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Conserved domains on  [gi|1761178565|ref|NP_001361693|]
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ankyrin repeat and SOCS box protein 2 isoform 2 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-352 4.72e-44

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.58  E-value: 4.72e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565  71 EALKIMIQDGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQQAYPGTIDQRTLQEETALYLATCREHLDCLLSLLQAGAEP 150
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 151 DISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVA 230
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 231 AQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLLP 310
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1761178565 311 VTSR-TRVRRSGISPLHLAAERNHDAVLEALLAARFDVNAPLA 352
Cdd:COG0666   241 AGADlNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
542-586 1.82e-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: 93.01  E-value: 1.82e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1761178565 542 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ 586
Cdd:cd03721     1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ 45
Ank_2 pfam12796
Ankyrin repeats (3 copies);
325-421 1.35e-09

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.12  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 325 LHLAAERNHDAVLEALLAARFDVNaplaperarLYEDRRSSALYFAVVNNNVYATELLLlAGADPNRDVI--SPLLVAIR 402
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDNgrTALHYAAR 70
                          90
                  ....*....|....*....
gi 1761178565 403 HGCLRTMQLLLDHGANIDA 421
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-352 4.72e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.58  E-value: 4.72e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565  71 EALKIMIQDGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQQAYPGTIDQRTLQEETALYLATCREHLDCLLSLLQAGAEP 150
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 151 DISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVA 230
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 231 AQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLLP 310
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1761178565 311 VTSR-TRVRRSGISPLHLAAERNHDAVLEALLAARFDVNAPLA 352
Cdd:COG0666   241 AGADlNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
PHA02876 PHA02876
ankyrin repeat protein; Provisional
105-421 1.49e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 108.23  E-value: 1.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 105 CLKVLQQAYPGTIDQRTLQEETALYLATCREHL--DCLL---SLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRY 179
Cdd:PHA02876  121 CIHILKEAISGNDIHYDKINESIEYMKLIKERIqqDELLiaeMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSY 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 180 NADAN-----------------------------HRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVA 230
Cdd:PHA02876  201 GADVNiialddlsvlecavdsknidtikaiidnrSNINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHA 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 231 AQSGQLEAL-RFLAKHGADINTQASDSASALYEASKNEHE-DVVEFLLSQGADANKANKDGLLPLHVASKKGNYR-IVQM 307
Cdd:PHA02876  281 SQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVIT 360
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 308 LLPVTSRTRVRR-SGISPLHLAAERNHDAVLEALLAARFDVNAplaperarlYEDRRSSALYFAVVNNNVY-ATELLLLA 385
Cdd:PHA02876  361 LLELGANVNARDyCDKTPIHYAAVRNNVVIINTLLDYGADIEA---------LSQKIGTALHFALCGTNPYmSVKTLIDR 431
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1761178565 386 GAD---PNRDVISPLLVAIRHGC-LRTMQLLLDHGANIDA 421
Cdd:PHA02876  432 GANvnsKNKDLSTPLHYACKKNCkLDVIEMLLDNGADVNA 471
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
542-586 1.82e-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: 93.01  E-value: 1.82e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1761178565 542 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ 586
Cdd:cd03721     1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ 45
Ank_2 pfam12796
Ankyrin repeats (3 copies);
128-220 1.17e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 128 LYLATCREHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYnADANHRCNrGWTALHESVSRNDLEVME 207
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1761178565 208 ILVSGGAKVEAKN 220
Cdd:pfam12796  79 LLLEKGADINVKD 91
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
543-581 4.00e-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: 57.95  E-value: 4.00e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1761178565 543 PPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLK 581
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
92-309 7.05e-10

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: 61.95  E-value: 7.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565  92 LPLHEAAYYGQLGCLKVLQQAYPGTIDQRTLQEETALYLATCREHLDCLLSLLQAGaePDISNKSRETPLYKacerknae 171
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAA--PELVNEPMTSDLYQ-------- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 172 avrilvrynadanhrcnrGWTALHESVSRNDLEVMEILVSGGAKV------------EAKNV--YSITPLFVAAQSGQLE 237
Cdd:cd22192    89 ------------------GETALHIAVVNQNLNLVRELIARGADVvspratgtffrpGPKNLiyYGEHPLSFAACVGNEE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 238 ALRFLAKHGADINTQASDSASALY----EASKNEHEDVVEFLLSQGADANKA------NKDGLLPLHVASKKGNYRIVQM 307
Cdd:cd22192   151 IVRLLIEHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQH 230

                  ..
gi 1761178565 308 LL 309
Cdd:cd22192   231 LV 232
Ank_2 pfam12796
Ankyrin repeats (3 copies);
325-421 1.35e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.12  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 325 LHLAAERNHDAVLEALLAARFDVNaplaperarLYEDRRSSALYFAVVNNNVYATELLLlAGADPNRDVI--SPLLVAIR 402
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDNgrTALHYAAR 70
                          90
                  ....*....|....*....
gi 1761178565 403 HGCLRTMQLLLDHGANIDA 421
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
545-583 4.24e-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: 4.24e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1761178565  545 RPLAHLCRLRVRKAIGKyriklLDTLPLPGRLIRYLKYE 583
Cdd:smart00969   1 RSLQHLCRLAIRRSLGG-----IDKLPLPPRLKDYLLYY 34
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
189-309 6.18e-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: 52.39  E-value: 6.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 189 RGWTALHESVSRNDLEVMEILVSGGAKVEAKNV--------------YSITPLFVAAQSGQLEALRFLAKHGADINTQAS 254
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1761178565 255 DS-----ASALYEASKNEHEDVV----EFLLSQGADANKA-------NKDGLLPLHVASKKGNYRIVQMLL 309
Cdd:TIGR00870 207 LGntllhLLVMENEFKAEYEELScqmyNFALSLLDKLRDSkelevilNHQGLTPLKLAAKEGRIVLFRLKL 277
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
291-438 1.06e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.47  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 291 LPLHVASKKGNYRIVQMLLpVTSRTRVRRSGI---SPLHLAAERNHDAVLEALL-AARFDVNAPLAPErarLYEDRrsSA 366
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLL-KCPSCDLFQRGAlgeTALHVAALYDNLEAAVVLMeAAPELVNEPMTSD---LYQGE--TA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 367 LYFAVVNNNVYATELLLLAGAD------------PNRDVI-----SPLLVAIRHGCLRTMQLLLDHGANIDA-------- 421
Cdd:cd22192    93 LHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIRAqdslgntv 172
                         170
                  ....*....|....*....
gi 1761178565 422 --YIATHPTAFPATIMFAM 438
Cdd:cd22192   173 lhILVLQPNKTFACQMYDL 191
PHA02884 PHA02884
ankyrin repeat protein; Provisional
336-455 1.41e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 47.29  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 336 VLEALLAARFDVNAPLAperarLYEDRRSSALYFAVVNNNVYATELLLLAGADPNR----DVISPLLVAIRHGCLRTMQL 411
Cdd:PHA02884   48 IIDAILKLGADPEAPFP-----LSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRyaeeAKITPLYISVLHGCLKCLEI 122
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1761178565 412 LLDHGANIDAYIATHPTAFPATIMFamkCLSLLKFLMdlgCDGE 455
Cdd:PHA02884  123 LLSYGADINIQTNDMVTPIELALMI---CNNFLAFMI---CDNE 160
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
289-421 6.84e-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: 42.76  E-value: 6.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 289 GLLPLHVASKKGNYRIVQMLLPVTSRtRVRrSGISPLHLAAERNHDAVLEALL----AARFDVNAPLAPERA--RLYEDR 362
Cdd:TIGR00870  52 GRSALFVAAIENENLELTELLLNLSC-RGA-VGDTLLHAISLEYVDAVEAILLhllaAFRKSGPLELANDQYtsEFTPGI 129
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1761178565 363 rsSALYFAVVNNNVYATELLLLAGAD-PNRD-----VISPLLVAIRHGCLR-----------TMQLLLDHGANIDA 421
Cdd:TIGR00870 130 --TALHLAAHRQNYEIVKLLLERGASvPARAcgdffVKSQGVDSFYHGESPlnaaaclgspsIVALLSEDPADILT 203
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
225-250 2.25e-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: 2.25e-03
                           10        20
                   ....*....|....*....|....*.
gi 1761178565  225 TPLFVAAQSGQLEALRFLAKHGADIN 250
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-352 4.72e-44

