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Conserved domains on  [gi|23956122|ref|NP_075536|]
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ankyrin repeat and SOCS box protein 2 isoform 1 [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];
119-400 1.50e-45

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 163.59  E-value: 1.50e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 119 EALKIMIQDGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQQAYPGTIDQRTLQEETALYLATCREHLDCLLSLLQAGAEP 198
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 199 DISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVA 278
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 279 AQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLLP 358
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 23956122 359 VTSR-TRVRRSGISPLHLAAERNHDAVLEALLAARFDVNAPLA 400
Cdd:COG0666 241 AGADlNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
SOCS super family cl02533
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
590-634 2.81e-23

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


The actual alignment was detected with superfamily member cd03721:

Pssm-ID: 470605  Cd Length: 45  Bit Score: 92.62  E-value: 2.81e-23
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 23956122 590 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ 634
Cdd:cd03721   1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ 45
Ank_2 pfam12796
Ankyrin repeats (3 copies);
373-469 5.22e-10

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 5.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122   373 LHLAAERNHDAVLEALLAARFDVNaplaperarLYEDRRSSALYFAVVNNNVYATELLLlAGADPNRDVI--SPLLVAIR 450
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDNgrTALHYAAR 70
                          90
                  ....*....|....*....
gi 23956122   451 HGCLRTMQLLLDHGANIDA 469
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
119-400 1.50e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 163.59  E-value: 1.50e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 119 EALKIMIQDGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQQAYPGTIDQRTLQEETALYLATCREHLDCLLSLLQAGAEP 198
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 199 DISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVA 278
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 279 AQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLLP 358
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 23956122 359 VTSR-TRVRRSGISPLHLAAERNHDAVLEALLAARFDVNAPLA 400
Cdd:COG0666 241 AGADlNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
PHA03095 PHA03095
ankyrin-like protein; Provisional
199-480 1.40e-24

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 107.42  E-value: 1.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  199 DISNKSRETPLYK---ACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRN---DLEVMEILVSGGAKVEAKNVYSI 272
Cdd:PHA03095   5 ESVDIIMEAALYDyllNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  273 TPLFVAAQSGQ-LEALRFLAKHGADINTQ--ASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHV--ASKK 347
Cdd:PHA03095  85 TPLHLYLYNATtLDVIKLLIKAGADVNAKdkVGRTPLHVYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVllKSRN 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  348 GNYRIVQMLLPVTSRTRVRRS-GISPLHLAAE--RNHDAVLEALLAARFDVNAPLAPERARLYED------RRS------ 412
Cdd:PHA03095 165 ANVELLRLLIDAGADVYAVDDrFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMatgsscKRSlvlpll 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  413 --------------SALYFAVVNNNVYATELLLLAGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHP 475
Cdd:PHA03095 245 iagisinarnrygqTPLHYAAVFNNPRACRRLIALGADINavsSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLN 324

                 ....*
gi 23956122  476 TAFPA 480
Cdd:PHA03095 325 TASVA 329
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
590-634 2.81e-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: 92.62  E-value: 2.81e-23
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 23956122 590 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ 634
Cdd:cd03721   1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ 45
Ank_2 pfam12796
Ankyrin repeats (3 copies);
176-268 3.63e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 3.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122   176 LYLATCREHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYnADANHRCNrGWTALHESVSRNDLEVME 255
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 23956122   256 ILVSGGAKVEAKN 268
Cdd:pfam12796  79 LLLEKGADINVKD 91
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
591-629 3.70e-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: 3.70e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 23956122   591 PPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLK 629
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
Ank_2 pfam12796
Ankyrin repeats (3 copies);
373-469 5.22e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 5.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122   373 LHLAAERNHDAVLEALLAARFDVNaplaperarLYEDRRSSALYFAVVNNNVYATELLLlAGADPNRDVI--SPLLVAIR 450
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDNgrTALHYAAR 70
                          90
                  ....*....|....*....
gi 23956122   451 HGCLRTMQLLLDHGANIDA 469
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
140-357 5.49e-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: 62.34  E-value: 5.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 140 LPLHEAAYYGQLGCLKVLQQAYPGTIDQRTLQEETALYLATCREHLDCLLSLLQAGaePDISNKSRETPLYKacerknae 219
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAA--PELVNEPMTSDLYQ-------- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 220 avrilvrynadanhrcnrGWTALHESVSRNDLEVMEILVSGGAKV------------EAKNV--YSITPLFVAAQSGQLE 285
Cdd:cd22192  89 ------------------GETALHIAVVNQNLNLVRELIARGADVvspratgtffrpGPKNLiyYGEHPLSFAACVGNEE 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 286 ALRFLAKHGADINTQASDSASALY----EASKNEHEDVVEFLLSQGADANKA------NKDGLLPLHVASKKGNYRIVQM 355
Cdd:cd22192 151 IVRLLIEHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQH 230

