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Conserved domains on  [gi|321117514|ref|NP_001189358|]
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ankyrin repeat and SOCS box protein 2 isoform 1 [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];
165-400 4.84e-49

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 172.83  E-value: 4.84e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 165 IDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHE 244
Cdd:COG0666   47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 245 SVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLL 324
Cdd:COG0666  127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 321117514 325 SQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSR-TRIRRSGVSPLHLAAERNHDEVLEALLSARFDVNTPLA 400
Cdd:COG0666  207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADlNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
 591-635 1.00e-23

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: 94.16  E-value: 1.00e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 321117514 591 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ 635
Cdd:cd03721    1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ 45
Ank_2 pfam12796
Ankyrin repeats (3 copies);
373-469 2.43e-12

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 2.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514  373 LHLAAERNHDEVLEALLSARFDVNtplaperarLYEDRRSSALYFAVVNNNVYATELLLQHgADPNRDVI--SPLLVAIR 450
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNgrTALHYAAR 70

                          90
                  ....*....|....*....
gi 321117514  451 HGCLRTMQLLLDHGANIDA 469
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
109-202 4.19e-12

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 4.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514  109 LIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGCLKVLQRAYPGtidQRTLQEETAVYLATCRGHLDCL 188
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 321117514  189 LSLLQAGAEPDISN 202
Cdd:pfam12796  78 KLLLEKGADINVKD 91
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
165-400 4.84e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 172.83  E-value: 4.84e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 165 IDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHE 244
Cdd:COG0666   47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 245 SVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLL 324
Cdd:COG0666  127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 321117514 325 SQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSR-TRIRRSGVSPLHLAAERNHDEVLEALLSARFDVNTPLA 400
Cdd:COG0666  207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADlNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 198-432 2.18e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 108.98  E-value: 2.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 198 PDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALH-----ESVSRNDLEVMQILVSGGAKVESKNAYGI 272
Cdd:PHA03100  28 NDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGI 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 273 TPLFVAAQ--SGQLEALRFLAKYGADINTQASDNASALYEACKNEHE--EVVEFLLSQGADANKTNK-DGLL-------- 339
Cdd:PHA03100 108 TPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRvNYLLsygvpini 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 340 -------PLHIASKKGNYRIVQMLLPVTSRTRIR-RSGVSPLHLAAERNHDEVLEALLSARFDVNTplaperarlyedRR 411
Cdd:PHA03100 188 kdvygftPLHYAVYNNNPEFVKYLLDLGANPNLVnKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT------------II 255

                        250       260
                 ....*....|....*....|..
gi 321117514 412 SSALYFAVVN-NNVYATELLLQ 432
Cdd:PHA03100 256 ETLLYFKDKDlNTITKIKMLKK 277
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
 591-635 1.00e-23

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: 94.16  E-value: 1.00e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 321117514 591 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ 635
Cdd:cd03721    1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ 45
Ank_2 pfam12796
Ankyrin repeats (3 copies);
209-300 2.42e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 2.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514  209 LYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSgGAKVESKNaYGITPLFVAAQSGQLEALR 288
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 321117514  289 FLAKYGADINTQ 300
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
373-469 2.43e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 2.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514  373 LHLAAERNHDEVLEALLSARFDVNtplaperarLYEDRRSSALYFAVVNNNVYATELLLQHgADPNRDVI--SPLLVAIR 450
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNgrTALHYAAR 70

                          90
                  ....*....|....*....
gi 321117514  451 HGCLRTMQLLLDHGANIDA 469
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
109-202 4.19e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 4.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514  109 LIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGCLKVLQRAYPGtidQRTLQEETAVYLATCRGHLDCL 188
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 321117514  189 LSLLQAGAEPDISN 202
Cdd:pfam12796  78 KLLLEKGADINVKD 91
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 592-630 2.32e-11

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


Pssm-ID: 462192  Cd Length: 39  Bit Score: 58.72  E-value: 2.32e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 321117514  592 PPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLK 630
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 140-357 3.73e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 66.19  E-value: 3.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 140 LPLHEAAYYGQVGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHLDCLLSLLQAGaePDISNKSRETPLYKacerknae 219
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAA--PELVNEPMTSDLYQ-------- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 220 avkilvqhnadtnhrcnrGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLE 285
Cdd:cd22192   89 ------------------GETALHIAVVNQNLNLVRELIARGADVVSPRAtgtffrpgpknliyYGEHPLSFAACVGNEE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 286 ALRFLAKYGADINTQASDNASALY----EACKNEHEEVVEFLLSQGADANK------TNKDGLLPLHIASKKGNYRIVQM 355
Cdd:cd22192  151 IVRLLIEHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQH 230


                 ..
gi 321117514 356 LL 357
Cdd:cd22192  231 LV 232
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
 594-632 2.55e-08

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


Pssm-ID: 198037  Cd Length: 34  Bit Score: 49.71  E-value: 2.55e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 321117514   594 RPLAHLCRLRVRKAIGKyriklLDTLPLPGRLIRYLKYE 632
Cdd:smart00969   1 RSLQHLCRLAIRRSLGG-----IDKLPLPPRLKDYLLYY 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 339-486 1.70e-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: 54.25  E-value: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 339 LPLHIASKKGNYRIVQMLLpVTSRTRIRRSGV---SPLHLAAERNHDEVLEALL-SARFDVNTPLAPErarLYEDRrsSA 414
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLL-KCPSCDLFQRGAlgeTALHVAALYDNLEAAVVLMeAAPELVNEPMTSD---LYQGE--TA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 415 LYFAVVNNNVYATELLLQHGAD------------PNRDVI-----SPLLVAIRHGCLRTMQLLLDHGANIDA-------- 469
Cdd:cd22192   93 LHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIRAqdslgntv 172

                        170
                 ....*....|....*....
gi 321117514 470 --YIATHPTAFPATIMFAM 486
Cdd:cd22192  173 lhILVLQPNKTFACQMYDL 191
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 237-357 4.31e-07

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: 53.16  E-value: 4.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514  237 RGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAKYGADINTQAS 302
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 321117514  303 -----DNASALYEACKNEHEEVV----EFLLSQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 357
Cdd:TIGR00870 207 lgntlLHLLVMENEFKAEYEELScqmyNFALSLLDKLRDSkelevilNHQGLTPLKLAAKEGRIVLFRLKL 277
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 353-503 1.42e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 50.37  E-value: 1.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 353 VQMLLPVTSRTRIRRSGVspLHLAAERNHDEVLEALLSARFDVNTPLAperarLYEDRRSSALYFAVVNNNVYATELLLQ 432
Cdd:PHA02884  19 IIFYIAIKKKNKICIANI--LYSSIKFHYTDIIDAILKLGADPEAPFP-----LSENSKTNPLIYAIDCDNDDAAKLLIR 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 321117514 433 HGADPNR----DVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAFPATIMFamkCLSLLKFLMdlgCDGE 503
Cdd:PHA02884  92 YGADVNRyaeeAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALMI---CNNFLAFMI---CDNE 160
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 270-298 1.63e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 1.63e-04
                           10        20
                   ....*....|....*....|....*....
gi 321117514   270 YGITPLFVAAQSGQLEALRFLAKYGADIN 298
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 443-469 8.17e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 8.17e-03
                           10        20
                   ....*....|....*....|....*..
gi 321117514   443 SPLLVAIRHGCLRTMQLLLDHGANIDA 469
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
165-400 4.84e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 172.83  E-value: 4.84e-49
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 165 IDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHE 244
Cdd:COG0666   47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 245 SVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLL 324
Cdd:COG0666  127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 321117514 325 SQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSR-TRIRRSGVSPLHLAAERNHDEVLEALLSARFDVNTPLA 400
Cdd:COG0666  207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADlNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
106-357 3.84e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.82  E-value: 3.84e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 106 ADPLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHL 185
Cdd:COG0666   21 LALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 186 DCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVE 265
Cdd:COG0666  101 EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 266 SKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIAS 345
Cdd:COG0666  181 ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260

