfADDVFYKD-GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD 162
                         170       180
                  ....*....|....*....|....*....
gi 1622854979 167 LycnEDNWQL-PIHAAAQMGHTKILDLLI 194
Cdd:PHA02875  163 I---EDCCGCtPLIIAMAKGDIAICKMLL 188
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
13-166 5.78e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.97  E-value: 5.78e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  13 AASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLKLLLQHGANV-----NGSHSMcgWNSL---HQASFQe 84
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVhirdaNGNTAL--WNAIsakHHKIFR- 608
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  85 naeiIKLLLKKGANEECQDDFgitpLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGAD 164
Cdd:PLN03192  609 ----ILYHFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680

                  ..
gi 1622854979 165 PD 166
Cdd:PLN03192  681 VD 682
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
9-161 5.84e-12

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: 67.73  E-value: 5.84e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979   9 ALHLAASQGHWKIVQILLEAgaDPNATTLEET-------TPLFLAVENGQIDVLKLLLQHGANVN-----------GSHS 70
Cdd:cd22192    54 ALHVAALYDNLEAAVVLMEA--APELVNEPMTsdlyqgeTALHIAVVNQNLNLVRELIARGADVVspratgtffrpGPKN 131
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  71 MC--GWNSLHQASFQENAEIIKLLLKKGANEECQDDFGITPLFV-AAQYGKL---ESLSILISSGANVNCQALDKA---- 140
Cdd:cd22192   132 LIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHIlVLQPNKTfacQMYDLILSYDKEDDLQPLDLVpnnq 211
                         170       180
                  ....*....|....*....|...
gi 1622854979 141 --TPLFIAAQEGHTKCVELLLSS 161
Cdd:cd22192   212 glTPFKLAAKEGNIVMFQHLVQK 234
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
387-430 7.92e-12

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: 59.41  E-value: 7.92e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1622854979 387 TIPSLTHLCRLEIRSSLKSERLrsdSYISELPLPRSLHNYLLYE 430
Cdd:cd03587     1 NPRSLQHLCRLAIRRCLGKRRL---DLIDKLPLPPRLKDYLLYK 41
PHA02874 PHA02874
ankyrin repeat protein; Provisional
1-164 8.04e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.91  E-value: 8.04e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979   1 MKTFegfcaLHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLKLLLQHGA--NVNGSHsmcGWNSLH 78
Cdd:PHA02874  124 LKTF-----LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAyaNVKDNN---GESPLH 195
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  79 QASFQENAEIIKLLLKKGANEECQDDFGITPLFVAAQYGKleSLSILISSGANVNCQALDKATPLFIAAQEGHTK-CVEL 157
Cdd:PHA02874  196 NAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR--SAIELLINNASINDQDIDGSTPLHHAINPPCDIdIIDI 273

                  ....*..
gi 1622854979 158 LLSSGAD 164
Cdd:PHA02874  274 LLYHKAD 280
PHA03100 PHA03100
ankyrin repeat protein; Provisional
87-299 3.97e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.69  E-value: 3.97e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  87 EIIKLLLKKGANEECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHT-----KCVELLLSS 161
Cdd:PHA03100   16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEY 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 162 GADPDLYCNEDNWQLPIHAAAQMGHTKILDLLIpltNRACDTELNKV---SPVYSAVFGGHED--CLEILLRNGYSPDAQ 236
Cdd:PHA03100   96 GANVNAPDNNGITPLLYAISKKSNSYSIVEYLL---DNGANVNIKNSdgeNLLHLYLESNKIDlkILKLLIDKGVDINAK 172
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622854979 237 aclvfgfsspvcmafqkewsCEffgiVNILLKYGARINE--------LHLAycLKYEKFSIFRYFLRKGCS 299
Cdd:PHA03100  173 --------------------NR----VNYLLSYGVPINIkdvygftpLHYA--VYNNNPEFVKYLLDLGAN 217
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
389-428 4.86e-10

SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more generic proteins that comprise a large family of E3 ubiquitin protein ligases.


Pssm-ID: 462192  Cd Length: 39  Bit Score: 54.48  E-value: 4.86e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622854979 389 PSLTHLCRLEIRSSLKSERLrsdSYISELPLPRSLHNYLL 428
Cdd:pfam07525   3 RSLQHLCRLAIRRALGKRRL---GAIDKLPLPPLLKDYLL 39
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
86-297 1.00e-09

