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Conserved domains on  [gi|1034654168|ref|XP_016867246|]
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ankyrin repeat and SOCS box protein 15 isoform X2 [Homo sapiens]

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];
66-313 2.06e-40

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.56  E-value: 2.06e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168  66 KYAMDEADEKGWFPLHEAVVQPIQQILEIVLDAsyKTLWEFKTCDGETPLTLAVKAGLVENVRTLLEKGVWPNTKNDKGE 145
Cdd:COG0666    44 LLALALADALGALLLLAAALAGDLLVALLLLAA--GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 146 TPLLIAVKKGSYDMVSTLIKHNTSLDQPCVKRWSAMHEAAKQGRKDIVALLLKHGGNVHLRDGFGVTPLGVAAEYGHCDV 225
Cdd:COG0666   122 TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 226 LEHLIHKGGDVLALADDGASVLFEAAGGGNPDCISLLLEYGGSGNVPNRAGHLPIHRAAYEGHYLALKYLIPVTSKNAIR 305
Cdd:COG0666   202 VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281

                  ....*...
gi 1034654168 306 KSGLTPIH 313
Cdd:COG0666   282 LLDLLTLL 289
SOCS super family cl02533
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
532-587 7.26e-31

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


The actual alignment was detected with superfamily member cd03731:

Pssm-ID: 470605  Cd Length: 56  Bit Score: 114.16  E-value: 7.26e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654168 532 ENPCSLKHLCRLKIRRLMGLQKLCQPASVEKLPLPPAIQRYILFKEYDLYGQELKL 587
Cdd:cd03731     1 ENPRPLKHLCRLKIRKLMGLQKLQQPSSMKKLPLPPALKRYILYKEYDLYGQELKL 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
191-439 6.07e-26

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.12  E-value: 6.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 191 DIVALLLKHGGNVHLRDGFGVTPLGVAAEYGHCDVLEHLIHKGGDVLALADDGASVLFEAAGGGNPDCISLLLEYGGSGN 270
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 271 VPNRAGHLPIHRAAYEGHYLALKYLI----PVtskNAIRKSGLTPIHSAADGQNAQCLELLIENGFDVNTLladhisqsy 346
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLeagaDV---NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ--------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 347 DDERKTALYFGVSNNDVHCTEVLLAAGADPNL---DPLNCLLVAVRANNYEIVRLLLSHGANVNcyfMHVNDTRFPSVIQ 423
Cdd:COG0666   150 DNDGNTPLHLAAANGNLEIVKLLLEAGADVNArdnDGETPLHLAAENGHLEIVKLLLEAGADVN---AKDNDGKTALDLA 226
                         250
                  ....*....|....*.
gi 1034654168 424 YALNDEVMLRLLLNNG 439
Cdd:COG0666   227 AENGNLEIVKLLLEAG 242
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
66-313 2.06e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.56  E-value: 2.06e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168  66 KYAMDEADEKGWFPLHEAVVQPIQQILEIVLDAsyKTLWEFKTCDGETPLTLAVKAGLVENVRTLLEKGVWPNTKNDKGE 145
Cdd:COG0666    44 LLALALADALGALLLLAAALAGDLLVALLLLAA--GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 146 TPLLIAVKKGSYDMVSTLIKHNTSLDQPCVKRWSAMHEAAKQGRKDIVALLLKHGGNVHLRDGFGVTPLGVAAEYGHCDV 225
Cdd:COG0666   122 TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 226 LEHLIHKGGDVLALADDGASVLFEAAGGGNPDCISLLLEYGGSGNVPNRAGHLPIHRAAYEGHYLALKYLIPVTSKNAIR 305
Cdd:COG0666   202 VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281

                  ....*...
gi 1034654168 306 KSGLTPIH 313
Cdd:COG0666   282 LLDLLTLL 289
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
532-587 7.26e-31

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: 114.16  E-value: 7.26e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654168 532 ENPCSLKHLCRLKIRRLMGLQKLCQPASVEKLPLPPAIQRYILFKEYDLYGQELKL 587
Cdd:cd03731     1 ENPRPLKHLCRLKIRKLMGLQKLQQPSSMKKLPLPPALKRYILYKEYDLYGQELKL 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
191-439 6.07e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.12  E-value: 6.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 191 DIVALLLKHGGNVHLRDGFGVTPLGVAAEYGHCDVLEHLIHKGGDVLALADDGASVLFEAAGGGNPDCISLLLEYGGSGN 270
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 271 VPNRAGHLPIHRAAYEGHYLALKYLI----PVtskNAIRKSGLTPIHSAADGQNAQCLELLIENGFDVNTLladhisqsy 346
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLeagaDV---NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ--------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 347 DDERKTALYFGVSNNDVHCTEVLLAAGADPNL---DPLNCLLVAVRANNYEIVRLLLSHGANVNcyfMHVNDTRFPSVIQ 423
Cdd:COG0666   150 DNDGNTPLHLAAANGNLEIVKLLLEAGADVNArdnDGETPLHLAAENGHLEIVKLLLEAGADVN---AKDNDGKTALDLA 226
                         250
                  ....*....|....*.
gi 1034654168 424 YALNDEVMLRLLLNNG 439
Cdd:COG0666   227 AENGNLEIVKLLLEAG 242
PHA02875 PHA02875
ankyrin repeat protein; Provisional
76-271 2.19e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 87.74  E-value: 2.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168  76 GWFPLHEAVvqPIQQILEIVLDASYKTLWEFKTCDGETPLTLAVKAGLVENVRTLLEKGVWPN-TKNDKGETPLLIAVKK 154
Cdd:PHA02875   35 GISPIKLAM--KFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATIL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 155 GSYDMVSTLIKHNTSLDQPCVKRWSAMHEAAKQGRKDIVALLLKHGGNVHLRDGFGVTPLGVAAEYGHCDVLEHLIHKGG 234
Cdd:PHA02875  113 KKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA 192
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1034654168 235 DVLALADDG-ASVLFEAAGGGNPDCISLLLEYGGSGNV 271
Cdd:PHA02875  193 NIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNI 230
Ank_2 pfam12796
Ankyrin repeats (3 copies);
115-207 9.92e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 9.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 115 LTLAVKAGLVENVRTLLEKGVWPNTKNDKGETPLLIAVKKGSYDMVSTLIKHNTSLDQpcVKRWSAMHEAAKQGRKDIVA 194
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK--DNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1034654168 195 LLLKHGGNVHLRD 207
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
280-378 3.06e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 3.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 280 IHRAAYEGHYLALKYLIPV-TSKNAIRKSGLTPIHSAADGQNAQCLELLIEngfdvntlladHISQSYDDERKTALYFGV 358
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENgADANLQDKNGRTALHLAAKNGHLEIVKLLLE-----------HADVNLKDNGRTALHYAA 69
                          90       100
                  ....*....|....*....|
gi 1034654168 359 SNNDVHCTEVLLAAGADPNL 378
Cdd:pfam12796  70 RSGHLEIVKLLLEKGADINV 89
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
533-574 8.91e-12

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: 59.87  E-value: 8.91e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034654168 533 NPCSLKHLCRLKIRRLMGLQKLCQpasVEKLPLPPAIQRYIL 574
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGA---IDKLPLPPLLKDYLL 39
PHA02874 PHA02874
ankyrin repeat protein; Provisional
221-442 1.22e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.91  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 221 GHCDVLEHLIHKGGDVLALA-DDGASVLFEAAGGGNPDCISLLLEYGGSGNVPNRAGHLPIHRAAYEGHYLALKYLIpvt 299
Cdd:PHA02874   12 GDIEAIEKIIKNKGNCINISvDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI--- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 300 sKNAIRKSGLtPIHSAadgqNAQCLELLIENGFDVNTlladhisqsYDDERKTALYFGVSNNDVHCTEVLLAAGADPNLD 379
Cdd:PHA02874   89 -DNGVDTSIL-PIPCI----EKDMIKTILDCGIDVNI---------KDAELKTFLHYAIKKGDLESIKMLFEYGADVNIE 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034654168 380 PLNC---LLVAVRANNYEIVRLLLSHGANVNcyfmhVNDTRFPSVIQYALN--DEVMLRLLLNNGYQV 442
Cdd:PHA02874  154 DDNGcypIHIAIKHNFFDIIKLLLEKGAYAN-----VKDNNGESPLHNAAEygDYACIKLLIDHGNHI 216
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
535-576 8.54e-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: 51.26  E-value: 8.54e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1034654168  535 CSLKHLCRLKIRRLMGLqklcqpasVEKLPLPPAIQRYILFK 576
Cdd:smart00969   1 RSLQHLCRLAIRRSLGG--------IDKLPLPPRLKDYLLYY 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
101-296 5.88e-07

