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Conserved domains on  [gi|19111154|ref|NP_579924|]
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ankyrin repeat and SOCS box protein 6 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-210 6.31e-30

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.36  E-value: 6.31e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   1 MPFLHGFRRIIFEYQPLVDAILGALGIQDLERQEPLDDSASSEESRILVLTELLEQKAHSPFYQEGVSNALLKMAELGLT 80
Cdd:COG0666  21 LALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDL 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154  81 RAAAVLLQSGANLNFEDPvTYYTALHIAVLRNQPDMVELLVRHGADINRRDRIHESsPLDLASEEpERLPCLQRLLDLGA 160
Cdd:COG0666 101 EIVKLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNT-PLHLAAAN-GNLEIVKLLLEAGA 177
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 19111154 161 DVNAADKNGKTALLHAlassdgVQIHNTENIRLLLEGGADVKATTKDGDT 210
Cdd:COG0666 178 DVNARDNDGETPLHLA------AENGHLEIVKLLLEAGADVNAKDNDGKT 221
SOCS_ASB6 cd03725
SOCS (suppressors of cytokine signaling) box of ASB6-like proteins. ASB family members have a ...
368-411 3.15e-24

SOCS (suppressors of cytokine signaling) box of ASB6-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ASB6 interacts with the adaptor protein APS and recruits elongin B/C to the insulin receptor signaling complex. 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: 239695  Cd Length: 44  Bit Score: 94.05  E-value: 3.15e-24
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 19111154 368 SYPPPLKHLCRVSIRLCLRPWPVDTKVKALPLPDRLKWYLLSAH 411
Cdd:cd03725   1 SYPPPLKHLCRVFIRLCLRPWPVDVKVKALPLPDRLKWYLLPEH 44
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-210 6.31e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.36  E-value: 6.31e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   1 MPFLHGFRRIIFEYQPLVDAILGALGIQDLERQEPLDDSASSEESRILVLTELLEQKAHSPFYQEGVSNALLKMAELGLT 80
Cdd:COG0666  21 LALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDL 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154  81 RAAAVLLQSGANLNFEDPvTYYTALHIAVLRNQPDMVELLVRHGADINRRDRIHESsPLDLASEEpERLPCLQRLLDLGA 160
Cdd:COG0666 101 EIVKLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNT-PLHLAAAN-GNLEIVKLLLEAGA 177
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 19111154 161 DVNAADKNGKTALLHAlassdgVQIHNTENIRLLLEGGADVKATTKDGDT 210
Cdd:COG0666 178 DVNARDNDGETPLHLA------AENGHLEIVKLLLEAGADVNAKDNDGKT 221
SOCS_ASB6 cd03725
SOCS (suppressors of cytokine signaling) box of ASB6-like proteins. ASB family members have a ...
368-411 3.15e-24

SOCS (suppressors of cytokine signaling) box of ASB6-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ASB6 interacts with the adaptor protein APS and recruits elongin B/C to the insulin receptor signaling complex. 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: 239695  Cd Length: 44  Bit Score: 94.05  E-value: 3.15e-24
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 19111154 368 SYPPPLKHLCRVSIRLCLRPWPVDTKVKALPLPDRLKWYLLSAH 411
Cdd:cd03725   1 SYPPPLKHLCRVFIRLCLRPWPVDVKVKALPLPDRLKWYLLPEH 44
PHA03095 PHA03095
ankyrin-like protein; Provisional
86-269 1.53e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.06  E-value: 1.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   86 LLQSGANLNFEDPVTYyTALHIAVLRNQP---DMVELLVRHGADINRRDRiHESSPLDLASEEPERLPCLQRLLDLGADV 162
Cdd:PHA03095  33 LLAAGADVNFRGEYGK-TPLHLYLHYSSEkvkDIVRLLLEAGADVNAPER-CGFTPLHLYLYNATTLDVIKLLIKAGADV 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154  163 NAADKNGKTAlLHALASSDGVqihNTENIRLLLEGGADVKATTKDGDTVFTCiifLLGETVCgdkeeapminrfCFQVTQ 242
Cdd:PHA03095 111 NAKDKVGRTP-LHVYLSGFNI---NPKVIRLLLRKGADVNALDLYGMTPLAV---LLKSRNA------------NVELLR 171
                        170       180
                 ....*....|....*....|....*...
gi 19111154  243 LLLAHGADPSECPA-HESLTHICLKSFK 269
Cdd:PHA03095 172 LLIDAGADVYAVDDrFRSLLHHHLQSFK 199
Ank_2 pfam12796
Ankyrin repeats (3 copies);
71-166 9.99e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.82  E-value: 9.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154    71 LLKMAELGLTRAAAVLLQSGANLNFEDPvTYYTALHIAVLRNQPDMVELLVRHgADINRRDriHESSPLDLASEEpERLP 150
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD--NGRTALHYAARS-GHLE 75
                          90
                  ....*....|....*.
gi 19111154   151 CLQRLLDLGADVNAAD 166
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
370-408 2.45e-09

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: 52.55  E-value: 2.45e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 19111154   370 PPPLKHLCRVSIRLCLRPWPvDTKVKALPLPDRLKWYLL 408
Cdd:pfam07525   2 PRSLQHLCRLAIRRALGKRR-LGAIDKLPLPPLLKDYLL 39
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
371-408 1.81e-06