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 59.20  E-value: 1.00e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  86 AEIIKLLLKKGANEECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGADP 165
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 166 DLycNEDNWQLPIHAAAQMGHTKILDLLIpltnrACDTELNKV-----SPVYSAVFGGHEDCLEILLRNGYSPDAQAclv 240
Cdd:COG0666    81 NA--KDDGGNTLLHAAARNGDLEIVKLLL-----EAGADVNARdkdgeTPLHLAAYNGNLEIVKLLLEAGADVNAQD--- 150
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622854979 241 FGFSSPVCMAFQKewscEFFGIVNILLKYGARINE--------LHLAycLKYEKFSIFRYFLRKG 297
Cdd:COG0666   151 NDGNTPLHLAAAN----GNLEIVKLLLEAGADVNArdndgetpLHLA--AENGHLEIVKLLLEAG 209
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
4-61 1.38e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.30  E-value: 1.38e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622854979   4 FEGFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLKLLLQH 61
Cdd:PTZ00322  113 YDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02989 PHA02989
ankyrin repeat protein; Provisional
20-133 4.17e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 58.60  E-value: 4.17e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  20 KIVQILLEAGADPNATTLEETTPLFLAVENGQI---DVLKLLLQHGANVNGSHSMCGWNSLHQ--ASFQENAEIIKLLLK 94
Cdd:PHA02989   89 KIVKLLLKFGADINLKTFNGVSPIVCFIYNSNInncDMLRFLLSKGINVNDVKNSRGYNLLHMylESFSVKKDVIKILLS 168
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622854979  95 KGANE-ECQDDFGITPLFV----AAQYGKLESLSILISSGANVN 133
Cdd:PHA02989  169 FGVNLfEKTSLYGLTPMNIylrnDIDVISIKVIKYLIKKGVNIE 212
Ank_4 pfam13637
Ankyrin repeats (many copies);
9-59 2.23e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 2.23e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622854979   9 ALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLKLLL 59
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
6-66 2.69e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 55.83  E-value: 2.69e-08
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622854979   6 GFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLKLLLQHGANVN 66
Cdd:PHA03100  192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
389-430 3.06e-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: 49.33  E-value: 3.06e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1622854979  389 PSLTHLCRLEIRSSLKSerlrsdsyISELPLPRSLHNYLLYE 430
Cdd:smart00969   1 RSLQHLCRLAIRRSLGG--------IDKLPLPPRLKDYLLYY 34
PHA03095 PHA03095
ankyrin-like protein; Provisional
86-300 3.12e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.80  E-value: 3.12e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  86 AEIIKLLLKKGANEECQDDFGITPLFVAAQYGK---LESLSILISSGANVNCQALDKATPLFIAAQEGHT-KCVELLLSS 161
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKA 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 162 GADPDLYCNEDNWQLPIHAAAQMGHTKILDLLIPLTNRACDTELNKVSPVysAVFGGHEDC----LEILLRNGYSP---- 233
Cdd:PHA03095  107 GADVNAKDKVGRTPLHVYLSGFNINPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSRNAnvelLRLLIDAGADVyavd 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 234 -----------------------------DAQACLVFGFSSPVCMAFQKewSCEFFGIVNILLKyGARINE--------L 276
Cdd:PHA03095  185 drfrsllhhhlqsfkprarivreliragcDPAATDMLGNTPLHSMATGS--SCKRSLVLPLLIA-GISINArnrygqtpL 261
                         250       260
                  ....*....|....*....|....
gi 1622854979 277 HLAYClkYEKFSIFRYFLRKGCSL 300
Cdd:PHA03095  262 HYAAV--FNNPRACRRLIALGADI 283
PHA02884 PHA02884
ankyrin repeat protein; Provisional
18-146 3.27e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 54.99  E-value: 3.27e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  18 HWKIVQILLEAGADPNA----TTLEETTPLFLAVENGQIDVLKLLLQHGANVNgshsmcgwnslhqaSFQENAEIiklll 93
Cdd:PHA02884   45 YTDIIDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVN--------------RYAEEAKI----- 105
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622854979  94 kkganeecqddfgiTPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIA 146
Cdd:PHA02884  106 --------------TPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELA 144
Ank_4 pfam13637
Ankyrin repeats (many copies);
108-159 3.60e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 3.60e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622854979 108 TPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLL 159
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02884 PHA02884
ankyrin repeat protein; Provisional
87-171 3.88e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 54.60  E-value: 3.88e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  87 EIIKLLLKKGANEECQDDFG----ITPLFVAAQYGKLESLSILISSGANVNCQALD-KATPLFIAAQEGHTKCVELLLSS 161
Cdd:PHA02884   47 DIIDAILKLGADPEAPFPLSenskTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEaKITPLYISVLHGCLKCLEILLSY 126
                          90
                  ....*....|
gi 1622854979 162 GADPDLYCNE 171
Cdd:PHA02884  127 GADINIQTND 136
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
124-234 3.91e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 3.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 124 ILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGADPDLYCNEDNwqLPIHAAAQMGHTKILDLLipLTNRACDT 203
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK--TPLELAEENGFREVVQLL--SRHSQCHF 175
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1622854979 204 ELNKVSPVYSavFGGHEDCLEILLRNGYSPD 234
Cdd:PTZ00322  176 ELGANAKPDS--FTGKPPSLEDSPISSHHPD 204
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
41-201 5.15e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 55.02  E-value: 5.15e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  41 TPLFLAV-ENGQIDVLKLLLQHGANV--NGSHsmcGWNSLHQASFQENAEIIKLLLKKG---ANEECQDDF--GITPLFV 112
Cdd:cd22192    19 SPLLLAAkENDVQAIKKLLKCPSCDLfqRGAL---GETALHVAALYDNLEAAVVLMEAApelVNEPMTSDLyqGETALHI 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 113 AAQYGKLESLSILISSGANVncqALDKAT-----------------PLFIAAQEGHTKCVELLLSSGADpdlycnednwq 175
Cdd:cd22192    96 AVVNQNLNLVRELIARGADV---VSPRATgtffrpgpknliyygehPLSFAACVGNEEIVRLLIEHGAD----------- 161
                         170       180
                  ....*....|....*....|....*...
gi 1622854979 176 lpIHAAAQMGHT--KILdLLIPLTNRAC 201
Cdd:cd22192   162 --IRAQDSLGNTvlHIL-VLQPNKTFAC 186
Ank_4 pfam13637
Ankyrin repeats (many copies);
141-194 6.23e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 6.23e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622854979 141 TPLFIAAQEGHTKCVELLLSSGADPDlYCNEDNWQlPIHAAAQMGHTKILDLLI 194
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADIN-AVDGNGET-ALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
39-93 7.74e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 7.74e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622854979  39 ETTPLFLAVENGQIDVLKLLLQHGANVNGSHSmCGWNSLHQASFQENAEIIKLLL 93
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
SOCS_ASB14 cd03730
SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a ...
390-431 9.12e-08

