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Conserved domains on  [gi|1953273907|ref|XP_038534702|]
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ankyrin repeat and SOCS box protein 3 isoform X1 [Canis lupus familiaris]

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];
16-250 3.19e-49

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.29  E-value: 3.19e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  16 LAAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIHA-VDssenyIKTKTFEGFCALHLAASQGHWK 94
Cdd:COG0666    60 AAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAgAD-----VNARDKDGETPLHLAAYNGNLE 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  95 IVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLRHGANVNGSHSMcGWNALHQATFQENAEIIKLLLKKGANKE 174
Cdd:COG0666   135 IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVN 213
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953273907 175 CQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHIECVELLVSSGADPDLYCNEDNWQL 250
Cdd:COG0666   214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
SOCS_ASB3 cd03722
SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a ...
459-509 5.65e-26

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: 100.25  E-value: 5.65e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953273907 459 ASVPSLAHLCRLEIRSSLKPEHLRSDSFICQLPLPRSLHNYLLYAEVLRMN 509
Cdd:cd03722     1 ASVPSLTHLCRLEIRSSLKSERLRSDSFICQLPLPRSLQDYLLYSDVLRMY 51
Ank_2 pfam12796
Ankyrin repeats (3 copies);
217-310 1.57e-15

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 1.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 217 LFIAAQEGHIECVELLVSSGADPDlyCNEDNWQLPIHAAAQMGHTKILDLLIPLTNrvCDTGPDKVSPVYSAVFGGHEEC 296
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN--LQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEI 76
                          90
                  ....*....|....
gi 1953273907 297 LEMLLQHGYSPDAQ 310
Cdd:pfam12796  77 VKLLLEKGADINVK 90
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
16-250 3.19e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.29  E-value: 3.19e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  16 LAAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIHA-VDssenyIKTKTFEGFCALHLAASQGHWK 94
Cdd:COG0666    60 AAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAgAD-----VNARDKDGETPLHLAAYNGNLE 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  95 IVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLRHGANVNGSHSMcGWNALHQATFQENAEIIKLLLKKGANKE 174
Cdd:COG0666   135 IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVN 213
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953273907 175 CQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHIECVELLVSSGADPDLYCNEDNWQL 250
Cdd:COG0666   214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
SOCS_ASB3 cd03722
SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a ...
459-509 5.65e-26

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: 100.25  E-value: 5.65e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953273907 459 ASVPSLAHLCRLEIRSSLKPEHLRSDSFICQLPLPRSLHNYLLYAEVLRMN 509
Cdd:cd03722     1 ASVPSLTHLCRLEIRSSLKSERLRSDSFICQLPLPRSLQDYLLYSDVLRMY 51
Ank_2 pfam12796
Ankyrin repeats (3 copies);
84-177 3.04e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 3.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  84 LHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLRHganVNGSHSMCGWNALHQATFQENAEII 163
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 1953273907 164 KLLLKKGANKECQD 177
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
22-238 6.74e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 98.20  E-value: 6.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  22 NVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIhavDSSENyIKTKTFEGFCALHLAASQGH-----WKIV 96
Cdd:PHA03100   14 KVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILL---DNGAD-INSSTKNNSTPLHYLSNIKYnltdvKEIV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  97 QILLEAGADPNATTLEETTPLFLAVEN--GQIDVLRLLLRHGANVNgSHSMCGWNALHQATFQ--ENAEIIKLLLKKGA- 171
Cdd:PHA03100   90 KLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVN-IKNSDGENLLHLYLESnkIDLKILKLLIDKGVd 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 172 -NKECQ--------------DDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHIECVELLVSSG 236
Cdd:PHA03100  169 iNAKNRvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248

                  ..
gi 1953273907 237 AD 238
Cdd:PHA03100  249 PS 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
217-310 1.57e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 1.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 217 LFIAAQEGHIECVELLVSSGADPDlyCNEDNWQLPIHAAAQMGHTKILDLLIPLTNrvCDTGPDKVSPVYSAVFGGHEEC 296
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN--LQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEI 76
                          90
                  ....*....|....
gi 1953273907 297 LEMLLQHGYSPDAQ 310
Cdd:pfam12796  77 VKLLLEKGADINVK 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
42-235 1.64e-15

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: 79.29  E-value: 1.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  42 RGW-MPIHEAAYHNSVECLRMLIHAVDssenyikTKTFE----GFCALHLAASQGHWKIVQILLEAgaDPNATTLEET-- 114
Cdd:cd22192    15 RISeSPLLLAAKENDVQAIKKLLKCPS-------CDLFQrgalGETALHVAALYDNLEAAVVLMEA--APELVNEPMTsd 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 115 -----TPLFLAVENGQIDVLRLLLRHGANVN-----------GSHSMC--GWNALHQATFQENAEIIKLLLKKGANKECQ 176
Cdd:cd22192    86 lyqgeTALHIAVVNQNLNLVRELIARGADVVspratgtffrpGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQ 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953273907 177 DDFGITPLFV-AAQYGKL---ESLSILISSGANVNCQALDKA------TPLFIAAQEGHIECVELLVSS 235
Cdd:cd22192   166 DSLGNTVLHIlVLQPNKTfacQMYDLILSYDKEDDLQPLDLVpnnqglTPFKLAAKEGNIVMFQHLVQK 234
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
460-501 4.43e-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: 54.86  E-value: 4.43e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1953273907 460 SVPSLAHLCRLEIRSSLKPehlRSDSFICQLPLPRSLHNYLL 501
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGK---RRLGAIDKLPLPPLLKDYLL 39
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
462-502 3.37e-09

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: 52.03  E-value: 3.37e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1953273907  462 PSLAHLCRLEIRSSLKpehlrsdsFICQLPLPRSLHNYLLY 502
Cdd:smart00969   1 RSLQHLCRLAIRRSLG--------GIDKLPLPPRLKDYLLY 33
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
198-308 3.04e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 3.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 198 ILISSGANVNCQALDKATPLFIAAQEGHIECVELLVSSGADPDLYCNEDNwqLPIHAAAQMGHTKILDLLipLTNRVCDT 277
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK--TPLELAEENGFREVVQLL--SRHSQCHF 175
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1953273907 278 GPDKVSPVYSavFGGHEECLEMLLQHGYSPD 308
Cdd:PTZ00322  176 ELGANAKPDS--FTGKPPSLEDSPISSHHPD 204
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
16-152 9.36e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.54  E-value: 9.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  16 LAAREGNVKVLRKLLK-KGRSVDVADNRgwmpIHEAA--YHNSVE-CLRMLIHAVDSSENY-----IKTKTF-EGFCALH 85
Cdd:TIGR00870  58 VAAIENENLELTELLLnLSCRGAVGDTL----LHAISleYVDAVEaILLHLLAAFRKSGPLelandQYTSEFtPGITALH 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  86 LAASQGHWKIVQILLEAGADPNAT-------TLEETT-------PLFLAVENGQIDVLRLLLRHGANVNGSHSMcGWNAL 151
Cdd:TIGR00870 134 LAAHRQNYEIVKLLLERGASVPARacgdffvKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSL-GNTLL 212