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: 44.32  E-value: 1.81e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 19111154    371 PPLKHLCRVSIRLCLRpwpvdtKVKALPLPDRLKWYLL 408
Cdd:smart00969   1 RSLQHLCRLAIRRSLG------GIDKLPLPPRLKDYLL 32
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
102-128 1.60e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 1.60e-05
                           10        20
                   ....*....|....*....|....*..
gi 19111154    102 YTALHIAVLRNQPDMVELLVRHGADIN 128
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
100-177 2.78e-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: 46.34  E-value: 2.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154 100 TYY---TALHIAVLRNQPDMVELLVRHGADINRRD-----RIHESSPLDLASEEPERLPCLQRLLDL----------GAD 161
Cdd:cd22196  90 SYYkgqTALHIAIERRNMHLVELLVQNGADVHARAsgeffKKKKGGPGFYFGELPLSLAACTNQLDIvkfllenphsPAD 169
                        90
                ....*....|....*.
gi 19111154 162 VNAADKNGKTaLLHAL 177
Cdd:cd22196 170 ISARDSMGNT-VLHAL 184
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
35-178 8.45e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.61  E-value: 8.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154    35 PLDDSA---SSEESRILVLTELLEQKAHSPFyqegVSNALLKMAELGLTRA----AAVLLQSGAN------LNFEDPVTY 101
Cdd:TIGR00870  50 RLGRSAlfvAAIENENLELTELLLNLSCRGA----VGDTLLHAISLEYVDAveaiLLHLLAAFRKsgplelANDQYTSEF 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   102 Y---TALHIAVLRNQPDMVELLVRHGADINRR---DRIHESSPLDLASEEPERL--------PCLQRLL-DLGADVNAAD 166
Cdd:TIGR00870 126 TpgiTALHLAAHRQNYEIVKLLLERGASVPARacgDFFVKSQGVDSFYHGESPLnaaaclgsPSIVALLsEDPADILTAD 205
                         170
                  ....*....|..
gi 19111154   167 KNGKTaLLHALA 178
Cdd:TIGR00870 206 SLGNT-LLHLLV 216
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-210 6.31e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.36  E-value: 6.31e-30
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   1 MPFLHGFRRIIFEYQPLVDAILGALGIQDLERQEPLDDSASSEESRILVLTELLEQKAHSPFYQEGVSNALLKMAELGLT 80
Cdd:COG0666  21 LALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDL 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154  81 RAAAVLLQSGANLNFEDPvTYYTALHIAVLRNQPDMVELLVRHGADINRRDRIHESsPLDLASEEpERLPCLQRLLDLGA 160
Cdd:COG0666 101 EIVKLLLEAGADVNARDK-DGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNT-PLHLAAAN-GNLEIVKLLLEAGA 177
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|
gi 19111154 161 DVNAADKNGKTALLHAlassdgVQIHNTENIRLLLEGGADVKATTKDGDT 210
Cdd:COG0666 178 DVNARDNDGETPLHLA------AENGHLEIVKLLLEAGADVNAKDNDGKT 221
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
17-251 2.21e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 107.35  E-value: 2.21e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154  17 LVDAILGALGIQDLERQEPLDDSASSEESRILVLTELLEQKAHSPFYQEGVSNALLKMAELGLTRAAAVLLQSGANLNFE 96
Cdd:COG0666   3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154  97 DPVTYYTALHIAVLRNQPDMVELLVRHGADINRRDRIHEsSPLDLASEEpERLPCLQRLLDLGADVNAADKNGKTALLHA 176
Cdd:COG0666  83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYN-GNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19111154 177 lassdgVQIHNTENIRLLLEGGADVKATTKDGDTVFTCIIFllgetvCGDKEeapminrfcfqVTQLLLAHGADP 251
Cdd:COG0666 161 ------AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE------NGHLE-----------IVKLLLEAGADV 212
SOCS_ASB6 cd03725
SOCS (suppressors of cytokine signaling) box of ASB6-like proteins. ASB family members have a ...
368-411 3.15e-24

SOCS (suppressors of cytokine signaling) box of ASB6-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ASB6 interacts with the adaptor protein APS and recruits elongin B/C to the insulin receptor signaling complex. 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: 239695  Cd Length: 44  Bit Score: 94.05  E-value: 3.15e-24
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....
gi 19111154 368 SYPPPLKHLCRVSIRLCLRPWPVDTKVKALPLPDRLKWYLLSAH 411
Cdd:cd03725   1 SYPPPLKHLCRVFIRLCLRPWPVDVKVKALPLPDRLKWYLLPEH 44
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
70-205 1.02e-16

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 80.00  E-value: 1.02e-16
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154  70 ALLKMAELGLTRAAAVLLQSGANLNFEDPvTYYTALHIAVLRNQPDMVELLVRHGADINRRDRIHEsSPLDLASEEpERL 149
Cdd:COG0666 156 PLHLAAANGNLEIVKLLLEAGADVNARDN-DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGK-TALDLAAEN-GNL 232
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 19111154 150 PCLQRLLDLGADVNAADKNGKTALLHALASSDGVQIHNTENIRLLLEGGADVKATT 205
Cdd:COG0666 233 EIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTL 288
PHA03095 PHA03095
ankyrin-like protein; Provisional
86-269 1.53e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.06  E-value: 1.53e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   86 LLQSGANLNFEDPVTYyTALHIAVLRNQP---DMVELLVRHGADINRRDRiHESSPLDLASEEPERLPCLQRLLDLGADV 162
Cdd:PHA03095  33 LLAAGADVNFRGEYGK-TPLHLYLHYSSEkvkDIVRLLLEAGADVNAPER-CGFTPLHLYLYNATTLDVIKLLIKAGADV 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154  163 NAADKNGKTAlLHALASSDGVqihNTENIRLLLEGGADVKATTKDGDTVFTCiifLLGETVCgdkeeapminrfCFQVTQ 242
Cdd:PHA03095 111 NAKDKVGRTP-LHVYLSGFNI---NPKVIRLLLRKGADVNALDLYGMTPLAV---LLKSRNA------------NVELLR 171
                        170       180
                 ....*....|....*....|....*...
gi 19111154  243 LLLAHGADPSECPA-HESLTHICLKSFK 269
Cdd:PHA03095 172 LLIDAGADVYAVDDrFRSLLHHHLQSFK 199
PHA03100 PHA03100
ankyrin repeat protein; Provisional
86-217 2.53e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.23  E-value: 2.53e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   86 LLQSGANLNfedPVTYY--TALHIAVLRNQPD--MVELLVRHGADINRRDRIhesspldlaseeperlpclQRLLDLGAD 161
Cdd:PHA03100 127 LLDNGANVN---IKNSDgeNLLHLYLESNKIDlkILKLLIDKGVDINAKNRV-------------------NYLLSYGVP 184
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19111154  162 VNAADKNGKTALLHAlassdgVQIHNTENIRLLLEGGADVKATTKDGDtvfTCIIF 217
Cdd:PHA03100 185 INIKDVYGFTPLHYA------VYNNNPEFVKYLLDLGANPNLVNKYGD---TPLHI 231
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
368-408 5.53e-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: 62.90  E-value: 5.53e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 19111154 368 SYPPPLKHLCRVSIRLCLRPWPvDTKVKALPLPDRLKWYLL 408
Cdd:cd03716   1 STPRSLQHLCRLAIRRCLGRRR-LELIKKLPLPPRLKDYLL 40
PHA03095 PHA03095
ankyrin-like protein; Provisional
131-283 1.44e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.82  E-value: 1.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154  131 DRIHESSPLD-LASEEPERLPCLQRLLDLGADVNAADKNGKTALlHALASSDGVQIhnTENIRLLLEGGADVKATTKDGD 209
Cdd:PHA03095   8 DIIMEAALYDyLLNASNVTVEEVRRLLAAGADVNFRGEYGKTPL-HLYLHYSSEKV--KDIVRLLLEAGADVNAPERCGF 84
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 19111154  210 TVFTCIIFLlgetvcgdKEEAPMINrfcfqvtqLLLAHGAD-PSECPAHESLTHICLKSFKLHFPLLCFLLESGA 283
Cdd:PHA03095  85 TPLHLYLYN--------ATTLDVIK--------LLIKAGADvNAKDKVGRTPLHVYLSGFNINPKVIRLLLRKGA 143
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
370-409 1.65e-11

