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Conserved domains on  [gi|18252778|ref|NP_057234|]
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ankyrin repeat and SOCS box protein 2 isoform 2 [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];
117-352 6.69e-49

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.68  E-value: 6.69e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 117 IDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHE 196
Cdd:COG0666  47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 197 SVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLL 276
Cdd:COG0666 127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18252778 277 SQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIR-RSGVSPLHLAAERNHDEVLEALLSARFDVNTPLA 352
Cdd:COG0666 207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKdKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
 543-587 1.73e-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: 93.39  E-value: 1.73e-23
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 18252778 543 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ 587
Cdd:cd03721   1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ 45
Ank_2 pfam12796
Ankyrin repeats (3 copies);
325-421 3.53e-12

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 3.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778   325 LHLAAERNHDEVLEALLSARFDVNtplaperarLYEDRRSSALYFAVVNNNVYATELLLQHgADPNRDVI--SPLLVAIR 402
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNgrTALHYAAR 70

                          90
                  ....*....|....*....
gi 18252778   403 HGCLRTMQLLLDHGANIDA 421
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
61-154 5.42e-12

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 5.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778    61 LIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGCLKVLQRAYPGtidQRTLQEETAVYLATCRGHLDCL 140
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 18252778   141 LSLLQAGAEPDISN 154
Cdd:pfam12796  78 KLLLEKGADINVKD 91
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
117-352 6.69e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.68  E-value: 6.69e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 117 IDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHE 196
Cdd:COG0666  47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 197 SVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLL 276
Cdd:COG0666 127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18252778 277 SQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIR-RSGVSPLHLAAERNHDEVLEALLSARFDVNTPLA 352
Cdd:COG0666 207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKdKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 150-384 1.76e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 108.98  E-value: 1.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  150 PDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALH-----ESVSRNDLEVMQILVSGGAKVESKNAYGI 224
Cdd:PHA03100  28 NDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGI 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  225 TPLFVAAQ--SGQLEALRFLAKYGADINTQASDNASALYEACKNEHE--EVVEFLLSQGADANKTNK-DGLL-------- 291
Cdd:PHA03100 108 TPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRvNYLLsygvpini 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  292 -------PLHIASKKGNYRIVQMLLPVTSRTRIR-RSGVSPLHLAAERNHDEVLEALLSARFDVNTplaperarlyedRR 363
Cdd:PHA03100 188 kdvygftPLHYAVYNNNPEFVKYLLDLGANPNLVnKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT------------II 255

                        250       260
                 ....*....|....*....|..
gi 18252778  364 SSALYFAVVN-NNVYATELLLQ 384
Cdd:PHA03100 256 ETLLYFKDKDlNTITKIKMLKK 277
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
 543-587 1.73e-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: 93.39  E-value: 1.73e-23
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 18252778 543 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ 587
Cdd:cd03721   1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ 45
Ank_2 pfam12796
Ankyrin repeats (3 copies);
161-252 3.54e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 3.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778   161 LYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSgGAKVESKNaYGITPLFVAAQSGQLEALR 240
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 18252778   241 FLAKYGADINTQ 252
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
325-421 3.53e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 3.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778   325 LHLAAERNHDEVLEALLSARFDVNtplaperarLYEDRRSSALYFAVVNNNVYATELLLQHgADPNRDVI--SPLLVAIR 402
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNgrTALHYAAR 70

                          90
                  ....*....|....*....
gi 18252778   403 HGCLRTMQLLLDHGANIDA 421
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
61-154 5.42e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 5.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778    61 LIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGCLKVLQRAYPGtidQRTLQEETAVYLATCRGHLDCL 140
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 18252778   141 LSLLQAGAEPDISN 154
Cdd:pfam12796  78 KLLLEKGADINVKD 91
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 544-582 3.23e-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: 58.33  E-value: 3.23e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 18252778   544 PPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLK 582
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 92-309 3.25e-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: 3.25e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  92 LPLHEAAYYGQVGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHLDCLLSLLQAGaePDISNKSRETPLYKacerknae 171
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAA--PELVNEPMTSDLYQ-------- 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 172 avkilvqhnadtnhrcnrGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLE 237
Cdd:cd22192  89 ------------------GETALHIAVVNQNLNLVRELIARGADVVSPRAtgtffrpgpknliyYGEHPLSFAACVGNEE 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 238 ALRFLAKYGADINTQASDNASALY----EACKNEHEEVVEFLLSQGADANK------TNKDGLLPLHIASKKGNYRIVQM 307
Cdd:cd22192 151 IVRLLIEHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQH 230


                ..
gi 18252778 308 LL 309
Cdd:cd22192 231 LV 232
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
 546-584 3.39e-08

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


Pssm-ID: 198037  Cd Length: 34  Bit Score: 49.33  E-value: 3.39e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 18252778    546 RPLAHLCRLRVRKAIGKyriklLDTLPLPGRLIRYLKYE 584
Cdd:smart00969   1 RSLQHLCRLAIRRSLGG-----IDKLPLPPRLKDYLLYY 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 291-438 1.51e-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: 1.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 291 LPLHIASKKGNYRIVQMLLpVTSRTRIRRSGV---SPLHLAAERNHDEVLEALL-SARFDVNTPLAPErarLYEDRrsSA 366
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLL-KCPSCDLFQRGAlgeTALHVAALYDNLEAAVVLMeAAPELVNEPMTSD---LYQGE--TA 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 367 LYFAVVNNNVYATELLLQHGAD------------PNRDVI-----SPLLVAIRHGCLRTMQLLLDHGANIDA-------- 421
Cdd:cd22192  93 LHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIRAqdslgntv 172

                       170
                ....*....|....*....
gi 18252778 422 --YIATHPTAFPATIMFAM 438
Cdd:cd22192 173 lhILVLQPNKTFACQMYDL 191
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 189-309 3.83e-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: 3.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778   189 RGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAKYGADINTQAS 254
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18252778   255 -----DNASALYEACKNEHEEVV----EFLLSQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 309
Cdd:TIGR00870 207 lgntlLHLLVMENEFKAEYEELScqmyNFALSLLDKLRDSkelevilNHQGLTPLKLAAKEGRIVLFRLKL 277
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 305-455 1.28e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 50.37  E-value: 1.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  305 VQMLLPVTSRTRIRRSGVspLHLAAERNHDEVLEALLSARFDVNTPLAperarLYEDRRSSALYFAVVNNNVYATELLLQ 384
Cdd:PHA02884  19 IIFYIAIKKKNKICIANI--LYSSIKFHYTDIIDAILKLGADPEAPFP-----LSENSKTNPLIYAIDCDNDDAAKLLIR 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18252778  385 HGADPNR----DVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAFPATIMFamkCLSLLKFLMdlgCDGE 455
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 ...
 222-250 2.09e-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: 38.72  E-value: 2.09e-04
                           10        20
                   ....*....|....*....|....*....
gi 18252778    222 YGITPLFVAAQSGQLEALRFLAKYGADIN 250
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
117-352 6.69e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.68  E-value: 6.69e-49
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 117 IDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHE 196
Cdd:COG0666  47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 197 SVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLL 276
Cdd:COG0666 127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18252778 277 SQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIR-RSGVSPLHLAAERNHDEVLEALLSARFDVNTPLA 352
Cdd:COG0666 207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKdKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
58-309 5.17e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 166.67  E-value: 5.17e-47
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  58 ADPLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHL 137
Cdd:COG0666  21 LALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDL 100