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: 52.32  E-value: 5.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 101 KTLWEFKTCD-------GETPLTLAVKAGLVENVRTLLEKGvwPNTKND-------KGETPLLIAVKKGSYDMVSTLIKH 166
Cdd:cd22192    34 KKLLKCPSCDlfqrgalGETALHVAALYDNLEAAVVLMEAA--PELVNEpmtsdlyQGETALHIAVVNQNLNLVRELIAR 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 167 NTSLDQPCVK----RWSA----------MHEAAKQGRKDIVALLLKHGGNVHLRDGFGVTPLgvaaeyghcdvleHLIhk 232
Cdd:cd22192   112 GADVVSPRATgtffRPGPknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL-------------HIL-- 176
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 233 ggdVLALADDGASVLFEaagggnpdcisLLLEYGGSGN------VPNRAGHLPIHRAAYEGHYLALKYLI 296
Cdd:cd22192   177 ---VLQPNKTFACQMYD-----------LILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLV 232
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
243-407 2.66e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.38  E-value: 2.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 243 GASVLFEAAGGGNP-DCISLLLEYGGSGNVpnraGHLPIHRAA---YEGHYLALKYLIPVTSK-------NAIRKS---- 307
Cdd:TIGR00870  52 GRSALFVAAIENENlELTELLLNLSCRGAV----GDTLLHAISleyVDAVEAILLHLLAAFRKsgplelaNDQYTSeftp 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 308 GLTPIHSAADGQNAQCLELLIENGFDVN---TLLADHISQsyddeRKTALYFGVSnndvhctevllaagadpnldPLN-- 382
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVParaCGDFFVKSQ-----GVDSFYHGES--------------------PLNaa 182
                         170       180
                  ....*....|....*....|....*.
gi 1034654168 383 -CLlvavraNNYEIVRLLLSHGANVN 407
Cdd:TIGR00870 183 aCL------GSPSIVALLSEDPADIL 202
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
245-406 3.94e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.46  E-value: 3.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 245 SVLFEAAGGGNPDCISLLLEYGgSGNVPNRA--GHLPIHRAAYEGHYLALKYLI---PVTSKNAIRKS---GLTPIHSAA 316
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCP-SCDLFQRGalGETALHVAALYDNLEAAVVLMeaaPELVNEPMTSDlyqGETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 317 DGQNAQCLELLIENGFDVNTlladhisqsyddERKTALYFGVSNndvHCtevLLAAGADPnldplncLLVAVRANNYEIV 396
Cdd:cd22192    98 VNQNLNLVRELIARGADVVS------------PRATGTFFRPGP---KN---LIYYGEHP-------LSFAACVGNEEIV 152
                         170
                  ....*....|
gi 1034654168 397 RLLLSHGANV 406
Cdd:cd22192   153 RLLIEHGADI 162
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
382-408 7.51e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 7.51e-04
                           10        20
                   ....*....|....*....|....*..
gi 1034654168  382 NCLLVAVRANNYEIVRLLLSHGANVNC 408
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
29-212 1.62e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.61  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168  29 KTALCPERFVPLSAQNRKLVEAIKQGHIP----ELQEYVKYKyaMDEADEKGWFPLHEAVVQPIQQILEIvldasyktLW 104
Cdd:TIGR00870   3 PLDIVPAEESPLSDEEKAFLPAAERGDLAsvyrDLEEPKKLN--INCPDRLGRSALFVAAIENENLELTE--------LL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 105 EFKTCDGETPLTLAVKA--GLVENVRTLL-------EKGVWPNTKND-------KGETPLLIAVKKGSYDMVSTLIKHNT 168
Cdd:TIGR00870  73 LNLSCRGAVGDTLLHAIslEYVDAVEAILlhllaafRKSGPLELANDqytseftPGITALHLAAHRQNYEIVKLLLERGA 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034654168 169 SLD-----QPCVKR---------WSAMHEAAKQGRKDIVALLLKHGGNVHLRDGFGVT 212
Cdd:TIGR00870 153 SVParacgDFFVKSqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNT 210
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
66-313 2.06e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.56  E-value: 2.06e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168  66 KYAMDEADEKGWFPLHEAVVQPIQQILEIVLDAsyKTLWEFKTCDGETPLTLAVKAGLVENVRTLLEKGVWPNTKNDKGE 145
Cdd:COG0666    44 LLALALADALGALLLLAAALAGDLLVALLLLAA--GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE 121
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 146 TPLLIAVKKGSYDMVSTLIKHNTSLDQPCVKRWSAMHEAAKQGRKDIVALLLKHGGNVHLRDGFGVTPLGVAAEYGHCDV 225
Cdd:COG0666   122 TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 226 LEHLIHKGGDVLALADDGASVLFEAAGGGNPDCISLLLEYGGSGNVPNRAGHLPIHRAAYEGHYLALKYLIPVTSKNAIR 305
Cdd:COG0666   202 VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAA 281

                  ....*...
gi 1034654168 306 KSGLTPIH 313
Cdd:COG0666   282 LLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
68-340 3.74e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.79  E-value: 3.74e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168  68 AMDEADEKGWFPLHEAVVQPIQQILEIVLDASYKTLWEFKTCDGETPLTLAVKAGLVENVRTLLEKGVWPNTKNDKGETP 147
Cdd:COG0666    11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTL 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 148 LLIAVKKGSYDMVSTLIKHNTSLDQPCVKRWSAMHEAAKQGRKDIVALLLKHGGNVHLRDGFGVTPLGVAAEYGHCDVLE 227
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVK 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 228 HLIHKGGDVLALADDGASVLFEAAGGGNPDCISLLLEYGGSGNVPNRAGHLPIHRAAYEGHYLALKYLIPVTSK-NAIRK 306
Cdd:COG0666   171 LLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADlNAKDK 250
                         250       260       270
                  ....*....|....*....|....*....|....
gi 1034654168 307 SGLTPIHSAADGQNAQCLELLIENGFDVNTLLAD 340
Cdd:COG0666   251 DGLTALLLAAAAGAALIVKLLLLALLLLAAALLD 284
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
130-407 3.97e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 125.45  E-value: 3.97e-32
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 130 LLEKGVWPNTKNDKGETPLLIAVKKGSYDMVSTLIKHNTSLDQPCVKRWSAMHEAAKQGRKDIVALLLKHGGNVHLRDGF 209
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 210 GVTPLGVAAEYGHCDVLEHLIHKGGDVLALADDGASVLFEAAGGGNPDCISLLLEYGGSGNVPNRAGHLPIHRAAYEGHY 289
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 290 LALKYLI----PVtskNAIRKSGLTPIHSAADGQNAQCLELLIENGFDVNTLladhisqsyDDERKTALYFGVSNNDVHC 365
Cdd:COG0666   167 EIVKLLLeagaDV---NARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK---------DNDGKTALDLAAENGNLEI 234
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|....*
gi 1034654168 366 TEVLLAAGADPNLDPLNC---LLVAVRANNYEIVRLLLSHGANVN 407
Cdd:COG0666   235 VKLLLEAGADLNAKDKDGltaLLLAAAAGAALIVKLLLLALLLLA 279
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
532-587 7.26e-31