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: 58.64  E-value: 1.65e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 19111154 370 PPPLKHLCRVSIRLCLRPWPVDtKVKALPLPDRLKWYLLS 409
Cdd:cd03587   2 PRSLQHLCRLAIRRCLGKRRLD-LIDKLPLPPRLKDYLLY 40
PHA03100 PHA03100
ankyrin repeat protein; Provisional
86-206 7.12e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.53  E-value: 7.12e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   86 LLQSGANLNFEDpVTYYTALHI-----AVLRNQPDMVELLVRHGADINRRDRIHESSPLDLASEEPERLPCLQRLLDLGA 160
Cdd:PHA03100  54 LLDNGADINSST-KNNSTPLHYlsnikYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVEYLLDNGA 132
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 19111154  161 DVNAADKNGKTaLLHALASSDGVqihNTENIRLLLEGGADVKATTK 206
Cdd:PHA03100 133 NVNIKNSDGEN-LLHLYLESNKI---DLKILKLLIDKGVDINAKNR 174
Ank_2 pfam12796
Ankyrin repeats (3 copies);
71-166 9.99e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.82  E-value: 9.99e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154    71 LLKMAELGLTRAAAVLLQSGANLNFEDPvTYYTALHIAVLRNQPDMVELLVRHgADINRRDriHESSPLDLASEEpERLP 150
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDK-NGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD--NGRTALHYAARS-GHLE 75
                          90
                  ....*....|....*.
gi 19111154   151 CLQRLLDLGADVNAAD 166
Cdd:pfam12796  76 IVKLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
85-269 6.95e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 60.66  E-value: 6.95e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   85 VLLQSGANLNFEDPVTYYTALHIAVLRNQPDMVELLVRHGADINRRDRIhESSPLDLASEEpERLPCLQRLLDLGADVNA 164
Cdd:PHA02878 152 LLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKT-NNSPLHHAVKH-YNKPIVHILLENGASTDA 229
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154  165 ADKNGKTALLHALASsdgvqIHNTENIRLLLEGGADVKATTkdgdtvftciiFLLGETVCGDKEEAPminrfcfQVTQLL 244
Cdd:PHA02878 230 RDKCGNTPLHISVGY-----CKDYDILKLLLEHGVDVNAKS-----------YILGLTALHSSIKSE-------RKLKLL 286
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 19111154  245 LAHGADP------SECPAHES-------------LTHICLKSFK 269
Cdd:PHA02878 287 LEYGADInslnsyKLTPLSSAvkqylcinigrilISNICLLKRI 330
PHA03100 PHA03100
ankyrin repeat protein; Provisional
101-250 8.79e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 60.06  E-value: 8.79e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154  101 YYTALHIAVLRNQPDMVELLVRHGADINRRDRIHeSSPLDLASEEPERLPCLQRLLDL----GADVNAADKNGKTALLHA 176
Cdd:PHA03100  35 PVLPLYLAKEARNIDVVKILLDNGADINSSTKNN-STPLHYLSNIKYNLTDVKEIVKLlleyGANVNAPDNNGITPLLYA 113
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 19111154  177 LASSDGvqihNTENIRLLLEGGADVKATTKDGDTvftciifLLGETVCGDKEEAPMInrfcfqvtQLLLAHGAD 250
Cdd:PHA03100 114 ISKKSN----SYSIVEYLLDNGANVNIKNSDGEN-------LLHLYLESNKIDLKIL--------KLLIDKGVD 168
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
370-408 2.45e-09

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: 52.55  E-value: 2.45e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 19111154   370 PPPLKHLCRVSIRLCLRPWPvDTKVKALPLPDRLKWYLL 408
Cdd:pfam07525   2 PRSLQHLCRLAIRRALGKRR-LGAIDKLPLPPLLKDYLL 39
Ank_2 pfam12796
Ankyrin repeats (3 copies);
105-204 3.10e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 53.58  E-value: 3.10e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   105 LHIAVLRNQPDMVELLVRHGADINRRDRIHEsSPLDLASEEpERLPCLQRLLDlGADVNAADkNGKTALLHALASsdgvq 184
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGR-TALHLAAKN-GHLEIVKLLLE-HADVNLKD-NGRTALHYAARS----- 71
                          90       100
                  ....*....|....*....|
gi 19111154   185 iHNTENIRLLLEGGADVKAT 204
Cdd:pfam12796  72 -GHLEIVKLLLEKGADINVK 90
PHA02876 PHA02876
ankyrin repeat protein; Provisional
75-204 2.23e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 56.23  E-value: 2.23e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   75 AELGLTRAAAVLLQSGANLNFeDPVTYYTALHIAVLRNQPDMVELLVRHGADINRRD----------------------- 131
Cdd:PHA02876 186 AERGNAKMVNLLLSYGADVNI-IALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDlsllkairnedletslllydagf 264
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19111154  132 -----RIHESSPLDLASEEPERLPCLQRLLDLGADVNAADKNGKTALLhaLASSDGvqiHNTENIRLLLEGGADVKAT 204
Cdd:PHA02876 265 svnsiDDCKNTPLHHASQAPSLSRLVPKLLERGADVNAKNIKGETPLY--LMAKNG---YDTENIRTLIMLGADVNAA 337
PHA02875 PHA02875
ankyrin repeat protein; Provisional
46-214 4.82e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 54.61  E-value: 4.82e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   46 RILVLTELLEQKAHSPFYQE-GVSNALLKMAELGLTRAAAVLLQSGanlNFEDPVTY---YTALHIAVLRNQPDMVELLV 121
Cdd:PHA02875  46 RDSEAIKLLMKHGAIPDVKYpDIESELHDAVEEGDVKAVEELLDLG---KFADDVFYkdgMTPLHLATILKKLDIMKLLI 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154  122 RHGAD--INRRDRiheSSPLDLASEEPErLPCLQRLLDLGADVNAADKNGKTALLHALASSdgvqihNTENIRLLLEGGA 199
Cdd:PHA02875 123 ARGADpdIPNTDK---FSPLHLAVMMGD-IKGIELLIDHKACLDIEDCCGCTPLIIAMAKG------DIAICKMLLDSGA 192
                        170
                 ....*....|....*
gi 19111154  200 DVKATTKDGDTVFTC 214
Cdd:PHA02875 193 NIDYFGKNGCVAALC 207
Ank_2 pfam12796
Ankyrin repeats (3 copies);
49-131 3.05e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 48.19  E-value: 3.05e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154    49 VLTELLEQKAHSPFYQEGVSNALLKMAELGLTRAAAVLLQsgaNLNFEDPVTYYTALHIAVLRNQPDMVELLVRHGADIN 128
Cdd:pfam12796  12 LVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADIN 88