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 138 DCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVE 217
Cdd:COG0666 101 EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 218 SKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIAS 297
Cdd:COG0666 181 ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260

                       250
                ....*....|..
gi 18252778 298 KKGNYRIVQMLL 309
Cdd:COG0666 261 AAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
117-390 1.66e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 159.73  E-value: 1.66e-44
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 117 IDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHE 196
Cdd:COG0666  14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHA 93

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 197 SVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLL 276
Cdd:COG0666  94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 277 SQGADANKTNKDGLLPLHIASKKGNYRIVQMLL----PVTSRTrirRSGVSPLHLAAERNHDEVLEALLSARFDVNTPLa 352
Cdd:COG0666 174 EAGADVNARDNDGETPLHLAAENGHLEIVKLLLeagaDVNAKD---NDGKTALDLAAENGNLEIVKLLLEAGADLNAKD- 249

                       250       260       270
                ....*....|....*....|....*....|....*...
gi 18252778 353 perarlyeDRRSSALYFAVVNNNVYATELLLQHGADPN 390
Cdd:COG0666 250 --------KDGLTALLLAAAAGAALIVKLLLLALLLLA 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
58-293 1.76e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 157.04  E-value: 1.76e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  58 ADPLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGCLKVLQRAyPGTIDQRTLQEETAVYLATCRGHL 137
Cdd:COG0666  55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNL 133

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 138 DCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVE 217
Cdd:COG0666 134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18252778 218 SKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPL 293
Cdd:COG0666 214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
140-430 4.97e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 155.88  E-value: 4.97e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 140 LLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESK 219
Cdd:COG0666   4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 220 NAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKK 299
Cdd:COG0666  84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 300 GNYRIVQMLL----PVTSRTrirRSGVSPLHLAAERNHDEVLEALLSARFDVNTPlaperarlyEDRRSSALYFAVVNNN 375
Cdd:COG0666 164 GNLEIVKLLLeagaDVNARD---NDGETPLHLAAENGHLEIVKLLLEAGADVNAK---------DNDGKTALDLAAENGN 231

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|....*...
gi 18252778 376 VYATELLLQHGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAF 430
Cdd:COG0666 232 LEIVKLLLEAGADLNakdKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
170-429 1.43e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 140.86  E-value: 1.43e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 170 AEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADI 249
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 250 NTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL----PVTSRTrirRSGVSPL 325
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLeagaDVNAQD---NDGNTPL 157

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 326 HLAAERNHDEVLEALLSARFDVNTPlaperarlyEDRRSSALYFAVVNNNVYATELLLQHGADPN---RDVISPLLVAIR 402
Cdd:COG0666 158 HLAAANGNLEIVKLLLEAGADVNAR---------DNDGETPLHLAAENGHLEIVKLLLEAGADVNakdNDGKTALDLAAE 228

                       250       260
                ....*....|....*....|....*..
gi 18252778 403 HGCLRTMQLLLDHGANIDAYIATHPTA 429
Cdd:COG0666 229 NGNLEIVKLLLEAGADLNAKDKDGLTA 255
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 150-384 1.76e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 108.98  E-value: 1.76e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  150 PDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALH-----ESVSRNDLEVMQILVSGGAKVESKNAYGI 224
Cdd:PHA03100  28 NDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGI 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  225 TPLFVAAQ--SGQLEALRFLAKYGADINTQASDNASALYEACKNEHE--EVVEFLLSQGADANKTNK-DGLL-------- 291
Cdd:PHA03100 108 TPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRvNYLLsygvpini 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  292 -------PLHIASKKGNYRIVQMLLPVTSRTRIR-RSGVSPLHLAAERNHDEVLEALLSARFDVNTplaperarlyedRR 363
Cdd:PHA03100 188 kdvygftPLHYAVYNNNPEFVKYLLDLGANPNLVnKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT------------II 255

                        250       260
                 ....*....|....*....|..
gi 18252778  364 SSALYFAVVN-NNVYATELLLQ 384
Cdd:PHA03100 256 ETLLYFKDKDlNTITKIKMLKK 277
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
 543-587 1.73e-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: 93.39  E-value: 1.73e-23
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 18252778 543 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ 587
Cdd:cd03721   1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ 45
PHA03095 PHA03095
ankyrin-like protein; Provisional
 151-432 3.63e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 102.80  E-value: 3.63e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  151 DISNKSRETPLYK---ACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRN---DLEVMQILVSGGAKVESKNAYGI 224
Cdd:PHA03095   5 ESVDIIMEAALYDyllNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  225 TPLFVAAQSGQ-LEALRFLAKYGADINTQ--ASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHI--ASKK 299
Cdd:PHA03095  85 TPLHLYLYNATtLDVIKLLIKAGADVNAKdkVGRTPLHVYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVllKSRN 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  300 GNYRIVQMLLPVTSRTRIRRS-GVSPLHLAAE--RNHDEVLEALLSARFDV-------NTPLaPERARLYEDRRS----- 364
Cdd:PHA03095 165 ANVELLRLLIDAGADVYAVDDrFRSLLHHHLQsfKPRARIVRELIRAGCDPaatdmlgNTPL-HSMATGSSCKRSlvlpl 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  365 ---------------SALYFAVVNNNVYATELLLQHGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATH 426
Cdd:PHA03095 244 liagisinarnrygqTPLHYAAVFNNPRACRRLIALGADINavsSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATL 323


                 ....*.
gi 18252778  427 PTAFPA 432
Cdd:PHA03095 324 NTASVA 329
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 117-421 1.09e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 102.45  E-value: 1.09e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  117 IDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVqhnaDTNHRCNRGWTALHE 196
Cdd:PHA02876 171 VNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII----DNRSNINKNDLSLLK 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  197 SVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEAL-RFLAKYGADINTQASDNASALYEACKNEHE-EVVEF 274
Cdd:PHA02876 247 AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRT 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  275 LLSQGADANKTNKDGLLPLHIASKKGNYR-IVQMLLPVTSRTRIRR-SGVSPLHLAAERNHDEVLEALLSARFDVNTpla 352
Cdd:PHA02876 327 LIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDyCDKTPIHYAAVRNNVVIINTLLDYGADIEA--- 403

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18252778  353 perarlYEDRRSSALYFAVVNNNVY-ATELLLQHGAD---PNRDVISPLLVAIRHGC-LRTMQLLLDHGANIDA 421
Cdd:PHA02876 404 ------LSQKIGTALHFALCGTNPYmSVKTLIDRGANvnsKNKDLSTPLHYACKKNCkLDVIEMLLDNGADVNA 471
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 129-309 2.07e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.04  E-value: 2.07e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  129 YLATCRGHLDCLLSLLQAGAEPDISNKSRETPL-----YKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSR--N 201
Cdd:PHA03100  40 YLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksN 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  202 DLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQ--LEALRFLAKYGADIN--------------TQASDN--ASALYEA 263
Cdd:PHA03100 120 SYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINaknrvnyllsygvpINIKDVygFTPLHYA 199