                  .
gi 1953273907 152 H 152
Cdd:TIGR00870 213 H 213
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
115-140 1.20e-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: 42.19  E-value: 1.20e-05
                           10        20
                   ....*....|....*....|....*.
gi 1953273907  115 TPLFLAVENGQIDVLRLLLRHGANVN 140
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
16-250 3.19e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.29  E-value: 3.19e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  16 LAAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIHA-VDssenyIKTKTFEGFCALHLAASQGHWK 94
Cdd:COG0666    60 AAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAgAD-----VNARDKDGETPLHLAAYNGNLE 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  95 IVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLRHGANVNGSHSMcGWNALHQATFQENAEIIKLLLKKGANKE 174
Cdd:COG0666   135 IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVN 213
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1953273907 175 CQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHIECVELLVSSGADPDLYCNEDNWQL 250
Cdd:COG0666   214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
47-304 3.61e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.29  E-value: 3.61e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  47 IHEAAYHNSVECLRMLIHAVDSSENYIKTKTFEGFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQI 126
Cdd:COG0666    21 LALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDL 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 127 DVLRLLLRHGANVNgSHSMCGWNALHQATFQENAEIIKLLLKKGANKECQDDFGITPLFVAAQYGKLESLSILISSGANV 206
Cdd:COG0666   101 EIVKLLLEAGADVN-ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADV 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 207 NCQALDKATPLFIAAQEGHIECVELLVSSGADPDLYCNEDNWqlPIHAAAQMGHTKILDLLIPLTNRVCDTGPDKVSPVY 286
Cdd:COG0666   180 NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKT--ALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257
                         250
                  ....*....|....*...
gi 1953273907 287 SAVFGGHEECLEMLLQHG 304
Cdd:COG0666   258 LAAAAGAALIVKLLLLAL 275
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
16-270 3.89e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.29  E-value: 3.89e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  16 LAAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIHAVDssenYIKTKTFEGFCALHLAASQGHWKI 95
Cdd:COG0666    27 AAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGA----DINAKDDGGNTLLHAAARNGDLEI 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  96 VQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLRHGANVNGSHSMcGWNALHQATFQENAEIIKLLLKKGANKEC 175
Cdd:COG0666   103 VKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNA 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 176 QDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHIECVELLVSSGADPDLYCNEDNwqLPIHAA 255
Cdd:COG0666   182 RDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGL--TALLLA 259
                         250
                  ....*....|....*
gi 1953273907 256 AQMGHTKILDLLIPL 270
Cdd:COG0666   260 AAAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
95-346 1.24e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.83  E-value: 1.24e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  95 IVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLRHGANVNGSHSMCGWNALHQATFQENAEIIKLLLKKGANKE 174
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 175 CQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHIECVELLVSSGADPDLYCNEDNwqLPIHA 254
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN--TPLHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 255 AAQMGHTKILDLLIpltNRVCD---TGPDKVSPVYSAVFGGHEECLEMLLQHGYSPDAQMCLifgFSSPMCMAFQKDCEf 331
Cdd:COG0666   160 AAANGNLEIVKLLL---EAGADvnaRDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND---GKTALDLAAENGNL- 232
                         250
                  ....*....|....*
gi 1953273907 332 fGIVNILLKYGAQLN 346
Cdd:COG0666   233 -EIVKLLLEAGADLN 246
SOCS_ASB3 cd03722
SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a ...
459-509 5.65e-26

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: 100.25  E-value: 5.65e-26
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953273907 459 ASVPSLAHLCRLEIRSSLKPEHLRSDSFICQLPLPRSLHNYLLYAEVLRMN 509
Cdd:cd03722     1 ASVPSLTHLCRLEIRSSLKSERLRSDSFICQLPLPRSLQDYLLYSDVLRMY 51
Ank_2 pfam12796
Ankyrin repeats (3 copies);
84-177 3.04e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 90.95  E-value: 3.04e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  84 LHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLRHganVNGSHSMCGWNALHQATFQENAEII 163
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 1953273907 164 KLLLKKGANKECQD 177
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
22-238 6.74e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 98.20  E-value: 6.74e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  22 NVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIhavDSSENyIKTKTFEGFCALHLAASQGH-----WKIV 96
Cdd:PHA03100   14 KVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILL---DNGAD-INSSTKNNSTPLHYLSNIKYnltdvKEIV 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  97 QILLEAGADPNATTLEETTPLFLAVEN--GQIDVLRLLLRHGANVNgSHSMCGWNALHQATFQ--ENAEIIKLLLKKGA- 171
Cdd:PHA03100   90 KLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVN-IKNSDGENLLHLYLESnkIDLKILKLLIDKGVd 168
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 172 -NKECQ--------------DDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHIECVELLVSSG 236
Cdd:PHA03100  169 iNAKNRvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248