                  ...
gi 19111154   129 RRD 131
Cdd:pfam12796  89 VKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
79-212 7.21e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.60  E-value: 7.21e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   79 LTRAAAVLLQSGANLNFEDpVTYYTALHIaVLRNQPDM--VELLVRHGADINRRDRIHeSSPLDLASEEPERLPCLQRLL 156
Cdd:PHA02876 286 LSRLVPKLLERGADVNAKN-IKGETPLYL-MAKNGYDTenIRTLIMLGADVNAADRLY-ITPLHQASTLDRNKDIVITLL 362
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19111154  157 DLGADVNAADKNGKTAlLHALASSDGVQIHNTenirlLLEGGADVKATTKDGDTVF 212
Cdd:PHA02876 363 ELGANVNARDYCDKTP-IHYAAVRNNVVIINT-----LLDYGADIEALSQKIGTAL 412
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
103-209 9.17e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.02  E-value: 9.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154  103 TALHIAVLRNQPDMVELLVRHGADINRRD-------------------RI-----HESSPL---DLASEEPER--LPCLQ 153
Cdd:PLN03192 560 TPLHIAASKGYEDCVLVLLKHACNVHIRDangntalwnaisakhhkifRIlyhfaSISDPHaagDLLCTAAKRndLTAMK 639
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 19111154  154 RLLDLGADVNAADKNGKTALLHALASSdgvqihNTENIRLLLEGGADVKATTKDGD 209
Cdd:PLN03192 640 ELLKQGLNVDSEDHQGATALQVAMAED------HVDMVRLLIMNGADVDKANTDDD 689
PHA03095 PHA03095
ankyrin-like protein; Provisional
103-219 9.94e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.79  E-value: 9.94e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154  103 TALHI--AVLRNQPDMVELLVRHGADINRRDRIHESSPLDLASEEPERLPCLQRLLDLGADVNAADKNGKTALLHALASS 180
Cdd:PHA03095 189 SLLHHhlQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFN 268
                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 19111154  181 dgvqihNTENIRLLLEGGADVKATTKDGdtvFTCIIFLL 219
Cdd:PHA03095 269 ------NPRACRRLIALGADINAVSSDG---NTPLSLMV 298
PHA02798 PHA02798
ankyrin-like protein; Provisional
94-210 1.21e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 50.60  E-value: 1.21e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   94 NFEDPVTYYTALHIAVLRNQP--DMVELLVRHGADINRRDRiHESSPL-DLAS---EEPERLPCLQRLLDLGADVNAADK 167
Cdd:PHA02798  29 NPNEIVNEYSIFQKYLQRDSPstDIVKLFINLGANVNGLDN-EYSTPLcTILSnikDYKHMLDIVKILIENGADINKKNS 107
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 19111154  168 NGKTALLHALASSdgvQIHNTENIRLLLEGGADVKATTKDGDT 210
Cdd:PHA02798 108 DGETPLYCLLSNG---YINNLEILLFMIENGADTTLLDKDGFT 147
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
371-408 1.81e-06