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: 48.69  E-value: 9.12e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1622854979 390 SLTHLCRLEIRSSLKSERLRSDSYISELPLPRSLHNYLLYED 431
Cdd:cd03730     5 SLKHLCRLKIRACMGRLRLRCPVFMSFLPLPNRLKAYILYKE 46
PHA02798 PHA02798
ankyrin-like protein; Provisional
20-133 1.20e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 53.69  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  20 KIVQILLEAGADPNATTLEETTPLFLAVEN-----GQIDVLKLLLQHGANVN-----GSHSMCgwnSLHQASFQENAEII 89
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINkknsdGETPLY---CLLSNGYINNLEIL 128
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1622854979  90 KLLLKKGANEECQDDFGITPLFVAAQYG---KLESLSILISSGANVN 133
Cdd:PHA02798  129 LFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDIN 175
PHA02878 PHA02878
ankyrin repeat protein; Provisional
7-276 1.28e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 53.73  E-value: 1.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979   7 FCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLKLLLqhgANVNGSHSMCGWNSLHQASFQENA 86
Cdd:PHA02878   38 FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI---RSINKCSVFYTLVAIKDAFNNRNV 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  87 EIIK-LLLKKGANEECQDDFGITPLFVAAQYgKLESLSILISSGANVNCQALDK-ATPLFIAAQEGHTKCVELLLSSGAD 164
Cdd:PHA02878  115 EIFKiILTNRYKNIQTIDLVYIDKKSKDDII-EAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGAN 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 165 PDLYCNEDNWqlPIHAAAQMGHTKILDLLipLTNRACDTELNKV--SPV-YSAVFGGHEDCLEILLRNGYSPDAQAClVF 241
Cdd:PHA02878  194 VNIPDKTNNS--PLHHAVKHYNKPIVHIL--LENGASTDARDKCgnTPLhISVGYCKDYDILKLLLEHGVDVNAKSY-IL 268
                         250       260       270
                  ....*....|....*....|....*....|....*
gi 1622854979 242 GFsSPVCMAFQKEwsceffGIVNILLKYGARINEL 276
Cdd:PHA02878  269 GL-TALHSSIKSE------RKLKLLLEYGADINSL 296
SOCS_SSB1_4 cd03718
SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box ...
390-430 2.06e-07

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: 47.30  E-value: 2.06e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622854979 390 SLTHLCRLEIRSSLKSERLRSdsyISELPLPRSLHNYLLYE 430
Cdd:cd03718     5 PLMDLCRRRVRVALGRDRLEE---IEQLPLPPSLKNYLLYQ 42
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
2-127 2.48e-07

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: 53.22  E-value: 2.48e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979   2 KTFEGFCALHLAASQGHWKIVQILLEAGADPNATTLEE--------------TTPLFLAVENGQIDVLKLLLQHGANVNG 67
Cdd:cd22194   137 EAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTNQPEIVQLLMEKESTDIT 216
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622854979  68 SHSMCGWNSLH------QASFQENAEIIKL---LLKKGAN---EECQDDFGITPLFVAAQYGKLESLSILIS 127
Cdd:cd22194   217 SQDSRGNTVLHalvtvaEDSKTQNDFVKRMydmILLKSENknlETIRNNEGLTPLQLAAKMGKAEILKYILS 288
PHA02798 PHA02798
ankyrin-like protein; Provisional
31-171 1.04e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 50.99  E-value: 1.04e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  31 DPNATTLEETT-PLFLAVENGQIDVLKLLLQHGANVNG-----SHSMCGWNSlHQASFQENAEIIKLLLKKGANEECQDD 104
Cdd:PHA02798   29 NPNEIVNEYSIfQKYLQRDSPSTDIVKLFINLGANVNGldneySTPLCTILS-NIKDYKHMLDIVKILIENGADINKKNS 107
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622854979 105 FGITPLFVAAQYG---KLESLSILISSGANVNCQALDKATPLFIAAQEGHT---KCVELLLSSGADPDLYCNE 171
Cdd:PHA02798  108 DGETPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNNK 180
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
11-65 1.11e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 1.11e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622854979  11 HLAASqGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLKLLLQHGANV 65
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP 141
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
388-429 1.35e-06