                  ..
gi 1953273907 237 AD 238
Cdd:PHA03100  249 PS 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
151-241 2.39e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 2.39e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 151 LHQATFQENAEIIKLLLKKGANKECQDDFGITPLFVAAQYGKLESLSILISSgANVNCQaLDKATPLFIAAQEGHIECVE 230
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|.
gi 1953273907 231 LLVSSGADPDL 241
Cdd:pfam12796  79 LLLEKGADINV 89
PHA03095 PHA03095
ankyrin-like protein; Provisional
23-247 4.95e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 95.86  E-value: 4.95e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  23 VKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVE-CLRMLI-HAVDssenyIKTKTFEGFCALH--LAASQGHWKIVQI 98
Cdd:PHA03095   63 KDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIkAGAD-----VNAKDKVGRTPLHvyLSGFNINPKVIRL 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  99 LLEAGADPNATTLEETTPLFLAVENGQIDV--LRLLLRHGANVNGShSMCGWNALHQ--ATFQENAEIIKLLLKKGANKE 174
Cdd:PHA03095  138 LLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV-DDRFRSLLHHhlQSFKPRARIVRELIRAGCDPA 216
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953273907 175 CQDDFGITPLFVAAQYGKLESLSI--LISSGANVNCQALDKATPLFIAAQEGHIECVELLVSSGADPDLYCNEDN 247
Cdd:PHA03095  217 ATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGN 291
PHA03095 PHA03095
ankyrin-like protein; Provisional
23-370 3.71e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 93.17  E-value: 3.71e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  23 VKVLRKLLKKGRSVDVADNRGWMPIHeaayhnsveclrMLIHavdssenyiktkTFEGFCAlhlaasqghwKIVQILLEA 102
Cdd:PHA03095   27 VEEVRRLLAAGADVNFRGEYGKTPLH------------LYLH------------YSSEKVK----------DIVRLLLEA 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 103 GADPNATTLEETTPLFLAVENGQ-IDVLRLLLRHGANVNGSHSmCGWNALHQ--ATFQENAEIIKLLLKKGANKECQDDF 179
Cdd:PHA03095   73 GADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDK-VGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLY 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 180 GITPLFVaaqygkleslsILISSGANVncqaldkatplfiaaqeghiECVELLVSSGADPdlYCNEDNWQLPIHAAAQMG 259
Cdd:PHA03095  152 GMTPLAV-----------LLKSRNANV--------------------ELLRLLIDAGADV--YAVDDRFRSLLHHHLQSF 198
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 260 HTKildllipltnrvcdtgpdkvspvysavfgghEECLEMLLQHGYSPDAQMclIFGFSSPMCMAFQKDCEFFGIVNILL 339
Cdd:PHA03095  199 KPR-------------------------------ARIVRELIRAGCDPAATD--MLGNTPLHSMATGSSCKRSLVLPLLI 245
                         330       340       350
                  ....*....|....*....|....*....|....*....
gi 1953273907 340 KyGAQLNE--------LHLAYClkYEKFSVFRYFLKKGC 370
Cdd:PHA03095  246 A-GISINArnrygqtpLHYAAV--FNNPRACRRLIALGA 281
PHA02875 PHA02875
ankyrin repeat protein; Provisional
21-241 2.13e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 90.44  E-value: 2.13e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  21 GNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLRMLI-HAVDSSENYIKTKTfegfcALHLAASQGHWKIVQIL 99
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMkHGAIPDVKYPDIES-----ELHDAVEEGDVKAVEEL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 100 LEAGADPNATTLEE-TTPLFLAVENGQIDVLRLLLRHGANVNGShSMCGWNALHQATFQENAEIIKLLLKKGANKECQDD 178
Cdd:PHA02875   88 LDLGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGADPDIP-NTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1953273907 179 FGITPLFVAAQYGKLESLSILISSGANVNCQALDK-ATPLFIAAQEGHIECVELLVSSGADPDL 241
Cdd:PHA02875  167 CGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA02876 PHA02876
ankyrin repeat protein; Provisional
47-398 2.17e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 91.66  E-value: 2.17e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  47 IHEAAYHNSVECLRMLIHAVDSSENYIKTKTFEG---------FC--ALHLAASQGHWKIVQILLEAGADPNATTLEETT 115
Cdd:PHA02876  134 IHYDKINESIEYMKLIKERIQQDELLIAEMLLEGgadvnakdiYCitPIHYAAERGNAKMVNLLLSYGADVNIIALDDLS 213
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 116 PLFLAVENGQIDVLRLLLRHGANVNGSHSmcgwnALHQATFQENAEIIKLLLKKGANKECQDDFGITPLFVAAQYGKLES 195
Cdd:PHA02876  214 VLECAVDSKNIDTIKAIIDNRSNINKNDL-----SLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSR 288
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 196 L-SILISSGANVNCQALDKATPLFIAAQEGH-IECVELLVSSGADPDlyCNEDNWQLPIHAAAQMGHTK-ILDLLIPLTN 272
Cdd:PHA02876  289 LvPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVN--AADRLYITPLHQASTLDRNKdIVITLLELGA 366
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 273 RV-----CDTGPDKVSPVYSAV--------FGGHEECLEMLLQ-------HGYSPDAQMCLIFG-----------FSSPM 321
Cdd:PHA02876  367 NVnardyCDKTPIHYAAVRNNVviintlldYGADIEALSQKIGtalhfalCGTNPYMSVKTLIDrganvnsknkdLSTPL 446
                         330       340       350       360       370       380       390       400
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 322 CMAFQKDC------------------------------EFFGIVNILLKYGAQLNELH-LAYCLKYEKFSvFRYFLKKGC 370
Cdd:PHA02876  447 HYACKKNCkldviemlldngadvnainiqnqypllialEYHGIVNILLHYGAELRDSRvLHKSLNDNMFS-FRYIIAHIC 525
                         410       420
                  ....*....|....*....|....*...
gi 1953273907 371 plapwnhISEFISHAVKAQIKYKEWLPS 398
Cdd:PHA02876  526 -------IQDFIRHDIRNEVNPLKRVPT 546
PHA03100 PHA03100
ankyrin repeat protein; Provisional
22-207 2.26e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 87.41  E-value: 2.26e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  22 NVKVLRKLLKKGRSVD--VADNRGWMPIHEAAYHNS---VECLRMLI-HAVDSSENYIKTKTfegfcALHLAASQ--GHW 93
Cdd:PHA03100   47 NIDVVKILLDNGADINssTKNNSTPLHYLSNIKYNLtdvKEIVKLLLeYGANVNAPDNNGIT-----PLLYAISKksNSY 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  94 KIVQILLEAGADPNATTLEETTPLFLAVENGQID--VLRLLLRHGANVN-----------GSH----SMCGWNALHQATF 156
Cdd:PHA03100  122 SIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINaknrvnyllsyGVPinikDVYGFTPLHYAVY 201
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953273907 157 QENAEIIKLLLKKGANKECQDDFGITPLFVAAQYGKLESLSILISSGANVN 207
Cdd:PHA03100  202 NNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
Ank_2 pfam12796
Ankyrin repeats (3 copies);
16-109 3.58e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 3.58e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  16 LAAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIhavdssENYIKTKTFEGFCALHLAASQGHWKI 95
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL------EHADVNLKDNGRTALHYAARSGHLEI 76
                          90
                  ....*....|....
gi 1953273907  96 VQILLEAGADPNAT 109
Cdd:pfam12796  77 VKLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
117-209 1.74e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 1.74e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 117 LFLAVENGQIDVLRLLLRHGANVNgSHSMCGWNALHQATFQENAEIIKLLLKKgANKECQDDfGITPLFVAAQYGKLESL 196
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN-LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIV 77
                          90
                  ....*....|...
gi 1953273907 197 SILISSGANVNCQ 209
Cdd:pfam12796  78 KLLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
17-268 2.82e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 84.24  E-value: 2.82e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  17 AAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLRMLI-HAVDSSEnyiktktfegfcalhLAASQGHWKI 95
Cdd:PHA02874   42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIdNGVDTSI---------------LPIPCIEKDM 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  96 VQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLRHGANVNgSHSMCGWNALHQATFQENAEIIKLLLKKGANKEC 175
Cdd:PHA02874  107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVN-IEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 176 QDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHiECVELLVSSGA--DPDLycnedNWQLPIH 253
Cdd:PHA02874  186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINNASinDQDI-----DGSTPLH 259
                         250
                  ....*....|....*.
gi 1953273907 254 AAAQMGHTK-ILDLLI 268
Cdd:PHA02874  260 HAINPPCDIdIIDILL 275
PHA03100 PHA03100
ankyrin repeat protein; Provisional
114-359 1.64e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 81.64  E-value: 1.64e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 114 TTPLFLAVENGQIDVLRLLLRHGANVNgSHSMCGWNALH-----QATFQENAEIIKLLLKKGANKECQDDFGITPLFVAA 188
Cdd:PHA03100   36 VLPLYLAKEARNIDVVKILLDNGADIN-SSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAI 114
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 189 QyGKLESLSI---LISSGANVNCQALDKATPLFIAAQEGHI--ECVELLVSSGADPDLYCNED---NWQLPIHAAAQMGH 260
Cdd:PHA03100  115 S-KKSNSYSIveyLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRVNyllSYGVPINIKDVYGF 193
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 261 TkildllipltnrvcdtgpdkvsPVYSAVFGGHEECLEMLLQHGYSPDAQMCliFGfSSPMCMAFQKDCEFfgIVNILLK 340
Cdd:PHA03100  194 T----------------------PLHYAVYNNNPEFVKYLLDLGANPNLVNK--YG-DTPLHIAILNNNKE--IFKLLLN 246
                         250
                  ....*....|....*....
gi 1953273907 341 YGAqlNELHLAYCLKYEKF 359
Cdd:PHA03100  247 NGP--SIKTIIETLLYFKD 263
Ank_2 pfam12796
Ankyrin repeats (3 copies);
184-268 3.46e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.61  E-value: 3.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 184 LFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHIECVELLVSSgADPDLYCNEDNwqlPIHAAAQMGHTKI 263
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRT---ALHYAARSGHLEI 76

                  ....*
gi 1953273907 264 LDLLI 268
Cdd:pfam12796  77 VKLLL 81
PHA02874 PHA02874
ankyrin repeat protein; Provisional
59-289 5.74e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 80.01  E-value: 5.74e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  59 LRMLIHAVDSS--ENYIKTKTF-------EGFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVL 129
Cdd:PHA02874    5 LRMCIYSGDIEaiEKIIKNKGNcinisvdETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDII 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 130 RLLLRHGANVN------------GSHSMCGWNA----------LHQATFQENAEIIKLLLKKGANKECQDDFGITPLFVA 187
Cdd:PHA02874   85 KLLIDNGVDTSilpipciekdmiKTILDCGIDVnikdaelktfLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 188 AQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHIECVELLVSSGADPDLYCNedNWQLPIHAAAqMGHTKILDLL 267
Cdd:PHA02874  165 IKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCK--NGFTPLHNAI-IHNRSAIELL 241
                         250       260
                  ....*....|....*....|...
gi 1953273907 268 IplTNR-VCDTGPDKVSPVYSAV 289
Cdd:PHA02874  242 I--NNAsINDQDIDGSTPLHHAI 262
Ank_2 pfam12796
Ankyrin repeats (3 copies);
217-310 1.57e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 1.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 217 LFIAAQEGHIECVELLVSSGADPDlyCNEDNWQLPIHAAAQMGHTKILDLLIPLTNrvCDTGPDKVSPVYSAVFGGHEEC 296
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN--LQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEI 76
                          90
                  ....*....|....
gi 1953273907 297 LEMLLQHGYSPDAQ 310
Cdd:pfam12796  77 VKLLLEKGADINVK 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
42-235 1.64e-15

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: 79.29  E-value: 1.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  42 RGW-MPIHEAAYHNSVECLRMLIHAVDssenyikTKTFE----GFCALHLAASQGHWKIVQILLEAgaDPNATTLEET-- 114
Cdd:cd22192    15 RISeSPLLLAAKENDVQAIKKLLKCPS-------CDLFQrgalGETALHVAALYDNLEAAVVLMEA--APELVNEPMTsd 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 115 -----TPLFLAVENGQIDVLRLLLRHGANVN-----------GSHSMC--GWNALHQATFQENAEIIKLLLKKGANKECQ 176
Cdd:cd22192    86 lyqgeTALHIAVVNQNLNLVRELIARGADVVspratgtffrpGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQ 165
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953273907 177 DDFGITPLFV-AAQYGKL---ESLSILISSGANVNCQALDKA------TPLFIAAQEGHIECVELLVSS 235
Cdd:cd22192   166 DSLGNTVLHIlVLQPNKTfacQMYDLILSYDKEDDLQPLDLVpnnqglTPFKLAAKEGNIVMFQHLVQK 234
PHA02878 PHA02878
ankyrin repeat protein; Provisional
24-234 1.85e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 75.69  E-value: 1.85e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  24 KVLRKLLKKGRSVDVAD-NRGWMPIHEAAYHNSVECLRMLI------HAVDSSENYiktktfegfcALHLAASQGHWKIV 96
Cdd:PHA02878  148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLsyganvNIPDKTNNS----------PLHHAVKHYNKPIV 217
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  97 QILLEAGADPNATTLEETTPLFLAVEN-GQIDVLRLLLRHGANVNGSHSMCGWNALHQATFQEnaEIIKLLLKKGANKEC 175
Cdd:PHA02878  218 HILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSE--RKLKLLLEYGADINS 295
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 176 QDDFGITPLFVAA-QYGKLESLSILISsgaNVNCQALDKAtplFIAAQEGHIECVELLVS 234
Cdd:PHA02878  296 LNSYKLTPLSSAVkQYLCINIGRILIS---NICLLKRIKP---DIKNSEGFIDNMDCITS 349
PHA02878 PHA02878
ankyrin repeat protein; Provisional
1-238 8.80e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 73.38  E-value: 8.80e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907   1 MDFTEAYSDTCSTVGL-----AAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIhavdssENYIKT 75
Cdd:PHA02878   23 IDHTENYSTSASLIPFiplhqAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI------RSINKC 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  76 KTFEGFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLRHGANVNGSHSMCGWNALHQAT 155
Cdd:PHA02878   97 SVFYTLVAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHKGNTALHYAT 176
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 156 FQENAEIIKLLLKKGANKECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQE-GHIECVELLVS 234
Cdd:PHA02878  177 ENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLE 256