                        250
                 ....*....|..
gi 321117514 346 KKGNYRIVQMLL 357
Cdd:COG0666  261 AAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
165-438 1.03e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 161.28  E-value: 1.03e-44
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 165 IDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHE 244
Cdd:COG0666   14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 245 SVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLL 324
Cdd:COG0666   94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 325 SQGADANKTNKDGLLPLHIASKKGNYRIVQMLL----PVTSRTrirRSGVSPLHLAAERNHDEVLEALLSARFDVNTPLa 400
Cdd:COG0666  174 EAGADVNARDNDGETPLHLAAENGHLEIVKLLLeagaDVNAKD---NDGKTALDLAAENGNLEIVKLLLEAGADLNAKD- 249

                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 321117514 401 perarlyeDRRSSALYFAVVNNNVYATELLLQHGADPN 438
Cdd:COG0666  250 --------KDGLTALLLAAAAGAALIVKLLLLALLLLA 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
106-341 1.24e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.19  E-value: 1.24e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 106 ADPLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGCLKVLQRAyPGTIDQRTLQEETAVYLATCRGHL 185
Cdd:COG0666   55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 186 DCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVE 265
Cdd:COG0666  134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 321117514 266 SKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPL 341
Cdd:COG0666  214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
188-478 3.21e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.04  E-value: 3.21e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 188 LLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESK 267
Cdd:COG0666    4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 268 NAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKK 347
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 348 GNYRIVQMLL----PVTSRTrirRSGVSPLHLAAERNHDEVLEALLSARFDVNTPlaperarlyEDRRSSALYFAVVNNN 423
Cdd:COG0666  164 GNLEIVKLLLeagaDVNARD---NDGETPLHLAAENGHLEIVKLLLEAGADVNAK---------DNDGKTALDLAAENGN 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 321117514 424 VYATELLLQHGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAF 478
Cdd:COG0666  232 LEIVKLLLEAGADLNakdKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
218-477 9.29e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.02  E-value: 9.29e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 218 AEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADI 297
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 298 NTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL----PVTSRTrirRSGVSPL 373
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLeagaDVNAQD---NDGNTPL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 374 HLAAERNHDEVLEALLSARFDVNTPlaperarlyEDRRSSALYFAVVNNNVYATELLLQHGADPN---RDVISPLLVAIR 450
Cdd:COG0666  158 HLAAANGNLEIVKLLLEAGADVNAR---------DNDGETPLHLAAENGHLEIVKLLLEAGADVNakdNDGKTALDLAAE 228

                        250       260
                 ....*....|....*....|....*..
gi 321117514 451 HGCLRTMQLLLDHGANIDAYIATHPTA 477
Cdd:COG0666  229 NGNLEIVKLLLEAGADLNAKDKDGLTA 255
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 198-432 2.18e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 108.98  E-value: 2.18e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 198 PDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALH-----ESVSRNDLEVMQILVSGGAKVESKNAYGI 272
Cdd:PHA03100  28 NDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGI 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 273 TPLFVAAQ--SGQLEALRFLAKYGADINTQASDNASALYEACKNEHE--EVVEFLLSQGADANKTNK-DGLL-------- 339
Cdd:PHA03100 108 TPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRvNYLLsygvpini 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 340 -------PLHIASKKGNYRIVQMLLPVTSRTRIR-RSGVSPLHLAAERNHDEVLEALLSARFDVNTplaperarlyedRR 411
Cdd:PHA03100 188 kdvygftPLHYAVYNNNPEFVKYLLDLGANPNLVnKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT------------II 255

                        250       260
                 ....*....|....*....|..
gi 321117514 412 SSALYFAVVN-NNVYATELLLQ 432
Cdd:PHA03100 256 ETLLYFKDKDlNTITKIKMLKK 277
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
 591-635 1.00e-23

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: 94.16  E-value: 1.00e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 321117514 591 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ 635
Cdd:cd03721    1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ 45
PHA03095 PHA03095
ankyrin-like protein; Provisional
 199-480 1.49e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 104.34  E-value: 1.49e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 199 DISNKSRETPLYK---ACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRN---DLEVMQILVSGGAKVESKNAYGI 272
Cdd:PHA03095   5 ESVDIIMEAALYDyllNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 273 TPLFVAAQSGQ-LEALRFLAKYGADINTQ--ASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHI--ASKK 347
Cdd:PHA03095  85 TPLHLYLYNATtLDVIKLLIKAGADVNAKdkVGRTPLHVYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVllKSRN 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 348 GNYRIVQMLLPVTSRTRIRRS-GVSPLHLAAE--RNHDEVLEALLSARFDV-------NTPLaPERARLYEDRRS----- 412
Cdd:PHA03095 165 ANVELLRLLIDAGADVYAVDDrFRSLLHHHLQsfKPRARIVRELIRAGCDPaatdmlgNTPL-HSMATGSSCKRSlvlpl 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 413 ---------------SALYFAVVNNNVYATELLLQHGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATH 474
Cdd:PHA03095 244 liagisinarnrygqTPLHYAAVFNNPRACRRLIALGADINavsSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATL 323


                 ....*.
gi 321117514 475 PTAFPA 480
Cdd:PHA03095 324 NTASVA 329
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 165-469 1.39e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 102.45  E-value: 1.39e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 165 IDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVqhnaDTNHRCNRGWTALHE 244
Cdd:PHA02876 171 VNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII----DNRSNINKNDLSLLK 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 245 SVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEAL-RFLAKYGADINTQASDNASALYEACKNEHE-EVVEF 322
Cdd:PHA02876 247 AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRT 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 323 LLSQGADANKTNKDGLLPLHIASKKGNYR-IVQMLLPVTSRTRIRR-SGVSPLHLAAERNHDEVLEALLSARFDVNTpla 400
Cdd:PHA02876 327 LIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDyCDKTPIHYAAVRNNVVIINTLLDYGADIEA--- 403

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 321117514 401 perarlYEDRRSSALYFAVVNNNVY-ATELLLQHGAD---PNRDVISPLLVAIRHGC-LRTMQLLLDHGANIDA 469
Cdd:PHA02876 404 ------LSQKIGTALHFALCGTNPYmSVKTLIDRGANvnsKNKDLSTPLHYACKKNCkLDVIEMLLDNGADVNA 471
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 177-357 2.45e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.04  E-value: 2.45e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 177 YLATCRGHLDCLLSLLQAGAEPDISNKSRETPL-----YKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSR--N 249
Cdd:PHA03100  40 YLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksN 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 250 DLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQ--LEALRFLAKYGADIN--------------TQASDN--ASALYEA 311
Cdd:PHA03100 120 SYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINaknrvnyllsygvpINIKDVygFTPLHYA 199