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 18252778  264 CKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 309
Cdd:PHA03100 200 VYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
Ank_2 pfam12796
Ankyrin repeats (3 copies);
161-252 3.54e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 3.54e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778   161 LYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSgGAKVESKNaYGITPLFVAAQSGQLEALR 240
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 18252778   241 FLAKYGADINTQ 252
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
260-349 7.87e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.40  E-value: 7.87e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778   260 LYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPvTSRTRIRRSGVSPLHLAAERNHDEVLEA 339
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|
gi 18252778   340 LLSARFDVNT 349
Cdd:pfam12796  80 LLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
194-286 6.58e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.70  E-value: 6.58e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778   194 LHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYgADINTQaSDNASALYEACKNEHEEVVE 273
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 18252778   274 FLLSQGADANKTN 286
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 151-351 8.53e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 89.25  E-value: 8.53e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  151 DISNKSRETPLYKACERKNAEAVKILVQHNADTNHRC----NRGWTALheSVSRNDL---------------------EV 205
Cdd:PHA02874  29 NISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINtkipHPLLTAI--KIGAHDIikllidngvdtsilpipciekDM 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  206 MQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKT 285
Cdd:PHA02874 107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18252778  286 NKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIR-RSGVSPLHLAAERNHdEVLEALLSARF----DVN--TPL 351
Cdd:PHA02874 187 DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKcKNGFTPLHNAIIHNR-SAIELLINNASindqDIDgsTPL 258
Ank_2 pfam12796
Ankyrin repeats (3 copies);
130-220 1.11e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.93  E-value: 1.11e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778   130 LATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHnADTNHRCNrGWTALHESVSRNDLEVMQIL 209
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 18252778   210 VSGGAKVESKN 220
Cdd:pfam12796  81 LEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 131-348 1.29e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 88.51  E-value: 1.29e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  131 ATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILV 210
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  211 SGGAKVES---KNayGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNK 287
Cdd:PHA02875  89 DLGKFADDvfyKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18252778  288 DGLLPLHIASKKGNYRIVQMLLPVTSRTRI--RRSGVSPLHLAAERNHDEVLEALLSARFDVN 348
Cdd:PHA02875 167 CGCTPLIIAMAKGDIAICKMLLDSGANIDYfgKNGCVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 60-250 4.19e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 86.97  E-value: 4.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778   60 PLIKAIKDGDEEALKTMIKEGK--NLAEPNKEGwlPLHEAAYYGQVGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHL 137
Cdd:PHA02875  38 PIKLAMKFRDSEAIKLLMKHGAipDVKYPDIES--ELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  138 DCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVE 217
Cdd:PHA02875 116 DIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 18252778  218 --SKNAyGITPLFVAAQSGQLEALRFLAKYGADIN 250
Cdd:PHA02875 196 yfGKNG-CVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 60-342 5.19e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 86.56  E-value: 5.19e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778   60 PLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAyygQVGCLKVLQRAYPGTIDqrtlqeeTAVYLATCRGHlDC 139
Cdd:PHA02874  38 PLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAI---KIGAHDIIKLLIDNGVD-------TSILPIPCIEK-DM 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  140 LLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESK 219
Cdd:PHA02874 107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  220 NAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKneHEEVVEFLLSQGADANKTNKDGLLPLHIA-SK 298
Cdd:PHA02874 187 DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAiNP 264

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 18252778  299 KGNYRIVQMLLPVTSRTRIR-RSGVSPLHLAAER-NHDEVLEALLS 342
Cdd:PHA02874 265 PCDIDIIDILLYHKADISIKdNKGENPIDTAFKYiNKDPVIKDIIA 310
Ank_2 pfam12796
Ankyrin repeats (3 copies);
227-309 5.55e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 5.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778   227 LFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQgADANKTNkDGLLPLHIASKKGNYRIVQ 306
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ...
gi 18252778   307 MLL 309
Cdd:pfam12796  79 LLL 81
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 136-415 6.65e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 86.86  E-value: 6.65e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  136 HLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQhnadTNHRCNRGWT--ALHESVSRNDLEVMQILVSGg 213
Cdd:PHA02878  49 NLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR----SINKCSVFYTlvAIKDAFNNRNVEIFKIILTN- 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  214 akvESKNAYGITPLFVAAQSG----QLEALRFLAKYGADINTQASDN-ASALYEACKNEHEEVVEFLLSQGADANKTNKD 288
Cdd:PHA02878 124 ---RYKNIQTIDLVYIDKKSKddiiEAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  289 GLLPLHIASKKGNYRIVQMLLPVTSRTRIRRS-GVSPLHLAAERNHD-EVLEALLSARFDVNtplaperARLYeDRRSSA 366
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKcGNTPLHISVGYCKDyDILKLLLEHGVDVN-------AKSY-ILGLTA 272

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 18252778  367 LYFAVVNNNVyaTELLLQHGADPNR---DVISPLLVAIR-HGCLRTMQLLLDH 415
Cdd:PHA02878 273 LHSSIKSERK--LKLLLEYGADINSlnsYKLTPLSSAVKqYLCINIGRILISN 323
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 44-299 7.38e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 83.39  E-value: 7.38e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778   44 KYSSSLFKTSQ------LAPADPLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLH---------------------- 95
Cdd:PHA02878  18 KYIEYIDHTENystsasLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHiickepnklgmkemirsinkcs 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778   96 ---------EAAYYGQVGCLK-VLQRAYPGTIDQRTLQEETAVYLATCRGHLDCLLslLQAGAEPDISNKSR-ETPLYKA 164
Cdd:PHA02878  98 vfytlvaikDAFNNRNVEIFKiILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLL--LSYGADINMKDRHKgNTALHYA 175

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  165 CERKNAEAVKILVQHNADTN--HRCNRgwTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQS-GQLEALRF 241
Cdd:PHA02878 176 TENKDQRLTELLLSYGANVNipDKTNN--SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKL 253

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 18252778  242 LAKYGADINTQAS-DNASALYEACKNEheEVVEFLLSQGADANKTNKDGLLPLHIASKK 299
Cdd:PHA02878 254 LLEHGVDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 61-319 4.14e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 81.65  E-value: 4.14e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778   61 LIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGCL--KVLQRAypGTIDQRTLQEETAVYLATCRGH-L 137
Cdd:PHA02876 244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvpKLLERG--ADVNAKNIKGETPLYLMAKNGYdT 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  138 DCLLSLLQAGAEPDISNKSRETPLYKACE-RKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKV 216
Cdd:PHA02876 322 ENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  217 ES-KNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHE-EVVEFLLSQGADANKTNKDGLLPLH 294
Cdd:PHA02876 402 EAlSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLL 481