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.58  E-value: 4.72e-44
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565  71 EALKIMIQDGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQQAYPGTIDQRTLQEETALYLATCREHLDCLLSLLQAGAEP 150
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 151 DISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVA 230
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 231 AQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLLP 310
Cdd:COG0666   161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|...
gi 1761178565 311 VTSR-TRVRRSGISPLHLAAERNHDAVLEALLAARFDVNAPLA 352
Cdd:COG0666   241 AGADlNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-309 2.82e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.57  E-value: 2.82e-42
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565  62 LKAIKEGDEEALKIMIQDGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQQAYPGTIDQRTLQEETALYLATCREHLDCLL 141
Cdd:COG0666    25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 142 SLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKNV 221
Cdd:COG0666   105 LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 222 YSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGN 301
Cdd:COG0666   185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGA 264

                  ....*...
gi 1761178565 302 YRIVQMLL 309
Cdd:COG0666   265 ALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
117-390 6.06e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.41  E-value: 6.06e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 117 IDQRTLQEETALYLATCREHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHE 196
Cdd:COG0666    14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHA 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 197 SVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLL 276
Cdd:COG0666    94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 277 SQGADANKANKDGLLPLHVASKKGNYRIVQMLL----PVTSRTRvrrSGISPLHLAAERNHDAVLEALLAARFDVNAPLa 352
Cdd:COG0666   174 EAGADVNARDNDGETPLHLAAENGHLEIVKLLLeagaDVNAKDN---DGKTALDLAAENGNLEIVKLLLEAGADLNAKD- 249
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1761178565 353 perarlyeDRRSSALYFAVVNNNVYATELLLLAGADPN 390
Cdd:COG0666   250 --------KDGLTALLLAAAAGAALIVKLLLLALLLLA 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
62-293 1.21e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.94  E-value: 1.21e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565  62 LKAIKEGDEEALKIMIQDGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQQAyPGTIDQRTLQEETALYLATCREHLDCLL 141
Cdd:COG0666    59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVK 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 142 SLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKNV 221
Cdd:COG0666   138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1761178565 222 YSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPL 293
Cdd:COG0666   218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
140-429 2.16e-34

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 132.00  E-value: 2.16e-34
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 140 LLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAK 219
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 220 NVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGllplhvaskk 299
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDG---------- 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 300 gnyrivqmllpvtsrtrvrrsgISPLHLAAERNHDAVLEALLAARFDVNAPlaperarlyEDRRSSALYFAVVNNNVYAT 379
Cdd:COG0666   154 ----------------------NTPLHLAAANGNLEIVKLLLEAGADVNAR---------DNDGETPLHLAAENGHLEIV 202
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1761178565 380 ELLLLAGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTA 429
Cdd:COG0666   203 KLLLEAGADVNakdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
PHA02876 PHA02876
ankyrin repeat protein; Provisional
105-421 1.49e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 108.23  E-value: 1.49e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 105 CLKVLQQAYPGTIDQRTLQEETALYLATCREHL--DCLL---SLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRY 179
Cdd:PHA02876  121 CIHILKEAISGNDIHYDKINESIEYMKLIKERIqqDELLiaeMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSY 200
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 180 NADAN-----------------------------HRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVA 230
Cdd:PHA02876  201 GADVNiialddlsvlecavdsknidtikaiidnrSNINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHA 280
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 231 AQSGQLEAL-RFLAKHGADINTQASDSASALYEASKNEHE-DVVEFLLSQGADANKANKDGLLPLHVASKKGNYR-IVQM 307
Cdd:PHA02876  281 SQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVIT 360
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 308 LLPVTSRTRVRR-SGISPLHLAAERNHDAVLEALLAARFDVNAplaperarlYEDRRSSALYFAVVNNNVY-ATELLLLA 385
Cdd:PHA02876  361 LLELGANVNARDyCDKTPIHYAAVRNNVVIINTLLDYGADIEA---------LSQKIGTALHFALCGTNPYmSVKTLIDR 431
                         330       340       350       360
                  ....*....|....*....|....*....|....*....|
gi 1761178565 386 GAD---PNRDVISPLLVAIRHGC-LRTMQLLLDHGANIDA 421
Cdd:PHA02876  432 GANvnsKNKDLSTPLHYACKKNCkLDVIEMLLDNGADVNA 471
PHA03095 PHA03095
ankyrin-like protein; Provisional
151-432 8.70e-24

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 104.72  E-value: 8.70e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 151 DISNKSRETPLYK---ACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRN---DLEVMEILVSGGAKVEAKNVYSI 224
Cdd:PHA03095    5 ESVDIIMEAALYDyllNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 225 TPLFVAAQSGQ-LEALRFLAKHGADINTQ--ASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHV--ASKK 299
Cdd:PHA03095   85 TPLHLYLYNATtLDVIKLLIKAGADVNAKdkVGRTPLHVYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVllKSRN 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 300 GNYRIVQMLLPVTSRTRVRRS-GISPLHLAAE--RNHDAVLEALLAARFDVNAPLAPERARLYED------RRS------ 364
Cdd:PHA03095  165 ANVELLRLLIDAGADVYAVDDrFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMatgsscKRSlvlpll 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 365 --------------SALYFAVVNNNVYATELLLLAGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHP 427
Cdd:PHA03095  245 iagisinarnrygqTPLHYAAVFNNPRACRRLIALGADINavsSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLN 324