                  ....
gi 1953273907 235 SGAD 238
Cdd:PHA02878  257 HGVD 260
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
459-502 2.07e-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: 64.44  E-value: 2.07e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1953273907 459 ASVPSLAHLCRLEIRSSLKPEHLrsdSFICQLPLPRSLHNYLLY 502
Cdd:cd03716     1 STPRSLQHLCRLAIRRCLGRRRL---ELIKKLPLPPRLKDYLLY 41
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
87-240 2.08e-13

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 72.98  E-value: 2.08e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  87 AASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLRHGANV-----NGSHSMcgWNAL---HQATFQe 158
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVhirdaNGNTAL--WNAIsakHHKIFR- 608
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 159 naeiIKLLLKKGANKECQDDFgitpLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHIECVELLVSSGAD 238
Cdd:PLN03192  609 ----ILYHFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680

                  ..
gi 1953273907 239 PD 240
Cdd:PLN03192  681 VD 682
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
160-369 3.15e-13

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 70.37  E-value: 3.15e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 160 AEIIKLLLKKGANKECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHIECVELLVSSGADP 239
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 240 DLycNEDNWQLPIHAAAQMGHTKILDLLIPLTNRVCDTGPDKVSPVYSAVFGGHEECLEMLLQHGYSPDAQmcLIFGFSS 319
Cdd:COG0666    81 NA--KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ--DNDGNTP 156
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1953273907 320 PMCMAFQKDCEffgIVNILLKYGAQLNE--------LHLAycLKYEKFSVFRYFLKKG 369
Cdd:COG0666   157 LHLAAANGNLE---IVKLLLEAGADVNArdndgetpLHLA--AENGHLEIVKLLLEAG 209
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
460-502 3.40e-13

SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region of CIS/SOCS family proteins (in combination with a SH2 domain), ASBs (ankyrin repeat-containing proteins with a SOCS box), SSBs (SPRY domain-containing proteins with a SOCS box), and WSBs (WD40 repeat-containing proteins with a SOCS box), as well as, other miscellaneous proteins. The function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239641  Cd Length: 41  Bit Score: 63.64  E-value: 3.40e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1953273907 460 SVPSLAHLCRLEIRSSLKPehlRSDSFICQLPLPRSLHNYLLY 502
Cdd:cd03587     1 NPRSLQHLCRLAIRRCLGK---RRLDLIDKLPLPPRLKDYLLY 40
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
17-184 2.00e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 69.90  E-value: 2.00e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  17 AAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLRMLI-HAVDssenyIKTKTFEGFCALHLAASQGHWKI 95
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLkHACN-----VHIRDANGNTALWNAISAKHHKI 606
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  96 VQIL--LEAGADPNATtleeTTPLFLAVENGQIDVLRLLLRHGANVNgSHSMCGWNALHQATFQENAEIIKLLLKKGANK 173
Cdd:PLN03192  607 FRILyhFASISDPHAA----GDLLCTAAKRNDLTAMKELLKQGLNVD-SEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
                         170
                  ....*....|....
gi 1953273907 174 EC---QDDFGITPL 184
Cdd:PLN03192  682 DKantDDDFSPTEL 695
PHA02875 PHA02875
ankyrin repeat protein; Provisional
87-346 2.82e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 68.48  E-value: 2.82e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  87 AASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLRHGA--NVN--GSHSmcgwnALHQATFQENAEI 162
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKypDIES-----ELHDAVEEGDVKA 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 163 IKLLLKkgANKECQDDF---GITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHIECVELLVSSGADP 239
Cdd:PHA02875   84 VEELLD--LGKFADDVFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL 161
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 240 DLycnEDNWqlpihaaaqmGHTkildllipltnrvcdtgpdkvsPVYSAVFGGHEECLEMLLQHGYSPDaqmclIFGFS- 318
Cdd:PHA02875  162 DI---EDCC----------GCT----------------------PLIIAMAKGDIAICKMLLDSGANID-----YFGKNg 201
                         250       260       270
                  ....*....|....*....|....*....|
gi 1953273907 319 --SPMCMAFQKDceFFGIVNILLKYGAQLN 346
Cdd:PHA02875  202 cvAALCYAIENN--KIDIVRLFIKRGADCN 229
PHA03100 PHA03100
ankyrin repeat protein; Provisional
162-392 2.47e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.46  E-value: 2.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 162 IIKLLLKKGANKE-----CQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHI-----ECVEL 231
Cdd:PHA03100   12 IIKVKNIKYIIMEddlndYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKL 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 232 LVSSGADPDLYCNEDNWQLPIHAAAQMGHTKILDLLIPLTNRVCDTGPDKVSPVYSAVFGGHE--ECLEMLLQHGYSPDA 309
Cdd:PHA03100   92 LLEYGANVNAPDNNGITPLLYAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINA 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 310 qmclifgfsspmcmafqKDceffgIVNILLKYGAQLNE--------LHLAycLKYEKFSVFRYFLKKGCPLapwNHISEF 381
Cdd:PHA03100  172 -----------------KN-----RVNYLLSYGVPINIkdvygftpLHYA--VYNNNPEFVKYLLDLGANP---NLVNKY 224
                         250
                  ....*....|....*
gi 1953273907 382 ----ISHAVKAQIKY 392
Cdd:PHA03100  225 gdtpLHIAILNNNKE 239
PHA02875 PHA02875
ankyrin repeat protein; Provisional
150-369 1.52e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.09  E-value: 1.52e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 150 ALHQATFQENAEIIKLLLKKGANKECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHIECV 229
Cdd:PHA02875    5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 230 ELLVSSG--ADPDLYcneDNWQLPIHAAAQMGHTKILDLLIPLTNRVCDTGPDKVSPVYSAVFGGHEECLEMLLQHGYSP 307
Cdd:PHA02875   85 EELLDLGkfADDVFY---KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL 161
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953273907 308 DAQMCliFGFSSPMCMAFQKDCEffgIVNILLKYGAQLNELH-------LAYCLKYEKFSVFRYFLKKG 369
Cdd:PHA02875  162 DIEDC--CGCTPLIIAMAKGDIA---ICKMLLDSGANIDYFGkngcvaaLCYAIENNKIDIVRLFIKRG 225
PHA02874 PHA02874
ankyrin repeat protein; Provisional
17-190 1.78e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.06  E-value: 1.78e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  17 AAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIhavdssEN--YIKTKTFEGFCALHLAASQGHWK 94
Cdd:PHA02874  131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLL------EKgaYANVKDNNGESPLHNAAEYGDYA 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  95 IVQILLEAGADPNATTLEETTPLFLAVENGQiDVLRLLLrHGANVNgSHSMCGWNALHQA-TFQENAEIIKLLLKKGANK 173
Cdd:PHA02874  205 CIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLI-NNASIN-DQDIDGSTPLHHAiNPPCDIDIIDILLYHKADI 281
                         170
                  ....*....|....*..
gi 1953273907 174 ECQDDFGITPLFVAAQY 190
Cdd:PHA02874  282 SIKDNKGENPIDTAFKY 298
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
460-501 4.43e-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: 54.86  E-value: 4.43e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1953273907 460 SVPSLAHLCRLEIRSSLKPehlRSDSFICQLPLPRSLHNYLL 501
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGK---RRLGAIDKLPLPPLLKDYLL 39
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
78-135 5.35e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.84  E-value: 5.35e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1953273907  78 FEGFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLRH 135
Cdd:PTZ00322  113 YDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02875 PHA02875
ankyrin repeat protein; Provisional
7-140 8.84e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.78  E-value: 8.84e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907   7 YSDTCSTVGLAAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIH---AVDSSENYiktktfeGFCA 83
Cdd:PHA02875   99 YKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDhkaCLDIEDCC-------GCTP 171
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1953273907  84 LHLAASQGHWKIVQILLEAGADPNATTLE-ETTPLFLAVENGQIDVLRLLLRHGANVN 140
Cdd:PHA02875  172 LIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02989 PHA02989
ankyrin repeat protein; Provisional
94-207 1.37e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 60.53  E-value: 1.37e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  94 KIVQILLEAGADPNATTLEETTPLFLAVENGQI---DVLRLLLRHGANVNGSHSMCGWNALHQ--ATFQENAEIIKLLLK 168
Cdd:PHA02989   89 KIVKLLLKFGADINLKTFNGVSPIVCFIYNSNInncDMLRFLLSKGINVNDVKNSRGYNLLHMylESFSVKKDVIKILLS 168
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1953273907 169 KGANK-ECQDDFGITPLFV----AAQYGKLESLSILISSGANVN 207
Cdd:PHA02989  169 FGVNLfEKTSLYGLTPMNIylrnDIDVISIKVIKYLIKKGVNIE 212
PHA02878 PHA02878
ankyrin repeat protein; Provisional
52-348 2.81e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 59.51  E-value: 2.81e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  52 YHNSVECLRMLIHAVDSSENYIKTKTFEGFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRL 131
Cdd:PHA02878    9 YTDNYETILKYIEYIDHTENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKE 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 132 LLRHGANVNGSHSMcgwNALHQATFQENAEIIKLLLKKGANKECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQAL 211
Cdd:PHA02878   89 MIRSINKCSVFYTL---VAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDR 165
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 212 DK-ATPLFIAAQEGHIECVELLVSSGADPDLYCNEDNWqlPIHAAAQMGHTKILDLLI---PLTN--RVCDTGPDKVSPV 285
Cdd:PHA02878  166 HKgNTALHYATENKDQRLTELLLSYGANVNIPDKTNNS--PLHHAVKHYNKPIVHILLengASTDarDKCGNTPLHISVG 243
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953273907 286 YSAVFggheECLEMLLQHGYSPDAQmCLIFGFsSPMCMAFQKDceffGIVNILLKYGAQLNEL 348
Cdd:PHA02878  244 YCKDY----DILKLLLEHGVDVNAK-SYILGL-TALHSSIKSE----RKLKLLLEYGADINSL 296
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
462-502 3.37e-09