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: 114.16  E-value: 7.26e-31
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654168 532 ENPCSLKHLCRLKIRRLMGLQKLCQPASVEKLPLPPAIQRYILFKEYDLYGQELKL 587
Cdd:cd03731     1 ENPRPLKHLCRLKIRKLMGLQKLQQPSSMKKLPLPPALKRYILYKEYDLYGQELKL 56
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
47-280 2.39e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 117.75  E-value: 2.39e-29
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168  47 LVEAIKQGHIPELQEYVKYKYAMDEADEKGWFPLHeavvqpiqqileivldasyktlwefktcdgetpltLAVKAGLVEN 126
Cdd:COG0666    91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLH-----------------------------------LAAYNGNLEI 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 127 VRTLLEKGVWPNTKNDKGETPLLIAVKKGSYDMVSTLIKHNTSLDQPCVKRWSAMHEAAKQGRKDIVALLLKHGGNVHLR 206
Cdd:COG0666   136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034654168 207 DGFGVTPLGVAAEYGHCDVLEHLIHKGGDVLALADDGASVLFEAAGGGNPDCISLLLEYGGSGNVPNRAGHLPI 280
Cdd:COG0666   216 DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
191-439 6.07e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.12  E-value: 6.07e-26
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 191 DIVALLLKHGGNVHLRDGFGVTPLGVAAEYGHCDVLEHLIHKGGDVLALADDGASVLFEAAGGGNPDCISLLLEYGGSGN 270
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 271 VPNRAGHLPIHRAAYEGHYLALKYLI----PVtskNAIRKSGLTPIHSAADGQNAQCLELLIENGFDVNTLladhisqsy 346
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLeagaDV---NARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQ--------- 149
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 347 DDERKTALYFGVSNNDVHCTEVLLAAGADPNL---DPLNCLLVAVRANNYEIVRLLLSHGANVNcyfMHVNDTRFPSVIQ 423
Cdd:COG0666   150 DNDGNTPLHLAAANGNLEIVKLLLEAGADVNArdnDGETPLHLAAENGHLEIVKLLLEAGADVN---AKDNDGKTALDLA 226
                         250
                  ....*....|....*.
gi 1034654168 424 YALNDEVMLRLLLNNG 439
Cdd:COG0666   227 AENGNLEIVKLLLEAG 242
PHA02875 PHA02875
ankyrin repeat protein; Provisional
76-271 2.19e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 87.74  E-value: 2.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168  76 GWFPLHEAVvqPIQQILEIVLDASYKTLWEFKTCDGETPLTLAVKAGLVENVRTLLEKGVWPN-TKNDKGETPLLIAVKK 154
Cdd:PHA02875   35 GISPIKLAM--KFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATIL 112
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 155 GSYDMVSTLIKHNTSLDQPCVKRWSAMHEAAKQGRKDIVALLLKHGGNVHLRDGFGVTPLGVAAEYGHCDVLEHLIHKGG 234
Cdd:PHA02875  113 KKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGA 192
                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1034654168 235 DVLALADDG-ASVLFEAAGGGNPDCISLLLEYGGSGNV 271
Cdd:PHA02875  193 NIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNI 230
Ank_2 pfam12796
Ankyrin repeats (3 copies);
115-207 9.92e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 9.92e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 115 LTLAVKAGLVENVRTLLEKGVWPNTKNDKGETPLLIAVKKGSYDMVSTLIKHNTSLDQpcVKRWSAMHEAAKQGRKDIVA 194
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLK--DNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1034654168 195 LLLKHGGNVHLRD 207
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
162-444 1.78e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.02  E-value: 1.78e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 162 TLIKHNTSLDQPCVKRWSAMHEAAKQGRKDIVALLLKHGGNVHLRDGFGVTPLGVAAEYGHcdVLEHlihkggdvlalad 241
Cdd:PHA03100   20 YIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKY--NLTD------------- 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 242 dgasvlfeaagggNPDCISLLLEYGGSGNVPNRAGHLPIHRAAYE--GHYLALKYLIPVTSK-NAIRKSGLTPIHSAADG 318
Cdd:PHA03100   85 -------------VKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANvNIKNSDGENLLHLYLES 151
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 319 --QNAQCLELLIENGFDVNT------LLADHISQSYDDER-KTALYFGVSNNDVHCTEVLLAAGADPNLDPLN---CLLV 386
Cdd:PHA03100  152 nkIDLKILKLLIDKGVDINAknrvnyLLSYGVPINIKDVYgFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYgdtPLHI 231
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034654168 387 AVRANNYEIVRLLLSHGANVN---CYFMHVNDTRFPSVIQYAL-NDEVMLRLLLNNGYQVEM 444
Cdd:PHA03100  232 AILNNNKEIFKLLLNNGPSIKtiiETLLYFKDKDLNTITKIKMlKKSIMYMFLLDPGFYKNR 293
SOCS_ASB14 cd03730
SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a ...
532-583 3.25e-16

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: 72.96  E-value: 3.25e-16
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034654168 532 ENPCSLKHLCRLKIRRLMGLQKLCQPASVEKLPLPPAIQRYILFKEYDLYGQ 583
Cdd:cd03730     1 TNPRSLKHLCRLKIRACMGRLRLRCPVFMSFLPLPNRLKAYILYKEYDLYGQ 52
PHA03100 PHA03100
ankyrin repeat protein; Provisional
113-337 3.96e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 80.86  E-value: 3.96e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 113 TPLTLAVKAGLVENVRTLLEKGVWPNTKNDKGETPL-----LIAVKKGSYDMVSTLIKHNTSLDQPCVKRWSAMHEAA-- 185
Cdd:PHA03100   37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAIsk 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 186 KQGRKDIVALLLKHGGNVHLRDGFGVTPLGVAAEYGHCD--VLEHLIHKGGDVLALaddgasvlfeaagggnpDCISLLL 263
Cdd:PHA03100  117 KSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINAK-----------------NRVNYLL 179
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034654168 264 EYGGSGNVPNRAGHLPIHRAAYEGHYLALKYLIPV-TSKNAIRKSGLTPIHSAADGQNAQCLELLIENGFDVNTL 337
Cdd:PHA03100  180 SYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLgANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTI 254
PHA02874 PHA02874
ankyrin repeat protein; Provisional
113-330 1.18e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.62  E-value: 1.18e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 113 TPLTLAVKAGLVENVRTLLEKGVWPNTKNDKGETPLLIAVKKGSYDMVSTLIKH--NTS-LDQPCV-------------- 175
Cdd:PHA02874   37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNgvDTSiLPIPCIekdmiktildcgid 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 176 ------KRWSAMHEAAKQGRKDIVALLLKHGGNVHLRDGFGVTPLGVAAEYGHCDVlehlihkggdvlaladdgasvlfe 249
Cdd:PHA02874  117 vnikdaELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDI------------------------ 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 250 aagggnpdcISLLLEYGGSGNVPNRAGHLPIHRAAYEGHYLALKYLIPVTSKNAIR-KSGLTPIHSAADgQNAQCLELLI 328
Cdd:PHA02874  173 ---------IKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKcKNGFTPLHNAII-HNRSAIELLI 242