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: 44.89  E-value: 1.35e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1622854979 388 IPSLTHLCRLEIRSSLKSERlrsdsyISELPLPRSLHNYLLY 429
Cdd:cd03717     3 VRSLQHLCRFVIRQCTRRDL------IDQLPLPRRLKDYLKE 38
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
41-194 1.81e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 50.46  E-value: 1.81e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  41 TPLF-LAVENGQIDVLKLLLQHGANVNgshsmCGWNSLHQAS--FQENAE-IIKLLLKKG--------ANEECQDDF--G 106
Cdd:TIGR00870  54 SALFvAAIENENLELTELLLNLSCRGA-----VGDTLLHAISleYVDAVEaILLHLLAAFrksgplelANDQYTSEFtpG 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 107 ITPLFVAAQYGKLESLSILISSGANVNCQAldkatplfiaaqeghtKCVELLLSSGADpDLYCNEdnwqLPIHAAAQMGH 186
Cdd:TIGR00870 129 ITALHLAAHRQNYEIVKLLLERGASVPARA----------------CGDFFVKSQGVD-SFYHGE----SPLNAAACLGS 187

                  ....*...
gi 1622854979 187 TKILDLLI 194
Cdd:TIGR00870 188 PSIVALLS 195
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
390-431 2.07e-06

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: 44.82  E-value: 2.07e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1622854979 390 SLTHLCRLEIRSSLKSERLRSDSYISELPLPRSLHNYLLYED 431
Cdd:cd03731     5 PLKHLCRLKIRKLMGLQKLQQPSSMKKLPLPPALKRYILYKE 46
PHA02876 PHA02876
ankyrin repeat protein; Provisional
83-143 2.41e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.06  E-value: 2.41e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622854979  83 QENAEIIKLLLKKGANEECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPL 143
Cdd:PHA02876  155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVL 215
PHA02946 PHA02946
ankyin-like protein; Provisional
5-161 2.65e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 49.67  E-value: 2.65e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979   5 EGFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFL--AVENGQIDVLKLLLQHGANVNGSHSMCGWNSLhQASF 82
Cdd:PHA02946   71 DGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKINNSVDEEGCGPL-LACT 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  83 QENAEIIKLLLKKGANEECQDDFGITPL--FVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQE--GHTKCVELL 158
Cdd:PHA02946  150 DPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKtvKNVDIINLL 229

                  ...
gi 1622854979 159 LSS 161
Cdd:PHA02946  230 LPS 232
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
41-66 4.08e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 43.35  E-value: 4.08e-06
                           10        20
                   ....*....|....*....|....*.
gi 1622854979   41 TPLFLAVENGQIDVLKLLLQHGANVN 66
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
SOCS_SSB4 cd03743
SOCS (suppressors of cytokine signaling) box of SSB4 (SPRY domain-containing SOCS box ...
391-430 5.69e-06

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: 43.02  E-value: 5.69e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622854979 391 LTHLCRLEIRSSLKSERLRsdsYISELPLPRSLHNYLLYE 430
Cdd:cd03743     6 LMDLCRRSARQALGRHRLH---HIQSLPLPQTLKNYLQYQ 42
SOCS_SSB1 cd03744
SOCS (suppressors of cytokine signaling) box of SSB1 (SPRY domain-containing SOCS box proteins) ...
390-430 5.93e-06

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: 43.05  E-value: 5.93e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622854979 390 SLTHLCRLEIRSSLKSERLrsdSYISELPLPRSLHNYLLYE 430
Cdd:cd03744     5 PLMDLCRRSVRLALGRERL---SEIHTLPLPASLKNYLLYQ 42
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
5-36 7.63e-06

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 42.66  E-value: 7.63e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1622854979   5 EGFCALHLAASQ-GHWKIVQILLEAGADPNATT 36
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
89-160 8.08e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 8.08e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622854979  89 IKLLLKKGANEECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLS 160
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
73-126 8.09e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 8.09e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622854979  73 GWNSLHQASFQENAEIIKLLLKKGANEECQDDFGITPLFVAAQYGKLESLSILI 126
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
4-127 9.30e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong 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: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 47.87  E-value: 9.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979   4 FEGFCALHLAASQGHWKIVQILLEAGADPNAT--------TLEET------TPLFLAVENGQIDVLKLLLQHG---ANVN 66
Cdd:cd22193    74 YEGQTALHIAIERRQGDIVALLVENGADVHAHakgrffqpKYQGEgfyfgeLPLSLAACTNQPDIVQYLLENEhqpADIE 153
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622854979  67 GSHSMcGWNSLHQA-----SFQENAEIIK----LLLKKGAN-------EECQDDFGITPLFVAAQYGKLESLSILIS 127
Cdd:cd22193   154 AQDSR-GNTVLHALvtvadNTKENTKFVTrmydMILIRGAKlcptvelEEIRNNDGLTPLQLAAKMGKIEILKYILQ 229
PHA02878 PHA02878
ankyrin repeat protein; Provisional
86-274 1.11e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.57  E-value: 1.11e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  86 AEIIKLLLKKGANEECQD-DFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGAD 164
Cdd:PHA02878  147 AEITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 165 PDLYCNEDNwqLPIHAAAqmGHTKILDLLIPLTNRACDTELNK----VSPVYSAVFGghEDCLEILLRNGYSPDAqacLV 240
Cdd:PHA02878  227 TDARDKCGN--TPLHISV--GYCKDYDILKLLLEHGVDVNAKSyilgLTALHSSIKS--ERKLKLLLEYGADINS---LN 297
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1622854979 241 FGFSSPVCMAFQKEWSCEFFGIV--NILLKygARIN 274
Cdd:PHA02878  298 SYKLTPLSSAVKQYLCINIGRILisNICLL--KRIK 331
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
387-430 1.53e-05