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: 52.03  E-value: 3.37e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 1953273907  462 PSLAHLCRLEIRSSLKpehlrsdsFICQLPLPRSLHNYLLY 502
Cdd:smart00969   1 RSLQHLCRLAIRRSLG--------GIDKLPLPPRLKDYLLY 33
PHA02884 PHA02884
ankyrin repeat protein; Provisional
92-220 6.90e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 57.30  E-value: 6.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  92 HWKIVQILLEAGADPNA----TTLEETTPLFLAVENGQIDVLRLLLRHGANVNgshsmcgwnalhqaTFQENAEIiklll 167
Cdd:PHA02884   45 YTDIIDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVN--------------RYAEEAKI----- 105
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1953273907 168 kkgankecqddfgiTPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIA 220
Cdd:PHA02884  106 --------------TPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELA 144
PHA03095 PHA03095
ankyrin-like protein; Provisional
22-184 7.03e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.11  E-value: 7.03e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  22 NVKVLRKLLKKGRSVDVADNRGWMPIHeaAY---HN-SVECLRMLIHAVdsseNYIKTKTFEGFCALH--LAASQGHWKI 95
Cdd:PHA03095  131 NPKVIRLLLRKGADVNALDLYGMTPLA--VLlksRNaNVELLRLLIDAG----ADVYAVDDRFRSLLHhhLQSFKPRARI 204
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  96 VQILLEAGADPNATTLEETTPLFLAVENGQID--VLRLLLRHGANVNGSHSMcGWNALHQATFQENAEIIKLLLKKGANK 173
Cdd:PHA03095  205 VRELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRY-GQTPLHYAAVFNNPRACRRLIALGADI 283
                         170
                  ....*....|.
gi 1953273907 174 ECQDDFGITPL 184
Cdd:PHA03095  284 NAVSSDGNTPL 294
Ank_4 pfam13637
Ankyrin repeats (many copies);
182-233 1.01e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 1.01e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1953273907 182 TPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHIECVELLV 233
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
58-201 1.13e-08

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: 57.85  E-value: 1.13e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  58 CLRMLIHAVDSSENYiktktfEGFCALHLAASQGHWKIVQILLEAGADPNATTLEE--------------TTPLFLAVEN 123
Cdd:cd22194   125 ILDRFINAEYTEEAY------EGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACT 198
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 124 GQIDVLRLLLRHGANVNGSHSMCGWNALHQ-ATFQENAE-----IIKL---LLKKGANKECQ---DDFGITPLFVAAQYG 191
Cdd:cd22194   199 NQPEIVQLLMEKESTDITSQDSRGNTVLHAlVTVAEDSKtqndfVKRMydmILLKSENKNLEtirNNEGLTPLQLAAKMG 278
                         170
                  ....*....|
gi 1953273907 192 KLESLSILIS 201
Cdd:cd22194   279 KAEILKYILS 288
Ank_4 pfam13637
Ankyrin repeats (many copies);
215-268 2.14e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 2.14e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953273907 215 TPLFIAAQEGHIECVELLVSSGADPDlYCNEDNWQlPIHAAAQMGHTKILDLLI 268
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADIN-AVDGNGET-ALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
83-133 4.01e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 4.01e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953273907  83 ALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLL 133
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SOCS_SSB1_4 cd03718
SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box ...
463-502 4.71e-08

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: 49.22  E-value: 4.71e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1953273907 463 SLAHLCRLEIRSSLKPEHLRSdsfICQLPLPRSLHNYLLY 502
Cdd:cd03718     5 PLMDLCRRRVRVALGRDRLEE---IEQLPLPPSLKNYLLY 41
Ank_4 pfam13637
Ankyrin repeats (many copies);
17-63 6.94e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 6.94e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 1953273907  17 AAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLRMLI 63
Cdd:pfam13637   8 AAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
113-167 1.19e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.19e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1953273907 113 ETTPLFLAVENGQIDVLRLLLRHGANVNGSHSmCGWNALHQATFQENAEIIKLLL 167
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
460-502 1.24e-07

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


Pssm-ID: 239687  Cd Length: 39  Bit Score: 47.98  E-value: 1.24e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1953273907 460 SVPSLAHLCRLEIRSSLKPEHlrsdsfICQLPLPRSLHNYLLY 502
Cdd:cd03717     2 SVRSLQHLCRFVIRQCTRRDL------IDQLPLPRRLKDYLKE 38
SOCS_ASB14 cd03730
SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a ...
463-504 1.38e-07