                ..
gi 23956122 356 LL 357
Cdd:cd22192 231 LV 232
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
593-631 4.03e-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: 4.03e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 23956122    593 RPLAHLCRLRVRKAIGKyriklLDTLPLPGRLIRYLKYE 631
Cdd:smart00969   1 RSLQHLCRLAIRRSLGG-----IDKLPLPPRLKDYLLYY 34
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
237-357 4.41e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 53.16  E-value: 4.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122   237 RGWTALHESVSRNDLEVMEILVSGGAKVEAKNV--------------YSITPLFVAAQSGQLEALRFLAKHGADINTQAS 302
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23956122   303 DS-----ASALYEASKNEHEDVV----EFLLSQGADANKA-------NKDGLLPLHVASKKGNYRIVQMLL 357
Cdd:TIGR00870 207 LGntllhLLVMENEFKAEYEELScqmyNFALSLLDKLRDSkelevilNHQGLTPLKLAAKEGRIVLFRLKL 277
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
339-486 8.07e-06

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: 48.86  E-value: 8.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 339 LPLHVASKKGNYRIVQMLLpVTSRTRVRRSGI---SPLHLAAERNHDAVLEALL-AARFDVNAPLAPErarLYEDRrsSA 414
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLL-KCPSCDLFQRGAlgeTALHVAALYDNLEAAVVLMeAAPELVNEPMTSD---LYQGE--TA 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 415 LYFAVVNNNVYATELLLLAGAD------------PNRDVI-----SPLLVAIRHGCLRTMQLLLDHGANIDA-------- 469
Cdd:cd22192  93 LHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIRAqdslgntv 172
                       170
                ....*....|....*....
gi 23956122 470 --YIATHPTAFPATIMFAM 486
Cdd:cd22192 173 lhILVLQPNKTFACQMYDL 191
PHA02884 PHA02884
ankyrin repeat protein; Provisional
384-503 1.57e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 47.29  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  384 VLEALLAARFDVNAPLAperarLYEDRRSSALYFAVVNNNVYATELLLLAGADPNR----DVISPLLVAIRHGCLRTMQL 459
Cdd:PHA02884  48 IIDAILKLGADPEAPFP-----LSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRyaeeAKITPLYISVLHGCLKCLEI 122
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 23956122  460 LLDHGANIDAYIATHPTAFPATIMFamkCLSLLKFLMdlgCDGE 503
Cdd:PHA02884 123 LLSYGADINIQTNDMVTPIELALMI---CNNFLAFMI---CDNE 160
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
337-469 4.96e-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: 43.15  E-value: 4.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122   337 GLLPLHVASKKGNYRIVQMLLPVTSRtRVRrSGISPLHLAAERNHDAVLEALL----AARFDVNAPLAPERA--RLYEDR 410
Cdd:TIGR00870  52 GRSALFVAAIENENLELTELLLNLSC-RGA-VGDTLLHAISLEYVDAVEAILLhllaAFRKSGPLELANDQYtsEFTPGI 129
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956122   411 rsSALYFAVVNNNVYATELLLLAGAD-PNRD-----VISPLLVAIRHGCLR-----------TMQLLLDHGANIDA 469
Cdd:TIGR00870 130 --TALHLAAHRQNYEIVKLLLERGASvPARAcgdffVKSQGVDSFYHGESPlnaaaclgspsIVALLSEDPADILT 203
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
273-298 1.47e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 1.47e-03
                           10        20
                   ....*....|....*....|....*.
gi 23956122    273 TPLFVAAQSGQLEALRFLAKHGADIN 298
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
119-400 1.50e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 163.59  E-value: 1.50e-45
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 119 EALKIMIQDGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQQAYPGTIDQRTLQEETALYLATCREHLDCLLSLLQAGAEP 198
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 199 DISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVA 278
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLA 160
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 279 AQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLLP 358
Cdd:COG0666 161 AANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLE 240
                       250       260       270       280
                ....*....|....*....|....*....|....*....|...
gi 23956122 359 VTSR-TRVRRSGISPLHLAAERNHDAVLEALLAARFDVNAPLA 400
Cdd:COG0666 241 AGADlNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
110-357 1.11e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 158.19  E-value: 1.11e-43
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 110 LKAIKEGDEEALKIMIQDGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQQAYPGTIDQRTLQEETALYLATCREHLDCLL 189
Cdd:COG0666  25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 190 SLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKNV 269
Cdd:COG0666 105 LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDN 184
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 270 YSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGN 349
Cdd:COG0666 185 DGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGA 264