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 321117514 312 CKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 357
Cdd:PHA03100 200 VYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
Ank_2 pfam12796
Ankyrin repeats (3 copies);
209-300 2.42e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.94  E-value: 2.42e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514  209 LYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSgGAKVESKNaYGITPLFVAAQSGQLEALR 288
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 321117514  289 FLAKYGADINTQ 300
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
308-397 5.49e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.78  E-value: 5.49e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514  308 LYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPvTSRTRIRRSGVSPLHLAAERNHDEVLEA 387
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|
gi 321117514  388 LLSARFDVNT 397
Cdd:pfam12796  80 LLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
242-334 4.67e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.09  E-value: 4.67e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514  242 LHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYgADINTQaSDNASALYEACKNEHEEVVE 321
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 321117514  322 FLLSQGADANKTN 334
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
178-268 7.52e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 7.52e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514  178 LATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHnADTNHRCNrGWTALHESVSRNDLEVMQIL 257
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 321117514  258 VSGGAKVESKN 268
Cdd:pfam12796  81 LEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 199-399 9.97e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 89.25  E-value: 9.97e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 199 DISNKSRETPLYKACERKNAEAVKILVQHNADTNHRC----NRGWTALheSVSRNDL---------------------EV 253
Cdd:PHA02874  29 NISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINtkipHPLLTAI--KIGAHDIikllidngvdtsilpipciekDM 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 254 MQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKT 333
Cdd:PHA02874 107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 321117514 334 NKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIR-RSGVSPLHLAAERNHdEVLEALLSARF----DVN--TPL 399
Cdd:PHA02874 187 DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKcKNGFTPLHNAIIHNR-SAIELLINNASindqDIDgsTPL 258
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 179-396 1.50e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 88.51  E-value: 1.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 179 ATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILV 258
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 259 SGGAKVES---KNayGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNK 335
Cdd:PHA02875  89 DLGKFADDvfyKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 321117514 336 DGLLPLHIASKKGNYRIVQMLLPVTSRTRI--RRSGVSPLHLAAERNHDEVLEALLSARFDVN 396
Cdd:PHA02875 167 CGCTPLIIAMAKGDIAICKMLLDSGANIDYfgKNGCVAALCYAIENNKIDIVRLFIKRGADCN 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
275-357 4.01e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 4.01e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514  275 LFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQgADANKTNkDGLLPLHIASKKGNYRIVQ 354
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ...
gi 321117514  355 MLL 357
Cdd:pfam12796  79 LLL 81
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 184-463 4.70e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 87.24  E-value: 4.70e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 184 HLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQhnadTNHRCNRGWT--ALHESVSRNDLEVMQILVSGg 261
Cdd:PHA02878  49 NLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR----SINKCSVFYTlvAIKDAFNNRNVEIFKIILTN- 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 262 akvESKNAYGITPLFVAAQSG----QLEALRFLAKYGADINTQASDN-ASALYEACKNEHEEVVEFLLSQGADANKTNKD 336
Cdd:PHA02878 124 ---RYKNIQTIDLVYIDKKSKddiiEAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 337 GLLPLHIASKKGNYRIVQMLLPVTSRTRIRRS-GVSPLHLAAERNHD-EVLEALLSARFDVNtplaperARLYeDRRSSA 414
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKcGNTPLHISVGYCKDyDILKLLLEHGVDVN-------AKSY-ILGLTA 272

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 321117514 415 LYFAVVNNNVyaTELLLQHGADPNR---DVISPLLVAIR-HGCLRTMQLLLDH 463
Cdd:PHA02878 273 LHSSIKSERK--LKLLLEYGADINSlnsYKLTPLSSAVKqYLCINIGRILISN 323
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 108-298 4.86e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 86.97  E-value: 4.86e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 108 PLIKAIKDGDEEALKTMIKEGK--NLAEPNKEGwlPLHEAAYYGQVGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHL 185
Cdd:PHA02875  38 PIKLAMKFRDSEAIKLLMKHGAipDVKYPDIES--ELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 186 DCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVE 265
Cdd:PHA02875 116 DIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 321117514 266 --SKNAyGITPLFVAAQSGQLEALRFLAKYGADIN 298
Cdd:PHA02875 196 yfGKNG-CVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 108-390 6.04e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 86.56  E-value: 6.04e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 108 PLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAyygQVGCLKVLQRAYPGTIDqrtlqeeTAVYLATCRGHlDC 187
Cdd:PHA02874  38 PLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAI---KIGAHDIIKLLIDNGVD-------TSILPIPCIEK-DM 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 188 LLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESK 267
Cdd:PHA02874 107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 268 NAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKneHEEVVEFLLSQGADANKTNKDGLLPLHIA-SK 346
Cdd:PHA02874 187 DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAiNP 264

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 321117514 347 KGNYRIVQMLLPVTSRTRIR-RSGVSPLHLAAER-NHDEVLEALLS 390
Cdd:PHA02874 265 PCDIDIIDILLYHKADISIKdNKGENPIDTAFKYiNKDPVIKDIIA 310
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 92-347 5.74e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 84.16  E-value: 5.74e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514  92 KYSSSLFKTSQ------LAPADPLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLH---------------------- 143
Cdd:PHA02878  18 KYIEYIDHTENystsasLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHiickepnklgmkemirsinkcs 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 144 ---------EAAYYGQVGCLK-VLQRAYPGTIDQRTLQEETAVYLATCRGHLDCLLslLQAGAEPDISNKSR-ETPLYKA 212
Cdd:PHA02878  98 vfytlvaikDAFNNRNVEIFKiILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLL--LSYGADINMKDRHKgNTALHYA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 213 CERKNAEAVKILVQHNADTN--HRCNRgwTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQS-GQLEALRF 289
Cdd:PHA02878 176 TENKDQRLTELLLSYGANVNipDKTNN--SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKL 253

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 321117514 290 LAKYGADINTQAS-DNASALYEACKNEheEVVEFLLSQGADANKTNKDGLLPLHIASKK 347
Cdd:PHA02878 254 LLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 109-367 4.92e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 81.65  E-value: 4.92e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 109 LIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGCL--KVLQRAypGTIDQRTLQEETAVYLATCRGH-L 185
Cdd:PHA02876 244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvpKLLERG--ADVNAKNIKGETPLYLMAKNGYdT 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 186 DCLLSLLQAGAEPDISNKSRETPLYKACE-RKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKV 264
Cdd:PHA02876 322 ENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 265 ES-KNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHE-EVVEFLLSQGADANKTNKDGLLPLH 342
Cdd:PHA02876 402 EAlSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLL 481

                        250       260
                 ....*....|....*....|....*
gi 321117514 343 IAskKGNYRIVQMLLPVTSRTRIRR 367
Cdd:PHA02876 482 IA--LEYHGIVNILLHYGAELRDSR 504
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 278-475 6.49e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.42  E-value: 6.49e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 278 AAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 357
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 358 PVTSRTR--IRRSGVSPLHLAAERNHDEVLEALLSARFDVNTPlaperarlyEDRRSSALYFAVVNNNVYATELLLQHGA 435
Cdd:PHA02875  89 DLGKFADdvFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP---------NTDKFSPLHLAVMMGDIKGIELLIDHKA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 321117514 436 DPNRDV---ISPLLVAIRHGCLRTMQLLLDHGANIDaYIATHP 475
Cdd:PHA02875 160 CLDIEDccgCTPLIIAMAKGDIAICKMLLDSGANID-YFGKNG 201
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 242-501 1.18e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.41  E-value: 1.18e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 242 LHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNAS--------------- 306
Cdd:PHA02876 149 IKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSvlecavdsknidtik 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 307 --------------ALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNY-RIVQMLLPVTSRTRIRR-SGV 370
Cdd:PHA02876 229 aiidnrsninkndlSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNiKGE 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 371 SPLHLAAERNHD-EVLEALLSARFDVN-------TPL--------------------APERARLYEDRrsSALYFAVVNN 422
Cdd:PHA02876 309 TPLYLMAKNGYDtENIRTLIMLGADVNaadrlyiTPLhqastldrnkdivitllelgANVNARDYCDK--TPIHYAAVRN 386

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 423 NVYATELLLQHGADPnrDVISPLLVAIRHGCL------RTMQLLLDHGANIDA---YIAThptafPATIMFAMKC-LSLL 492
Cdd:PHA02876 387 NVVIINTLLDYGADI--EALSQKIGTALHFALcgtnpyMSVKTLIDRGANVNSknkDLST-----PLHYACKKNCkLDVI 459