                  ....*
gi 1761178565 428 TAFPA 432
Cdd:PHA03095  325 TASVA 329
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
542-586 1.82e-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: 93.01  E-value: 1.82e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1761178565 542 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ 586
Cdd:cd03721     1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ 45
PHA03100 PHA03100
ankyrin repeat protein; Provisional
128-349 1.60e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.43  E-value: 1.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 128 LYLATCREHLDCLLSLLQAGAEPDISNKSRETPL-----YKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSR-- 200
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKks 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 201 NDLEVMEILVSGGAKVEAKNVYSITPLFVAAQSGQ--LEALRFLAKHGADINTqasdsasalyeasknehEDVVEFLLSQ 278
Cdd:PHA03100  119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINA-----------------KNRVNYLLSY 181
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1761178565 279 GADANKANKDGLLPLHVASKKGNYRIVQMLLPVTSRTRVR-RSGISPLHLAAERNHDAVLEALLAARFDVNA 349
Cdd:PHA03100  182 GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVnKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
236-453 4.13e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.78  E-value: 4.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 236 LEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLL-PVTSR 314
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLaAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 315 TRVRRSGISPLHLAAERNHDAVLEALLAARFDVNAPlaperarlyEDRRSSALYFAVVNNNVYATELLLLAGADPN---R 391
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR---------DKDGETPLHLAAYNGNLEIVKLLLEAGADVNaqdN 151
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1761178565 392 DVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAfpatIMFAMKC--LSLLKFLMDLGCD 453
Cdd:COG0666   152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP----LHLAAENghLEIVKLLLEAGAD 211
PHA02874 PHA02874
ankyrin repeat protein; Provisional
44-358 5.55e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 86.56  E-value: 5.55e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565  44 KYSSNLFKTSQMAAMDPVLKAIKEGDEEALKIMIQDGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLqqaypgtIDQRTlq 123
Cdd:PHA02874   22 KNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLL-------IDNGV-- 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 124 eETALYLATCREHlDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRNDL 203
Cdd:PHA02874   93 -DTSILPIPCIEK-DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFF 170
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 204 EVMEILVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNeHEDVVEFLLSQgADAN 283
Cdd:PHA02874  171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLINN-ASIN 248
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1761178565 284 KANKDGLLPLHVA-SKKGNYRIVQMLLPVTSRTRVR-RSGISPLHLAAER-NHDAVLEALLAarfdvNAPLAPERARL 358
Cdd:PHA02874  249 DQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKdNKGENPIDTAFKYiNKDPVIKDIIA-----NAVLIKEADKL 321
Ank_2 pfam12796
Ankyrin repeats (3 copies);
128-220 1.17e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 1.17e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 128 LYLATCREHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYnADANHRCNrGWTALHESVSRNDLEVME 207
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1761178565 208 ILVSGGAKVEAKN 220
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
136-415 3.45e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 84.55  E-value: 3.45e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 136 HLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVR-YNadanhRCNRGWT--ALHESVSRNDLEVMEILVSG 212
Cdd:PHA02878   49 NLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsIN-----KCSVFYTlvAIKDAFNNRNVEIFKIILTN 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 213 gakvEAKNVYSITPLFVAAQSG----QLEALRFLAKHGADINTQASDS-ASALYEASKNEHEDVVEFLLSQGADANKANK 287
Cdd:PHA02878  124 ----RYKNIQTIDLVYIDKKSKddiiEAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDK 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 288 DGLLPLHVASKKGNYRIVQMLLPVTSRTRVRRS-GISPLHLAAERNHD-AVLEALLAARFDVNAPLAPerarlyedRRSS 365
Cdd:PHA02878  200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKcGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYI--------LGLT 271
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1761178565 366 ALYFAVVNNNVyaTELLLLAGADPNR---DVISPLLVAIR-HGCLRTMQLLLDH 415
Cdd:PHA02878  272 ALHSSIKSERK--LKLLLEYGADINSlnsYKLTPLSSAVKqYLCINIGRILISN 323
Ank_2 pfam12796
Ankyrin repeats (3 copies);
260-349 8.22e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.54  E-value: 8.22e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 260 LYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLLPvTSRTRVRRSGISPLHLAAERNHDAVLEA 339
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKL 79
                          90
                  ....*....|
gi 1761178565 340 LLAARFDVNA 349
Cdd:pfam12796  80 LLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
219-425 1.09e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.41  E-value: 1.09e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 219 KNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEH--EDVVE---FLLSQGADANKANKDGLLPL 293
Cdd:PHA03100   31 SYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnlTDVKEivkLLLEYGANVNAPDNNGITPL 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 294 HVAS--KKGNYRIVQMLLPVTSRTRVRRS-GISPLHLAAERNHD--AVLEALLAARFDVNA------------PLapera 356
Cdd:PHA03100  111 LYAIskKSNSYSIVEYLLDNGANVNIKNSdGENLLHLYLESNKIdlKILKLLIDKGVDINAknrvnyllsygvPI----- 185
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1761178565 357 rLYEDRR-SSALYFAVVNNNVYATELLLLAGADPN-RDVI--SPLLVAIRHGCLRTMQLLLDHGANIDAYIAT 425
Cdd:PHA03100  186 -NIKDVYgFTPLHYAVYNNNPEFVKYLLDLGANPNlVNKYgdTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02878 PHA02878
ankyrin repeat protein; Provisional
126-265 4.31e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 81.08  E-value: 4.31e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 126 TALYLATCREHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSR-NDLE 204
Cdd:PHA02878  170 TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYD 249
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1761178565 205 VMEILVSGGAKVEAKN-VYSITPLFVAAQSGQleALRFLAKHGADINTQASDSASALYEASK 265
Cdd:PHA02878  250 ILKLLLEHGVDVNAKSyILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA02875 PHA02875
ankyrin repeat protein; Provisional
60-250 5.57e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.42  E-value: 5.57e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565  60 PVLKAIKEGDEEALKIMIQDGK--NLAEPNKEGwlPLHEAAYYGQLGCLKVLQQAYPGTIDQRTLQEETALYLATCREHL 137
Cdd:PHA02875   38 PIKLAMKFRDSEAIKLLMKHGAipDVKYPDIES--ELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKL 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 138 DCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVE 217
Cdd:PHA02875  116 DIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1761178565 218 --AKNVySITPLFVAAQSGQLEALRFLAKHGADIN 250
Cdd:PHA02875  196 yfGKNG-CVAALCYAIENNKIDIVRLFIKRGADCN 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
194-286 9.94e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 9.94e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 194 LHESVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHgADINTQASDSaSALYEASKNEHEDVVE 273
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1761178565 274 FLLSQGADANKAN 286
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
227-309 1.54e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 1.54e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 227 LFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQgADANKANkDGLLPLHVASKKGNYRIVQ 306