                  ..
gi 1034654168 329 EN 330
Cdd:PHA02874  243 NN 244
PHA02876 PHA02876
ankyrin repeat protein; Provisional
113-337 1.74e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 79.72  E-value: 1.74e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 113 TPLTLAVKA-GLVENVRTLLEKGVWPNTKNDKGETPLLIAVKKGsYDM--VSTLIKHNTSLDQPCVKRWSAMHEAAKQGR 189
Cdd:PHA02876  275 TPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNG-YDTenIRTLIMLGADVNAADRLYITPLHQASTLDR 353
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 190 -KDIVALLLKHGGNVHLRDGFGVTPLGVAAEYGHCDVLEHLIHKGGDVLALADDGASVLFEAAGGGNPdcisllleyggs 268
Cdd:PHA02876  354 nKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNP------------ 421
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034654168 269 gnvpnraghlpihraayeghYLALKYLIP----VTSKNairKSGLTPIHSAADGQ-NAQCLELLIENGFDVNTL 337
Cdd:PHA02876  422 --------------------YMSVKTLIDrganVNSKN---KDLSTPLHYACKKNcKLDVIEMLLDNGADVNAI 472
PHA03095 PHA03095
ankyrin-like protein; Provisional
111-401 3.79e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 78.14  E-value: 3.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 111 GETPLTLAVKAGL---VENVRTLLEKGVWPNTKNDKGETPL-LIAVKKGSYDMVSTLIKHNTSLDQPCVKRWSAMHE--A 184
Cdd:PHA03095   47 GKTPLHLYLHYSSekvKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVylS 126
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 185 AKQGRKDIVALLLKHGGNVHLRDGFGVTPLGVAAEYGHCDV--LEHLIHKGGDVLALADDGASVL------FEAagggNP 256
Cdd:PHA03095  127 GFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAVDDRFRSLLhhhlqsFKP----RA 202
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 257 DCISLLLEYGGSGNVPNRAGHLPIHRAAYEG---HYLALKYLIPVTSKNAIRKSGLTPIHSAAdgqnaqclelliengfd 333
Cdd:PHA03095  203 RIVRELIRAGCDPAATDMLGNTPLHSMATGSsckRSLVLPLLIAGISINARNRYGQTPLHYAA----------------- 265
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034654168 334 vntlladhisqsydderktalyfgVSNNDVHCtEVLLAAGADPNL---DPLNCLLVAVRANNYEIVRLLLS 401
Cdd:PHA03095  266 ------------------------VFNNPRAC-RRLIALGADINAvssDGNTPLSLMVRNNNGRAVRAALA 311
Ank_2 pfam12796
Ankyrin repeats (3 copies);
247-336 1.29e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.37  E-value: 1.29e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 247 LFEAAGGGNPDCISLLLEYGGSGNVPNRAGHLPIHRAAYEGHYLALKYLIPVTSKNaIRKSGLTPIHSAADGQNAQCLEL 326
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVN-LKDNGRTALHYAARSGHLEIVKL 79
                          90
                  ....*....|
gi 1034654168 327 LIENGFDVNT 336
Cdd:pfam12796  80 LLEKGADINV 89
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
532-576 2.43e-14

SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB (SPRY domain-containing SOCS box proteins) protein families. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence of a variable number of repeats. SSB proteins contain a central SPRY domain and a C-terminal SOCS. Recently, it has been shown that all four SSB proteins interact with the MET, the receptor protein-tyrosine kinase for hepatocyte growth factor (HGF), and that SSB-1, SSB-2, and SSB-4 interact with prostate apoptosis response protein-4. Both types of interactions are mediated through the SPRY domain.


Pssm-ID: 239686  Cd Length: 42  Bit Score: 67.14  E-value: 2.43e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1034654168 532 ENPCSLKHLCRLKIRRLMGLQKLCQpasVEKLPLPPAIQRYILFK 576
Cdd:cd03716     1 STPRSLQHLCRLAIRRCLGRRRLEL---IKKLPLPPRLKDYLLYE 42
PHA03100 PHA03100
ankyrin repeat protein; Provisional
91-268 2.94e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 75.09  E-value: 2.94e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168  91 ILEIVLDASYKTlwEFKTCDGETPLTLAVKAGLVEN-----VRTLLEKGVWPNTKNDKGETPLLIAV--KKGSYDMVSTL 163
Cdd:PHA03100   50 VVKILLDNGADI--NSSTKNNSTPLHYLSNIKYNLTdvkeiVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYL 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 164 IKHNTSLDQPCVKRWSAMHEAAKQGRKDI------------------VALLLKHGGNVHLRDGFGVTPLGVAAEYGHCDV 225
Cdd:PHA03100  128 LDNGANVNIKNSDGENLLHLYLESNKIDLkilkllidkgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEF 207
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1034654168 226 LEHLIHKGGDVLALADDGASVLFEAAGGGNPDCISLLLEYGGS 268
Cdd:PHA03100  208 VKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
181-273 1.04e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.06  E-value: 1.04e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 181 MHEAAKQGRKDIVALLLKHGGNVHLRDGFGVTPLGVAAEYGHCDVLEHLI-HKGGDVlalADDGASVLFEAAGGGNPDCI 259
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLeHADVNL---KDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 1034654168 260 SLLLEYGGSGNVPN 273
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
114-337 2.16e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 72.61  E-value: 2.16e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 114 PLTLAVKAGLVENVRTLLEKGVWPNTKNDKGETPLLIAV----KKGSYDMVSTLIKHNTSLDQPCVK------------- 176
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICkepnKLGMKEMIRSINKCSVFYTLVAIKdafnnrnveifki 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 177 ---------RWSAMHEAAKQGRKD-----IVALLLKHGGNVHLRD-GFGVTPLGVAAEYGHCDVLEHLIHKGGDVLALAD 241
Cdd:PHA02878  120 iltnrykniQTIDLVYIDKKSKDDiieaeITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDK 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 242 DGASVLFEAAGGGNPDCISLLLEYGGSGNVPNRAGHLPIHRAA-----YEGHYLALKYLIPVTSKNAIRksGLTPIHSAA 316
Cdd:PHA02878  200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgyckdYDILKLLLEHGVDVNAKSYIL--GLTALHSSI 277
                         250       260
                  ....*....|....*....|.
gi 1034654168 317 dgQNAQCLELLIENGFDVNTL 337
Cdd:PHA02878  278 --KSERKLKLLLEYGADINSL 296
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
533-576 5.45e-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: 63.26  E-value: 5.45e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1034654168 533 NPCSLKHLCRLKIRRLMGLQKLCQpasVEKLPLPPAIQRYILFK 576
Cdd:cd03587     1 NPRSLQHLCRLAIRRCLGKRRLDL---IDKLPLPPRLKDYLLYK 41
Ank_2 pfam12796
Ankyrin repeats (3 copies);
280-378 3.06e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 3.06e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 280 IHRAAYEGHYLALKYLIPV-TSKNAIRKSGLTPIHSAADGQNAQCLELLIEngfdvntlladHISQSYDDERKTALYFGV 358
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENgADANLQDKNGRTALHLAAKNGHLEIVKLLLE-----------HADVNLKDNGRTALHYAA 69
                          90       100
                  ....*....|....*....|
gi 1034654168 359 SNNDVHCTEVLLAAGADPNL 378
Cdd:pfam12796  70 RSGHLEIVKLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
312-407 6.35e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.67  E-value: 6.35e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 312 IHSAADGQNAQCLELLIENGFDVNTLladhisqsyDDERKTALYFGVSNNDVHCTEVLLA-AGADPNLDPLNCLLVAVRA 390
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQ---------DKNGRTALHLAAKNGHLEIVKLLLEhADVNLKDNGRTALHYAARS 71
                          90
                  ....*....|....*..
gi 1034654168 391 NNYEIVRLLLSHGANVN 407
Cdd:pfam12796  72 GHLEIVKLLLEKGADIN 88
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
533-574 8.91e-12