                 ....*....
gi 321117514 493 KFLMDLGCD 501
Cdd:PHA02876 460 EMLLDNGAD 468
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 188-336 1.85e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 76.83  E-value: 1.85e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 188 LLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGgAKVESK 267
Cdd:PLN03192 541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-ASISDP 619

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 321117514 268 NAYGiTPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKD 336
Cdd:PLN03192 620 HAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
 591-632 4.80e-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: 66.37  E-value: 4.80e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 321117514 591 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 632
Cdd:cd03716    1 STPRSLQHLCRLAIRRCLGRRRLELIKKLPLPPRLKDYLLYE 42
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
 593-632 9.02e-14

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: 65.57  E-value: 9.02e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 321117514 593 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 632
Cdd:cd03587    2 PRSLQHLCRLAIRRCLGKRRLDLIDKLPLPPRLKDYLLYK 41
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 202-348 4.91e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 68.31  E-value: 4.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 202 NKSRETPLYKACERKNA--EAVKILVQHNADTNHRC-NRGWTALHESVSRN---DLEVMQILVSGGAKVESKNAYGITPL 275
Cdd:PHA02859  48 NDLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTrDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLL 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 321117514 276 --FVAAQSGQLEALRFLAKYGADINTQASDNASALYEACK-NEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKG 348
Cdd:PHA02859 128 hmYMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILfHSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
Ank_2 pfam12796
Ankyrin repeats (3 copies);
373-469 2.43e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 2.43e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514  373 LHLAAERNHDEVLEALLSARFDVNtplaperarLYEDRRSSALYFAVVNNNVYATELLLQHgADPNRDVI--SPLLVAIR 450
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNgrTALHYAAR 70

                          90
                  ....*....|....*....
gi 321117514  451 HGCLRTMQLLLDHGANIDA 469
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 281-475 3.21e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.84  E-value: 3.21e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 281 SGQLEALRFLAKYGAD-INTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPv 359
Cdd:PHA02874  11 SGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 360 tsrtrirrSGVSPLHLAAERNHDEVLEALLSARFDVNTplaperarlyEDRRSSA-LYFAVVNNNVYATELLLQHGADPN 438
Cdd:PHA02874  90 --------NGVDTSILPIPCIEKDMIKTILDCGIDVNI----------KDAELKTfLHYAIKKGDLESIKMLFEYGADVN 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 321117514 439 RDVIS---PLLVAIRHGCLRTMQLLLDHGA--NIDAYIATHP 475
Cdd:PHA02874 152 IEDDNgcyPIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGESP 193
Ank_2 pfam12796
Ankyrin repeats (3 copies);
109-202 4.19e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 4.19e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514  109 LIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGCLKVLQRAYPGtidQRTLQEETAVYLATCRGHLDCL 188
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 321117514  189 LSLLQAGAEPDISN 202
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 174-304 1.03e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.97  E-value: 1.03e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 174 TAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCnrGWTALHESVSRNDLEV 253
Cdd:PLN03192 560 TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKRNDLTA 637

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 321117514 254 MQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDN 304
Cdd:PLN03192 638 MKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDD 688
Ank_4 pfam13637
Ankyrin repeats (many copies);
306-357 1.64e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.60  E-value: 1.64e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 321117514  306 SALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 357
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 592-630 2.32e-11

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


Pssm-ID: 462192  Cd Length: 39  Bit Score: 58.72  E-value: 2.32e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 321117514  592 PPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLK 630
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 140-357 3.73e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 66.19  E-value: 3.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 140 LPLHEAAYYGQVGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHLDCLLSLLQAGaePDISNKSRETPLYKacerknae 219
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAA--PELVNEPMTSDLYQ-------- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 220 avkilvqhnadtnhrcnrGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLE 285
Cdd:cd22192   89 ------------------GETALHIAVVNQNLNLVRELIARGADVVSPRAtgtffrpgpknliyYGEHPLSFAACVGNEE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 286 ALRFLAKYGADINTQASDNASALY----EACKNEHEEVVEFLLSQGADANK------TNKDGLLPLHIASKKGNYRIVQM 355
Cdd:cd22192  151 IVRLLIEHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQH 230


                 ..
gi 321117514 356 LL 357
Cdd:cd22192  231 LV 232
PHA03095 PHA03095
ankyrin-like protein; Provisional
 117-316 8.44e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 64.66  E-value: 8.44e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 117 DEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQV-GCLKVLQRA-----YPGTIDQRTLQeetaVYLATCRGHLDCLLS 190
Cdd:PHA03095  62 VKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAgadvnAKDKVGRTPLH----VYLSGFNINPKVIRL 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 191 LLQAGAEPDISNKSRETPLYKACERKNA--EAVKILVQHNADTNHRCNRGWTALH---------ESVSRNDLE------- 252
Cdd:PHA03095 138 LLRKGADVNALDLYGMTPLAVLLKSRNAnvELLRLLIDAGADVYAVDDRFRSLLHhhlqsfkprARIVRELIRagcdpaa 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 253 ---------------------VMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEA 311
Cdd:PHA03095 218 tdmlgntplhsmatgssckrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297


                 ....*
gi 321117514 312 CKNEH 316
Cdd:PHA03095 298 VRNNN 302
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 272-467 8.69e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.60  E-value: 8.69e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 272 ITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANktnkdgLLPLHIASKKGNYR 351
Cdd:PHA02874  36 TTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTS------ILPIPCIEKDMIKT 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 352 IVQMLLPVTSRTRIRRSGvspLHLAAERNHDEVLEALLSARFDVNtplaperarLYEDRRSSALYFAVVNNNVYATELLL 431
Cdd:PHA02874 110 ILDCGIDVNIKDAELKTF---LHYAIKKGDLESIKMLFEYGADVN---------IEDDNGCYPIHIAIKHNFFDIIKLLL 177

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 321117514 432 QHGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANI 467
Cdd:PHA02874 178 EKGAYANvkdNNGESPLHNAAEYGDYACIKLLIDHGNHI 216
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 308-473 9.91e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.30  E-value: 9.91e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 308 LYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIAS----------------------------------------KK 347
Cdd:PHA03100  39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynltdvkeivkllleyganvnapdnngitpllyaiskKS 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 348 GNYRIVQMLLPVTSRTRIRRS-GVSPLHLAAERNHD--EVLEALLSARFDVNtplAPERARLY----------EDRRSSA 414
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSdGENLLHLYLESNKIdlKILKLLIDKGVDIN---AKNRVNYLlsygvpinikDVYGFTP 195

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 321117514 415 LYFAVVNNNVYATELLLQHGADPN-RDVI--SPLLVAIRHGCLRTMQLLLDHGANIDAYIAT 473
Cdd:PHA03100 196 LHYAVYNNNPEFVKYLLDLGANPNlVNKYgdTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 300-469 2.91e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.98  E-value: 2.91e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 300 QASDNASA-----LYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIRRSGVSpLH 374
Cdd:PHA02878  28 NYSTSASLipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVA-IK 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 375 LAAERNHDEVLEALLSARFDVN--------------TPLAPERARLY-----------EDRRSSALYFAVVNNNVYATEL 429
Cdd:PHA02878 107 DAFNNRNVEIFKIILTNRYKNIqtidlvyidkkskdDIIEAEITKLLlsygadinmkdRHKGNTALHYATENKDQRLTEL 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 321117514 430 LLQHGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDA 469
Cdd:PHA02878 187 LLSYGANVNipdKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
Ank_4 pfam13637
Ankyrin repeats (many copies);
273-324 3.53e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.74  E-value: 3.53e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 321117514  273 TPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLL 324
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 191-375 9.35e-09