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                  ...
gi 1761178565 307 MLL 309
Cdd:pfam12796  79 LLL 81
PHA02875 PHA02875
ankyrin repeat protein; Provisional
137-348 2.71e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 78.11  E-value: 2.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 137 LDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKv 216
Cdd:PHA02875   15 LDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKF- 93
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 217 eAKNVY---SITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPL 293
Cdd:PHA02875   94 -ADDVFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1761178565 294 HVASKKGNYRIVQMLLPVTSRTRV--RRSGISPLHLAAERNHDAVLEALLAARFDVN 348
Cdd:PHA02875  173 IIAMAKGDIAICKMLLDSGANIDYfgKNGCVAALCYAIENNKIDIVRLFIKRGADCN 229
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
140-288 2.79e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 79.14  E-value: 2.79e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 140 LLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAkveAK 219
Cdd:PLN03192  541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS---IS 617
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 220 NVYSITPLF-VAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKD 288
Cdd:PLN03192  618 DPHAAGDLLcTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
PHA02876 PHA02876
ankyrin repeat protein; Provisional
194-453 1.83e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.64  E-value: 1.83e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 194 LHESVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEA--SKN----- 266
Cdd:PHA02876  149 IKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAvdSKNidtik 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 267 --------------------EHED------------------------------------VVEFLLSQGADANKANKDGL 290
Cdd:PHA02876  229 aiidnrsninkndlsllkaiRNEDletslllydagfsvnsiddckntplhhasqapslsrLVPKLLERGADVNAKNIKGE 308
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 291 LPLHVASKKG----NYRIVQMLLPVTSRTrvRRSGISPLHLAA--ERNHDAVLeALLAARFDVNaplaperARLYEDRrs 364
Cdd:PHA02876  309 TPLYLMAKNGydteNIRTLIMLGADVNAA--DRLYITPLHQAStlDRNKDIVI-TLLELGANVN-------ARDYCDK-- 376
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 365 SALYFAVVNNNVYATELLLLAGADPnrDVISPLLVAIRHGCL------RTMQLLLDHGANIDA---YIAThptafPATIM 435
Cdd:PHA02876  377 TPIHYAAVRNNVVIINTLLDYGADI--EALSQKIGTALHFALcgtnpyMSVKTLIDRGANVNSknkDLST-----PLHYA 449
                         330
                  ....*....|....*....
gi 1761178565 436 FAMKC-LSLLKFLMDLGCD 453
Cdd:PHA02876  450 CKKNCkLDVIEMLLDNGAD 468
PHA02876 PHA02876
ankyrin repeat protein; Provisional
61-319 2.45e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.26  E-value: 2.45e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565  61 VLKAIKEGDEEALKIMIQDGKNLAEPNKEGWLPLHEAAYYGQLGCL--KVLQQAypGTIDQRTLQEETALYL-ATCREHL 137
Cdd:PHA02876  244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvpKLLERG--ADVNAKNIKGETPLYLmAKNGYDT 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 138 DCLLSLLQAGAEPDISNKSRETPLYKACE-RKNAEAVRILVRYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKV 216
Cdd:PHA02876  322 ENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 217 EAKNVYSITPL-FVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHE-DVVEFLLSQGADANKANKDGLLPLH 294
Cdd:PHA02876  402 EALSQKIGTALhFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLL 481
                         250       260
                  ....*....|....*....|....*
gi 1761178565 295 VAskKGNYRIVQMLLPVTSRTRVRR 319
Cdd:PHA02876  482 IA--LEYHGIVNILLHYGAELRDSR 504
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
542-583 9.87e-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: 65.21  E-value: 9.87e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1761178565 542 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 583
Cdd:cd03716     1 STPRSLQHLCRLAIRRCLGRRRLELIKKLPLPPRLKDYLLYE 42
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
544-583 1.59e-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: 1.59e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1761178565 544 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 583
Cdd:cd03587     2 PRSLQHLCRLAIRRCLGKRRLDLIDKLPLPPRLKDYLLYK 41
PHA03095 PHA03095
ankyrin-like protein; Provisional
62-310 6.02e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 71.21  E-value: 6.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565  62 LKAIKEGDEEALKIMIQDGKNLAEPNKEGWLPLHEAAYYGQ-LGCLKVLQQA-----YPGTIDQRTLQeetaLYLATCRE 135
Cdd:PHA03095   55 LHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAgadvnAKDKVGRTPLH----VYLSGFNI 130
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 136 HLDCLLSLLQAGAEPDISNKSRETPLYKACERKNA--EAVRILVRYNADANHRCNRGWTALH---ESVsRNDLEVMEILV 210
Cdd:PHA03095  131 NPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNAnvELLRLLIDAGADVYAVDDRFRSLLHhhlQSF-KPRARIVRELI 209
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 211 SGGAKVEAKNVYSITPLFVAAQSGQLEA--LRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKD 288
Cdd:PHA03095  210 RAGCDPAATDMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSD 289
                         250       260
                  ....*....|....*....|..
gi 1761178565 289 GLLPLHVASKKGNYRIVQMLLP 310
Cdd:PHA03095  290 GNTPLSLMVRNNNGRAVRAALA 311
PHA02875 PHA02875
ankyrin repeat protein; Provisional
230-427 9.42e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.41  E-value: 9.42e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 230 AAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLL 309
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 310 PVTSRTR--VRRSGISPLHLAAERNHDAVLEALLAARFDVNAPlaperarlyEDRRSSALYFAVVNNNVYATELLLLAGA 387
Cdd:PHA02875   89 DLGKFADdvFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP---------NTDKFSPLHLAVMMGDIKGIELLIDHKA 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1761178565 388 DPNRD---VISPLLVAIRHGCLRTMQLLLDHGANIDaYIATHP 427
Cdd:PHA02875  160 CLDIEdccGCTPLIIAMAKGDIAICKMLLDSGANID-YFGKNG 201
Ank_2 pfam12796
Ankyrin repeats (3 copies);
64-154 3.84e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 59.74  E-value: 3.84e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565  64 AIKEGDEEALKIMIQDGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQQAYPGtidQRTLQEETALYLATCREHLDCLLSL 143
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEIVKLL 80
                          90
                  ....*....|.
gi 1761178565 144 LQAGAEPDISN 154
Cdd:pfam12796  81 LEKGADINVKD 91
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
543-581 4.00e-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: 57.95  E-value: 4.00e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1761178565 543 PPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLK 581
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
PHA02874 PHA02874
ankyrin repeat protein; Provisional
223-419 1.23e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.83  E-value: 1.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 223 SITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANkankdgLLPLHVASKKGNY 302
Cdd:PHA02874   35 TTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTS------ILPIPCIEKDMIK 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 303 RIVQMLLPVTSRTRVRRSGispLHLAAERNHDAVLEALLAARFDVNaplaperarLYEDRRSSALYFAVVNNNVYATELL 382
Cdd:PHA02874  109 TILDCGIDVNIKDAELKTF---LHYAIKKGDLESIKMLFEYGADVN---------IEDDNGCYPIHIAIKHNFFDIIKLL 176
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|
gi 1761178565 383 LLAGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANI 419
Cdd:PHA02874  177 LEKGAYANvkdNNGESPLHNAAEYGDYACIKLLIDHGNHI 216
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
92-309 7.05e-10