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


Pssm-ID: 239693  Cd Length: 48  Bit Score: 42.04  E-value: 1.53e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1622854979 387 TIPSLTHLCRLEIRSSLKSerlRSDSYISELPLPRSLHNYLLYE 430
Cdd:cd03723     2 TPRSLQHLCRCAIRKLLGS---RCHKLVPQLSLPTSLKNYLLLE 42
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
4-126 1.65e-05

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. 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: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 47.11  E-value: 1.65e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979   4 FEGFCALHLAASQGHWKIVQILLEAGADPNATTLEE--------------TTPLFLAVENGQIDVLKLLLQH---GANVN 66
Cdd:cd22196    92 YKGQTALHIAIERRNMHLVELLVQNGADVHARASGEffkkkkggpgfyfgELPLSLAACTNQLDIVKFLLENphsPADIS 171
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622854979  67 GSHSMcGWNSLHQA-----SFQENAEIIKL----LLKKGAN-------EECQDDFGITPLFVAAQYGKLESLSILI 126
Cdd:cd22196   172 ARDSM-GNTVLHALvevadNTPENTKFVTKmyneILILGAKirpllklEEITNKKGLTPLKLAAKTGKIGIFAYIL 246
SOCS_WSB_SWIP cd03733
SOCS (suppressors of cytokine signaling) box of WSB/SWiP-like proteins. This subfamily ...
387-429 2.30e-05

SOCS (suppressors of cytokine signaling) box of WSB/SWiP-like proteins. This subfamily contains WSB-1 (SOCS-box-containing WD-40 protein), part of an E3 ubiquitin ligase for the thyroid-hormone-activating type 2 iodothyronine deiodinase (D2), and SWiP-1 (SOCS box and WD-repeats in Protein), a WD40-containing protein that is expressed in embryonic structures of chickens and regulated by Sonic Hedgehog (Shh), as well as, their isoforms WSB-2 and SWiP-2. 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: 239702  Cd Length: 39  Bit Score: 41.25  E-value: 2.30e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1622854979 387 TIPSLTHLCRLEIRSSLKSERlrsdsyISELPLPRSLHNYLLY 429
Cdd:cd03733     2 VVSSLQHLCRMALRRVMTTQQ------VLALPIPKKMKEFLTY 38
Ank_2 pfam12796
Ankyrin repeats (3 copies);
5-35 3.29e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.41  E-value: 3.29e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1622854979   5 EGFCALHLAASQGHWKIVQILLEAGADPNAT 35
Cdd:pfam12796  60 NGRTALHYAARSGHLEIVKLLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
107-306 7.72e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.95  E-value: 7.72e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 107 ITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGADPDLycnednwqLPIHAAAQMGH 186
Cdd:PHA02874   36 TTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI--------LPIPCIEKDMI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 187 TKILDLLIPLTNRacDTELNKVspVYSAVFGGHEDCLEILLRngYSPDAQACLVFGfSSPVCMAFQKewscEFFGIVNIL 266
Cdd:PHA02874  108 KTILDCGIDVNIK--DAELKTF--LHYAIKKGDLESIKMLFE--YGADVNIEDDNG-CYPIHIAIKH----NFFDIIKLL 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1622854979 267 LKYGARIN------ELHLAYCLKYEKFSIFRYFLRKGcslgpwNHI 306
Cdd:PHA02874  177 LEKGAYANvkdnngESPLHNAAEYGDYACIKLLIDHG------NHI 216
SOCS_SSB2 cd03719
SOCS (suppressors of cytokine signaling) box of SSB2 (SPRY domain-containing SOCS box proteins) ...
390-430 9.77e-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: 39.62  E-value: 9.77e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622854979 390 SLTHLCRLEIRSSLKSERLrsdSYISELPLPRSLHNYLLYE 430
Cdd:cd03719     5 SLLHLSRLCVRHALGDTRL---GQVSALPLPPAMKRYLLYQ 42
SOCS_WSB1_SWIP1 cd03746
SOCS (suppressors of cytokine signaling) box of WSB1/SWiP1-like proteins. This subfamily ...
388-430 9.90e-05