                        250       260
                 ....*....|....*....|....*
gi 18252778  295 IAskKGNYRIVQMLLPVTSRTRIRR 319
Cdd:PHA02876 482 IA--LEYHGIVNILLHYGAELRDSR 504
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 230-427 5.63e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.42  E-value: 5.63e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  230 AAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 309
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  310 PVTSRTR--IRRSGVSPLHLAAERNHDEVLEALLSARFDVNTPlaperarlyEDRRSSALYFAVVNNNVYATELLLQHGA 387
Cdd:PHA02875  89 DLGKFADdvFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP---------NTDKFSPLHLAVMMGDIKGIELLIDHKA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 18252778  388 DPNRDV---ISPLLVAIRHGCLRTMQLLLDHGANIDaYIATHP 427
Cdd:PHA02875 160 CLDIEDccgCTPLIIAMAKGDIAICKMLLDSGANID-YFGKNG 201
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 194-453 1.01e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.41  E-value: 1.01e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  194 LHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNAS--------------- 258
Cdd:PHA02876 149 IKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSvlecavdsknidtik 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  259 --------------ALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNY-RIVQMLLPVTSRTRIRR-SGV 322
Cdd:PHA02876 229 aiidnrsninkndlSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNiKGE 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  323 SPLHLAAERNHD-EVLEALLSARFDVN-------TPL--------------------APERARLYEDRrsSALYFAVVNN 374
Cdd:PHA02876 309 TPLYLMAKNGYDtENIRTLIMLGADVNaadrlyiTPLhqastldrnkdivitllelgANVNARDYCDK--TPIHYAAVRN 386

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  375 NVYATELLLQHGADPnrDVISPLLVAIRHGCL------RTMQLLLDHGANIDA---YIAThptafPATIMFAMKC-LSLL 444
Cdd:PHA02876 387 NVVIINTLLDYGADI--EALSQKIGTALHFALcgtnpyMSVKTLIDRGANVNSknkDLST-----PLHYACKKNCkLDVI 459


                 ....*....
gi 18252778  445 KFLMDLGCD 453
Cdd:PHA02876 460 EMLLDNGAD 468
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 140-288 1.57e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 76.83  E-value: 1.57e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  140 LLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGgAKVESK 219
Cdd:PLN03192 541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-ASISDP 619

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18252778  220 NAYGiTPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKD 288
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 ...
 543-584 7.67e-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: 65.59  E-value: 7.67e-14
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 18252778 543 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 584
Cdd:cd03716   1 STPRSLQHLCRLAIRRCLGRRRLELIKKLPLPPRLKDYLLYE 42
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
 545-584 1.31e-13

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


Pssm-ID: 239641  Cd Length: 41  Bit Score: 64.80  E-value: 1.31e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 18252778 545 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 584
Cdd:cd03587   2 PRSLQHLCRLAIRRCLGKRRLDLIDKLPLPPRLKDYLLYK 41
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 154-300 4.43e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 68.31  E-value: 4.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  154 NKSRETPLYKACERKNA--EAVKILVQHNADTNHRC-NRGWTALHESVSRN---DLEVMQILVSGGAKVESKNAYGITPL 227
Cdd:PHA02859  48 NDLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTrDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLL 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 18252778  228 --FVAAQSGQLEALRFLAKYGADINTQASDNASALYEACK-NEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKG 300
Cdd:PHA02859 128 hmYMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILfHSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 233-427 2.81e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.84  E-value: 2.81e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  233 SGQLEALRFLAKYGAD-INTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPv 311
Cdd:PHA02874  11 SGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  312 tsrtrirrSGVSPLHLAAERNHDEVLEALLSARFDVNTplaperarlyEDRRSSA-LYFAVVNNNVYATELLLQHGADPN 390
Cdd:PHA02874  90 --------NGVDTSILPIPCIEKDMIKTILDCGIDVNI----------KDAELKTfLHYAIKKGDLESIKMLFEYGADVN 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 18252778  391 RDVIS---PLLVAIRHGCLRTMQLLLDHGA--NIDAYIATHP 427
Cdd:PHA02874 152 IEDDNgcyPIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGESP 193
Ank_2 pfam12796
Ankyrin repeats (3 copies);
325-421 3.53e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.44  E-value: 3.53e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778   325 LHLAAERNHDEVLEALLSARFDVNtplaperarLYEDRRSSALYFAVVNNNVYATELLLQHgADPNRDVI--SPLLVAIR 402
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNgrTALHYAAR 70

                          90
                  ....*....|....*....
gi 18252778   403 HGCLRTMQLLLDHGANIDA 421
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
61-154 5.42e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 5.42e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778    61 LIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGCLKVLQRAYPGtidQRTLQEETAVYLATCRGHLDCL 140
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 18252778   141 LSLLQAGAEPDISN 154
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 126-256 8.92e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.97  E-value: 8.92e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  126 TAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCnrGWTALHESVSRNDLEV 205
Cdd:PLN03192 560 TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKRNDLTA 637

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 18252778  206 MQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDN 256
Cdd:PLN03192 638 MKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDD 688
Ank_4 pfam13637
Ankyrin repeats (many copies);
258-309 2.30e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.83  E-value: 2.30e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 18252778   258 SALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 309
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 544-582 3.23e-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: 58.33  E-value: 3.23e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 18252778   544 PPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLK 582
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 92-309 3.25e-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: 3.25e-11
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  92 LPLHEAAYYGQVGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHLDCLLSLLQAGaePDISNKSRETPLYKacerknae 171
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAA--PELVNEPMTSDLYQ-------- 88

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 172 avkilvqhnadtnhrcnrGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLE 237
Cdd:cd22192  89 ------------------GETALHIAVVNQNLNLVRELIARGADVVSPRAtgtffrpgpknliyYGEHPLSFAACVGNEE 150

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 238 ALRFLAKYGADINTQASDNASALY----EACKNEHEEVVEFLLSQGADANK------TNKDGLLPLHIASKKGNYRIVQM 307
Cdd:cd22192 151 IVRLLIEHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQH 230


                ..
gi 18252778 308 LL 309
Cdd:cd22192 231 LV 232
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 224-419 7.65e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.60  E-value: 7.65e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  224 ITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANktnkdgLLPLHIASKKGNYR 303
Cdd:PHA02874  36 TTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTS------ILPIPCIEKDMIKT 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  304 IVQMLLPVTSRTRIRRSGvspLHLAAERNHDEVLEALLSARFDVNtplaperarLYEDRRSSALYFAVVNNNVYATELLL 383
Cdd:PHA02874 110 ILDCGIDVNIKDAELKTF---LHYAIKKGDLESIKMLFEYGADVN---------IEDDNGCYPIHIAIKHNFFDIIKLLL 177

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 18252778  384 QHGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANI 419
Cdd:PHA02874 178 EKGAYANvkdNNGESPLHNAAEYGDYACIKLLIDHGNHI 216
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 260-425 8.73e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.30  E-value: 8.73e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  260 LYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIAS----------------------------------------KK 299
Cdd:PHA03100  39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynltdvkeivkllleyganvnapdnngitpllyaiskKS 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  300 GNYRIVQMLLPVTSRTRIRRS-GVSPLHLAAERNHD--EVLEALLSARFDVNtplAPERARLY----------EDRRSSA 366
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSdGENLLHLYLESNKIdlKILKLLIDKGVDIN---AKNRVNYLlsygvpinikDVYGFTP 195