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: 59.87  E-value: 8.91e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034654168 533 NPCSLKHLCRLKIRRLMGLQKLCQpasVEKLPLPPAIQRYIL 574
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGA---IDKLPLPPLLKDYLL 39
PHA02874 PHA02874
ankyrin repeat protein; Provisional
221-442 1.22e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.91  E-value: 1.22e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 221 GHCDVLEHLIHKGGDVLALA-DDGASVLFEAAGGGNPDCISLLLEYGGSGNVPNRAGHLPIHRAAYEGHYLALKYLIpvt 299
Cdd:PHA02874   12 GDIEAIEKIIKNKGNCINISvDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI--- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 300 sKNAIRKSGLtPIHSAadgqNAQCLELLIENGFDVNTlladhisqsYDDERKTALYFGVSNNDVHCTEVLLAAGADPNLD 379
Cdd:PHA02874   89 -DNGVDTSIL-PIPCI----EKDMIKTILDCGIDVNI---------KDAELKTFLHYAIKKGDLESIKMLFEYGADVNIE 153
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1034654168 380 PLNC---LLVAVRANNYEIVRLLLSHGANVNcyfmhVNDTRFPSVIQYALN--DEVMLRLLLNNGYQV 442
Cdd:PHA02874  154 DDNGcypIHIAIKHNFFDIIKLLLEKGAYAN-----VKDNNGESPLHNAAEygDYACIKLLIDHGNHI 216
PHA02875 PHA02875
ankyrin repeat protein; Provisional
217-415 1.42e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 66.55  E-value: 1.42e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 217 AAEYGHCDVLEHLIHKGGDVLALADDGASVLFEAAGGGNPDCISLLLEYGGSGNVPNRAGHLPIHRAAYEGHYLALKYLI 296
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 297 PVTS--KNAIRKSGLTPIHSAADGQNAQCLELLIENGFDVNT----------------------LLADHISQS--YDDER 350
Cdd:PHA02875   89 DLGKfaDDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIpntdkfsplhlavmmgdikgieLLIDHKACLdiEDCCG 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1034654168 351 KTALYFGVSNNDVHCTEVLLAAGADPNLDPLN----CLLVAVRANNYEIVRLLLSHGANVNCYFMHVND 415
Cdd:PHA02875  169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgcvaALCYAIENNKIDIVRLFIKRGADCNIMFMIEGE 237
PHA02874 PHA02874
ankyrin repeat protein; Provisional
99-279 2.73e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 65.76  E-value: 2.73e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168  99 SYKTLWEF------KTCDGETPLTLAVKAGLVENVRTLLEKGVWPNTKNDKGETPLLIAVKKGSYDMVSTLIKHNTSLDQ 172
Cdd:PHA02874  139 SIKMLFEYgadvniEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMN 218
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 173 PCVKRWSAMHEAAKQGRKdiVALLLKHGGNVHLRDGFGVTPLGVAAEYGhC--DVLEHLIHKGGDVLALADDGASVLFEA 250
Cdd:PHA02874  219 KCKNGFTPLHNAIIHNRS--AIELLINNASINDQDIDGSTPLHHAINPP-CdiDIIDILLYHKADISIKDNKGENPIDTA 295
                         170       180
                  ....*....|....*....|....*....
gi 1034654168 251 AGGGNPDciSLLLEYGGSGNVPNRAGHLP 279
Cdd:PHA02874  296 FKYINKD--PVIKDIIANAVLIKEADKLK 322
PHA03095 PHA03095
ankyrin-like protein; Provisional
191-406 3.26e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.82  E-value: 3.26e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 191 DIVALLLKHGGNVHLRDGFGVTPLGVaaeyghcdvlehLIHKGGDVLaladdgasvlfeaagggnPDCISLLLEYGGSGN 270
Cdd:PHA03095   28 EEVRRLLAAGADVNFRGEYGKTPLHL------------YLHYSSEKV------------------KDIVRLLLEAGADVN 77
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 271 VPNRAGHLPIHraayegHYLALKYLIPVtsknairksgltpihsaadgqnaqcLELLIENGFDVNtlladhisqSYDDER 350
Cdd:PHA03095   78 APERCGFTPLH------LYLYNATTLDV-------------------------IKLLIKAGADVN---------AKDKVG 117
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034654168 351 KTAL--YFGVSNNDVHCTEVLLAAGADPN------LDPLNCLLVAVRAnNYEIVRLLLSHGANV 406
Cdd:PHA03095  118 RTPLhvYLSGFNINPKVIRLLLRKGADVNaldlygMTPLAVLLKSRNA-NVELLRLLIDAGADV 180
PHA02876 PHA02876
ankyrin repeat protein; Provisional
181-443 4.89e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 65.47  E-value: 4.89e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 181 MHEAAKQGRKDIVALLLKHGGNVHLRDGFGVTPLGVAAEYGHCDVLEHLIHKGGDVLALADDGASVLFEAAGGGNPDCIS 260
Cdd:PHA02876  149 IKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 261 LLLEYGGSGNVPNRAGHLPIHRAAYEGHYLALKYLIPVTSKNAIRKsglTPIHSAADGQN-AQCLELLIENGFDVNtllA 339
Cdd:PHA02876  229 AIIDNRSNINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKN---TPLHHASQAPSlSRLVPKLLERGADVN---A 302
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 340 DHIsqsyddERKTALYFGVSNN-DVHCTEVLLAAGADPN------LDPLNclLVAVRANNYEIVRLLLSHGANVNcyfmh 412
Cdd:PHA02876  303 KNI------KGETPLYLMAKNGyDTENIRTLIMLGADVNaadrlyITPLH--QASTLDRNKDIVITLLELGANVN----- 369
                         250       260       270
                  ....*....|....*....|....*....|...
gi 1034654168 413 VNDTRFPSVIQYAL--NDEVMLRLLLNNGYQVE 443
Cdd:PHA02876  370 ARDYCDKTPIHYAAvrNNVVIINTLLDYGADIE 402
PHA02874 PHA02874
ankyrin repeat protein; Provisional
47-231 1.59e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.44  E-value: 1.59e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168  47 LVEAIKQGHIPELQEYVKYKYAMDEADEKGWFPLHEAVVQPIQQILEIVLD---------------ASYKTLWE------ 105
Cdd:PHA02874   39 LIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDngvdtsilpipciekDMIKTILDcgidvn 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 106 FKTCDGETPLTLAVKAGLVENVRTLLEKGVWPNTKNDKGETPLLIAVKKGSYDMVSTLIKHNTSLDQPCVKRWSAMHEAA 185
Cdd:PHA02874  119 IKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAA 198
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 1034654168 186 KQGRKDIVALLLKHGGNVHLRDGFGVTPLGVAAEYGHcDVLEHLIH 231
Cdd:PHA02874  199 EYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLIN 243
PHA02878 PHA02878
ankyrin repeat protein; Provisional
127-283 1.96e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.36  E-value: 1.96e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 127 VRTLLEKGVWPNTKN-DKGETPLLIAVKKGSYDMVSTLIKHNTSLDQPCVKRWSAMHEAAKQGRKDIVALLLKHGGNVHL 205
Cdd:PHA02878  150 TKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 206 RDGFGVTPLGVAAeyGHC---DVLEHLIHKGGDVLALAD-DGASVLFEAAggGNPDCISLLLEYGGSGNVPNRAGHLPIH 281
Cdd:PHA02878  230 RDKCGNTPLHISV--GYCkdyDILKLLLEHGVDVNAKSYiLGLTALHSSI--KSERKLKLLLEYGADINSLNSYKLTPLS 305