SOCS (suppressors of cytokine signaling) box of WSB1/SWiP1-like proteins. This subfamily contains WSB-1 (SOCS-box-containing WD-40 protein), part of an E3 ubiquitin ligase for the thyroid-hormone-activating type 2 iodothyronine deiodinase (D2) and SWiP-1 (SOCS box and WD-repeats in Protein), a WD40-containing protein that is expressed in embryonic structures of chickens and regulated by Sonic Hedgehog (Shh). 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: 239715  Cd Length: 40  Bit Score: 39.41  E-value: 9.90e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1622854979 388 IPSLTHLCRLEIRsslkseRLRSDSYISELPLPRSLHNYLLYE 430
Cdd:cd03746     3 VASLQHLCRMAIR------RVMPTQQVKELPIPSKLLEFLTYR 39
Ank_2 pfam12796
Ankyrin repeats (3 copies);
178-274 1.00e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.87  E-value: 1.00e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 178 IHAAAQMGHTKILDLLIPLTNRACDTELNKVSPVYSAVFGGHEDCLEILLRNgyspdAQACLVFGFSSPVCMAFQkewsC 257
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-----ADVNLKDNGRTALHYAAR----S 71
                          90
                  ....*....|....*..
gi 1622854979 258 EFFGIVNILLKYGARIN 274
Cdd:pfam12796  72 GHLEIVKLLLEKGADIN 88
Ank_4 pfam13637
Ankyrin repeats (many copies);
177-227 1.10e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 1.10e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622854979 177 PIHAAAQMGHTKILDLLIPLTNRACDTELNKVSPVYSAVFGGHEDCLEILL 227
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SOCS_SOCS7 cd03741
SOCS (suppressors of cytokine signaling) box of SOCS7-like proteins. Together with CIS1, the ...
390-429 1.28e-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: 39.31  E-value: 1.28e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622854979 390 SLTHLCRLEIRSSLkserlRSDsYISELPLPRSLHNYLLY 429
Cdd:cd03741     5 SLQHLCRFVIRKLV-----RRD-HIPALPLPRRLIDYLRE 38
Ank_5 pfam13857
Ankyrin repeats (many copies);
5-46 1.34e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.64  E-value: 1.34e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1622854979   5 EGFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLA 46
Cdd:pfam13857  15 EGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SOCS smart00253
suppressors of cytokine signalling; suppressors of cytokine signalling
389-429 1.81e-04

suppressors of cytokine signalling; suppressors of cytokine signalling


Pssm-ID: 128549  Cd Length: 43  Bit Score: 38.82  E-value: 1.81e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1622854979  389 PSLTHLCRLEIRSSLKSErlrsdsYISELPLPRSLHNYLLY 429
Cdd:smart00253   8 PSLQHLCRFTIRRCTRTD------QIKTLPLPPKLKDYLSY 42
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
4-120 2.07e-04

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: 43.69  E-value: 2.07e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979   4 FEGFCALHLAASQGHWKIVQILLEAGADPNATTLEE-------------TTPLFLAVENGQIDVLKLLLQHG---ANVNG 67
Cdd:cd22197    92 YRGHSALHIAIEKRSLQCVKLLVENGADVHARACGRffqkkqgtcfyfgELPLSLAACTKQWDVVNYLLENPhqpASLQA 171
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622854979  68 SHSMcGWNSLHQASF-----QENAEII----KLLLKKGAN-------EECQDDFGITPLFVAAQYGKLE 120
Cdd:cd22197   172 QDSL-GNTVLHALVMiadnsPENSALVikmyDGLLQAGARlcptvqlEEISNHEGLTPLKLAAKEGKIE 239
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
4-139 2.08e-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: 43.72  E-value: 2.08e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979   4 FEGFCALHLAASQGHWKIVQILLEAGAD----PNATTLEETT---------PLFLAVENGQIDVLKLLLQHGANVNGSHS 70
Cdd:cd21882    71 YQGQTALHIAIENRNLNLVRLLVENGADvsarATGRFFRKSPgnlfyfgelPLSLAACTNQEEIVRLLLENGAQPAALEA 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  71 M--CGWNSLHQASFQEN---------AEIIKLLLKKGAN-------EECQDDFGITPLFVAAQYGKLESLSILISSGANV 132
Cdd:cd21882   151 QdsLGNTVLHALVLQADntpensafvCQMYNLLLSYGAHldptqqlEEIPNHQGLTPLKLAAVEGKIVMFQHILQREFSG 230

                  ....*..
gi 1622854979 133 NCQALDK 139
Cdd:cd21882   231 PYQPLSR 237
PHA02859 PHA02859
ankyrin repeat protein; Provisional
41-112 2.39e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.11  E-value: 2.39e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622854979  41 TPLFLAVENGQI--DVLKLLLQHGANVNGSHSMCGWNSLHQ-ASFQENA--EIIKLLLKKGANEECQDDFGITPLFV 112
Cdd:PHA02859   53 TPIFSCLEKDKVnvEILKFLIENGADVNFKTRDNNLSALHHyLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHM 129
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
2-67 3.11e-04

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 42.63  E-value: 3.11e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622854979   2 KTFEGFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLKLLLQHGANVNG 67
Cdd:COG0666   215 KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
41-66 3.31e-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: 38.04  E-value: 3.31e-04
                          10        20
                  ....*....|....*....|....*..
gi 1622854979  41 TPLFLAV-ENGQIDVLKLLLQHGANVN 66
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVN 30
SOCS_WSB2_SWIP2 cd03745
SOCS (suppressors of cytokine signaling) box of WSB2/SWiP2-like proteins. This family consists ...
387-429 3.88e-04