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 18252778  367 LYFAVVNNNVYATELLLQHGADPN-RDVI--SPLLVAIRHGCLRTMQLLLDHGANIDAYIAT 425
Cdd:PHA03100 196 LHYAVYNNNPEFVKYLLDLGANPNlVNKYgdTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA03095 PHA03095
ankyrin-like protein; Provisional
 69-268 1.55e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.51  E-value: 1.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778   69 DEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQV-GCLKVLQRA-----YPGTIDQRTLQeetaVYLATCRGHLDCLLS 142
Cdd:PHA03095  62 VKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAgadvnAKDKVGRTPLH----VYLSGFNINPKVIRL 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  143 LLQAGAEPDISNKSRETPLYKACERKNA--EAVKILVQHNADTNHRCNRGWTALH---------ESVSRNDLE------- 204
Cdd:PHA03095 138 LLRKGADVNALDLYGMTPLAVLLKSRNAnvELLRLLIDAGADVYAVDDRFRSLLHhhlqsfkprARIVRELIRagcdpaa 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  205 ---------------------VMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEA 263
Cdd:PHA03095 218 tdmlgntplhsmatgssckrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297


                 ....*
gi 18252778  264 CKNEH 268
Cdd:PHA03095 298 VRNNN 302
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 252-421 3.27e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.59  E-value: 3.27e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  252 QASDNASA-----LYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIRRSGVSpLH 326
Cdd:PHA02878  28 NYSTSASLipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVA-IK 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  327 LAAERNHDEVLEALLSARFDVN--------------TPLAPERARLY-----------EDRRSSALYFAVVNNNVYATEL 381
Cdd:PHA02878 107 DAFNNRNVEIFKIILTNRYKNIqtidlvyidkkskdDIIEAEITKLLlsygadinmkdRHKGNTALHYATENKDQRLTEL 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 18252778  382 LLQHGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDA 421
Cdd:PHA02878 187 LLSYGANVNipdKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
Ank_4 pfam13637
Ankyrin repeats (many copies);
225-276 4.91e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 4.91e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 18252778   225 TPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLL 276
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 60-244 1.09e-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: 1.09e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  60 PLIKAIKDGDEEALKTMIK-EGKNLAEPNKEGWLPLHEAAYYGQVGCLKVLQRAYPGTIDQRTLQE----ETAVYLATCR 134
Cdd:cd22192  20 PLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDlyqgETALHIAVVN 99

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 135 GHLDCLLSLLQAGAepDISN---------KSR-------ETPL-YKACErKNAEAVKILVQHNADTNHRCNRGWTALHES 197
Cdd:cd22192 100 QNLNLVRELIARGA--DVVSpratgtffrPGPknliyygEHPLsFAACV-GNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*..
gi 18252778 198 VSRND----LEVMQILVSGGAKVES------KNAYGITPLFVAAQSGQLEALRFLAK 244
Cdd:cd22192 177 VLQPNktfaCQMYDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
PHA02946 PHA02946
ankyin-like protein; Provisional
 143-327 1.20e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 57.37  E-value: 1.20e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  143 LLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRND--LEVMQILVSGGAKVE-SK 219
Cdd:PHA02946  58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINnSV 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  220 NAYGITPLFVAAQSGQLEALRFLA-KYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASK 298
Cdd:PHA02946 138 DEEGCGPLLACTDPSERVFKKIMSiGFEARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCS 217

                        170       180       190
                 ....*....|....*....|....*....|.
gi 18252778  299 K--GNYRIVQMLLPVTSRTRIRRSGVSPLHL 327
Cdd:PHA02946 218 KtvKNVDIINLLLPSTDVNKQNKFGDSPLTL 248
PHA02798 PHA02798
ankyrin-like protein; Provisional
 173-402 2.07e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 56.77  E-value: 2.07e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  173 VKILVQHNADTNHRCNRGWTALHESVSR---NDLEVMQILVSGGAKVESKNAYGITPLFVAAQSG---QLEALRFLAKYG 246
Cdd:PHA02798  92 VKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKG 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  247 ADINTQASDNA-SALYEACKNEHE----EVVEFLLSQGADANKTNK-------DGLLPLHIASKKGNYRIVQMLLPVTSR 314
Cdd:PHA02798 172 VDINTHNNKEKyDTLHCYFKYNIDridaDILKLFVDNGFIINKENKshkkkfmEYLNSLLYDNKRFKKNILDFIFSYIDI 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  315 TRIRRSGVSPLHLAAERNHDEVLEALLSARFDVN--TPLAperarlyedrrSSALYFAVVNNNVYATELLLQHgaDPNRD 392
Cdd:PHA02798 252 NQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINiiTELG-----------NTCLFTAFENESKFIFNSILNK--KPNKN 318

                        250
                 ....*....|
gi 18252778  393 VISPLLVAIR 402
Cdd:PHA02798 319 TISYTYYKLR 328
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 231-309 2.56e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 2.56e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 18252778  231 AQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 309
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
 546-584 3.39e-08

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


Pssm-ID: 198037  Cd Length: 34  Bit Score: 49.33  E-value: 3.39e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 18252778    546 RPLAHLCRLRVRKAIGKyriklLDTLPLPGRLIRYLKYE 584
Cdd:smart00969   1 RSLQHLCRLAIRRSLGG-----IDKLPLPPRLKDYLLYY 34
SOCS_SSB1_4 cd03718
SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box ...
 545-584 5.25e-08

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


Pssm-ID: 239688  Cd Length: 42  Bit Score: 49.22  E-value: 5.25e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 18252778 545 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 584
Cdd:cd03718   3 PLPLMDLCRRRVRVALGRDRLEEIEQLPLPPSLKNYLLYQ 42
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 157-344 9.48e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 55.02  E-value: 9.48e-08
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 157 RETPLYKACERKNAEAVK-ILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAK-----VESKNAYGITPLFVA 230
Cdd:cd22192  17 SESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIA 96

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 231 AQSGQLEALRFLAKYGADINTQA------SDNASAL---------YEACKNeHEEVVEFLLSQGADANKTNKDGLLPLHI 295
Cdd:cd22192  97 VVNQNLNLVRELIARGADVVSPRatgtffRPGPKNLiyygehplsFAACVG-NEEIVRLLIEHGADIRAQDSLGNTVLHI 175

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 296 ----ASKKGNYRIVQMLL-------PVTSRTRIRRSGVSPLHLAAERNHDEVLEALLSAR 344
Cdd:cd22192 176 lvlqPNKTFACQMYDLILsydkeddLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
Ank_4 pfam13637
Ankyrin repeats (many copies);
157-210 1.06e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 1.06e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 18252778   157 RETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILV 210
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
59-109 1.16e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.16e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 18252778    59 DPLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGCLKVL 109
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 60-222 1.17e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.29  E-value: 1.17e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778   60 PLIKAI--KDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGcLKVLQraypgtidqrTLQEETAVYLATCRghL 137
Cdd:PHA03100 109 PLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKID-LKILK----------LLIDKGVDINAKNR--V 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  138 DCLLSLlqaGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVE 217
Cdd:PHA03100 176 NYLLSY---GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252


                 ....*
gi 18252778  218 SKNAY 222
Cdd:PHA03100 253 TIIET 257
SOCS_ASB1 cd03720
SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a ...
 545-584 1.46e-07