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: 44.32  E-value: 1.81e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 19111154    371 PPLKHLCRVSIRLCLRpwpvdtKVKALPLPDRLKWYLL 408
Cdd:smart00969   1 RSLQHLCRLAIRRSLG------GIDKLPLPPRLKDYLL 32
PHA02875 PHA02875
ankyrin repeat protein; Provisional
33-200 1.84e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.60  E-value: 1.84e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   33 QEPLDDSAssEESRILVLTELLEQK--AHSPFYQEGVSNALL--KMAELGLTRaaaVLLQSGANLNFEDpVTYYTALHIA 108
Cdd:PHA02875  69 ESELHDAV--EEGDVKAVEELLDLGkfADDVFYKDGMTPLHLatILKKLDIMK---LLIARGADPDIPN-TDKFSPLHLA 142
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154  109 VLRNQPDMVELLVRHGADINRRDrIHESSPLDLASEEPERLPClQRLLDLGADVNAADKNGKTALLhalasSDGVQIHNT 188
Cdd:PHA02875 143 VMMGDIKGIELLIDHKACLDIED-CCGCTPLIIAMAKGDIAIC-KMLLDSGANIDYFGKNGCVAAL-----CYAIENNKI 215
                        170
                 ....*....|..
gi 19111154  189 ENIRLLLEGGAD 200
Cdd:PHA02875 216 DIVRLFIKRGAD 227
PHA02876 PHA02876
ankyrin repeat protein; Provisional
86-203 3.20e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.29  E-value: 3.20e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   86 LLQSGANLNFEDpvtYY--TALHIAVLRNQPDMVELLVRHGADINR-RDRIHESSPLDLASEEPerLPCLQRLLDLGADV 162
Cdd:PHA02876 361 LLELGANVNARD---YCdkTPIHYAAVRNNVVIINTLLDYGADIEAlSQKIGTALHFALCGTNP--YMSVKTLIDRGANV 435
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 19111154  163 NAADKNGKTALLHALASSDGVQIhntenIRLLLEGGADVKA 203
Cdd:PHA02876 436 NSKNKDLSTPLHYACKKNCKLDV-----IEMLLDNGADVNA 471
PHA02876 PHA02876
ankyrin repeat protein; Provisional
103-202 6.04e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 6.04e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154  103 TALHIAVLRNQPDM-VELLVRHGADINRRDRiHESSPLDLASEEPERLPCLQRLLDLGADVNAADKNGKTALLHALassd 181
Cdd:PHA02876 410 TALHFALCGTNPYMsVKTLIDRGANVNSKNK-DLSTPLHYACKKNCKLDVIEMLLDNGADVNAINIQNQYPLLIAL---- 484
                         90       100
                 ....*....|....*....|.
gi 19111154  182 gvQIHNTENIrlLLEGGADVK 202
Cdd:PHA02876 485 --EYHGIVNI--LLHYGAELR 501
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
102-132 8.69e-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: 42.28  E-value: 8.69e-06
                          10        20        30
                  ....*....|....*....|....*....|..
gi 19111154   102 YTALHIAVLR-NQPDMVELLVRHGADINRRDR 132
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PHA02876 PHA02876
ankyrin repeat protein; Provisional
71-210 1.02e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.75  E-value: 1.02e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   71 LLKMAELGL-TRAAAVLLQSGANLNFEDPVtYYTALHIA-VLRNQPDMVELLVRHGADINRRDrIHESSPLDLASEEpER 148
Cdd:PHA02876 311 LYLMAKNGYdTENIRTLIMLGADVNAADRL-YITPLHQAsTLDRNKDIVITLLELGANVNARD-YCDKTPIHYAAVR-NN 387
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 19111154  149 LPCLQRLLDLGADVNAADKNGKTALLHALASSDGVQihnteNIRLLLEGGADVKATTKDGDT 210
Cdd:PHA02876 388 VVIINTLLDYGADIEALSQKIGTALHFALCGTNPYM-----SVKTLIDRGANVNSKNKDLST 444
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
49-173 1.18e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 46.87  E-value: 1.18e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154  49 VLTELLEQKAHSPFYQEGVSNALLKMAELGLTRAAAVLLQSGANLNFEDPvTYYTALHIAVLRNQPDMVELLVRHGADIN 128
Cdd:COG0666 168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN-DGKTALDLAAENGNLEIVKLLLEAGADLN 246
                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*
gi 19111154 129 RRDRIHESSPLDLASEEPERLpcLQRLLDLGADVNAADKNGKTAL 173
Cdd:COG0666 247 AKDKDGLTALLLAAAAGAALI--VKLLLLALLLLAAALLDLLTLL 289
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
102-128 1.60e-05

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 41.42  E-value: 1.60e-05
                           10        20
                   ....*....|....*....|....*..
gi 19111154    102 YTALHIAVLRNQPDMVELLVRHGADIN 128
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02798 PHA02798
ankyrin-like protein; Provisional
86-201 1.80e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 46.75  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   86 LLQSGANLNFEDPvTYYTAL-----HIAVLRNQPDMVELLVRHGADINRRDRIHEsSPLD--LASEEPERLPCLQRLLDL 158
Cdd:PHA02798  57 FINLGANVNGLDN-EYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDGE-TPLYclLSNGYINNLEILLFMIEN 134
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 19111154  159 GADVNAADKNGKTALLHALASSDGVQIhntENIRLLLEGGADV 201
Cdd:PHA02798 135 GADTTLLDKDGFTMLQVYLQSNHHIDI---EIIKLLLEKGVDI 174
Ank_5 pfam13857
Ankyrin repeats (many copies);
102-142 1.94e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.95  E-value: 1.94e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 19111154   102 YTALHIAVLRNQPDMVELLVRHGADINRRDRiHESSPLDLA 142
Cdd:pfam13857  17 YTPLHVAAKYGALEIVRVLLAYGVDLNLKDE-EGLTALDLA 56
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
100-177 2.78e-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: 46.34  E-value: 2.78e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154 100 TYY---TALHIAVLRNQPDMVELLVRHGADINRRD-----RIHESSPLDLASEEPERLPCLQRLLDL----------GAD 161
Cdd:cd22196  90 SYYkgqTALHIAIERRNMHLVELLVQNGADVHARAsgeffKKKKGGPGFYFGELPLSLAACTNQLDIvkfllenphsPAD 169
                        90
                ....*....|....*.
gi 19111154 162 VNAADKNGKTaLLHAL 177
Cdd:cd22196 170 ISARDSMGNT-VLHAL 184
PHA02859 PHA02859
ankyrin repeat protein; Provisional
115-211 4.30e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.42  E-value: 4.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154  115 DMVELLVRHGADINRRDRIHESSPLD--LASEEPERLPCLQRLLDLGADVNAADKNGKTaLLHALASSDGVQIhntENIR 192
Cdd:PHA02859  67 EILKFLIENGADVNFKTRDNNLSALHhyLSFNKNVEPEILKILIDSGSSITEEDEDGKN-LLHMYMCNFNVRI---NVIK 142
                         90
                 ....*....|....*....
gi 19111154  193 LLLEGGADVKATTKDGDTV 211
Cdd:PHA02859 143 LLIDSGVSFLNKDFDNNNI 161
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
101-128 4.57e-05

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 40.32  E-value: 4.57e-05
                          10        20
                  ....*....|....*....|....*...
gi 19111154   101 YYTALHIAVLRNQPDMVELLVRHGADIN 128
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
PHA02792 PHA02792
ankyrin-like protein; Provisional
63-216 6.38e-05

ankyrin-like protein; Provisional


Pssm-ID: 165155 [Multi-domain]  Cd Length: 631  Bit Score: 45.33  E-value: 6.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   63 YQEGVSNALLKMAELGLTRAAAV--LLQSGANL-NFEDPVTYYTALHiavlRNQPDMVELLVRHGADI-NRRDRIHESSP 138
Cdd:PHA02792 302 YTDSIQDLLSEYVSYHTVYINVIkcMIDEGATLyRFKHINKYFQKFD----NRDPKVVEYILKNGNVVvEDDDNIINIMP 377
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154  139 L--DLASEEPERLPCLQRLLDLGADVNAADKNGKTALLHALASsdgvqiHNTENIRLLLEGGADVKATTKDGDTVFT-CI 215
Cdd:PHA02792 378 LfpTLSIHESDVLSILKLCKPYIDDINKIDKHGRSILYYCIES------HSVSLVEWLIDNGADINITTKYGSTCIGiCV 451