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: 48.30  E-value: 1.38e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1953273907 463 SLAHLCRLEIRSSLKPEHLRSDSFICQLPLPRSLHNYLLYAE 504
Cdd:cd03730     5 SLKHLCRLKIRACMGRLRLRCPVFMSFLPLPNRLKAYILYKE 46
PHA02884 PHA02884
ankyrin repeat protein; Provisional
123-245 1.90e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 52.68  E-value: 1.90e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 123 NGQIDVLRLLLR-----HGANVNGSHSMCGWNALHQATFQENAEIIKLLLKKGANKECQDDFG----ITPLFVAAQYGKL 193
Cdd:PHA02884    4 INLIDIITLLCRifyiiFYIAIKKKNKICIANILYSSIKFHYTDIIDAILKLGADPEAPFPLSenskTNPLIYAIDCDND 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1953273907 194 ESLSILISSGANVNCQALD-KATPLFIAAQEGHIECVELLVSSGADPDLYCNE 245
Cdd:PHA02884   84 DAAKLLIRYGADVNRYAEEaKITPLYISVLHGCLKCLEILLSYGADINIQTND 136
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
198-308 3.04e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 3.04e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 198 ILISSGANVNCQALDKATPLFIAAQEGHIECVELLVSSGADPDLYCNEDNwqLPIHAAAQMGHTKILDLLipLTNRVCDT 277
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK--TPLELAEENGFREVVQLL--SRHSQCHF 175
                          90       100       110
                  ....*....|....*....|....*....|.
gi 1953273907 278 GPDKVSPVYSavFGGHEECLEMLLQHGYSPD 308
Cdd:PTZ00322  176 ELGANAKPDS--FTGKPPSLEDSPISSHHPD 204
PHA02798 PHA02798
ankyrin-like protein; Provisional
94-207 4.45e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 52.53  E-value: 4.45e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  94 KIVQILLEAGADPNATTLEETTPLFLAVEN-----GQIDVLRLLLRHGANVN-----GSHSMCGwnALHQATFQeNAEII 163
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINkknsdGETPLYC--LLSNGYIN-NLEIL 128
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 1953273907 164 KLLLKKGANKECQDDFGITPLFVAAQYG---KLESLSILISSGANVN 207
Cdd:PHA02798  129 LFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDIN 175
PHA02874 PHA02874
ankyrin repeat protein; Provisional
11-140 4.79e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.27  E-value: 4.79e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  11 CSTVGLAAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIhavdSSENYIKTKTFEGFCALHLAASq 90
Cdd:PHA02874  158 CYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI----DHGNHIMNKCKNGFTPLHNAII- 232
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953273907  91 gHWKIVQILLEAGADPNATTLEETTPLFLAVENG-QIDVLRLLLRHGANVN 140
Cdd:PHA02874  233 -HNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADIS 282
PHA03095 PHA03095
ankyrin-like protein; Provisional
24-134 7.15e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.56  E-value: 7.15e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  24 KVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSveCLRMLIH-------AVDSSENYiktktfeGFCALHLAASQGHWKIV 96
Cdd:PHA03095  203 RIVRELIRAGCDPAATDMLGNTPLHSMATGSS--CKRSLVLplliagiSINARNRY-------GQTPLHYAAVFNNPRAC 273
                          90       100       110
                  ....*....|....*....|....*....|....*...
gi 1953273907  97 QILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLR 134
Cdd:PHA03095  274 RRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
85-139 7.93e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.82  E-value: 7.93e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1953273907  85 HLAASqGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLRHGANV 139
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADP 141
PHA02798 PHA02798
ankyrin-like protein; Provisional
105-245 9.24e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 51.37  E-value: 9.24e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 105 DPNATTLEETT-PLFLAVENGQIDVLRLLLRHGANVNG-----SHSMCGWNAlHQATFQENAEIIKLLLKKGANKECQDD 178
Cdd:PHA02798   29 NPNEIVNEYSIfQKYLQRDSPSTDIVKLFINLGANVNGldneySTPLCTILS-NIKDYKHMLDIVKILIENGADINKKNS 107
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953273907 179 FGITPLFVAAQYG---KLESLSILISSGANVNCQALDKATPLFIAAQEGH---IECVELLVSSGADPDLYCNE 245
Cdd:PHA02798  108 DGETPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHhidIEIIKLLLEKGVDINTHNNK 180
PHA02989 PHA02989
ankyrin repeat protein; Provisional
24-229 2.75e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 49.74  E-value: 2.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  24 KVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIHAVDSSENYIKTKTFEGFCALH--LAASQGHWKIVQILLE 101
Cdd:PHA02989   89 KIVKLLLKFGADINLKTFNGVSPIVCFIYNSNINNCDMLRFLLSKGINVNDVKNSRGYNLLHmyLESFSVKKDVIKILLS 168
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 102 AGADP-NATTLEETTPLFLAVENG----QIDVLRLLLRHGANVNGShsmcgwNALHQA---TFQENAEI-----IKLL-- 166
Cdd:PHA02989  169 FGVNLfEKTSLYGLTPMNIYLRNDidviSIKVIKYLIKKGVNIETN------NNGSESvleSFLDNNKIlskkeFKVLnf 242
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1953273907 167 LKKGANKECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHIECV 229
Cdd:PHA02989  243 ILKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDML 305
PHA02874 PHA02874
ankyrin repeat protein; Provisional
191-379 3.11e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.58  E-value: 3.11e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 191 GKLESLSILISSGAN-VNCQALDKATPLFIAAQEGHIECVELLVSSGADpdlyCNEDNWQLP--IHAAAQMGHTKILDLL 267
Cdd:PHA02874   12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGAD----INHINTKIPhpLLTAIKIGAHDIIKLL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 268 I----------------PLTNRVCDTGPD-------KVSPVYSAVFGGHEECLEMLLQhgYSPDAQMCLIFGfSSPMCMA 324
Cdd:PHA02874   88 IdngvdtsilpipciekDMIKTILDCGIDvnikdaeLKTFLHYAIKKGDLESIKMLFE--YGADVNIEDDNG-CYPIHIA 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1953273907 325 FQKDceFFGIVNILLKYGAQLN------ELHLAYCLKYEKFSVFRYFLKKGcplapwNHIS 379
Cdd:PHA02874  165 IKHN--FFDIIKLLLEKGAYANvkdnngESPLHNAAEYGDYACIKLLIDHG------NHIM 217
PHA02946 PHA02946
ankyin-like protein; Provisional
79-235 5.74e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 48.90  E-value: 5.74e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  79 EGFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFL--AVENGQIDVLRLLLRHGANVNGSHSMCGWNALHQATf 156
Cdd:PHA02946   71 DGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKINNSVDEEGCGPLLACT- 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 157 QENAEIIKLLLKKGANKECQDDFGITPL--FVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQE--GHIECVELL 232
Cdd:PHA02946  150 DPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKtvKNVDIINLL 229

                  ...
gi 1953273907 233 VSS 235
Cdd:PHA02946  230 LPS 232
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
79-110 8.61e-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: 8.61e-06
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1953273907  79 EGFCALHLAASQ-GHWKIVQILLEAGADPNATT 110
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
16-152 9.36e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 48.54  E-value: 9.36e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  16 LAAREGNVKVLRKLLK-KGRSVDVADNRgwmpIHEAA--YHNSVE-CLRMLIHAVDSSENY-----IKTKTF-EGFCALH 85
Cdd:TIGR00870  58 VAAIENENLELTELLLnLSCRGAVGDTL----LHAISleYVDAVEaILLHLLAAFRKSGPLelandQYTSEFtPGITALH 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  86 LAASQGHWKIVQILLEAGADPNAT-------TLEETT-------PLFLAVENGQIDVLRLLLRHGANVNGSHSMcGWNAL 151
Cdd:TIGR00870 134 LAAHRQNYEIVKLLLERGASVPARacgdffvKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSL-GNTLL 212

                  .
gi 1953273907 152 H 152
Cdd:TIGR00870 213 H 213
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
163-234 9.54e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 9.54e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1953273907 163 IKLLLKKGANKECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHIECVELLVS 234
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
115-140 1.20e-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: 42.19  E-value: 1.20e-05
                           10        20
                   ....*....|....*....|....*.
gi 1953273907  115 TPLFLAVENGQIDVLRLLLRHGANVN 140
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
463-504 1.37e-05

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: 42.51  E-value: 1.37e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1953273907 463 SLAHLCRLEIRSSLKPEHLRSDSFICQLPLPRSLHNYLLYAE 504
Cdd:cd03731     5 PLKHLCRLKIRKLMGLQKLQQPSSMKKLPLPPALKRYILYKE 46
SOCS_SOCS7 cd03741
SOCS (suppressors of cytokine signaling) box of SOCS7-like proteins. Together with CIS1, the ...
461-502 2.00e-05