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: 47.80  E-value: 1.46e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 18252778 545 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 584
Cdd:cd03720   3 PRSLLSLCRIAVRRALGKQRLSLICSLPLPDPIKKFLLHE 42
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 291-438 1.51e-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: 1.51e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 291 LPLHIASKKGNYRIVQMLLpVTSRTRIRRSGV---SPLHLAAERNHDEVLEALL-SARFDVNTPLAPErarLYEDRrsSA 366
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLL-KCPSCDLFQRGAlgeTALHVAALYDNLEAAVVLMeAAPELVNEPMTSD---LYQGE--TA 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 367 LYFAVVNNNVYATELLLQHGAD------------PNRDVI-----SPLLVAIRHGCLRTMQLLLDHGANIDA-------- 421
Cdd:cd22192  93 LHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIRAqdslgntv 172

                       170
                ....*....|....*....
gi 18252778 422 --YIATHPTAFPATIMFAM 438
Cdd:cd22192 173 lhILVLQPNKTFACQMYDL 191
SOCS_ASB14 cd03730
SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a ...
 543-584 1.84e-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: 47.92  E-value: 1.84e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 18252778 543 EPPRPLAHLCRLRVRKAIGKYRIK---LLDTLPLPGRLIRYLKYE 584
Cdd:cd03730   1 TNPRSLKHLCRLKIRACMGRLRLRcpvFMSFLPLPNRLKAYILYK 45
SOCS_SSB4 cd03743
SOCS (suppressors of cytokine signaling) box of SSB4 (SPRY domain-containing SOCS box ...
 545-584 3.33e-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: 3.33e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 18252778 545 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 584
Cdd:cd03743   3 PLPLMDLCRRSARQALGRHRLHHIQSLPLPQTLKNYLQYQ 42
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
 545-583 3.51e-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: 3.51e-07
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 18252778 545 PRPLAHLCRLRVRKAIGKYRIkllDTLPLPGRLIRYLKY 583
Cdd:cd03717   3 VRSLQHLCRFVIRQCTRRDLI---DQLPLPRRLKDYLKE 38
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 189-309 3.83e-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: 3.83e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778   189 RGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAKYGADINTQAS 254
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18252778   255 -----DNASALYEACKNEHEEVV----EFLLSQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 309
Cdd:TIGR00870 207 lgntlLHLLVMENEFKAEYEELScqmyNFALSLLDKLRDSkelevilNHQGLTPLKLAAKEGRIVLFRLKL 277
SOCS_SOCS7 cd03741
SOCS (suppressors of cytokine signaling) box of SOCS7-like proteins. Together with CIS1, the ...
 546-585 7.28e-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: 46.24  E-value: 7.28e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 18252778 546 RPLAHLCRLRVRKAIgkyRIKLLDTLPLPGRLIRYLKYEN 585
Cdd:cd03741   4 QSLQHLCRFVIRKLV---RRDHIPALPLPRRLIDYLREKH 40
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 305-455 1.28e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 50.37  E-value: 1.28e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  305 VQMLLPVTSRTRIRRSGVspLHLAAERNHDEVLEALLSARFDVNTPLAperarLYEDRRSSALYFAVVNNNVYATELLLQ 384
Cdd:PHA02884  19 IIFYIAIKKKNKICIANI--LYSSIKFHYTDIIDAILKLGADPEAPFP-----LSENSKTNPLIYAIDCDNDDAAKLLIR 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 18252778  385 HGADPNR----DVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAFPATIMFamkCLSLLKFLMdlgCDGE 455
Cdd:PHA02884  92 YGADVNRyaeeAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALMI---CNNFLAFMI---CDNE 160
SOCS smart00253
suppressors of cytokine signalling; suppressors of cytokine signalling
 539-583 2.75e-06

suppressors of cytokine signalling; suppressors of cytokine signalling


Pssm-ID: 128549  Cd Length: 43  Bit Score: 44.21  E-value: 2.75e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 18252778    539 KEKAEPPRPLAHLCRLRVRKAIGKYRIKlldTLPLPGRLIRYLKY 583
Cdd:smart00253   1 LPRPSNVPSLQHLCRFTIRRCTRTDQIK---TLPLPPKLKDYLSY 42
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 180-309 3.91e-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: 49.76  E-value: 3.91e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 180 NADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAKY 245
Cdd:cd22194 131 NAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPEIVQLLMEK 210

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 246 GADI--------NT------QASDNASA-------LYE----ACKNEHEEVVefllsqgadankTNKDGLLPLHIASKKG 300
Cdd:cd22194 211 ESTDitsqdsrgNTvlhalvTVAEDSKTqndfvkrMYDmillKSENKNLETI------------RNNEGLTPLQLAAKMG 278


                ....*....
gi 18252778 301 NYRIVQMLL 309
Cdd:cd22194 279 KAEILKYIL 287
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 189-309 3.98e-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: 49.88  E-value: 3.98e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 189 RGWTALHESVSRNDLEVMQILVSGGAKVESKNA-------------YGITPLFVAAQSGQLEALRFLAKYGADI-NTQAS 254
Cdd:cd21882  72 QGQTALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQPaALEAQ 151

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18252778 255 DNAS-----ALYEACKNEHE------EVVEFLLSQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 309
Cdd:cd21882 152 DSLGntvlhALVLQADNTPEnsafvcQMYNLLLSYGAHLDPTqqleeipNHQGLTPLKLAAVEGKIVMFQHIL 224
Ank_5 pfam13857
Ankyrin repeats (many copies);
143-195 5.26e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.87  E-value: 5.26e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 18252778   143 LLQAG-AEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALH 195
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
190-242 7.07e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 7.07e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 18252778   190 GWTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFL 242
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 194-388 8.58e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.71  E-value: 8.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  194 LHESVSRNDLEVMQILVSGGAkvESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVE 273
Cdd:PLN03192 498 LQHHKELHDLNVGDLLGDNGG--EHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVL 575

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  274 FLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIRRSGvSPLHLAAERNHDEVLEALLSARFDVNTplap 353
Cdd:PLN03192 576 VLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDS---- 650

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 18252778  354 erarlyEDRR-SSALYFAVVNNNVYATELLLQHGAD 388
Cdd:PLN03192 651 ------EDHQgATALQVAMAEDHVDMVRLLIMNGAD 680
SOCS_SSB2 cd03719
SOCS (suppressors of cytokine signaling) box of SSB2 (SPRY domain-containing SOCS box proteins) ...
 543-584 8.69e-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: 8.69e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 18252778 543 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 584
Cdd:cd03719   1 AEPHSLLHLSRLCVRHALGDTRLGQVSALPLPPAMKRYLLYQ 42
SOCS_SSB1 cd03744
SOCS (suppressors of cytokine signaling) box of SSB1 (SPRY domain-containing SOCS box proteins) ...
 545-584 9.66e-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: 42.66  E-value: 9.66e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 18252778 545 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 584
Cdd:cd03744   3 PLPLMDLCRRSVRLALGRERLSEIHTLPLPASLKNYLLYQ 42
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
 543-584 1.45e-05