                  ..
gi 1034654168 282 RA 283
Cdd:PHA02878  306 SA 307
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
148-296 1.36e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 61.04  E-value: 1.36e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 148 LLIAVKKGSYDMVSTLIKHNTSLDQPCVKRWSAMHEAAKQGRKDIVALLLKHGGNVHLRDGFGVTPLGVAAEYGHCDVLE 227
Cdd:PLN03192  529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFR 608
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1034654168 228 HLIHkggdvLALADD---GASVLFEAAGGGNPDCISLLLEYGGSGNVPNRAGHLPIHRAAYEGHYLALKYLI 296
Cdd:PLN03192  609 ILYH-----FASISDphaAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLI 675
Ank_2 pfam12796
Ankyrin repeats (3 copies);
47-141 1.73e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.74  E-value: 1.73e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168  47 LVEAIKQGHIPELQEYVKYKYAMDEADEKGWFPLHEAVVQPIQQILEIVLDASYKTLwefkTCDGETPLTLAVKAGLVEN 126
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL----KDNGRTALHYAARSGHLEI 76
                          90
                  ....*....|....*
gi 1034654168 127 VRTLLEKGVWPNTKN 141
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA03100 PHA03100
ankyrin repeat protein; Provisional
70-236 6.79e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 6.79e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168  70 DEADEKGWFPLHEAVVQPIQQ--ILEIVLDASYKTlwEFKTCDGETPLTLAVKAGLVEN--VRTLLEKGVWPNTKNDkge 145
Cdd:PHA03100  100 NAPDNNGITPLLYAISKKSNSysIVEYLLDNGANV--NIKNSDGENLLHLYLESNKIDLkiLKLLIDKGVDINAKNR--- 174
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 146 tplliavkkgsydmVSTLIKHNTSLDQPCVKRWSAMHEAAKQGRKDIVALLLKHGGNVHLRDGFGVTPLGVAAEYGHCDV 225
Cdd:PHA03100  175 --------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI 240
                         170
                  ....*....|.
gi 1034654168 226 LEHLIHKGGDV 236
Cdd:PHA03100  241 FKLLLNNGPSI 251
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
121-236 7.83e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.73  E-value: 7.83e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 121 AGLVENvrtLLEKGVWPNTKNDKGETPLLIAVKKGSYDMVSTLIKH-----------NTSLdqpcvkrWSAM---H---- 182
Cdd:PLN03192  538 AALLEE---LLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHacnvhirdangNTAL-------WNAIsakHhkif 607
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034654168 183 --------------------EAAKQGRKDIVALLLKHGGNVHLRDGFGVTPLGVAAEYGHCDVLEHLIHKGGDV 236
Cdd:PLN03192  608 rilyhfasisdphaagdllcTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
535-576 8.54e-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: 51.26  E-value: 8.54e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 1034654168  535 CSLKHLCRLKIRRLMGLqklcqpasVEKLPLPPAIQRYILFK 576
Cdd:smart00969   1 RSLQHLCRLAIRRSLGG--------IDKLPLPPRLKDYLLYY 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
177-230 2.26e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 2.26e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034654168 177 RWSAMHEAAKQGRKDIVALLLKHGGNVHLRDGFGVTPLGVAAEYGHCDVLEHLI 230
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
113-164 4.15e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.97  E-value: 4.15e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034654168 113 TPLTLAVKAGLVENVRTLLEKGVWPNTKNDKGETPLLIAVKKGSYDMVSTLI 164
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
130-442 7.43e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.45  E-value: 7.43e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 130 LLEKGVWPNTKNDKGETPLLIAVKKGSYDMVSTLIKHNTSLDQPCVKRWSAMHEAAKQGRKDIVALLLKHGGNVHLRD-- 207
Cdd:PHA02876  164 LLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDls 243
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 208 -------------------GFGV--------TPLGVAAEYGHCDVL-EHLIHKGGDVLALADDGASVLFEAAGGG-NPDC 258
Cdd:PHA02876  244 llkairnedletslllydaGFSVnsiddcknTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGyDTEN 323
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 259 ISLLLEYGGSGNVPNRAGHLPIHRAAYEGHY--LALKYLIPVTSKNAIRKSGLTPIHSAADGQNAQCLELLIENGFDVNT 336
Cdd:PHA02876  324 IRTLIMLGADVNAADRLYITPLHQASTLDRNkdIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEA 403
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 337 LladhiSQSYDderkTALYFGV-SNNDVHCTEVLLAAGAD---PNLDPLNCLLVAVRAN-NYEIVRLLLSHGANVNCYFM 411
Cdd:PHA02876  404 L-----SQKIG----TALHFALcGTNPYMSVKTLIDRGANvnsKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINI 474
                         330       340       350
                  ....*....|....*....|....*....|.
gi 1034654168 412 HvndTRFPSVIqyALNDEVMLRLLLNNGYQV 442
Cdd:PHA02876  475 Q---NQYPLLI--ALEYHGIVNILLHYGAEL 500
SOCS_SSB2 cd03719
SOCS (suppressors of cytokine signaling) box of SSB2 (SPRY domain-containing SOCS box proteins) ...
532-576 2.26e-07

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


Pssm-ID: 239689  Cd Length: 42  Bit Score: 47.32  E-value: 2.26e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1034654168 532 ENPCSLKHLCRLKIRRLMGLQKLCQpasVEKLPLPPAIQRYILFK 576
Cdd:cd03719     1 AEPHSLLHLSRLCVRHALGDTRLGQ---VSALPLPPAMKRYLLYQ 42
PHA02878 PHA02878
ankyrin repeat protein; Provisional
247-442 3.74e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 52.96  E-value: 3.74e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 247 LFEAAGGGNPDCISLLLEYGGSGNVPNRAGHLPIHRAAYEGHYLALKYLIPVTSKNAIRKSgLTPIHSAADGQNAQCLEL 326
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYT-LVAIKDAFNNRNVEIFKI 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 327 LIENGFDVN----------------------TLLADH---ISQSYDDERKTALYFGVSNNDVHCTEVLLAAGADPNLdPL 381
Cdd:PHA02878  120 ILTNRYKNIqtidlvyidkkskddiieaeitKLLLSYgadINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNI-PD 198
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1034654168 382 NC----LLVAVRANNYEIVRLLLSHGANVNCYFMHVNdTRFPSVIQYALNDEVmLRLLLNNGYQV 442
Cdd:PHA02878  199 KTnnspLHHAVKHYNKPIVHILLENGASTDARDKCGN-TPLHISVGYCKDYDI-LKLLLEHGVDV 261
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
101-296 5.88e-07

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: 52.32  E-value: 5.88e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 101 KTLWEFKTCD-------GETPLTLAVKAGLVENVRTLLEKGvwPNTKND-------KGETPLLIAVKKGSYDMVSTLIKH 166
Cdd:cd22192    34 KKLLKCPSCDlfqrgalGETALHVAALYDNLEAAVVLMEAA--PELVNEpmtsdlyQGETALHIAVVNQNLNLVRELIAR 111
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 167 NTSLDQPCVK----RWSA----------MHEAAKQGRKDIVALLLKHGGNVHLRDGFGVTPLgvaaeyghcdvleHLIhk 232
Cdd:cd22192   112 GADVVSPRATgtffRPGPknliyygehpLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL-------------HIL-- 176
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 233 ggdVLALADDGASVLFEaagggnpdcisLLLEYGGSGN------VPNRAGHLPIHRAAYEGHYLALKYLI 296
Cdd:cd22192   177 ---VLQPNKTFACQMYD-----------LILSYDKEDDlqpldlVPNNQGLTPFKLAAKEGNIVMFQHLV 232
PHA03095 PHA03095
ankyrin-like protein; Provisional
109-264 6.42e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.95  E-value: 6.42e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 109 CDGETPLTLAVKAG--LVENVRTLLEKGVWPNTKNDKGETPL---LIAVKKgSYDMVSTLIKHNTSLDQPCVKRWSAMHE 183
Cdd:PHA03095  150 LYGMTPLAVLLKSRnaNVELLRLLIDAGADVYAVDDRFRSLLhhhLQSFKP-RARIVRELIRAGCDPAATDMLGNTPLHS 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 184 AAKQG--RKDIVALLLKHGGNVHLRDGFGVTPLGVAAEYGHCDVLEHLIHKGGDVLALADDGASVLFEAAGGGNPDCISL 261
Cdd:PHA03095  229 MATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRA 308

                  ...
gi 1034654168 262 LLE 264
Cdd:PHA03095  309 ALA 311
Ank_4 pfam13637
Ankyrin repeats (many copies);
245-296 7.48e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.11  E-value: 7.48e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034654168 245 SVLFEAAGGGNPDCISLLLEYGGSGNVPNRAGHLPIHRAAYEGHYLALKYLI 296
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
79-217 8.62e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.80  E-value: 8.62e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168  79 PLHEAVVQPIQQILEIVLdaSYKTLWEFKTCDGETPLTLAVKAGLVENVRTLLEKGVWPNTKNDKGETPLLIAVKK-GSY 157
Cdd:PHA02878  171 ALHYATENKDQRLTELLL--SYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDY 248
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034654168 158 DMVSTLIKHNTSLD-QPCVKRWSAMHEAAKQGRKdiVALLLKHGGNVHLRDGFGVTPLGVA 217
Cdd:PHA02878  249 DILKLLLEHGVDVNaKSYILGLTALHSSIKSERK--LKLLLEYGADINSLNSYKLTPLSSA 307
SOCS_ASB8 cd03727
SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a ...
534-576 9.58e-07

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


Pssm-ID: 239697  Cd Length: 43  Bit Score: 45.60  E-value: 9.58e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1034654168 534 PCSLKHLCRLKIRRLMGLQKLcqPASVEKLPLPPAIQRYILFK 576
Cdd:cd03727     3 PGTLKALARYAVRRSLGVQYL--PEAVKQLPLPRSVKEYLLLL 43
SOCS smart00253
suppressors of cytokine signalling; suppressors of cytokine signalling
532-574 1.05e-06

suppressors of cytokine signalling; suppressors of cytokine signalling


Pssm-ID: 128549  Cd Length: 43  Bit Score: 45.36  E-value: 1.05e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|...
gi 1034654168  532 ENPCSLKHLCRLKIRRLMGLQklcqpaSVEKLPLPPAIQRYIL 574
Cdd:smart00253   5 SNVPSLQHLCRFTIRRCTRTD------QIKTLPLPPKLKDYLS 41
PHA03100 PHA03100
ankyrin repeat protein; Provisional
111-171 1.54e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 50.82  E-value: 1.54e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1034654168 111 GETPLTLAVKAGLVENVRTLLEKGVWPNTKNDKGETPLLIAVKKGSYDMVSTLIKHNTSLD 171
Cdd:PHA03100  192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
SOCS_SSB1_4 cd03718
SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box ...
534-576 2.93e-06