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: 42.01  E-value: 2.00e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1953273907 461 VPSLAHLCRLEIRSSLKPEHlrsdsfICQLPLPRSLHNYLLY 502
Cdd:cd03741     3 VQSLQHLCRFVIRKLVRRDH------IPALPLPRRLIDYLRE 38
Ank_4 pfam13637
Ankyrin repeats (many copies);
147-200 3.42e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 3.42e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1953273907 147 GWNALHQATFQENAEIIKLLLKKGANKECQDDFGITPLFVAAQYGKLESLSILI 200
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
251-301 3.56e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 3.56e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953273907 251 PIHAAAQMGHTKILDLLIPLTNRVCDTGPDKVSPVYSAVFGGHEECLEMLL 301
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
115-268 3.62e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.61  E-value: 3.62e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 115 TPLF-LAVENGQIDVLRLLLRHGANVNgshsmCGWNALHQAT--FQENAE-IIKLLLKKG--------ANKECQDDF--G 180
Cdd:TIGR00870  54 SALFvAAIENENLELTELLLNLSCRGA-----VGDTLLHAISleYVDAVEaILLHLLAAFrksgplelANDQYTSEFtpG 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 181 ITPLFVAAQYGKLESLSILISSGANVNCQAldkatplfiaaqeghiECVELLVSSGADpDLYCNEdnwqLPIHAAAQMGH 260
Cdd:TIGR00870 129 ITALHLAAHRQNYEIVKLLLERGASVPARA----------------CGDFFVKSQGVD-SFYHGE----SPLNAAACLGS 187

                  ....*...
gi 1953273907 261 TKILDLLI 268
Cdd:TIGR00870 188 PSIVALLS 195
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
463-501 6.52e-05

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


Pssm-ID: 239693  Cd Length: 48  Bit Score: 40.50  E-value: 6.52e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1953273907 463 SLAHLCRLEIRSSLkpeHLRSDSFICQLPLPRSLHNYLL 501
Cdd:cd03723     5 SLQHLCRCAIRKLL---GSRCHKLVPQLSLPTSLKNYLL 40
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
212-241 1.01e-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: 39.49  E-value: 1.01e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 1953273907  212 DKATPLFIAAQEGHIECVELLVSSGADPDL 241
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
159-270 1.23e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 43.27  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 159 NAEIIKLLLKKGANKECQ-DDFGITPLFVAAQYGK---LESLSILISSGANVNCQALDKATPL--FIAAQEGHIECVELL 232
Cdd:PHA02859   65 NVEILKFLIENGADVNFKtRDNNLSALHHYLSFNKnvePEILKILIDSGSSITEEDEDGKNLLhmYMCNFNVRINVIKLL 144
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1953273907 233 VSSGADPdlyCNEDNWQLPIHAAAQMGHT--KILDLLIPL 270
Cdd:PHA02859  145 IDSGVSF---LNKDFDNNNILYSYILFHSdkKIFDFLTSL 181
Ank_5 pfam13857
Ankyrin repeats (many copies);
75-120 1.25e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 1.25e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1953273907  75 TKTFEGFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLA 120
Cdd:pfam13857  11 RLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
57-201 1.43e-04

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: 44.40  E-value: 1.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  57 ECLRMLIHAVDSSEN---YIKTK----TFEGFCALHLAASQGHWKIVQILLEAGADPNAT--------TLEET------T 115
Cdd:cd22193    46 DTIRILLDIAEKTDNlkrFINAEytdeYYEGQTALHIAIERRQGDIVALLVENGADVHAHakgrffqpKYQGEgfyfgeL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 116 PLFLAVENGQIDVLRLLLRHG---ANVNGSHSMcGWNALHQAT-----FQENAEIIK----LLLKKGAN-------KECQ 176
Cdd:cd22193   126 PLSLAACTNQPDIVQYLLENEhqpADIEAQDSR-GNTVLHALVtvadnTKENTKFVTrmydMILIRGAKlcptvelEEIR 204
                         170       180
                  ....*....|....*....|....*
gi 1953273907 177 DDFGITPLFVAAQYGKLESLSILIS 201
Cdd:cd22193   205 NNDGLTPLQLAAKMGKIEILKYILQ 229
SOCS_WSB_SWIP cd03733
SOCS (suppressors of cytokine signaling) box of WSB/SWiP-like proteins. This subfamily ...
460-502 1.54e-04

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: 39.33  E-value: 1.54e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1953273907 460 SVPSLAHLCRLEIRSSLkpehlrSDSFICQLPLPRSLHNYLLY 502
Cdd:cd03733     2 VVSSLQHLCRMALRRVM------TTQQVLALPIPKKMKEFLTY 38
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
69-200 1.93e-04

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: 44.03  E-value: 1.93e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  69 SENYIKTKTfegfcALHLAASQGHWKIVQILLEAGADPNATTLEE--------------TTPLFLAVENGQIDVLRLLLR 134
Cdd:cd22196    88 TDSYYKGQT-----ALHIAIERRNMHLVELLVQNGADVHARASGEffkkkkggpgfyfgELPLSLAACTNQLDIVKFLLE 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 135 H---GANVNGSHSMcGWNALHQA-----TFQENAEIIKL----LLKKGAN-------KECQDDFGITPLFVAAQYGKLES 195
Cdd:cd22196   163 NphsPADISARDSM-GNTVLHALvevadNTPENTKFVTKmyneILILGAKirpllklEEITNKKGLTPLKLAAKTGKIGI 241

                  ....*
gi 1953273907 196 LSILI 200
Cdd:cd22196   242 FAYIL 246
PHA02859 PHA02859
ankyrin repeat protein; Provisional
115-186 3.42e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.11  E-value: 3.42e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1953273907 115 TPLFLAVENGQI--DVLRLLLRHGANVNGSHSMCGWNALHQ-ATFQENA--EIIKLLLKKGANKECQDDFGITPLFV 186
Cdd:PHA02859   53 TPIFSCLEKDKVnvEILKFLIENGADVNFKTRDNNLSALHHyLSFNKNVepEILKILIDSGSSITEEDEDGKNLLHM 129
SOCS smart00253
suppressors of cytokine signalling; suppressors of cytokine signalling
460-502 4.46e-04

suppressors of cytokine signalling; suppressors of cytokine signalling


Pssm-ID: 128549  Cd Length: 43  Bit Score: 38.05  E-value: 4.46e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1953273907  460 SVPSLAHLCRLEIRSSLKPEHlrsdsfICQLPLPRSLHNYLLY 502
Cdd:smart00253   6 NVPSLQHLCRFTIRRCTRTDQ------IKTLPLPPKLKDYLSY 42
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
115-140 4.59e-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: 4.59e-04
                          10        20
                  ....*....|....*....|....*.
gi 1953273907 115 TPLFLAVENGQIDVLRLLLRHGANVN 140
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
83-108 5.21e-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: 5.21e-04
                           10        20
                   ....*....|....*....|....*.
gi 1953273907   83 ALHLAASQGHWKIVQILLEAGADPNA 108
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
SOCS_SSB1 cd03744
SOCS (suppressors of cytokine signaling) box of SSB1 (SPRY domain-containing SOCS box proteins) ...
463-502 5.76e-04

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


Pssm-ID: 239713  Cd Length: 42  Bit Score: 37.65  E-value: 5.76e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1953273907 463 SLAHLCRLEIRSSLKPEHLrsdSFICQLPLPRSLHNYLLY 502
Cdd:cd03744     5 PLMDLCRRSVRLALGRERL---SEIHTLPLPASLKNYLLY 41
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
215-241 5.99e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.27  E-value: 5.99e-04
                          10        20
                  ....*....|....*....|....*...
gi 1953273907 215 TPLFIAA-QEGHIECVELLVSSGADPDL 241
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVNA 31
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
78-213 7.40e-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: 42.17  E-value: 7.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  78 FEGFCALHLAASQGHWKIVQILLEAGAD----PNATTLEETT---------PLFLAVENGQIDVLRLLLRHGANVNGSHS 144
Cdd:cd21882    71 YQGQTALHIAIENRNLNLVRLLVENGADvsarATGRFFRKSPgnlfyfgelPLSLAACTNQEEIVRLLLENGAQPAALEA 150
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 145 M--CGWNALHQATFQEN---------AEIIKLLLKKGAN-------KECQDDFGITPLFVAAQYGKLESLSILISSGANV 206
Cdd:cd21882   151 QdsLGNTVLHALVLQADntpensafvCQMYNLLLSYGAHldptqqlEEIPNHQGLTPLKLAAVEGKIVMFQHILQREFSG 230