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: 61.95  E-value: 7.05e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565  92 LPLHEAAYYGQLGCLKVLQQAYPGTIDQRTLQEETALYLATCREHLDCLLSLLQAGaePDISNKSRETPLYKacerknae 171
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAA--PELVNEPMTSDLYQ-------- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 172 avrilvrynadanhrcnrGWTALHESVSRNDLEVMEILVSGGAKV------------EAKNV--YSITPLFVAAQSGQLE 237
Cdd:cd22192    89 ------------------GETALHIAVVNQNLNLVRELIARGADVvspratgtffrpGPKNLiyYGEHPLSFAACVGNEE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 238 ALRFLAKHGADINTQASDSASALY----EASKNEHEDVVEFLLSQGADANKA------NKDGLLPLHVASKKGNYRIVQM 307
Cdd:cd22192   151 IVRLLIEHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQH 230

                  ..
gi 1761178565 308 LL 309
Cdd:cd22192   231 LV 232
Ank_2 pfam12796
Ankyrin repeats (3 copies);
325-421 1.35e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 55.12  E-value: 1.35e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 325 LHLAAERNHDAVLEALLAARFDVNaplaperarLYEDRRSSALYFAVVNNNVYATELLLlAGADPNRDVI--SPLLVAIR 402
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDNgrTALHYAAR 70
                          90
                  ....*....|....*....
gi 1761178565 403 HGCLRTMQLLLDHGANIDA 421
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
Ank_4 pfam13637
Ankyrin repeats (many copies);
225-276 1.53e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.82  E-value: 1.53e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1761178565 225 TPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLL 276
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
258-309 2.46e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 2.46e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1761178565 258 SALYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLL 309
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
252-421 6.76e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.35  E-value: 6.76e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 252 QASDSASA-----LYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLLPVTSRTRV--------- 317
Cdd:PHA02878   28 NYSTSASLipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVfytlvaikd 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 318 ----------------RRSGISPLHLAA--ERNHDAVLEA-----LLAARFDVNaplaperaRLYEDRRSSALYFAVVNN 374
Cdd:PHA02878  108 afnnrnveifkiiltnRYKNIQTIDLVYidKKSKDDIIEAeitklLLSYGADIN--------MKDRHKGNTALHYATENK 179
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|
gi 1761178565 375 NVYATELLLLAGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDA 421
Cdd:PHA02878  180 DQRLTELLLSYGANVNipdKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
PHA03100 PHA03100
ankyrin repeat protein; Provisional
63-251 9.85e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.75  E-value: 9.85e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565  63 KAIKEGDEEALKIMIQDGKNLAEPNKEGWLPLHEAAYY--GQLGCLKVLQQaYPGTIDQRTLQEETAL--YLATCREHLD 138
Cdd:PHA03100   79 KYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLD-NGANVNIKNSDGENLLhlYLESNKIDLK 157
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 139 CLLSLLQAGAepDISNKSRetplykacerknaeaVRILVRYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEA 218
Cdd:PHA03100  158 ILKLLIDKGV--DINAKNR---------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNL 220
                         170       180       190
                  ....*....|....*....|....*....|...
gi 1761178565 219 KNVYSITPLFVAAQSGQLEALRFLAKHGADINT 251
Cdd:PHA03100  221 VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA02859 PHA02859
ankyrin repeat protein; Provisional
154-300 2.87e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 54.44  E-value: 2.87e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 154 NKSRETPLYKACERKNA--EAVRILVRYNADANHRC-NRGWTALHESVSRN---DLEVMEILVSGGAKVEAKNVYSITPL 227
Cdd:PHA02859   48 NDLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTrDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLL 127
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1761178565 228 --FVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHED-VVEFLLSQGADANKANKDGLLPLHVASKKG 300
Cdd:PHA02859  128 hmYMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKkIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
545-583 4.24e-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: 4.24e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1761178565  545 RPLAHLCRLRVRKAIGKyriklLDTLPLPGRLIRYLKYE 583
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 ...
544-583 5.45e-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: 5.45e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1761178565 544 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 583
Cdd:cd03718     3 PLPLMDLCRRRVRVALGRDRLEEIEQLPLPPSLKNYLLYQ 42
PHA03095 PHA03095
ankyrin-like protein; Provisional
70-278 7.90e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.03  E-value: 7.90e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565  70 EEALKIMIQDGKNLAEPNKEGWLPLHEaayygqlgCLKVLQqAYPGTIdqRTLQEETA------LYLATcreHLDCLLS- 142
Cdd:PHA03095   97 LDVIKLLIKAGADVNAKDKVGRTPLHV--------YLSGFN-INPKVI--RLLLRKGAdvnaldLYGMT---PLAVLLKs 162
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 143 ----------LLQAGAEPDISNKSRETPLYKACE--RKNAEAVRILVRYNADANHRCNRGWTALHE--SVSRNDLEVMEI 208
Cdd:PHA03095  163 rnanvellrlLIDAGADVYAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSmaTGSSCKRSLVLP 242
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 209 LVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQ 278
Cdd:PHA03095  243 LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
SOCS_ASB1 cd03720
SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a ...
544-583 1.41e-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: 1.41e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1761178565 544 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 583
Cdd:cd03720     3 PRSLLSLCRIAVRRALGKQRLSLICSLPLPDPIKKFLLHE 42
SOCS_ASB14 cd03730
SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a ...
542-583 2.00e-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: 2.00e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1761178565 542 EPPRPLAHLCRLRVRKAIGKYRIK---LLDTLPLPGRLIRYLKYE 583
Cdd:cd03730     1 TNPRSLKHLCRLKIRACMGRLRLRcpvFMSFLPLPNRLKAYILYK 45
PHA02798 PHA02798
ankyrin-like protein; Provisional
173-402 2.17e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 53.69  E-value: 2.17e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 173 VRILVRYNADANHRCNRGWTALHESVSR---NDLEVMEILVSGGAKVEAKNVYSITPLFVAAQSG---QLEALRFLAKHG 246
Cdd:PHA02798   92 VKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKG 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 247 ADINTQAS----DSASALYEASKNEHE-DVVEFLLSQGADANKANK-------DGLLPLHVASKKGNYRIVQMLLPVTSR 314
Cdd:PHA02798  172 VDINTHNNkekyDTLHCYFKYNIDRIDaDILKLFVDNGFIINKENKshkkkfmEYLNSLLYDNKRFKKNILDFIFSYIDI 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 315 TRVRRSGISPLHLAAERNHDAVLEALLAARFDVNaplaperarLYEDRRSSALYFAVVNNNVYATELLLlaGADPNRDVI 394
Cdd:PHA02798  252 NQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDIN---------IITELGNTCLFTAFENESKFIFNSIL--NKKPNKNTI 320