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 58.14  E-value: 9.35e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 191 LLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRND--LEVMQILVSGGAKVE-SK 267
Cdd:PHA02946  58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINnSV 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 268 NAYGITPLFVAAQSGQLEALRFLA-KYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASK 346
Cdd:PHA02946 138 DEEGCGPLLACTDPSERVFKKIMSiGFEARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCS 217

                        170       180       190
                 ....*....|....*....|....*....|.
gi 321117514 347 K--GNYRIVQMLLPVTSRTRIRRSGVSPLHL 375
Cdd:PHA02946 218 KtvKNVDIINLLLPSTDVNKQNKFGDSPLTL 248
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 108-292 1.24e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 58.10  E-value: 1.24e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 108 PLIKAIKDGDEEALKTMIK-EGKNLAEPNKEGWLPLHEAAYYGQVGCLKVLQRAYPGTIDQRTLQE----ETAVYLATCR 182
Cdd:cd22192   20 PLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDlyqgETALHIAVVN 99

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 183 GHLDCLLSLLQAGAepDISN---------KSR-------ETPL-YKACErKNAEAVKILVQHNADTNHRCNRGWTALHES 245
Cdd:cd22192  100 QNLNLVRELIARGA--DVVSpratgtffrPGPknliyygEHPLsFAACV-GNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 321117514 246 VSRND----LEVMQILVSGGAKVES------KNAYGITPLFVAAQSGQLEALRFLAK 292
Cdd:cd22192  177 VLQPNktfaCQMYDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
PHA02798 PHA02798
ankyrin-like protein; Provisional
 221-450 2.34e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 56.77  E-value: 2.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 221 VKILVQHNADTNHRCNRGWTALHESVSR---NDLEVMQILVSGGAKVESKNAYGITPLFVAAQSG---QLEALRFLAKYG 294
Cdd:PHA02798  92 VKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKG 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 295 ADINTQASDNA-SALYEACKNEHE----EVVEFLLSQGADANKTNK-------DGLLPLHIASKKGNYRIVQMLLPVTSR 362
Cdd:PHA02798 172 VDINTHNNKEKyDTLHCYFKYNIDridaDILKLFVDNGFIINKENKshkkkfmEYLNSLLYDNKRFKKNILDFIFSYIDI 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 363 TRIRRSGVSPLHLAAERNHDEVLEALLSARFDVN--TPLAperarlyedrrSSALYFAVVNNNVYATELLLQHgaDPNRD 440
Cdd:PHA02798 252 NQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINiiTELG-----------NTCLFTAFENESKFIFNSILNK--KPNKN 318

                        250
                 ....*....|
gi 321117514 441 VISPLLVAIR 450
Cdd:PHA02798 319 TISYTYYKLR 328
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
 594-632 2.55e-08

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


Pssm-ID: 198037  Cd Length: 34  Bit Score: 49.71  E-value: 2.55e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 321117514   594 RPLAHLCRLRVRKAIGKyriklLDTLPLPGRLIRYLKYE 632
Cdd:smart00969   1 RSLQHLCRLAIRRSLGG-----IDKLPLPPRLKDYLLYY 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 279-357 3.00e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 3.00e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 321117514 279 AQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 357
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
SOCS_SSB1_4 cd03718
SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box ...
 593-632 4.53e-08

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


Pssm-ID: 239688  Cd Length: 42  Bit Score: 49.61  E-value: 4.53e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 321117514 593 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 632
Cdd:cd03718    3 PLPLMDLCRRRVRVALGRDRLEEIEQLPLPPSLKNYLLYQ 42
Ank_4 pfam13637
Ankyrin repeats (many copies);
205-258 8.16e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 8.16e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 321117514  205 RETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILV 258
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
107-157 9.09e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 9.09e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 321117514  107 DPLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGCLKVL 157
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
SOCS_ASB1 cd03720
SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a ...
 593-632 9.99e-08

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: 48.57  E-value: 9.99e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 321117514 593 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 632
Cdd:cd03720    3 PRSLLSLCRIAVRRALGKQRLSLICSLPLPDPIKKFLLHE 42
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 205-392 1.07e-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: 55.02  E-value: 1.07e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 205 RETPLYKACERKNAEAVK-ILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAK-----VESKNAYGITPLFVA 278
Cdd:cd22192   17 SESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIA 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 279 AQSGQLEALRFLAKYGADINTQA------SDNASAL---------YEACKNeHEEVVEFLLSQGADANKTNKDGLLPLHI 343
Cdd:cd22192   97 VVNQNLNLVRELIARGADVVSPRatgtffRPGPKNLiyygehplsFAACVG-NEEIVRLLIEHGADIRAQDSLGNTVLHI 175

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 344 ----ASKKGNYRIVQMLL-------PVTSRTRIRRSGVSPLHLAAERNHDEVLEALLSAR 392
Cdd:cd22192  176 lvlqPNKTFACQMYDLILsydkeddLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 108-270 1.32e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.29  E-value: 1.32e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 108 PLIKAI--KDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGcLKVLQraypgtidqrTLQEETAVYLATCRghL 185
Cdd:PHA03100 109 PLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKID-LKILK----------LLIDKGVDINAKNR--V 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 186 DCLLSLlqaGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVE 265
Cdd:PHA03100 176 NYLLSY---GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252


                 ....*
gi 321117514 266 SKNAY 270
Cdd:PHA03100 253 TIIET 257
SOCS_ASB14 cd03730
SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a ...
 591-632 1.34e-07

SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239700  Cd Length: 57  Bit Score: 48.69  E-value: 1.34e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 321117514 591 EPPRPLAHLCRLRVRKAIGKYRIK---LLDTLPLPGRLIRYLKYE 632
Cdd:cd03730    1 TNPRSLKHLCRLKIRACMGRLRLRcpvFMSFLPLPNRLKAYILYK 45
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 339-486 1.70e-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: 54.25  E-value: 1.70e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 339 LPLHIASKKGNYRIVQMLLpVTSRTRIRRSGV---SPLHLAAERNHDEVLEALL-SARFDVNTPLAPErarLYEDRrsSA 414
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLL-KCPSCDLFQRGAlgeTALHVAALYDNLEAAVVLMeAAPELVNEPMTSD---LYQGE--TA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 415 LYFAVVNNNVYATELLLQHGAD------------PNRDVI-----SPLLVAIRHGCLRTMQLLLDHGANIDA-------- 469
Cdd:cd22192   93 LHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIRAqdslgntv 172

                        170
                 ....*....|....*....
gi 321117514 470 --YIATHPTAFPATIMFAM 486
Cdd:cd22192  173 lhILVLQPNKTFACQMYDL 191
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
 593-631 3.03e-07

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


Pssm-ID: 239687  Cd Length: 39  Bit Score: 46.82  E-value: 3.03e-07
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 321117514 593 PRPLAHLCRLRVRKAIGKYRIkllDTLPLPGRLIRYLKY 631
Cdd:cd03717    3 VRSLQHLCRFVIRQCTRRDLI---DQLPLPRRLKDYLKE 38
SOCS_SSB4 cd03743
SOCS (suppressors of cytokine signaling) box of SSB4 (SPRY domain-containing SOCS box ...
 593-632 3.27e-07

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


Pssm-ID: 239712  Cd Length: 42  Bit Score: 46.87  E-value: 3.27e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 321117514 593 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 632
Cdd:cd03743    3 PLPLMDLCRRSARQALGRHRLHHIQSLPLPQTLKNYLQYQ 42
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 237-357 4.31e-07

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: 53.16  E-value: 4.31e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514  237 RGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAKYGADINTQAS 302
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 321117514  303 -----DNASALYEACKNEHEEVV----EFLLSQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 357
Cdd:TIGR00870 207 lgntlLHLLVMENEFKAEYEELScqmyNFALSLLDKLRDSkelevilNHQGLTPLKLAAKEGRIVLFRLKL 277
SOCS_SOCS7 cd03741
SOCS (suppressors of cytokine signaling) box of SOCS7-like proteins. Together with CIS1, the ...
 594-633 6.05e-07