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


Pssm-ID: 239688  Cd Length: 42  Bit Score: 44.22  E-value: 2.93e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1034654168 534 PCSLKHLCRLKIRRLMGLQKLcqpASVEKLPLPPAIQRYILFK 576
Cdd:cd03718     3 PLPLMDLCRRRVRVALGRDRL---EEIEQLPLPPSLKNYLLYQ 42
SOCS_ASB3 cd03722
SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a ...
536-577 3.28e-06

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: 44.40  E-value: 3.28e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034654168 536 SLKHLCRLKIRRLMGLQKLCQPASVEKLPLPPAIQRYILFKE 577
Cdd:cd03722     5 SLTHLCRLEIRSSLKSERLRSDSFICQLPLPRSLQDYLLYSD 46
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
533-574 5.35e-06

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: 43.58  E-value: 5.35e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034654168 533 NPCSLKHLCRLKIRRLMGlqKLCQpASVEKLPLPPAIQRYIL 574
Cdd:cd03723     2 TPRSLQHLCRCAIRKLLG--SRCH-KLVPQLSLPTSLKNYLL 40
SOCS_ASB1 cd03720
SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a ...
533-574 5.47e-06

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


Pssm-ID: 239690  Cd Length: 42  Bit Score: 43.56  E-value: 5.47e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1034654168 533 NPCSLKHLCRLKIRRLMGLQKLcqpASVEKLPLPPAIQRYIL 574
Cdd:cd03720     2 NPRSLLSLCRIAVRRALGKQRL---SLICSLPLPDPIKKFLL 40
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
532-577 6.11e-06

SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ASB2 targets specific proteins to destruction by the proteasome in leukemia cells that have been induced to differentiate. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239691  Cd Length: 45  Bit Score: 43.32  E-value: 6.11e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1034654168 532 ENPCSLKHLCRLKIRRLMGLQKLcqpASVEKLPLPPAIQRYILFKE 577
Cdd:cd03721     1 EPPRPLAHLCRLKVRTLIGINRI---KLIDTLPLPPRLIRYLNHQE 43
SOCS_WSB1_SWIP1 cd03746
SOCS (suppressors of cytokine signaling) box of WSB1/SWiP1-like proteins. This subfamily ...
536-576 1.72e-05

SOCS (suppressors of cytokine signaling) box of WSB1/SWiP1-like proteins. This subfamily contains WSB-1 (SOCS-box-containing WD-40 protein), part of an E3 ubiquitin ligase for the thyroid-hormone-activating type 2 iodothyronine deiodinase (D2) and SWiP-1 (SOCS box and WD-repeats in Protein), a WD40-containing protein that is expressed in embryonic structures of chickens and regulated by Sonic Hedgehog (Shh). The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239715  Cd Length: 40  Bit Score: 42.11  E-value: 1.72e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1034654168 536 SLKHLCRLKIRRLMGLQKlcqpasVEKLPLPPAIQRYILFK 576
Cdd:cd03746     5 SLQHLCRMAIRRVMPTQQ------VKELPIPSKLLEFLTYR 39
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
243-407 2.66e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.38  E-value: 2.66e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 243 GASVLFEAAGGGNP-DCISLLLEYGGSGNVpnraGHLPIHRAA---YEGHYLALKYLIPVTSK-------NAIRKS---- 307
Cdd:TIGR00870  52 GRSALFVAAIENENlELTELLLNLSCRGAV----GDTLLHAISleyVDAVEAILLHLLAAFRKsgplelaNDQYTSeftp 127
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 308 GLTPIHSAADGQNAQCLELLIENGFDVN---TLLADHISQsyddeRKTALYFGVSnndvhctevllaagadpnldPLN-- 382
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVParaCGDFFVKSQ-----GVDSFYHGES--------------------PLNaa 182
                         170       180
                  ....*....|....*....|....*.
gi 1034654168 383 -CLlvavraNNYEIVRLLLSHGANVN 407
Cdd:TIGR00870 183 aCL------GSPSIVALLSEDPADIL 202
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
536-578 3.05e-05

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


Pssm-ID: 239687  Cd Length: 39  Bit Score: 41.43  E-value: 3.05e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1034654168 536 SLKHLCRLKIRRLMGLQKlcqpasVEKLPLPPAIQRYIlfKEY 578
Cdd:cd03717     5 SLQHLCRFVIRQCTRRDL------IDQLPLPRRLKDYL--KEY 39
SOCS_WSB_SWIP cd03733
SOCS (suppressors of cytokine signaling) box of WSB/SWiP-like proteins. This subfamily ...
536-576 3.37e-05