SOCS (suppressors of cytokine signaling) box of WSB2/SWiP2-like proteins. This family consists of WSB-2 (SOCS-box-containing WD-40 protein) and SWiP-2 (SOCS box and WD-repeats in Protein). No functional information is available for WSB2 or SWiP-2, but limited information is available for the isoforms WSB-1 and SWiP-1. 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: 239714  Cd Length: 39  Bit Score: 37.95  E-value: 3.88e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1622854979 387 TIPSLTHLCRLEIRSSLKSERlrsdsyISELPLPRSLHNYLLY 429
Cdd:cd03745     2 VLPSLRHLCRKALRHFLTTYQ------VLALPIPKKMKEFLTY 38
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
41-66 3.91e-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.


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 3.91e-04
                          10        20
                  ....*....|....*....|....*.
gi 1622854979  41 TPLFLAVENGQIDVLKLLLQHGANVN 66
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADIN 29
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
391-431 4.18e-04

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: 37.92  E-value: 4.18e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622854979 391 LTHLCRLEIRSSLKSERLRsdsYISELPLPRSLHNYLLYED 431
Cdd:cd03721     6 LAHLCRLKVRTLIGINRIK---LIDTLPLPPRLIRYLNHQE 43
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
138-167 4.19e-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: 37.57  E-value: 4.19e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1622854979  138 DKATPLFIAAQEGHTKCVELLLSSGADPDL 167
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
9-34 4.53e-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: 37.57  E-value: 4.53e-04
                           10        20
                   ....*....|....*....|....*.
gi 1622854979    9 ALHLAASQGHWKIVQILLEAGADPNA 34
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
141-167 4.62e-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: 37.65  E-value: 4.62e-04
                          10        20
                  ....*....|....*....|....*...
gi 1622854979 141 TPLFIAA-QEGHTKCVELLLSSGADPDL 167
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVNA 31
SOCS_CIS1 cd03734
SOCS (suppressors of cytokine signaling) box of CIS (cytokine-inducible SH2 protein) 1-like ...
387-427 5.35e-04

SOCS (suppressors of cytokine signaling) box of CIS (cytokine-inducible SH2 protein) 1-like proteins. Together with the SOCS proteins, the CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 domain. CIS1, like SOCS1 and SOCS3, is involved in the down-regulation of the JAK/STAT pathway. CIS1 binds to cytokine receptors at STAT5-docking sites, which prohibits recruitment of STAT5 to the receptor signaling complex and results in the down-regulation of activation by STAT5.


Pssm-ID: 239703  Cd Length: 41  Bit Score: 37.64  E-value: 5.35e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622854979 387 TIPSLTHLCRLEIrsslksERLRSDsyISELPLPRSLHNYL 427
Cdd:cd03734     2 SARSLQHLCRLVI------NRLVTD--VDCLPLPRRMADYL 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
147-228 1.08e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 1.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 147 AQEGHTKCVELLLSSGADPDlyCNEDNWQLPIHAAAQMGHTKILDLLIPLTNRACDTELNKVSPVYSAVFGGHEDCLEIL 226
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPN--CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167

                  ..
gi 1622854979 227 LR 228
Cdd:PTZ00322  168 SR 169
SOCS_ASB1 cd03720
SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a ...
390-430 1.27e-03

SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239690  Cd Length: 42  Bit Score: 36.63  E-value: 1.27e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622854979 390 SLTHLCRLEIRSSLKSERLrsdSYISELPLPRSLHNYLLYE 430
Cdd:cd03720     5 SLLSLCRIAVRRALGKQRL---SLICSLPLPDPIKKFLLHE 42
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
5-34 1.42e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.08  E-value: 1.42e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1622854979   5 EGFCALHLAASQGHWKIVQILLEAGADPNA 34
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
40-196 1.74e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.80  E-value: 1.74e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  40 TTPLFLAVENGQIDVLKLLLQHGANVNGSHSmcgwNSLHQASFQENA--EIIKLLLKKGANEECQ-DDFGITPLFVAAQY 116
Cdd:PHA02859   22 CNPLFYYVEKDDIEGVKKWIKFVNDCNDLYE----TPIFSCLEKDKVnvEILKFLIENGADVNFKtRDNNLSALHHYLSF 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 117 GK---LESLSILISSGANVNCQALDKATPLFIAAQEGHTK--CVELLLSSGADPdlyCNEDNWQLPIHAAAQMGHT--KI 189
Cdd:PHA02859   98 NKnvePEILKILIDSGSSITEEDEDGKNLLHMYMCNFNVRinVIKLLIDSGVSF---LNKDFDNNNILYSYILFHSdkKI 174