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


Pssm-ID: 239701  Cd Length: 56  Bit Score: 42.51  E-value: 1.45e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 18252778 543 EPPRPLAHLCRLRVRKAIGKYRIKLLDT---LPLPGRLIRYLKYE 584
Cdd:cd03731   1 ENPRPLKHLCRLKIRKLMGLQKLQQPSSmkkLPLPPALKRYILYK 45
PHA02946 PHA02946
ankyin-like protein; Provisional
 252-309 1.93e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 47.36  E-value: 1.93e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  252 QASDNASALYEAC--KNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 309
Cdd:PHA02946  33 EPSGNYHILHAYCgiKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLL 92
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 216-348 1.99e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.97  E-value: 1.99e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  216 VESKNAYGITPLF--VAAQSGQLEALRFLAKYGADINTQASD-NASALYEAC---KNEHEEVVEFLLSQGADANKTNKDG 289
Cdd:PHA02859  44 VNDCNDLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRDnNLSALHHYLsfnKNVEPEILKILIDSGSSITEEDEDG 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  290 LLPLHIASKKGNYRIVQMLLpvtsrtrIRRSGVSPLHLAAERNH-----------DEVLEALLSARFDVN 348
Cdd:PHA02859 124 KNLLHMYMCNFNVRINVIKL-------LIDSGVSFLNKDFDNNNilysyilfhsdKKIFDFLTSLGIDIN 186
Ank_4 pfam13637
Ankyrin repeats (many copies);
134-177 2.02e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 2.02e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 18252778   134 RGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILV 177
Cdd:pfam13637  11 SGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 207-277 2.52e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 2.52e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 18252778  207 QILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLS 277
Cdd:PTZ00322  99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
SOCS_ASB13 cd03729
SOCS (suppressors of cytokine signaling) box of ASB13-like proteins. ASB family members have a ...
 545-583 3.53e-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: 3.53e-05
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 18252778 545 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKY 583
Cdd:cd03729   3 PLSLQQLCRINLRKALGTRALEKIAKLNIPNRIIDYLSY 41
SOCS_ASB7 cd03726
SOCS (suppressors of cytokine signaling) box of ASB7-like proteins. ASB family members have a ...
 545-584 4.19e-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: 40.99  E-value: 4.19e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 18252778 545 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 584
Cdd:cd03726   3 PRTLQDLCRIKIRHCIGLQNLKLLDELPIAKVMKDYLKHK 42
SOCS_ASB5 cd03724
SOCS (suppressors of cytokine signaling) box of ASB5-like proteins. ASB family members have a ...
 545-583 4.67e-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: 4.67e-05
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 18252778 545 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKY 583
Cdd:cd03724   3 PSSLCQLCRLCIRNYIGRSRLHLIPQLQLPTLLKNFLQY 41
Ank_5 pfam13857
Ankyrin repeats (many copies);
242-296 1.21e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 1.21e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 18252778   242 LAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIA 296
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 195-276 1.47e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 44.73  E-value: 1.47e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  195 HESVSRNDLEVMQILVSGgAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEF 274
Cdd:PHA02989 229 NKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNR 307


                 ..
gi 18252778  275 LL 276
Cdd:PHA02989 308 IL 309
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 189-309 1.70e-04

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 44.40  E-value: 1.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 189 RGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFL---AKYGADINT 251
Cdd:cd22193  75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKgrffqpkyqgegfyFGELPLSLAACTNQPDIVQYLlenEHQPADIEA 154

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18252778 252 QASDNAS---ALYEACKNEHEE------VVEFLLSQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 309
Cdd:cd22193 155 QDSRGNTvlhALVTVADNTKENtkfvtrMYDMILIRGAKLCPTveleeirNNDGLTPLQLAAKMGKIEILKYIL 228
Ank_2 pfam12796
Ankyrin repeats (3 copies);
60-109 1.70e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.87  E-value: 1.70e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 18252778    60 PLIKAIKDGDEEALKTMIKegKNLAEPNKEGWLPLHEAAYYGQVGCLKVL 109
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVKLL 80
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 222-251 1.95e-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: 38.78  E-value: 1.95e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 18252778   222 YGITPLFVAAQSGQLEALRFLAKYGADINT 251
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 222-250 2.09e-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: 38.72  E-value: 2.09e-04
                           10        20
                   ....*....|....*....|....*....
gi 18252778    222 YGITPLFVAAQSGQLEALRFLAKYGADIN 250
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 189-309 3.26e-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: 3.26e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 189 RGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAK---YGADINT 251
Cdd:cd22196  93 KGQTALHIAIERRNMHLVELLVQNGADVHARASgeffkkkkggpgfyFGELPLSLAACTNQLDIVKFLLEnphSPADISA 172

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18252778 252 QASDNAS---ALYEACKNEHE------EVVEFLLSQGADANK-------TNKDGLLPLHIASKKGNYRIVQMLL 309
Cdd:cd22196 173 RDSMGNTvlhALVEVADNTPEntkfvtKMYNEILILGAKIRPllkleeiTNKKGLTPLKLAAKTGKIGIFAYIL 246
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
 545-585 4.04e-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: 38.19  E-value: 4.04e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 18252778 545 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYEN 585
Cdd:cd03723   3 PRSLQHLCRCAIRKLLGSRCHKLVPQLSLPTSLKNYLLLEP 43
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 321-348 4.08e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 4.08e-04
                           10        20
                   ....*....|....*....|....*...
gi 18252778    321 GVSPLHLAAERNHDEVLEALLSARFDVN 348
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 216-390 8.50e-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: 8.50e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778   216 VESKNAYGITPLFVAAQSGQLEALRFLAKYgadINTQASDNASALYEACKNEHEeVVEFLLSQGADANKtnKDGLLPLHI 295
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISLEYVD-AVEAILLHLLAAFR--KSGPLELAN 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778   296 ASKKGNYrivqmllpvtsrTRirrsGVSPLHLAAERNHDEVLEALLSARFDVNTP-------LAPERARLYEDRRSSALY 368
Cdd:TIGR00870 119 DQYTSEF------------TP----GITALHLAAHRQNYEIVKLLLERGASVPARacgdffvKSQGVDSFYHGESPLNAA 182

                         170       180
                  ....*....|....*....|..
gi 18252778   369 FAVVNNNVYAteLLLQHGADPN 390
Cdd:TIGR00870 183 ACLGSPSIVA--LLSEDPADIL 202
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 137-227 8.67e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 42.21  E-value: 8.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  137 LDCLLSLLQAGAEPDISNKSRETPLYKACERKN--AEAVKILVQHNADTNHRCNRGWTALHESVSR------------ND 202
Cdd:PHA02716 297 ISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMlsvvnildpetdND 376

                         90       100
                 ....*....|....*....|....*..
gi 18252778  203 --LEVMQILVSGGAKVESKNAYGITPL 227
Cdd:PHA02716 377 irLDVIQCLISLGADITAVNCLGYTPL 403
Ank_4 pfam13637
Ankyrin repeats (many copies);
363-413 1.53e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 1.53e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 18252778   363 RSSALYFAVVNNNVYATELLLQHGADPNR---DVISPLLVAIRHGCLRTMQLLL 413
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAvdgNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 362-453 1.54e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.19  E-value: 1.54e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  362 RRSSALYFAVVNNNVYATELLLQHGADPNRDV-----ISPLLVAIRHGC---LRTMQLLLDHGANIDAYIATHPTAFPAT 433
Cdd:PHA03100  34 KPVLPLYLAKEARNIDVVKILLDNGADINSSTknnstPLHYLSNIKYNLtdvKEIVKLLLEYGANVNAPDNNGITPLLYA 113