                 .
gi 19111154  216 I 216
Cdd:PHA02792 452 I 452
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
370-409 7.57e-05

SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 domain. These intracellular proteins regulate the responses of immune cells to cytokines. Identified as negative regulators of the cytokine-JAK-STAT pathway, they seem to play a role in many immunological and pathological processes. The function of the SOCS box is the recruitment of the ubiquitin-transferase system. Related SOCS boxes are also present in Rab40-like proteins and insect proteins of unknown function that also contain a NEUZ (domain in neuralized proteins) domain.


Pssm-ID: 239687  Cd Length: 39  Bit Score: 39.89  E-value: 7.57e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 19111154 370 PPPLKHLCRVSIRLCLRpwpVDtKVKALPLPDRLKWYLLS 409
Cdd:cd03717   3 VRSLQHLCRFVIRQCTR---RD-LIDQLPLPRRLKDYLKE 38
SOCS_ASB14 cd03730
SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a ...
370-413 8.62e-05

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: 40.21  E-value: 8.62e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 19111154 370 PPPLKHLCRVSIRLCLRPWPVDTKV--KALPLPDRLKWYLLSAHSD 413
Cdd:cd03730   3 PRSLKHLCRLKIRACMGRLRLRCPVfmSFLPLPNRLKAYILYKEYD 48
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
44-178 9.70e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 44.62  E-value: 9.70e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154  44 ESRILVLTELLEQKAHSPFYQEGVSNALLKMAELGLTRAAAVLLQSGANLNFEDPVT--YY---TALHIAVLRNQPDMVE 118
Cdd:cd22192  27 ENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTsdLYqgeTALHIAVVNQNLNLVR 106
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 19111154 119 LLVRHGADINR--------RDRIHE-----SSPLDLA----SEEPERLpclqrLLDLGADVNAADKNGKTaLLHALA 178
Cdd:cd22192 107 ELIARGADVVSpratgtffRPGPKNliyygEHPLSFAacvgNEEIVRL-----LIEHGADIRAQDSLGNT-VLHILV 177
PHA02874 PHA02874
ankyrin repeat protein; Provisional
81-187 1.22e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.18  E-value: 1.22e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   81 RAAAVLLQSGANLNFEDpVTYYTALHIAVlrNQP---DMVELLVRHGADINRRDRIHEsSPLDLASEEPERLPCLQRLLD 157
Cdd:PHA02874 235 RSAIELLINNASINDQD-IDGSTPLHHAI--NPPcdiDIIDILLYHKADISIKDNKGE-NPIDTAFKYINKDPVIKDIIA 310
                         90       100       110
                 ....*....|....*....|....*....|
gi 19111154  158 LGADVNAADKNGKTALLHALASSDGVQIHN 187
Cdd:PHA02874 311 NAVLIKEADKLKDSDFLEHIEIKDNKEFSD 340
SOCS_SOCS2 cd03736
SOCS (suppressors of cytokine signaling) box of SOCS2-like proteins. Together with CIS1, the ...
371-407 1.42e-04

SOCS (suppressors of cytokine signaling) box of SOCS2-like proteins. Together with CIS1, the CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 domain. SOCS2 has recently been shown to regulate neuronal differentiation by controlling expression of a neurogenic transcription factor, Neurogenin-1. SOCS2 binds to GH receptors and inhibits the activation of STAT5b induced by GH. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239705  Cd Length: 41  Bit Score: 39.06  E-value: 1.42e-04
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 19111154 371 PPLKHLCRVSIRLCLRpwpvdtKVKALPLPDRLKWYL 407
Cdd:cd03736   4 PSLQHLCRITINKCTR------QIQELPLPTRLKDYL 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
135-181 1.43e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 1.43e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 19111154   135 ESSPLDLASEEpERLPCLQRLLDLGADVNAADKNGKTALLHALASSD 181
Cdd:pfam13637   1 ELTALHAAAAS-GHLELLRLLLEKGADINAVDGNGETALHFAASNGN 46
PHA02874 PHA02874
ankyrin repeat protein; Provisional
86-217 1.44e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 43.80  E-value: 1.44e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   86 LLQSGANLNFEDpVTYYTALHIAVLRNQPDMVELLVRHGADINRRDrIHESSPLDLASEEpERLPCLQRLLDLGADVNAA 165
Cdd:PHA02874 110 ILDCGIDVNIKD-AELKTFLHYAIKKGDLESIKMLFEYGADVNIED-DNGCYPIHIAIKH-NFFDIIKLLLEKGAYANVK 186
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 19111154  166 DKNGKTALLHALASSDgvqihnTENIRLLLEGGADVKATTKDGDT-VFTCIIF 217
Cdd:PHA02874 187 DNNGESPLHNAAEYGD------YACIKLLIDHGNHIMNKCKNGFTpLHNAIIH 233
SOCS smart00253
suppressors of cytokine signalling; suppressors of cytokine signalling
368-409 1.56e-04