                  ....*...
gi 1761178565 395 SPLLVAIR 402
Cdd:PHA02798  321 SYTYYKLR 328
SOCS_SSB4 cd03743
SOCS (suppressors of cytokine signaling) box of SSB4 (SPRY domain-containing SOCS box ...
544-583 2.63e-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: 47.26  E-value: 2.63e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1761178565 544 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 583
Cdd:cd03743     3 PLPLMDLCRRSARQALGRHRLHHIQSLPLPQTLKNYLQYQ 42
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
544-582 3.05e-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: 3.05e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1761178565 544 PRPLAHLCRLRVRKAIGKYRIkllDTLPLPGRLIRYLKY 582
Cdd:cd03717     3 VRSLQHLCRFVIRQCTRRDLI---DQLPLPRRLKDYLKE 38
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
231-309 3.14e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 3.14e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1761178565 231 AQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLL 309
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
58-109 5.45e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 5.45e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1761178565  58 MDPVLKAIKEGDEEALKIMIQDGKNLAEPNKEGWLPLHEAAYYGQLGCLKVL 109
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
189-309 6.18e-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: 52.39  E-value: 6.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 189 RGWTALHESVSRNDLEVMEILVSGGAKVEAKNV--------------YSITPLFVAAQSGQLEALRFLAKHGADINTQAS 254
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1761178565 255 DS-----ASALYEASKNEHEDVV----EFLLSQGADANKA-------NKDGLLPLHVASKKGNYRIVQMLL 309
Cdd:TIGR00870 207 LGntllhLLVMENEFKAEYEELScqmyNFALSLLDKLRDSkelevilNHQGLTPLKLAAKEGRIVLFRLKL 277
SOCS_SOCS7 cd03741
SOCS (suppressors of cytokine signaling) box of SOCS7-like proteins. Together with CIS1, the ...
545-584 8.26e-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: 45.86  E-value: 8.26e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1761178565 545 RPLAHLCRLRVRKAIgkyRIKLLDTLPLPGRLIRYLKYEN 584
Cdd:cd03741     4 QSLQHLCRFVIRKLV---RRDHIPALPLPRRLIDYLREKH 40
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
194-388 1.69e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.02  E-value: 1.69e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 194 LHESVSRNDLEVMEILVSGGAkvEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVE 273
Cdd:PLN03192  498 LQHHKELHDLNVGDLLGDNGG--EHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVL 575
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 274 FLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLLPVTSRTRVRRSGiSPLHLAAERNHDAVLEALLAARFDVNAplap 353
Cdd:PLN03192  576 VLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDS---- 650
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 1761178565 354 erarlyEDRR-SSALYFAVVNNNVYATELLLLAGAD 388
Cdd:PLN03192  651 ------EDHQgATALQVAMAEDHVDMVRLLIMNGAD 680
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
189-309 1.78e-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: 51.03  E-value: 1.78e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 189 RGWTALHESVSRNDLEVMEILVSGGAKVEAKNV-------------YSITPLFVAAQSGQLEALRFLAKHGADI-NTQAS 254
Cdd:cd21882    72 QGQTALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQPaALEAQ 151
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1761178565 255 DSAS-----ALYEASKNEHED------VVEFLLSQGADANK-------ANKDGLLPLHVASKKGNYRIVQMLL 309
Cdd:cd21882   152 DSLGntvlhALVLQADNTPENsafvcqMYNLLLSYGAHLDPtqqleeiPNHQGLTPLKLAAVEGKIVMFQHIL 224
Ank_5 pfam13857
Ankyrin repeats (many copies);
143-195 2.01e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.03  E-value: 2.01e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1761178565 143 LLQAG-AEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALH 195
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
SOCS smart00253
suppressors of cytokine signalling; suppressors of cytokine signalling
538-582 2.35e-06

suppressors of cytokine signalling; suppressors of cytokine signalling


Pssm-ID: 128549  Cd Length: 43  Bit Score: 44.59  E-value: 2.35e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1761178565  538 KEKAEPPRPLAHLCRLRVRKAIGKYRIKlldTLPLPGRLIRYLKY 582
Cdd:smart00253   1 LPRPSNVPSLQHLCRFTIRRCTRTDQIK---TLPLPPKLKDYLSY 42
Ank_4 pfam13637
Ankyrin repeats (many copies);
157-210 4.15e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 4.15e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1761178565 157 RETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRNDLEVMEILV 210
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
143-327 7.02e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 48.90  E-value: 7.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 143 LLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHeSVSRNDLEVME---ILVSGGAKVE-A 218
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY-YLSGTDDEVIErinLLVQYGAKINnS 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 219 KNVYSITPLFVAAQSGQLEALRFLA-KHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVAS 297
Cdd:PHA02946  137 VDEEGCGPLLACTDPSERVFKKIMSiGFEARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVC 216
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1761178565 298 KK--GNYRIVQMLLPVTSRTRVRRSGISPLHL 327
Cdd:PHA02946  217 SKtvKNVDIINLLLPSTDVNKQNKFGDSPLTL 248
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
171-309 7.76e-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: 48.99  E-value: 7.76e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 171 EAVRILVRY-----------NADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKN--------------VYSIT 225
Cdd:cd22194   111 EIVRILLAFaeengildrfiNAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykhegfYFGET 190
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 226 PLFVAAQSGQLEALRFLAKHGADINTqASDSAS-----ALYEASKN--EHEDVV----EFLLSQGADAN---KANKDGLL 291
Cdd:cd22194   191 PLALAACTNQPEIVQLLMEKESTDIT-SQDSRGntvlhALVTVAEDskTQNDFVkrmyDMILLKSENKNletIRNNEGLT 269
                         170
                  ....*....|....*...
gi 1761178565 292 PLHVASKKGNYRIVQMLL 309
Cdd:cd22194   270 PLQLAAKMGKAEILKYIL 287
SOCS_SSB2 cd03719
SOCS (suppressors of cytokine signaling) box of SSB2 (SPRY domain-containing SOCS box proteins) ...
542-583 9.39e-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: 42.70  E-value: 9.39e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1761178565 542 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 583
Cdd:cd03719     1 AEPHSLLHLSRLCVRHALGDTRLGQVSALPLPPAMKRYLLYQ 42
SOCS_SSB1 cd03744
SOCS (suppressors of cytokine signaling) box of SSB1 (SPRY domain-containing SOCS box proteins) ...
544-583 9.93e-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: 9.93e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1761178565 544 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 583
Cdd:cd03744     3 PLPLMDLCRRSVRLALGRERLSEIHTLPLPASLKNYLLYQ 42
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
291-438 1.06e-05