SOCS (suppressors of cytokine signaling) box of SOCS7-like proteins. Together with CIS1, the CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 domain. SOCS7 is important in the functioning of neuronal cells. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239710  Cd Length: 49  Bit Score: 46.63  E-value: 6.05e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 321117514 594 RPLAHLCRLRVRKAIgkyRIKLLDTLPLPGRLIRYLKYEN 633
Cdd:cd03741    4 QSLQHLCRFVIRKLV---RRDHIPALPLPRRLIDYLREKH 40
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 353-503 1.42e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 50.37  E-value: 1.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 353 VQMLLPVTSRTRIRRSGVspLHLAAERNHDEVLEALLSARFDVNTPLAperarLYEDRRSSALYFAVVNNNVYATELLLQ 432
Cdd:PHA02884  19 IIFYIAIKKKNKICIANI--LYSSIKFHYTDIIDAILKLGADPEAPFP-----LSENSKTNPLIYAIDCDNDDAAKLLIR 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 321117514 433 HGADPNR----DVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAFPATIMFamkCLSLLKFLMdlgCDGE 503
Cdd:PHA02884  92 YGADVNRyaeeAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALMI---CNNFLAFMI---CDNE 160
SOCS smart00253
suppressors of cytokine signalling; suppressors of cytokine signalling
 587-631 2.52e-06

suppressors of cytokine signalling; suppressors of cytokine signalling


Pssm-ID: 128549  Cd Length: 43  Bit Score: 44.59  E-value: 2.52e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 321117514   587 KEKAEPPRPLAHLCRLRVRKAIGKYRIKlldTLPLPGRLIRYLKY 631
Cdd:smart00253   1 LPRPSNVPSLQHLCRFTIRRCTRTDQIK---TLPLPPKLKDYLSY 42
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 237-357 3.45e-06

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 50.26  E-value: 3.45e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 237 RGWTALHESVSRNDLEVMQILVSGGAKVESKNA-------------YGITPLFVAAQSGQLEALRFLAKYGADI-NTQAS 302
Cdd:cd21882   72 QGQTALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQPaALEAQ 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 321117514 303 DNAS-----ALYEACKNEHE------EVVEFLLSQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 357
Cdd:cd21882  152 DSLGntvlhALVLQADNTPEnsafvcQMYNLLLSYGAHLDPTqqleeipNHQGLTPLKLAAVEGKIVMFQHIL 224
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 228-357 3.69e-06

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 50.14  E-value: 3.69e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 228 NADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAKY 293
Cdd:cd22194  131 NAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPEIVQLLMEK 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 294 GADI--------NT------QASDNASA-------LYE----ACKNEHEEVVefllsqgadankTNKDGLLPLHIASKKG 348
Cdd:cd22194  211 ESTDitsqdsrgNTvlhalvTVAEDSKTqndfvkrMYDmillKSENKNLETI------------RNNEGLTPLQLAAKMG 278


                 ....*....
gi 321117514 349 NYRIVQMLL 357
Cdd:cd22194  279 KAEILKYIL 287
Ank_5 pfam13857
Ankyrin repeats (many copies);
191-243 4.17e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.26  E-value: 4.17e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 321117514  191 LLQAG-AEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALH 243
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
238-290 5.82e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 5.82e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 321117514  238 GWTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFL 290
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
SOCS_SSB2 cd03719
SOCS (suppressors of cytokine signaling) box of SSB2 (SPRY domain-containing SOCS box proteins) ...
 591-632 7.65e-06

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: 43.09  E-value: 7.65e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 321117514 591 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 632
Cdd:cd03719    1 AEPHSLLHLSRLCVRHALGDTRLGQVSALPLPPAMKRYLLYQ 42
SOCS_SSB1 cd03744
SOCS (suppressors of cytokine signaling) box of SSB1 (SPRY domain-containing SOCS box proteins) ...
 593-632 8.34e-06

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


Pssm-ID: 239713  Cd Length: 42  Bit Score: 43.05  E-value: 8.34e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 321117514 593 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 632
Cdd:cd03744    3 PLPLMDLCRRSVRLALGRERLSEIHTLPLPASLKNYLLYQ 42
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 242-436 9.62e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.71  E-value: 9.62e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 242 LHESVSRNDLEVMQILVSGGAkvESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVE 321
Cdd:PLN03192 498 LQHHKELHDLNVGDLLGDNGG--EHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVL 575

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 322 FLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIRRSGvSPLHLAAERNHDEVLEALLSARFDVNTplap 401
Cdd:PLN03192 576 VLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDS---- 650

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 321117514 402 erarlyEDRR-SSALYFAVVNNNVYATELLLQHGAD 436
Cdd:PLN03192 651 ------EDHQgATALQVAMAEDHVDMVRLLIMNGAD 680
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
 591-632 1.07e-05

SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. Human ASB15 is expressed predominantly in skeletal muscle and participates in the regulation of protein turnover and muscle cell development by stimulating protein synthesis and regulating differentiation of muscle cells. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239701  Cd Length: 56  Bit Score: 43.28  E-value: 1.07e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 321117514 591 EPPRPLAHLCRLRVRKAIGKYRIKLLDT---LPLPGRLIRYLKYE 632
Cdd:cd03731    1 ENPRPLKHLCRLKIRKLMGLQKLQQPSSmkkLPLPPALKRYILYK 45
Ank_4 pfam13637
Ankyrin repeats (many copies);
182-225 1.60e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.65  E-value: 1.60e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 321117514  182 RGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILV 225
Cdd:pfam13637  11 SGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 300-357 1.78e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 47.74  E-value: 1.78e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 300 QASDNASALYEAC--KNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 357
Cdd:PHA02946  33 EPSGNYHILHAYCgiKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLL 92
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 264-396 2.20e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.97  E-value: 2.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 264 VESKNAYGITPLF--VAAQSGQLEALRFLAKYGADINTQASD-NASALYEAC---KNEHEEVVEFLLSQGADANKTNKDG 337
Cdd:PHA02859  44 VNDCNDLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRDnNLSALHHYLsfnKNVEPEILKILIDSGSSITEEDEDG 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 338 LLPLHIASKKGNYRIVQMLLpvtsrtrIRRSGVSPLHLAAERNH-----------DEVLEALLSARFDVN 396
Cdd:PHA02859 124 KNLLHMYMCNFNVRINVIKL-------LIDSGVSFLNKDFDNNNilysyilfhsdKKIFDFLTSLGIDIN 186
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 255-325 2.75e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 2.75e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 321117514 255 QILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLS 325
Cdd:PTZ00322  99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
SOCS_ASB7 cd03726
SOCS (suppressors of cytokine signaling) box of ASB7-like proteins. ASB family members have a ...
 593-632 3.69e-05

SOCS (suppressors of cytokine signaling) box of ASB7-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239696  Cd Length: 45  Bit Score: 41.37  E-value: 3.69e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 321117514 593 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 632
Cdd:cd03726    3 PRTLQDLCRIKIRHCIGLQNLKLLDELPIAKVMKDYLKHK 42
SOCS_ASB13 cd03729
SOCS (suppressors of cytokine signaling) box of ASB13-like proteins. ASB family members have a ...
 593-631 3.93e-05

SOCS (suppressors of cytokine signaling) box of ASB13-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239699  Cd Length: 42  Bit Score: 41.31  E-value: 3.93e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 321117514 593 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKY 631
Cdd:cd03729    3 PLSLQQLCRINLRKALGTRALEKIAKLNIPNRIIDYLSY 41
SOCS_ASB5 cd03724
SOCS (suppressors of cytokine signaling) box of ASB5-like proteins. ASB family members have a ...
 593-631 4.44e-05