SOCS (suppressors of cytokine signaling) box of WSB/SWiP-like proteins. This subfamily contains WSB-1 (SOCS-box-containing WD-40 protein), part of an E3 ubiquitin ligase for the thyroid-hormone-activating type 2 iodothyronine deiodinase (D2), and SWiP-1 (SOCS box and WD-repeats in Protein), a WD40-containing protein that is expressed in embryonic structures of chickens and regulated by Sonic Hedgehog (Shh), as well as, their isoforms WSB-2 and SWiP-2. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239702  Cd Length: 39  Bit Score: 41.25  E-value: 3.37e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1034654168 536 SLKHLCRLKIRRLMGLQKlcqpasVEKLPLPPAIQRYILFK 576
Cdd:cd03733     5 SLQHLCRMALRRVMTTQQ------VLALPIPKKMKEFLTYR 39
PHA02989 PHA02989
ankyrin repeat protein; Provisional
127-264 4.22e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 46.27  E-value: 4.22e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 127 VRTLLEKGVWP-NTKNDKGETPLLIAVKKG----SYDMVSTLIKHNTSLDQPcvkrwSAMHEAAKQG---------RKDI 192
Cdd:PHA02989  163 IKILLSFGVNLfEKTSLYGLTPMNIYLRNDidviSIKVIKYLIKKGVNIETN-----NNGSESVLESfldnnkilsKKEF 237
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1034654168 193 VAL--LLKHGgNVHLRDGFGVTPLGVAAEYGHCDVLEHLIHKGGDVLALADDGASVLFEAAGGGNPDCISLLLE 264
Cdd:PHA02989  238 KVLnfILKYI-KINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRILQ 310
Ank_4 pfam13637
Ankyrin repeats (many copies);
308-370 6.85e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 6.85e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1034654168 308 GLTPIHSAADGQNAQCLELLIENGFDVNTLladhisqsyDDERKTALYFGVSNNDVHCTEVLL 370
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAV---------DGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
279-328 7.63e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 7.63e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034654168 279 PIHRAAYEGHYLALKYLI----PVtskNAIRKSGLTPIHSAADGQNAQCLELLI 328
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLekgaDI---NAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
210-263 1.11e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 1.11e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1034654168 210 GVTPLGVAAEYGHCDVLEHLIHKGGDVLALADDGASVLFEAAGGGNPDCISLLL 263
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
146-197 1.38e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 1.38e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034654168 146 TPLLIAVKKGSYDMVSTLIKHNTSLDQPCVKRWSAMHEAAKQGRKDIVALLL 197
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
110-166 1.64e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.50  E-value: 1.64e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1034654168 110 DGETPLTLAVKAGLVENVRTLLEKGVWPNTKNDKGETPLLIAVKKGSYDMVSTLIKH 166
Cdd:PTZ00322  114 DGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02989 PHA02989
ankyrin repeat protein; Provisional
324-407 2.45e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 43.96  E-value: 2.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 324 LELLIENGFDVN------TLLADHISQSYDDERKTAlyfgvsnndvHCTEVLLAAGADPNLDPLN------CLLVAVRAN 391
Cdd:PHA02989   53 VKLLIDNGADVNykgyieTPLCAVLRNREITSNKIK----------KIVKLLLKFGADINLKTFNgvspivCFIYNSNIN 122
                          90
                  ....*....|....*.
gi 1034654168 392 NYEIVRLLLSHGANVN 407
Cdd:PHA02989  123 NCDMLRFLLSKGINVN 138
Ank_5 pfam13857
Ankyrin repeats (many copies);
111-151 2.85e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 2.85e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1034654168 111 GETPLTLAVKAGLVENVRTLLEKGVWPNTKNDKGETPLLIA 151
Cdd:pfam13857  16 GYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
196-247 3.76e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 3.76e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034654168 196 LLKHGG-NVHLRDGFGVTPLGVAAEYGHCDVLEHLIHKGGDVLALADDGASVL 247
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
245-406 3.94e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.46  E-value: 3.94e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 245 SVLFEAAGGGNPDCISLLLEYGgSGNVPNRA--GHLPIHRAAYEGHYLALKYLI---PVTSKNAIRKS---GLTPIHSAA 316
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCP-SCDLFQRGalGETALHVAALYDNLEAAVVLMeaaPELVNEPMTSDlyqGETALHIAV 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 317 DGQNAQCLELLIENGFDVNTlladhisqsyddERKTALYFGVSNndvHCtevLLAAGADPnldplncLLVAVRANNYEIV 396
Cdd:cd22192    98 VNQNLNLVRELIARGADVVS------------PRATGTFFRPGP---KN---LIYYGEHP-------LSFAACVGNEEIV 152
                         170
                  ....*....|
gi 1034654168 397 RLLLSHGANV 406
Cdd:cd22192   153 RLLIEHGADI 162
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
80-232 4.98e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.08  E-value: 4.98e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168  80 LHEAVVQPIQQILEIVLDASYKTLWEFKTCD---GETPLTLAVKAGLVENVRTLLEKGVWPNT---------KNDK---- 143
Cdd:cd22192    55 LHVAALYDNLEAAVVLMEAAPELVNEPMTSDlyqGETALHIAVVNQNLNLVRELIARGADVVSpratgtffrPGPKnliy 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 144 -GETPLLIAVKKGSYDMVSTLIKH-----------NTSLD----QPCVKRWSAMHE--AAKQGRKDIVALllkhggnVHL 205
Cdd:cd22192   135 yGEHPLSFAACVGNEEIVRLLIEHgadiraqdslgNTVLHilvlQPNKTFACQMYDliLSYDKEDDLQPL-------DLV 207
                         170       180
                  ....*....|....*....|....*..
gi 1034654168 206 RDGFGVTPLGVAAEYGHCDVLEHLIHK 232
Cdd:cd22192   208 PNNQGLTPFKLAAKEGNIVMFQHLVQK 234
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
382-408 7.51e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 7.51e-04
                           10        20
                   ....*....|....*....|....*..
gi 1034654168  382 NCLLVAVRANNYEIVRLLLSHGANVNC 408
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
130-184 1.57e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 1.57e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654168 130 LLEKGVW-PNTKNDKGETPLLIAVKKGSYDMVSTLIKHNTSLDQPCVKRWSAMHEA 184
Cdd:pfam13857   1 LLEHGPIdLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
29-212 1.62e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 41.61  E-value: 1.62e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168  29 KTALCPERFVPLSAQNRKLVEAIKQGHIP----ELQEYVKYKyaMDEADEKGWFPLHEAVVQPIQQILEIvldasyktLW 104
Cdd:TIGR00870   3 PLDIVPAEESPLSDEEKAFLPAAERGDLAsvyrDLEEPKKLN--INCPDRLGRSALFVAAIENENLELTE--------LL 72
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 105 EFKTCDGETPLTLAVKA--GLVENVRTLL-------EKGVWPNTKND-------KGETPLLIAVKKGSYDMVSTLIKHNT 168
Cdd:TIGR00870  73 LNLSCRGAVGDTLLHAIslEYVDAVEAILlhllaafRKSGPLELANDqytseftPGITALHLAAHRQNYEIVKLLLERGA 152
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1034654168 169 SLD-----QPCVKR---------WSAMHEAAKQGRKDIVALLLKHGGNVHLRDGFGVT 212
Cdd:TIGR00870 153 SVParacgDFFVKSqgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNT 210
PHA02989 PHA02989
ankyrin repeat protein; Provisional
324-442 1.82e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 41.27  E-value: 1.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 324 LELLIENGFDVNTlladhisqSYDDERKTALYFGVSNNDVHCTEVLLAAGADPNLD-----PLNCLLvavraNNYEI--- 395
Cdd:PHA02989   19 LEFLLRTGFDVNE--------EYRGNSILLLYLKRKDVKIKIVKLLIDNGADVNYKgyietPLCAVL-----RNREItsn 85
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1034654168 396 -----VRLLLSHGANVNCYFMHVNDTRFPSVIQYALNDEVMLRLLLNNGYQV 442
Cdd:PHA02989   86 kikkiVKLLLKFGADINLKTFNGVSPIVCFIYNSNINNCDMLRFLLSKGINV 137
SOCS_CIS1 cd03734
SOCS (suppressors of cytokine signaling) box of CIS (cytokine-inducible SH2 protein) 1-like ...
536-578 2.44e-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: 36.09  E-value: 2.44e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1034654168 536 SLKHLCRLKIRRLMglqklcqpASVEKLPLPPAIQRYIlfKEY 578
Cdd:cd03734     5 SLQHLCRLVINRLV--------TDVDCLPLPRRMADYL--RQY 37
Ank_5 pfam13857
Ankyrin repeats (many copies);
163-217 2.67e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 2.67e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1034654168 163 LIKHNT-SLDQPCVKRWSAMHEAAKQGRKDIVALLLKHGGNVHLRDGFGVTPLGVA 217
Cdd:pfam13857   1 LLEHGPiDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
92-247 5.43e-03

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: 39.79  E-value: 5.43e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168  92 LEIVLDASYKTL--WEFKtcDGETPLTLAVKAGLveNVRtllekgvwpNTKNDKGETPLLIAVKKGSY-DMVstlikhNT 168
Cdd:cd22196    25 LLEYLMRTKKRLtdSEFK--DPETGKTCLLKAML--NLH---------NGQNDTISLLLDIAEKTGNLkEFV------NA 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 169 SLDQPCVKRWSAMHEAAKQGRKDIVALLLKHGGNVHLR------------DG--FGVTPLGVAAEYGHCDVLEHLI---H 231
Cdd:cd22196    86 AYTDSYYKGQTALHIAIERRNMHLVELLVQNGADVHARasgeffkkkkggPGfyFGELPLSLAACTNQLDIVKFLLenpH 165
                         170
                  ....*....|....*.
gi 1034654168 232 KGGDVLALADDGASVL 247
Cdd:cd22196   166 SPADISARDSMGNTVL 181
PHA02730 PHA02730
ankyrin-like protein; Provisional
322-427 5.59e-03

ankyrin-like protein; Provisional


Pssm-ID: 165098 [Multi-domain]  Cd Length: 672  Bit Score: 39.62  E-value: 5.59e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1034654168 322 QCLELLIENGFDVNTLLADHISQsYDDERKTALYFGVSNNDVHCTEVLLAAGADPNLDPLNCLLVAV------RANNYEI 395
Cdd:PHA02730  435 HCYETILIDVFDILSKYMDDIDM-IDNENKTLLYYAVDVNNIQFARRLLEYGASVNTTSRSIINTAIqkssyrRENKTKL 513
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1034654168 396 VRLLLSH---------GANVNCYFMH------------VNDTRFPSVIQYALN 427
Cdd:PHA02730  514 VDLLLSYhptletmidAFNRDIRYLYpepllaciryalILDNDFPSKVKYDIA 566
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
178-207 7.61e-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: 34.19  E-value: 7.61e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 1034654168 178 WSAMHEAAKQ-GRKDIVALLLKHGGNVHLRD 207
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
 
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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