suppressors of cytokine signalling; suppressors of cytokine signalling


Pssm-ID: 128549  Cd Length: 43  Bit Score: 38.82  E-value: 1.56e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 19111154    368 SYPPPLKHLCRVSIRLCLRPWPVDTkvkaLPLPDRLKWYLLS 409
Cdd:smart00253   5 SNVPSLQHLCRFTIRRCTRTDQIKT----LPLPPKLKDYLSY 42
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
155-261 1.57e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.12  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154  155 LLDLGADVNAADKNGKTaLLHaLASSDG-VQIhntenIRLLLEGGADVKATTKDGDTVFTciifLLGETVCGDkeeapmi 233
Cdd:PTZ00322 101 LLTGGADPNCRDYDGRT-PLH-IACANGhVQV-----VRVLLEFGADPTLLDKDGKTPLE----LAEENGFRE------- 162
                         90       100       110
                 ....*....|....*....|....*....|.
gi 19111154  234 nrfcfqVTQLLLAHGADPSE---CPAHESLT 261
Cdd:PTZ00322 163 ------VVQLLSRHSQCHFElgaNAKPDSFT 187
PHA02875 PHA02875
ankyrin repeat protein; Provisional
66-128 2.56e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.06  E-value: 2.56e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19111154   66 GVSNALLKMAElGLTRAAAVLLQSGANLNFEDPVTYYTALHIAVLRNQPDMVELLVRHGADIN 128
Cdd:PHA02875 168 GCTPLIIAMAK-GDIAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA03095 PHA03095
ankyrin-like protein; Provisional
120-182 3.01e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 42.70  E-value: 3.01e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19111154  120 LVRHGADINRRDRiHESSPLDLASEEPERLPCLqRLLDLGADVNAADKNGKTALLHALASSDG 182
Cdd:PHA03095 243 LLIAGISINARNR-YGQTPLHYAAVFNNPRACR-RLIALGADINAVSSDGNTPLSLMVRNNNG 303
PHA02876 PHA02876
ankyrin repeat protein; Provisional
85-203 3.12e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.13  E-value: 3.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   85 VLLQSGANLNFEDpVTYYTALHIAVlrNQPDMVEL---LVRHGADINRRDrIHESSPLDLASEEPERLPCLQRLLDLGAD 161
Cdd:PHA02876 258 LLYDAGFSVNSID-DCKNTPLHHAS--QAPSLSRLvpkLLERGADVNAKN-IKGETPLYLMAKNGYDTENIRTLIMLGAD 333
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 19111154  162 VNAADKNGKTAlLHALASSDgvqiHNTENIRLLLEGGADVKA 203
Cdd:PHA02876 334 VNAADRLYITP-LHQASTLD----RNKDIVITLLELGANVNA 370
PHA03100 PHA03100
ankyrin repeat protein; Provisional
72-168 4.49e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.34  E-value: 4.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   72 LKMAELgltraaavLLQSGANLNFEDPVTY---------------YTALHIAVLRNQPDMVELLVRHGADINRRDRIhES 136
Cdd:PHA03100 156 LKILKL--------LIDKGVDINAKNRVNYllsygvpinikdvygFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKY-GD 226
                         90       100       110
                 ....*....|....*....|....*....|..
gi 19111154  137 SPLDLASeEPERLPCLQRLLDLGADVNAADKN 168
Cdd:PHA03100 227 TPLHIAI-LNNNKEIFKLLLNNGPSIKTIIET 257
SOCS_SSB1_4 cd03718
SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box ...
370-408 4.68e-04

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


Pssm-ID: 239688  Cd Length: 42  Bit Score: 37.67  E-value: 4.68e-04
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 19111154 370 PPPLKHLCRVSIRLCLRPWPvDTKVKALPLPDRLKWYLL 408
Cdd:cd03718   3 PLPLMDLCRRRVRVALGRDR-LEEIEQLPLPPSLKNYLL 40
PHA02874 PHA02874
ankyrin repeat protein; Provisional
31-210 5.12e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 42.26  E-value: 5.12e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   31 ERQEPLDDSASSEESRILVLteLLEQKAHSPFYQEGVSNALLKMAELGLTRAAAVLLQSGANLnfedpvtyyTALHIAVL 110
Cdd:PHA02874  34 ETTTPLIDAIRSGDAKIVEL--FIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDT---------SILPIPCI 102
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154  111 RNqpDMVELLVRHGADINRRDRihESSPLDLASEEPERLPCLQRLLDLGADVNAADKNGKTAlLHALASSDGVQIhnten 190
Cdd:PHA02874 103 EK--DMIKTILDCGIDVNIKDA--ELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYP-IHIAIKHNFFDI----- 172
                        170       180
                 ....*....|....*....|
gi 19111154  191 IRLLLEGGADVKATTKDGDT 210
Cdd:PHA02874 173 IKLLLEKGAYANVKDNNGES 192
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
117-173 5.12e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 5.12e-04
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 19111154  117 VELLVRHGADINRRDrIHESSPLDLASEEpERLPCLQRLLDLGADVNAADKNGKTAL 173
Cdd:PTZ00322  98 ARILLTGGADPNCRD-YDGRTPLHIACAN-GHVQVVRVLLEFGADPTLLDKDGKTPL 152
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
370-413 7.26e-04

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: 37.50  E-value: 7.26e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 19111154 370 PPPLKHLCRVSIRLCLRPWPVD--TKVKALPLPDRLKWYLLSAHSD 413
Cdd:cd03731   3 PRPLKHLCRLKIRKLMGLQKLQqpSSMKKLPLPPALKRYILYKEYD 48
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
35-178 8.45e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.61  E-value: 8.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154    35 PLDDSA---SSEESRILVLTELLEQKAHSPFyqegVSNALLKMAELGLTRA----AAVLLQSGAN------LNFEDPVTY 101
Cdd:TIGR00870  50 RLGRSAlfvAAIENENLELTELLLNLSCRGA----VGDTLLHAISLEYVDAveaiLLHLLAAFRKsgplelANDQYTSEF 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   102 Y---TALHIAVLRNQPDMVELLVRHGADINRR---DRIHESSPLDLASEEPERL--------PCLQRLL-DLGADVNAAD 166
Cdd:TIGR00870 126 TpgiTALHLAAHRQNYEIVKLLLERGASVPARacgDFFVKSQGVDSFYHGESPLnaaaclgsPSIVALLsEDPADILTAD 205
                         170
                  ....*....|..
gi 19111154   167 KNGKTaLLHALA 178
Cdd:TIGR00870 206 SLGNT-LLHLLV 216
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
52-174 1.03e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.42  E-value: 1.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   52 ELLEQKAHSPFY----QEGVSNALLKMAELGLTRAAA--------VLLQSGANLNFEDpvtYY--TALHIAVLRNQPDMV 117
Cdd:PTZ00322  55 EATENKDATPDHnlttEEVIDPVVAHMLTVELCQLAAsgdavgarILLTGGADPNCRD---YDgrTPLHIACANGHVQVV 131
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 19111154  118 ELLVRHGADINRRDRiHESSPLDLASEEPER------LPCLQRLLDLGADVNAADKNGKTALL 174
Cdd:PTZ00322 132 RVLLEFGADPTLLDK-DGKTPLELAEENGFRevvqllSRHSQCHFELGANAKPDSFTGKPPSL 193
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
86-173 1.72e-03