SOCS (suppressors of cytokine signaling) box of ASB5-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ASB5 has been implicated in the initiation of arteriogenesis. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239694  Cd Length: 42  Bit Score: 41.02  E-value: 4.44e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 321117514 593 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKY 631
Cdd:cd03724    3 PSSLCQLCRLCIRNYIGRSRLHLIPQLQLPTLLKNFLQY 41
Ank_5 pfam13857
Ankyrin repeats (many copies);
290-344 1.02e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.41  E-value: 1.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 321117514  290 LAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIA 344
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 270-299 1.41e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 1.41e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 321117514  270 YGITPLFVAAQSGQLEALRFLAKYGADINT 299
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank_2 pfam12796
Ankyrin repeats (3 copies);
108-157 1.47e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.87  E-value: 1.47e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 321117514  108 PLIKAIKDGDEEALKTMIKegKNLAEPNKEGWLPLHEAAYYGQVGCLKVL 157
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVKLL 80
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 237-357 1.52e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 44.79  E-value: 1.52e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 237 RGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFL---AKYGADINT 299
Cdd:cd22193   75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKgrffqpkyqgegfyFGELPLSLAACTNQPDIVQYLlenEHQPADIEA 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 321117514 300 QASDNAS---ALYEACKNEHEE------VVEFLLSQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 357
Cdd:cd22193  155 QDSRGNTvlhALVTVADNTKENtkfvtrMYDMILIRGAKLCPTveleeirNNDGLTPLQLAAKMGKIEILKYIL 228
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 243-324 1.63e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 44.73  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 243 HESVSRNDLEVMQILVSGgAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEF 322
Cdd:PHA02989 229 NKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNR 307


                 ..
gi 321117514 323 LL 324
Cdd:PHA02989 308 IL 309
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 270-298 1.63e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.11  E-value: 1.63e-04
                           10        20
                   ....*....|....*....|....*....
gi 321117514   270 YGITPLFVAAQSGQLEALRFLAKYGADIN 298
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 369-396 3.22e-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: 38.34  E-value: 3.22e-04
                           10        20
                   ....*....|....*....|....*...
gi 321117514   369 GVSPLHLAAERNHDEVLEALLSARFDVN 396
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
 593-633 3.45e-04

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: 38.58  E-value: 3.45e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 321117514 593 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYEN 633
Cdd:cd03723    3 PRSLQHLCRCAIRKLLGSRCHKLVPQLSLPTSLKNYLLLEP 43
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 237-357 3.63e-04

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 (TRPV1), a capsaicin (vanilloid) receptor, is the founding member of the vanilloid TRP subfamily (TRPV). In humans, it is expressed in the brain, kidney, pancreas, testis, uterus, spleen, stomach, small intestine, lung and liver. TRPV1 has been implicated to have function in thermo-sensation (heat), autonomic thermoregulation, nociception, food intake regulation, and multiple functions in the gastrointestinal (GI) tract. The receptor has also been involved in growth cone guidance, long-term depression, endocannabinoid signaling and osmosensing in the central nervous system. TRPV1 is up regulated in several human pathological conditions including vulvodynia, GI inflammation, Crohn's disease and ulcerative colitis. TRPV1 knock-out mice exhibit impaired sensation to thermal-mechanical acute pain. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 43.64  E-value: 3.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 237 RGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAK---YGADINT 299
Cdd:cd22196   93 KGQTALHIAIERRNMHLVELLVQNGADVHARASgeffkkkkggpgfyFGELPLSLAACTNQLDIVKFLLEnphSPADISA 172

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 321117514 300 QASDNAS---ALYEACKNEHE------EVVEFLLSQGADANK-------TNKDGLLPLHIASKKGNYRIVQMLL 357
Cdd:cd22196  173 RDSMGNTvlhALVEVADNTPEntkfvtKMYNEILILGAKIRPllkleeiTNKKGLTPLKLAAKTGKIGIFAYIL 246
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 264-438 9.45e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.38  E-value: 9.45e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514  264 VESKNAYGITPLFVAAQSGQLEALRFLAKYgadINTQASDNASALYEACKNEHEeVVEFLLSQGADANKtnKDGLLPLHI 343
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISLEYVD-AVEAILLHLLAAFR--KSGPLELAN 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514  344 ASKKGNYrivqmllpvtsrTRirrsGVSPLHLAAERNHDEVLEALLSARFDVNTP-------LAPERARLYEDRRSSALY 416
Cdd:TIGR00870 119 DQYTSEF------------TP----GITALHLAAHRQNYEIVKLLLERGASVPARacgdffvKSQGVDSFYHGESPLNAA 182

                         170       180
                  ....*....|....*....|..
gi 321117514  417 FAVVNNNVYAteLLLQHGADPN 438
Cdd:TIGR00870 183 ACLGSPSIVA--LLSEDPADIL 202
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 185-275 9.64e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 42.21  E-value: 9.64e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 185 LDCLLSLLQAGAEPDISNKSRETPLYKACERKN--AEAVKILVQHNADTNHRCNRGWTALHESVSR------------ND 250
Cdd:PHA02716 297 ISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMlsvvnildpetdND 376

                         90       100
                 ....*....|....*....|....*..
gi 321117514 251 --LEVMQILVSGGAKVESKNAYGITPL 275
Cdd:PHA02716 377 irLDVIQCLISLGADITAVNCLGYTPL 403
Ank_4 pfam13637
Ankyrin repeats (many copies);
411-461 1.26e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 37.25  E-value: 1.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 321117514  411 RSSALYFAVVNNNVYATELLLQHGADPNR---DVISPLLVAIRHGCLRTMQLLL 461
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAvdgNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
224-275 1.40e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 1.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 321117514  224 LVQH-NADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPL 275
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
323-376 1.61e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 1.61e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 321117514  323 LLSQG-ADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIR-RSGVSPLHLA 376
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKdEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 410-501 1.71e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.19  E-value: 1.71e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 410 RRSSALYFAVVNNNVYATELLLQHGADPNRDV-----ISPLLVAIRHGC---LRTMQLLLDHGANIDAYIATHPTAFPAT 481
Cdd:PHA03100  34 KPVLPLYLAKEARNIDVVKILLDNGADINSSTknnstPLHYLSNIKYNLtdvKEIVKLLLEYGANVNAPDNNGITPLLYA 113

                         90       100
                 ....*....|....*....|
gi 321117514 482 IMFAMKCLSLLKFLMDLGCD 501
Cdd:PHA03100 114 ISKKSNSYSIVEYLLDNGAN 133
Ank_4 pfam13637
Ankyrin repeats (many copies);
369-431 1.83e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 1.83e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 321117514  369 GVSPLHLAAERNHDEVLEALLSARFDVNtplaperARLYEDRrsSALYFAVVNNNVYATELLL 431
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADIN-------AVDGNGE--TALHFAASNGNVEVLKLLL 54
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 237-357 2.10e-03

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 40.99  E-value: 2.10e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 237 RGWTALHESVSRNDLEVMQILVSGGAKVESKNA-------------YGITPLFVAAQSGQLEALRFLAKYGADI-NTQAS 302
Cdd:cd22197   93 RGHSALHIAIEKRSLQCVKLLVENGADVHARACgrffqkkqgtcfyFGELPLSLAACTKQWDVVNYLLENPHQPaSLQAQ 172