                  ....*..
gi 1953273907 207 NCQALDK 213
Cdd:cd21882   231 PYQPLSR 237
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
78-194 1.01e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely related to TRPV1, sharing high sequence identity (>50%), but TRPV2 shows a higher temperature threshold and sensitivity for activation than TRPV1. TRPV2 can be stimulated by ligands or lipids, and is involved in osmosensation and mechanosensation. TRPV2 is expressed in both neuronal and non-neuronal tissues, and it has been implicated in diverse physiological and pathophysiological processes, including cardiac-structure maintenance, innate immunity, and cancer. TRPV2 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 41.76  E-value: 1.01e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  78 FEGFCALHLAASQGHWKIVQILLEAGADPNATTLEE-------------TTPLFLAVENGQIDVLRLLLRHG---ANVNG 141
Cdd:cd22197    92 YRGHSALHIAIEKRSLQCVKLLVENGADVHARACGRffqkkqgtcfyfgELPLSLAACTKQWDVVNYLLENPhqpASLQA 171
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1953273907 142 SHSMcGWNALHQATF-----QENAEI-IKL---LLKKGAN-------KECQDDFGITPLFVAAQYGKLE 194
Cdd:cd22197   172 QDSL-GNTVLHALVMiadnsPENSALvIKMydgLLQAGARlcptvqlEEISNHEGLTPLKLAAKEGKIE 239
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
115-140 1.04e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.50  E-value: 1.04e-03
                          10        20
                  ....*....|....*....|....*..
gi 1953273907 115 TPLFLAV-ENGQIDVLRLLLRHGANVN 140
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVN 30
SOCS_SSB4 cd03743
SOCS (suppressors of cytokine signaling) box of SSB4 (SPRY domain-containing SOCS box ...
464-502 1.17e-03

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: 36.86  E-value: 1.17e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1953273907 464 LAHLCRLEIRSSLKPEHLRSdsfICQLPLPRSLHNYLLY 502
Cdd:cd03743     6 LMDLCRRSARQALGRHRLHH---IQSLPLPQTLKNYLQY 41
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
79-108 1.26e-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: 36.47  E-value: 1.26e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 1953273907  79 EGFCALHLAASQGHWKIVQILLEAGADPNA 108
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
99-154 1.29e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 1.29e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1953273907  99 LLEAG-ADPNATTLEETTPLFLAVENGQIDVLRLLLRHGANVNgSHSMCGWNALHQA 154
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLN-LKDEEGLTALDLA 56
SOCS_WSB1_SWIP1 cd03746
SOCS (suppressors of cytokine signaling) box of WSB1/SWiP1-like proteins. This subfamily ...
460-502 2.17e-03

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: 35.94  E-value: 2.17e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1953273907 460 SVPSLAHLCRLEIRSSLKPEHLRsdsficQLPLPRSLHNYLLY 502
Cdd:cd03746     2 QVASLQHLCRMAIRRVMPTQQVK------ELPIPSKLLEFLTY 38
SOCS_CIS1 cd03734
SOCS (suppressors of cytokine signaling) box of CIS (cytokine-inducible SH2 protein) 1-like ...
460-500 2.45e-03

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: 35.71  E-value: 2.45e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1953273907 460 SVPSLAHLCRLEIRsslkpehlRSDSFICQLPLPRSLHNYL 500
Cdd:cd03734     2 SARSLQHLCRLVIN--------RLVTDVDCLPLPRRMADYL 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
229-303 2.50e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.65  E-value: 2.50e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1953273907 229 VELLVSSGADPDlyCNEDNWQLPIHAAAQMGHTKILDLLIPLTNRVCDTGPDKVSPVYSAVFGGHEECLEMLLQH 303
Cdd:PTZ00322   98 ARILLTGGADPN--CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
180-208 2.77e-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: 2.77e-03
                           10        20
                   ....*....|....*....|....*....
gi 1953273907  180 GITPLFVAAQYGKLESLSILISSGANVNC 208
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
SOCS_WSB2_SWIP2 cd03745
SOCS (suppressors of cytokine signaling) box of WSB2/SWiP2-like proteins. This family consists ...
461-502 3.11e-03

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: 35.64  E-value: 3.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1953273907 461 VPSLAHLCRLEIRSSLKPEHlrsdsfICQLPLPRSLHNYLLY 502
Cdd:cd03745     3 LPSLRHLCRKALRHFLTTYQ------VLALPIPKKMKEFLTY 38
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
151-313 3.49e-03

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 40.00  E-value: 3.49e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 151 LHQATFQENAEIIKLLLKKGANKECQ-DDFGITPLFVAAQYGKLESLSILISSGAN-VN----CQALDKATPLFIAAQEG 224
Cdd:cd22192    21 LLLAAKENDVQAIKKLLKCPSCDLFQrGALGETALHVAALYDNLEAAVVLMEAAPElVNepmtSDLYQGETALHIAVVNQ 100
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 225 HIECVELLVSSGADPdlycnednwqlpihaaaqmghtkildllipLTNRVCDT----GPDKV-----SPVYSAVFGGHEE 295
Cdd:cd22192   101 NLNLVRELIARGADV------------------------------VSPRATGTffrpGPKNLiyygeHPLSFAACVGNEE 150
                         170
                  ....*....|....*...
gi 1953273907 296 CLEMLLQHGYSPDAQMCL 313
Cdd:cd22192   151 IVRLLIEHGADIRAQDSL 168
PHA02876 PHA02876
ankyrin repeat protein; Provisional
17-142 3.60e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.05  E-value: 3.60e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  17 AAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAY-HNSVECLRMLIHA---VDSSENYIKTktfegfcALHLAASQG- 91
Cdd:PHA02876  382 AAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCgTNPYMSVKTLIDRganVNSKNKDLST-------PLHYACKKNc 454
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1953273907  92 HWKIVQILLEAGADPNATTLEETTPLFLAVENGQIdvLRLLLRHGANVNGS 142
Cdd:PHA02876  455 KLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGI--VNILLHYGAELRDS 503
SOCS_SOCS6 cd03740
SOCS (suppressors of cytokine signaling) box of SOCS6-like proteins. Together with CIS1, the ...
461-501 4.51e-03

SOCS (suppressors of cytokine signaling) box of SOCS6-like proteins. Together with CIS1, the CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 domain. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239709  Cd Length: 41  Bit Score: 35.09  E-value: 4.51e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1953273907 461 VPSLAHLCRLEIRSSLKPEHLRSdsficqLPLPRSLHNYLL 501
Cdd:cd03740     3 VRSLQYLCRFVIRQYTRIDLIQK------LPLPNKMKGYLL 37
SOCS_ASB6 cd03725
SOCS (suppressors of cytokine signaling) box of ASB6-like proteins. ASB family members have a ...
462-501 5.44e-03

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: 35.11  E-value: 5.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1953273907 462 PSLAHLCRLEIRSSLKPEHLrsDSFICQLPLPRSLHNYLL 501
Cdd:cd03725     4 PPLKHLCRVFIRLCLRPWPV--DVKVKALPLPDRLKWYLL 41
SOCS_ASB1 cd03720
SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a ...
463-502 6.06e-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: 34.70  E-value: 6.06e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1953273907 463 SLAHLCRLEIRSSLKPEHLrsdSFICQLPLPRSLHNYLLY 502
Cdd:cd03720     5 SLLSLCRIAVRRALGKQRL---SLICSLPLPDPIKKFLLH 41
PHA02741 PHA02741
hypothetical protein; Provisional
48-135 6.38e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 37.71  E-value: 6.38e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907  48 HEAAYHNSVECLRMLIHAV--DSSENYIKTKTFEGFCALHLAA----SQGHWKIVQILLEAGADPNA-TTLEETTPLFLA 120
Cdd:PHA02741   26 HEAARCGCFDIIARFTPFIrgDCHAAALNATDDAGQMCIHIAAekheAQLAAEIIDHLIELGADINAqEMLEGDTALHLA 105
                          90
                  ....*....|....*
gi 1953273907 121 VENGQIDVLRLLLRH 135
Cdd:PHA02741  106 AHRRDHDLAEWLCCQ 120
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
147-178 6.74e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.57  E-value: 6.74e-03
                          10        20        30
                  ....*....|....*....|....*....|...
gi 1953273907 147 GWNALHQATFQE-NAEIIKLLLKKGANKECQDD 178
Cdd:pfam00023   2 GNTPLHLAAGRRgNLEIVKLLLSKGADVNARDK 34
PHA02736 PHA02736
Viral ankyrin protein; Provisional
126-204 7.42e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.16  E-value: 7.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1953273907 126 IDVLRLLLRHGANVNGSHSMCGWNALHQATFQENAEIIKLLLKK-GANKECQDDFGITPLFVAAQYGKLESLSILISSGA 204
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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