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 40.67  E-value: 1.72e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   86 LLQSGANLNFEDPVTYyTALHIAVLRN--QPDMVELLVRHGADINRRDRIHES------------SPLDLASEEPERLPC 151
Cdd:PHA02716 303 FLQPGVKLHYKDSAGR-TCLHQYILRHniSTDIIKLLHEYGNDLNEPDNIGNTvlhtylsmlsvvNILDPETDNDIRLDV 381
                         90       100
                 ....*....|....*....|..
gi 19111154  152 LQRLLDLGADVNAADKNGKTAL 173
Cdd:PHA02716 382 IQCLISLGADITAVNCLGYTPL 403
PHA02989 PHA02989
ankyrin repeat protein; Provisional
113-263 1.74e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 40.49  E-value: 1.74e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154  113 QPDMVELLVRHGADINRRDRIheSSPL-------DLASEEPERLpcLQRLLDLGADVNAADKNGKTALLHALASSDgvqI 185
Cdd:PHA02989  49 KIKIVKLLIDNGADVNYKGYI--ETPLcavlrnrEITSNKIKKI--VKLLLKFGADINLKTFNGVSPIVCFIYNSN---I 121
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 19111154  186 HNTENIRLLLEGGADVKaTTKDGDTVFTCIIFLlgetvcgdkeEAPMINRfcfQVTQLLLAHGADPSECPAHESLTHI 263
Cdd:PHA02989 122 NNCDMLRFLLSKGINVN-DVKNSRGYNLLHMYL----------ESFSVKK---DVIKILLSFGVNLFEKTSLYGLTPM 185
PHA02884 PHA02884
ankyrin repeat protein; Provisional
85-163 2.56e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.58  E-value: 2.56e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154   85 VLLQSGANLNFEDP---VTYYTALHIAVLRNQPDMVELLVRHGADINRRDRIHESSPLDLaSEEPERLPCLQRLLDLGAD 161
Cdd:PHA02884  51 AILKLGADPEAPFPlseNSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYI-SVLHGCLKCLEILLSYGAD 129

                 ..
gi 19111154  162 VN 163
Cdd:PHA02884 130 IN 131
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
103-193 2.73e-03

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: 40.13  E-value: 2.73e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154 103 TALHIAVLRNQPDMVELLVRHGADINRRDR--------IHE-----SSPLDLA--SEEPErlpCLQRLLDLGAD-VNAAD 166
Cdd:cd22194 143 TALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkyKHEgfyfgETPLALAacTNQPE---IVQLLMEKESTdITSQD 219
                        90       100
                ....*....|....*....|....*...
gi 19111154 167 KNGKTaLLHALAS-SDGVQIHNTENIRL 193
Cdd:cd22194 220 SRGNT-VLHALVTvAEDSKTQNDFVKRM 246
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
101-177 3.01e-03

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: 39.78  E-value: 3.01e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154 101 YY---TALHIAVLRNQPDMVELLVRHGADINRRDR-------------IHESSPLDLA--SEEPERLPCLQRLLDLGADV 162
Cdd:cd22193  73 YYegqTALHIAIERRQGDIVALLVENGADVHAHAKgrffqpkyqgegfYFGELPLSLAacTNQPDIVQYLLENEHQPADI 152
                        90
                ....*....|....*
gi 19111154 163 NAADKNGKTaLLHAL 177
Cdd:cd22193 153 EAQDSRGNT-VLHAL 166
Ank_5 pfam13857
Ankyrin repeats (many copies);
119-176 3.14e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 3.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 19111154   119 LLVRHGADINRRDRiHESSPLDLASEEPeRLPCLQRLLDLGADVNAADKNGKTALLHA 176
Cdd:pfam13857   1 LLEHGPIDLNRLDG-EGYTPLHVAAKYG-ALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SOCS_WSB_SWIP cd03733
SOCS (suppressors of cytokine signaling) box of WSB/SWiP-like proteins. This subfamily ...
371-407 3.77e-03

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: 35.09  E-value: 3.77e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 19111154 371 PPLKHLCRVSIRLCLRPWpvdtKVKALPLPDRLKWYL 407
Cdd:cd03733   4 SSLQHLCRMALRRVMTTQ----QVLALPIPKKMKEFL 36
Ank_4 pfam13637
Ankyrin repeats (many copies);
101-156 5.46e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.94  E-value: 5.46e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 19111154   101 YYTALHIAVLRNQPDMVELLVRHGADINRRDRIHEsSPLDLASEEpERLPCLQRLL 156
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGE-TALHFAASN-GNVEVLKLLL 54
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
370-415 5.49e-03

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: 34.84  E-value: 5.49e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*.
gi 19111154 370 PPPLKHLCRVSIRLCLRPWPVdTKVKALPLPDRLKWYLlsAHSDTQ 415
Cdd:cd03721   3 PRPLAHLCRLKVRTLIGINRI-KLIDTLPLPPRLIRYL--NHQETQ 45
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
47-261 7.10e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 38.71  E-value: 7.10e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154  47 ILVLTELLEQKAHSPFYQEGVS--NALLKMA---ELGLTRAAAVLLQSGANLNFEDPVT-------YY---TALHIAVLR 111
Cdd:cd21882   4 LLGLLECLRWYLTDSAYQRGATgkTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKELVnapctdeFYqgqTALHIAIEN 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154 112 NQPDMVELLVRHGADINRR--DRIHESSPLDLA--SEEPerlpclqrlLDLGADVNAADKngktallhalassdgvqihn 187
Cdd:cd21882  84 RNLNLVRLLVENGADVSARatGRFFRKSPGNLFyfGELP---------LSLAACTNQEEI-------------------- 134
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 19111154 188 tenIRLLLEGGADVKATTKD---GDTVFTCIIFLLGETVCGDKeeapminrFCFQVTQLLLAHGA--DPS----ECPAHE 258
Cdd:cd21882 135 ---VRLLLENGAQPAALEAQdslGNTVLHALVLQADNTPENSA--------FVCQMYNLLLSYGAhlDPTqqleEIPNHQ 203

                ...
gi 19111154 259 SLT 261
Cdd:cd21882 204 GLT 206
 
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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