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 321117514 303 DNAS-----ALYEACKN--EHEEVV----EFLLSQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 357
Cdd:cd22197  173 DSLGntvlhALVMIADNspENSALVikmyDGLLQAGARLCPTvqleeisNHEGLTPLKLAAKEGKIEIFRHIL 245
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 207-232 2.14e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.03  E-value: 2.14e-03
                           10        20
                   ....*....|....*....|....*.
gi 321117514   207 TPLYKACERKNAEAVKILVQHNADTN 232
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 186-303 2.29e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.35  E-value: 2.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 186 DCLLSLLQAGAEPDI----SNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNrgwtalhesvsrndlevmqilvsgg 261
Cdd:PHA02884  47 DIIDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAE------------------------- 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 321117514 262 akvESKnaygITPLFVAAQSGQLEALRFLAKYGADINTQASD 303
Cdd:PHA02884 102 ---EAK----ITPLYISVLHGCLKCLEILLSYGADINIQTND 136
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 142-290 3.05e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 40.63  E-value: 3.05e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 142 LHEAAYY---GQVGCLKVLQRAYPGTIDQRTL----------QEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSR--- 205
Cdd:cd21882   30 LHKAALNlndGVNEAIMLLLEAAPDSGNPKELvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSARATGRffr 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 206 ----------ETPLYKACERKNAEAVKILVQHNADTNHRCNR---GWTALHESVSRND---------LEVMQILVSGGAK 263
Cdd:cd21882  110 kspgnlfyfgELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHALVLQADntpensafvCQMYNLLLSYGAH 189

                        170       180       190
                 ....*....|....*....|....*....|....
gi 321117514 264 V-------ESKNAYGITPLFVAAQSGQLEALRFL 290
Cdd:cd21882  190 LdptqqleEIPNHQGLTPLKLAAVEGKIVMFQHI 223
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 285-356 3.21e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 38.70  E-value: 3.21e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 321117514 285 EALRFLAKYGADINTQASDNA-SALYEACKNEHEEVVEFLLSQ-GADANKTNKDGLLPLHIASKKGNYRIVQML 356
Cdd:PHA02736  72 EKLKLLMEWGADINGKERVFGnTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNIL 145
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 171-290 3.83e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are thermo-sensing channels that function directly in temperature-sensing and nociception; they share substantial structural and functional properties. Transient Receptor Potential (TRP) ion channels activated by temperature (thermo TRPs) are important molecular players in acute, inflammatory, and chronic pain states. So far, 11 TRP channels in mammalian cells have been identified as thermosensitive TRP (thermo-TRP) channels. TRPV1-4 channels are activated by different heat temperatures, for example, TRPV1 and TRPV2 are activated by high temperatures (>43C and >55C, respectively). TRPV1-4 belong to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.16  E-value: 3.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 171 QEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSR--------------ETPLYKACERKNAEAVKILVQH---NADTNH 233
Cdd:cd22193   75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRffqpkyqgegfyfgELPLSLAACTNQPDIVQYLLENehqPADIEA 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 321117514 234 RCNRGWTALH-------ESVSRNDL--EVMQILVSGGAKV-------ESKNAYGITPLFVAAQSGQLEALRFL 290
Cdd:cd22193  155 QDSRGNTVLHalvtvadNTKENTKFvtRMYDMILIRGAKLcptveleEIRNNDGLTPLQLAAKMGKIEILKYI 227
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 369-396 4.55e-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: 34.96  E-value: 4.55e-03
                          10        20
                  ....*....|....*....|....*....
gi 321117514  369 GVSPLHLAAER-NHDEVLEALLSARFDVN 396
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
SOCS_WSB_SWIP cd03733
SOCS (suppressors of cytokine signaling) box of WSB/SWiP-like proteins. This subfamily ...
 596-631 5.55e-03

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


Pssm-ID: 239702  Cd Length: 39  Bit Score: 35.09  E-value: 5.55e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 321117514 596 LAHLCRLRVRKAIGKYRIKlldTLPLPGRLIRYLKY 631
Cdd:cd03733    6 LQHLCRMALRRVMTTQQVL---ALPIPKKMKEFLTY 38
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 303-335 5.82e-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: 34.96  E-value: 5.82e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 321117514  303 DNASALYEAC-KNEHEEVVEFLLSQGADANKTNK 335
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 108-227 6.03e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.48  E-value: 6.03e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 108 PLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEA-AYYGQVGCLKVLQRAYPGTIDQRTLQEETAVYLATcrGHLD 186
Cdd:PHA02878 204 PLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSI--KSER 281

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 321117514 187 CLLSLLQAGAEPDISNKSRETPLYKAC-ERKNAEAVKILVQH 227
Cdd:PHA02878 282 KLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRILISN 323
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 303-332 6.64e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 6.64e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 321117514   303 DNASALYEACKNEHEEVVEFLLSQGADANK 332
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 152-290 6.73e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a temperature-sensitive Transient Receptor Potential (TRP) ion channel that is activated by warm temperatures, synthetic small-molecule chemicals, and natural compounds from plants. TRPV3 function is regulated by physiological factors such as extracellular divalent cations and acidic pH, intracellular adenosine triphosphate, membrane voltage, and arachidonic acid. It is expressed in both neuronal and non-neuronal tissues including epidermal keratinocytes, epithelial cells in the gut, endothelial cells in blood vessels, and neurons in dorsal root ganglia and CNS. TRPV3 null mice have abnormal hair morphogenesis and compromised skin barrier function. It may play roles in inflammatory skin disorders, such as itch and pain sensation. TRPV3 is also expressed by many neuronal and non-neuronal tissues, showing that TRPV3 might play roles in other unknown cellular and physiological functions. TRPV3 belongs to the vanilloid TRP subfamily (TRPV), named after the founding member vanilloid receptor 1 (TRPV1). The structure of TRPV shows the typical topology features of all TRP ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains.


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 39.74  E-value: 6.73e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 152 GCLKVL------QRAYPGtidqrtlqeETAVYLATCRGHLDCLLSLLQAGAEPDISNKSR--------------ETPLYK 211
Cdd:cd22194  124 GILDRFinaeytEEAYEG---------QTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLAL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 212 ACERKNAEAVKILVQhNADTNHRC--NRGWTALH-------ESVSRNDLEV----MQILVSGGAKVES-KNAYGITPLFV 277
Cdd:cd22194  195 AACTNQPEIVQLLME-KESTDITSqdSRGNTVLHalvtvaeDSKTQNDFVKrmydMILLKSENKNLETiRNNEGLTPLQL 273

                        170
                 ....*....|...
gi 321117514 278 AAQSGQLEALRFL 290
Cdd:cd22194  274 AAKMGKAEILKYI 286
SOCS_ASB3 cd03722
SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a ...
 596-633 7.42e-03

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: 35.15  E-value: 7.42e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 321117514 596 LAHLCRLRVRKAIGKYRIK---LLDTLPLPGRLIRYLKYEN 633
Cdd:cd03722    6 LTHLCRLEIRSSLKSERLRsdsFICQLPLPRSLQDYLLYSD 46
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 443-469 8.17e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 8.17e-03
                           10        20
                   ....*....|....*....|....*..
gi 321117514   443 SPLLVAIRHGCLRTMQLLLDHGANIDA 469
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 369-397 9.20e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.16  E-value: 9.20e-03
                          10        20
                  ....*....|....*....|....*....
gi 321117514  369 GVSPLHLAAERNHDEVLEALLSARFDVNT 397
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 217-293 9.24e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.11  E-value: 9.24e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 321117514 217 NAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKY 293
Cdd:PTZ00322  94 DAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 266-346 9.47e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 38.43  E-value: 9.47e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 321117514 266 SKNAYgITPLFVAAQSGQLEALRFLAKYGADINTQASD-NASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIA 344
Cdd:PHA02884  66 SENSK-TNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEaKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELA 144


                 ..
gi 321117514 345 SK 346
Cdd:PHA02884 145 LM 146
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 237-265 9.84e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 9.84e-03
                           10        20
                   ....*....|....*....|....*....
gi 321117514   237 RGWTALHESVSRNDLEVMQILVSGGAKVE 265
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
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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