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 48.47  E-value: 1.06e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 291 LPLHVASKKGNYRIVQMLLpVTSRTRVRRSGI---SPLHLAAERNHDAVLEALL-AARFDVNAPLAPErarLYEDRrsSA 366
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLL-KCPSCDLFQRGAlgeTALHVAALYDNLEAAVVLMeAAPELVNEPMTSD---LYQGE--TA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 367 LYFAVVNNNVYATELLLLAGAD------------PNRDVI-----SPLLVAIRHGCLRTMQLLLDHGANIDA-------- 421
Cdd:cd22192    93 LHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIRAqdslgntv 172
                         170
                  ....*....|....*....
gi 1761178565 422 --YIATHPTAFPATIMFAM 438
Cdd:cd22192   173 lhILVLQPNKTFACQMYDL 191
PHA02884 PHA02884
ankyrin repeat protein; Provisional
336-455 1.41e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 47.29  E-value: 1.41e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 336 VLEALLAARFDVNAPLAperarLYEDRRSSALYFAVVNNNVYATELLLLAGADPNR----DVISPLLVAIRHGCLRTMQL 411
Cdd:PHA02884   48 IIDAILKLGADPEAPFP-----LSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRyaeeAKITPLYISVLHGCLKCLEI 122
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1761178565 412 LLDHGANIDAYIATHPTAFPATIMFamkCLSLLKFLMdlgCDGE 455
Cdd:PHA02884  123 LLSYGADINIQTNDMVTPIELALMI---CNNFLAFMI---CDNE 160
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
542-583 1.44e-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: 1.44e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1761178565 542 EPPRPLAHLCRLRVRKAIGKYRIKLLDT---LPLPGRLIRYLKYE 583
Cdd:cd03731     1 ENPRPLKHLCRLKIRKLMGLQKLQQPSSmkkLPLPPALKRYILYK 45
SOCS_ASB13 cd03729
SOCS (suppressors of cytokine signaling) box of ASB13-like proteins. ASB family members have a ...
544-582 3.56e-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: 3.56e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1761178565 544 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKY 582
Cdd:cd03729     3 PLSLQQLCRINLRKALGTRALEKIAKLNIPNRIIDYLSY 41
SOCS_ASB5 cd03724
SOCS (suppressors of cytokine signaling) box of ASB5-like proteins. ASB family members have a ...
544-582 3.98e-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: 3.98e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1761178565 544 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKY 582
Cdd:cd03724     3 PSSLCQLCRLCIRNYIGRSRLHLIPQLQLPTLLKNFLQY 41
SOCS_ASB7 cd03726
SOCS (suppressors of cytokine signaling) box of ASB7-like proteins. ASB family members have a ...
544-583 6.14e-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: 40.60  E-value: 6.14e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1761178565 544 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 583
Cdd:cd03726     3 PRTLQDLCRIKIRHCIGLQNLKLLDELPIAKVMKDYLKHK 42
PHA02859 PHA02859
ankyrin repeat protein; Provisional
220-304 6.99e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.42  E-value: 6.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 220 NVYSITPLF--VAAQSGQLEALRFLAKHGADINTQASD---SASALYEA-SKNEHEDVVEFLLSQGADANKANKDGLLPL 293
Cdd:PHA02859   48 NDLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRDnnlSALHHYLSfNKNVEPEILKILIDSGSSITEEDEDGKNLL 127
                          90
                  ....*....|.
gi 1761178565 294 HVASKKGNYRI 304
Cdd:PHA02859  128 HMYMCNFNVRI 138
PHA02878 PHA02878
ankyrin repeat protein; Provisional
60-177 7.05e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 45.64  E-value: 7.05e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565  60 PVLKAIKEGDEEALKIMIQDGKNLAEPNKEGWLPLHEA-AYYGQLGCLKVLQQAYPGTIDQRTLQEETALYLATCREhlD 138
Cdd:PHA02878  204 PLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSE--R 281
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|
gi 1761178565 139 CLLSLLQAGAEPDISNKSRETPLYKAC-ERKNAEAVRILV 177
Cdd:PHA02878  282 KLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRILI 321
Ank_4 pfam13637
Ankyrin repeats (many copies);
190-242 1.27e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 1.27e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1761178565 190 GWTALHESVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFL 242
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02798 PHA02798
ankyrin-like protein; Provisional
174-390 1.46e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.44  E-value: 1.46e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 174 RILVRYNADANHRcnrGWTALHESVSRND--LEVMEILVSGGAKVEAKNVYSITPLF-----VAAQSGQLEALRFLAKHG 246
Cdd:PHA02798   23 LLIKSCNPNEIVN---EYSIFQKYLQRDSpsTDIVKLFINLGANVNGLDNEYSTPLCtilsnIKDYKHMLDIVKILIENG 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 247 ADINTQASDSASALYEASKNEH---EDVVEFLLSQGADANKANKDGLLPLHVASKKGNY---RIVQMLLP--VTSRTRVR 318
Cdd:PHA02798  100 ADINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEkgVDINTHNN 179
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 319 RSGISPLHLAAERNHDA----VLEALLAARFDVNAPLAPERAR--------LYEDRRS---------------------- 364
Cdd:PHA02798  180 KEKYDTLHCYFKYNIDRidadILKLFVDNGFIINKENKSHKKKfmeylnslLYDNKRFkknildfifsyidinqvdelgf 259
                         250       260
                  ....*....|....*....|....*.
gi 1761178565 365 SALYFAVVNNNVYATELLLLAGADPN 390
Cdd:PHA02798  260 NPLYYSVSHNNRKIFEYLLQLGGDIN 285
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
189-309 2.21e-04