                         90       100
                 ....*....|....*....|
gi 18252778  434 IMFAMKCLSLLKFLMDLGCD 453
Cdd:PHA03100 114 ISKKSNSYSIVEYLLDNGAN 133
Ank_5 pfam13857
Ankyrin repeats (many copies);
176-227 1.66e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.94  E-value: 1.66e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 18252778   176 LVQH-NADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPL 227
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
275-328 1.96e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 1.96e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 18252778   275 LLSQG-ADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIR-RSGVSPLHLA 328
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKdEEGLTALDLA 56
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 138-255 2.07e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.35  E-value: 2.07e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  138 DCLLSLLQAGAEPDI----SNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNrgwtalhesvsrndlevmqilvsgg 213
Cdd:PHA02884  47 DIIDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAE------------------------- 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 18252778  214 akvESKnaygITPLFVAAQSGQLEALRFLAKYGADINTQASD 255
Cdd:PHA02884 102 ---EAK----ITPLYISVLHGCLKCLEILLSYGADINIQTND 136
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 189-309 2.12e-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: 2.12e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 189 RGWTALHESVSRNDLEVMQILVSGGAKVESKNA-------------YGITPLFVAAQSGQLEALRFLAKYGADI-NTQAS 254
Cdd:cd22197  93 RGHSALHIAIEKRSLQCVKLLVENGADVHARACgrffqkkqgtcfyFGELPLSLAACTKQWDVVNYLLENPHQPaSLQAQ 172

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18252778 255 DNAS-----ALYEACKN--EHEEVV----EFLLSQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 309
Cdd:cd22197 173 DSLGntvlhALVMIADNspENSALVikmyDGLLQAGARLCPTvqleeisNHEGLTPLKLAAKEGKIEIFRHIL 245
Ank_4 pfam13637
Ankyrin repeats (many copies);
321-383 2.44e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 2.44e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18252778   321 GVSPLHLAAERNHDEVLEALLSARFDVNtplaperARLYEDRrsSALYFAVVNNNVYATELLL 383
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADIN-------AVDGNGE--TALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 159-184 2.54e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.64  E-value: 2.54e-03
                           10        20
                   ....*....|....*....|....*.
gi 18252778    159 TPLYKACERKNAEAVKILVQHNADTN 184
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 237-308 2.77e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 38.70  E-value: 2.77e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 18252778  237 EALRFLAKYGADINTQASDNA-SALYEACKNEHEEVVEFLLSQ-GADANKTNKDGLLPLHIASKKGNYRIVQML 308
Cdd:PHA02736  72 EKLKLLMEWGADINGKERVFGnTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNIL 145
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 94-242 3.59e-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: 40.25  E-value: 3.59e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  94 LHEAAYY---GQVGCLKVLQRAYPGTIDQRTL----------QEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSR--- 157
Cdd:cd21882  30 LHKAALNlndGVNEAIMLLLEAAPDSGNPKELvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSARATGRffr 109

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 158 ----------ETPLYKACERKNAEAVKILVQHNADTNHRCNR---GWTALHESVSRND---------LEVMQILVSGGAK 215
Cdd:cd21882 110 kspgnlfyfgELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHALVLQADntpensafvCQMYNLLLSYGAH 189

                       170       180       190
                ....*....|....*....|....*....|....
gi 18252778 216 V-------ESKNAYGITPLFVAAQSGQLEALRFL 242
Cdd:cd21882 190 LdptqqleEIPNHQGLTPLKLAAVEGKIVMFQHI 223
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 123-242 3.93e-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: 3.93e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 123 QEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSR--------------ETPLYKACERKNAEAVKILVQH---NADTNH 185
Cdd:cd22193  75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRffqpkyqgegfyfgELPLSLAACTNQPDIVQYLLENehqPADIEA 154

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 18252778 186 RCNRGWTALH-------ESVSRNDL--EVMQILVSGGAKV-------ESKNAYGITPLFVAAQSGQLEALRFL 242
Cdd:cd22193 155 QDSRGNTVLHalvtvadNTKENTKFvtRMYDMILIRGAKLcptveleEIRNNDGLTPLQLAAKMGKIEILKYI 227
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 321-348 5.12e-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: 5.12e-03
                          10        20
                  ....*....|....*....|....*....
gi 18252778   321 GVSPLHLAAER-NHDEVLEALLSARFDVN 348
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
SOCS_WSB_SWIP cd03733
SOCS (suppressors of cytokine signaling) box of WSB/SWiP-like proteins. This subfamily ...
 548-583 5.50e-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: 5.50e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 18252778 548 LAHLCRLRVRKAIGKYRIKlldTLPLPGRLIRYLKY 583
Cdd:cd03733   6 LQHLCRMALRRVMTTQQVL---ALPIPKKMKEFLTY 38
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 255-287 6.36e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.57  E-value: 6.36e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 18252778   255 DNASALYEAC-KNEHEEVVEFLLSQGADANKTNK 287
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 60-179 6.53e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 39.48  E-value: 6.53e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778   60 PLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEA-AYYGQVGCLKVLQRAYPGTIDQRTLQEETAVYLATcrGHLD 138
Cdd:PHA02878 204 PLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSI--KSER 281

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 18252778  139 CLLSLLQAGAEPDISNKSRETPLYKAC-ERKNAEAVKILVQH 179
Cdd:PHA02878 282 KLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRILISN 323
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 104-242 6.56e-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: 39.36  E-value: 6.56e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 104 GCLKVL------QRAYPGtidqrtlqeETAVYLATCRGHLDCLLSLLQAGAEPDISNKSR--------------ETPLYK 163
Cdd:cd22194 124 GILDRFinaeytEEAYEG---------QTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLAL 194

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778 164 ACERKNAEAVKILVQhNADTNHRC--NRGWTALH-------ESVSRNDLEV----MQILVSGGAKVES-KNAYGITPLFV 229
Cdd:cd22194 195 AACTNQPEIVQLLME-KESTDITSqdSRGNTVLHalvtvaeDSKTQNDFVKrmydMILLKSENKNLETiRNNEGLTPLQL 273

                       170
                ....*....|...
gi 18252778 230 AAQSGQLEALRFL 242
Cdd:cd22194 274 AAKMGKAEILKYI 286
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 255-284 7.94e-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: 7.94e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 18252778    255 DNASALYEACKNEHEEVVEFLLSQGADANK 284
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 169-245 8.34e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.11  E-value: 8.34e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 18252778  169 NAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKY 245
Cdd:PTZ00322  94 DAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 218-298 8.58e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 38.43  E-value: 8.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 18252778  218 SKNAYgITPLFVAAQSGQLEALRFLAKYGADINTQASD-NASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIA 296
Cdd:PHA02884  66 SENSK-TNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEaKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELA 144


                 ..
gi 18252778  297 SK 298
Cdd:PHA02884 145 LM 146
SOCS_ASB3 cd03722
SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a ...
 548-585 8.68e-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: 34.77  E-value: 8.68e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 18252778 548 LAHLCRLRVRKAIGKYRIK---LLDTLPLPGRLIRYLKYEN 585
Cdd:cd03722   6 LTHLCRLEIRSSLKSERLRsdsFICQLPLPRSLQDYLLYSD 46
 
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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