                  ....*..
gi 1622854979 190 LDLLIPL 196
Cdd:PHA02859  175 FDFLTSL 181
PHA02876 PHA02876
ankyrin repeat protein; Provisional
115-167 2.09e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.43  E-value: 2.09e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622854979 115 QYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGADPDL 167
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNI 206
PHA02874 PHA02874
ankyrin repeat protein; Provisional
117-323 2.41e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.95  E-value: 2.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 117 GKLESLSILISSGAN-VNCQALDKATPLFIAAQEGHTKCVELLLSSGADpdlyCNEDNWQL--PIHAAAQMGHTKILDLL 193
Cdd:PHA02874   12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGAD----INHINTKIphPLLTAIKIGAHDIIKLL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979 194 IpltNRACDTELNKVSPVYSAVFGGHEDC-LEILLRNGYSpdaQACLVFGFsspvcmafqKEWSCEffgIVNILLKYGAR 272
Cdd:PHA02874   88 I---DNGVDTSILPIPCIEKDMIKTILDCgIDVNIKDAEL---KTFLHYAI---------KKGDLE---SIKMLFEYGAD 149
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1622854979 273 IN--------ELHLAycLKYEKFSIFRYFLRKGCSLGPWNHiyeFVNHAIKAQAKYKEW 323
Cdd:PHA02874  150 VNieddngcyPIHIA--IKHNFFDIIKLLLEKGAYANVKDN---NGESPLHNAAEYGDY 203
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
106-134 2.50e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 2.50e-03
                           10        20
                   ....*....|....*....|....*....
gi 1622854979  106 GITPLFVAAQYGKLESLSILISSGANVNC 134
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
SOCS_ASB5 cd03724
SOCS (suppressors of cytokine signaling) box of ASB5-like proteins. ASB family members have a ...
386-429 2.86e-03

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: 35.62  E-value: 2.86e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1622854979 386 ATIPSLTHLCRLEIRSSLKSERLRsdsYISELPLPRSLHNYLLY 429
Cdd:cd03724     1 ATPSSLCQLCRLCIRNYIGRSRLH---LIPQLQLPTLLKNFLQY 41
SOCS_ASB8 cd03727
SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a ...
389-428 3.59e-03

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


Pssm-ID: 239697  Cd Length: 43  Bit Score: 35.20  E-value: 3.59e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622854979 389 PSLTHLCRLEIRSSLkSERLRSDSyISELPLPRSLHNYLL 428
Cdd:cd03727     4 GTLKALARYAVRRSL-GVQYLPEA-VKQLPLPRSVKEYLL 41
PHA03095 PHA03095
ankyrin-like protein; Provisional
6-59 6.13e-03

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 38.85  E-value: 6.13e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622854979   6 GFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLKLLL 59
Cdd:PHA03095  257 GQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
PHA02989 PHA02989
ankyrin repeat protein; Provisional
20-165 6.35e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 38.95  E-value: 6.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  20 KIVQILLEAGADPNATTLEETT-PLFLAVENGQIDVLKLLLQHGANVNG----SHSMCGWNSLHQASFQENAEIIKLLLK 94
Cdd:PHA02989   17 NALEFLLRTGFDVNEEYRGNSIlLLYLKRKDVKIKIVKLLIDNGADVNYkgyiETPLCAVLRNREITSNKIKKIVKLLLK 96
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1622854979  95 KGANEECQDDFGITPL--FV-AAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEG---HTKCVELLLSSGADP 165
Cdd:PHA02989   97 FGADINLKTFNGVSPIvcFIyNSNINNCDMLRFLLSKGINVNDVKNSRGYNLLHMYLESfsvKKDVIKILLSFGVNL 173
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
4-78 8.25e-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: 38.52  E-value: 8.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979   4 FEGFCALHLAASQGHWKIVQILLEAGADPNAT-------TLEETT-------PLFLAVENGQIDVLKLLLQHGANVNGSH 69
Cdd:TIGR00870 126 TPGITALHLAAHRQNYEIVKLLLERGASVPARacgdffvKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTAD 205

                  ....*....
gi 1622854979  70 SMcGWNSLH 78
Cdd:TIGR00870 206 SL-GNTLLH 213
SOCS_SOCS2 cd03736
SOCS (suppressors of cytokine signaling) box of SOCS2-like proteins. Together with CIS1, the ...
389-427 8.62e-03

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: 34.05  E-value: 8.62e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622854979 389 PSLTHLCRLEIRsslkserlRSDSYISELPLPRSLHNYL 427
Cdd:cd03736     4 PSLQHLCRITIN--------KCTRQIQELPLPTRLKDYL 34
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
41-108 8.92e-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: 38.52  E-value: 8.92e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  41 TPLFLAVENGQIDVLKLLLQHGANVN----------GSHSMCGWNSLHQASFQE---NAEIIKLLLKKGANEECQDDFGI 107
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVParacgdffvkSQGVDSFYHGESPLNAAAclgSPSIVALLSEDPADILTADSLGN 209

                  .
gi 1622854979 108 T 108
Cdd:TIGR00870 210 T 210
PHA02736 PHA02736
Viral ankyrin protein; Provisional
52-130 9.08e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 36.78  E-value: 9.08e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622854979  52 IDVLKLLLQHGANVNGSHSMCGWNSLHQASFQENAEIIKLLLKK-GANEECQDDFGITPLFVAAQYGKLESLSILISSGA 130
Cdd:PHA02736   71 QEKLKLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
 
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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