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 44.03  E-value: 2.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 189 RGWTALHESVSRNDLEVMEILVSGGAKVEAKN--------------VYSITPLFVAAQSGQLEALRFLAKH---GADINt 251
Cdd:cd22196    93 KGQTALHIAIERRNMHLVELLVQNGADVHARAsgeffkkkkggpgfYFGELPLSLAACTNQLDIVKFLLENphsPADIS- 171
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1761178565 252 qASDSAS-----ALYEASKNEHEDvVEF-------LLSQGADANK-------ANKDGLLPLHVASKKGNYRIVQMLL 309
Cdd:cd22196   172 -ARDSMGntvlhALVEVADNTPEN-TKFvtkmyneILILGAKIRPllkleeiTNKKGLTPLKLAAKTGKIGIFAYIL 246
PHA02884 PHA02884
ankyrin repeat protein; Provisional
128-230 2.49e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 43.43  E-value: 2.49e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 128 LYLATCREHLDCLLSLLQAGAEPDI----SNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRG-WTALHESVSRND 202
Cdd:PHA02884   37 LYSSIKFHYTDIIDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkITPLYISVLHGC 116
                          90       100
                  ....*....|....*....|....*...
gi 1761178565 203 LEVMEILVSGGAKVEAKNVYSITPLFVA 230
Cdd:PHA02884  117 LKCLEILLSYGADINIQTNDMVTPIELA 144
Ank_4 pfam13637
Ankyrin repeats (many copies);
126-177 2.79e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 2.79e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1761178565 126 TALYLATCREHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILV 177
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
189-309 3.90e-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: 43.25  E-value: 3.90e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 189 RGWTALHESVSRNDLEVMEILVSGGAKVEAKN--------------VYSITPLFVAAQSGQLEALRFLAKHG-ADINTQA 253
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLAACTNQPDIVQYLLENEhQPADIEA 154
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1761178565 254 SDSAS-----ALYEASKNEHED------VVEFLLSQGADANKA-------NKDGLLPLHVASKKGNYRIVQMLL 309
Cdd:cd22193   155 QDSRGntvlhALVTVADNTKENtkfvtrMYDMILIRGAKLCPTveleeirNNDGLTPLQLAAKMGKIEILKYIL 228
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
544-584 4.03e-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: 4.03e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1761178565 544 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYEN 584
Cdd:cd03723     3 PRSLQHLCRCAIRKLLGSRCHKLVPQLSLPTSLKNYLLLEP 43
PHA02946 PHA02946
ankyin-like protein; Provisional
261-309 5.79e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 42.73  E-value: 5.79e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1761178565 261 YEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLL 309
Cdd:PHA02946   44 YCGIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLL 92
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
289-421 6.84e-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: 42.76  E-value: 6.84e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 289 GLLPLHVASKKGNYRIVQMLLPVTSRtRVRrSGISPLHLAAERNHDAVLEALL----AARFDVNAPLAPERA--RLYEDR 362
Cdd:TIGR00870  52 GRSALFVAAIENENLELTELLLNLSC-RGA-VGDTLLHAISLEYVDAVEAILLhllaAFRKSGPLELANDQYtsEFTPGI 129
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1761178565 363 rsSALYFAVVNNNVYATELLLLAGAD-PNRD-----VISPLLVAIRHGCLR-----------TMQLLLDHGANIDA 421
Cdd:TIGR00870 130 --TALHLAAHRQNYEIVKLLLERGASvPARAcgdffVKSQGVDSFYHGESPlnaaaclgspsIVALLSEDPADILT 203
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
208-277 7.71e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 7.71e-04
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 208 ILVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLS 277
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
225-250 2.25e-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: 2.25e-03
                           10        20
                   ....*....|....*....|....*.
gi 1761178565  225 TPLFVAAQSGQLEALRFLAKHGADIN 250
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02798 PHA02798
ankyrin-like protein; Provisional
202-293 2.35e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.59  E-value: 2.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 202 DLEVMEILVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHE-----DVVEFLL 276
Cdd:PHA02798   17 KLSTVKLLIKSCNPNEIVNEYSIFQKYLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILI 96
                          90
                  ....*....|....*..
gi 1761178565 277 SQGADANKANKDGLLPL 293
Cdd:PHA02798   97 ENGADINKKNSDGETPL 113
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
180-309 2.73e-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: 40.61  E-value: 2.73e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 180 NADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKN-------------VYSITPLFVAAQSGQLEALRFLAKHG 246
Cdd:cd22197    84 NAQCTDEYYRGHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqkkqgtcfYFGELPLSLAACTKQWDVVNYLLENP 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 247 ADI-NTQASDSAS-----ALYEASKNEHED---VVEF---LLSQGADANKA-------NKDGLLPLHVASKKGNYRIVQM 307
Cdd:cd22197   164 HQPaSLQAQDSLGntvlhALVMIADNSPENsalVIKMydgLLQAGARLCPTvqleeisNHEGLTPLKLAAKEGKIEIFRH 243

                  ..
gi 1761178565 308 LL 309
Cdd:cd22197   244 IL 245
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
263-349 3.31e-03

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 40.45  E-value: 3.31e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 263 ASKNEHEDVVEFLLSQGADAnkANKDGLLplHVASKkGNYRIVQMLL------------------PVTSRTRVrrsGISP 324
Cdd:TIGR00870  60 AIENENLELTELLLNLSCRG--AVGDTLL--HAISL-EYVDAVEAILlhllaafrksgplelandQYTSEFTP---GITA 131
                          90       100
                  ....*....|....*....|....*
gi 1761178565 325 LHLAAERNHDAVLEALLAARFDVNA 349
Cdd:TIGR00870 132 LHLAAHRQNYEIVKLLLERGASVPA 156
PHA03100 PHA03100
ankyrin repeat protein; Provisional
260-421 3.67e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.03  E-value: 3.67e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 260 LYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLLPVTSRTRVRRSGIS-PLHLAAERNHDA--- 335
Cdd:PHA03100    6 VLTKSRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNStPLHYLSNIKYNLtdv 85
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 336 --VLEALLAARFDVNAplaperarlYEDRRSSALYFAVVN--NNVYATELLLLAGADPN---RDVISPLLVAIRHGC--L 406
Cdd:PHA03100   86 keIVKLLLEYGANVNA---------PDNNGITPLLYAISKksNSYSIVEYLLDNGANVNiknSDGENLLHLYLESNKidL 156
                         170
                  ....*....|....*
gi 1761178565 407 RTMQLLLDHGANIDA 421
Cdd:PHA03100  157 KILKLLIDKGVDINA 171
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
225-251 4.19e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 4.19e-03
                          10        20
                  ....*....|....*....|....*..
gi 1761178565 225 TPLFVAAQSGQLEALRFLAKHGADINT 251
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
321-349 4.80e-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: 34.87  E-value: 4.80e-03
                           10        20
                   ....*....|....*....|....*....
gi 1761178565  321 GISPLHLAAERNHDAVLEALLAARFDVNA 349
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
242-296 4.80e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 4.80e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1761178565 242 LAKHG-ADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVA 296
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SOCS_WSB_SWIP cd03733
SOCS (suppressors of cytokine signaling) box of WSB/SWiP-like proteins. This subfamily ...
547-582 4.98e-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: 4.98e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1761178565 547 LAHLCRLRVRKAIGKYRIKlldTLPLPGRLIRYLKY 582
Cdd:cd03733     6 LQHLCRMALRRVMTTQQVL---ALPIPKKMKEFLTY 38
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
60-161 5.06e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 39.17  E-value: 5.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565  60 PVLKAIKEGDEEALKIMIQDGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQQAYpGTIDQRTLQEETALYLATCREHLDC 139
Cdd:COG0666   189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG-ADLNAKDKDGLTALLLAAAAGAALI 267
                          90       100
                  ....*....|....*....|..
gi 1761178565 140 LLSLLQAGAEPDISNKSRETPL 161
Cdd:COG0666   268 VKLLLLALLLLAAALLDLLTLL 289
Ank_5 pfam13857
Ankyrin repeats (many copies);
280-328 5.40e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 5.40e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1761178565 280 ADANKANKDGLLPLHVASKKGNYRIVQMLL-PVTSRTRVRRSGISPLHLA 328
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLaYGVDLNLKDEEGLTALDLA 56
PHA02989 PHA02989
ankyrin repeat protein; Provisional
195-276 5.87e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 39.34  E-value: 5.87e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1761178565 195 HESVSRNDLEVMEILVSGgAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEF 274
Cdd:PHA02989  229 NKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNR 307

                  ..
gi 1761178565 275 LL 276
Cdd:PHA02989  308 IL 309
PHA03100 PHA03100
ankyrin repeat protein; Provisional
117-188 6.17e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.26  E-value: 6.17e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1761178565 117 IDQRTLQEETALYLATCREHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCN 188
Cdd:PHA03100  185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
SOCS_ASB3 cd03722
SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a ...
547-584 8.75e-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: 8.75e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1761178565 547 LAHLCRLRVRKAIGKYRIK---LLDTLPLPGRLIRYLKYEN 584
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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