                ....*...
gi 23956122 350 YRIVQMLL 357
Cdd:COG0666 265 ALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
165-438 1.63e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.42  E-value: 1.63e-41
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 165 IDQRTLQEETALYLATCREHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHE 244
Cdd:COG0666  14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHA 93
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 245 SVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLL 324
Cdd:COG0666  94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 325 SQGADANKANKDGLLPLHVASKKGNYRIVQMLL----PVTSRTRvrrSGISPLHLAAERNHDAVLEALLAARFDVNAPLa 400
Cdd:COG0666 174 EAGADVNARDNDGETPLHLAAENGHLEIVKLLLeagaDVNAKDN---DGKTALDLAAENGNLEIVKLLLEAGADLNAKD- 249
                       250       260       270
                ....*....|....*....|....*....|....*...
gi 23956122 401 perarlyeDRRSSALYFAVVNNNVYATELLLLAGADPN 438
Cdd:COG0666 250 --------KDGLTALLLAAAAGAALIVKLLLLALLLLA 279
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
110-341 5.16e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.18  E-value: 5.16e-40
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 110 LKAIKEGDEEALKIMIQDGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQQAyPGTIDQRTLQEETALYLATCREHLDCLL 189
Cdd:COG0666  59 LAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLEIVK 137
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 190 SLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKNV 269
Cdd:COG0666 138 LLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDN 217
                       170       180       190       200       210       220       230
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23956122 270 YSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPL 341
Cdd:COG0666 218 DGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
188-477 6.47e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 136.62  E-value: 6.47e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 188 LLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAK 267
Cdd:COG0666   4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 268 NVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGllplhvaskk 347
Cdd:COG0666  84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDG---------- 153
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 348 gnyrivqmllpvtsrtrvrrsgISPLHLAAERNHDAVLEALLAARFDVNAPlaperarlyEDRRSSALYFAVVNNNVYAT 427
Cdd:COG0666 154 ----------------------NTPLHLAAANGNLEIVKLLLEAGADVNAR---------DNDGETPLHLAAENGHLEIV 202
                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|...
gi 23956122 428 ELLLLAGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTA 477
Cdd:COG0666 203 KLLLEAGADVNakdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTA 255
PHA03095 PHA03095
ankyrin-like protein; Provisional
199-480 1.40e-24

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 107.42  E-value: 1.40e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  199 DISNKSRETPLYK---ACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRN---DLEVMEILVSGGAKVEAKNVYSI 272
Cdd:PHA03095   5 ESVDIIMEAALYDyllNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGF 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  273 TPLFVAAQSGQ-LEALRFLAKHGADINTQ--ASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHV--ASKK 347
Cdd:PHA03095  85 TPLHLYLYNATtLDVIKLLIKAGADVNAKdkVGRTPLHVYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVllKSRN 164
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  348 GNYRIVQMLLPVTSRTRVRRS-GISPLHLAAE--RNHDAVLEALLAARFDVNAPLAPERARLYED------RRS------ 412
Cdd:PHA03095 165 ANVELLRLLIDAGADVYAVDDrFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMatgsscKRSlvlpll 244
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  413 --------------SALYFAVVNNNVYATELLLLAGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHP 475
Cdd:PHA03095 245 iagisinarnrygqTPLHYAAVFNNPRACRRLIALGADINavsSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLN 324

                 ....*
gi 23956122  476 TAFPA 480
Cdd:PHA03095 325 TASVA 329
PHA02876 PHA02876
ankyrin repeat protein; Provisional
153-469 1.95e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 108.23  E-value: 1.95e-24
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  153 CLKVLQQAYPGTIDQRTLQEETALYLATCREHL--DCLL---SLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRY 227
Cdd:PHA02876 121 CIHILKEAISGNDIHYDKINESIEYMKLIKERIqqDELLiaeMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSY 200
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  228 NADAN-----------------------------HRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVA 278
Cdd:PHA02876 201 GADVNiialddlsvlecavdsknidtikaiidnrSNINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHA 280
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  279 AQSGQLEAL-RFLAKHGADINTQASDSASALYEASKNEHE-DVVEFLLSQGADANKANKDGLLPLHVASKKGNYR-IVQM 355
Cdd:PHA02876 281 SQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVIT 360
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  356 LLPVTSRTRVRR-SGISPLHLAAERNHDAVLEALLAARFDVNAplaperarlYEDRRSSALYFAVVNNNVY-ATELLLLA 433
Cdd:PHA02876 361 LLELGANVNARDyCDKTPIHYAAVRNNVVIINTLLDYGADIEA---------LSQKIGTALHFALCGTNPYmSVKTLIDR 431
                        330       340       350       360
                 ....*....|....*....|....*....|....*....|
gi 23956122  434 GAD---PNRDVISPLLVAIRHGC-LRTMQLLLDHGANIDA 469
Cdd:PHA02876 432 GANvnsKNKDLSTPLHYACKKNCkLDVIEMLLDNGADVNA 471
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
590-634 2.81e-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: 92.62  E-value: 2.81e-23
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 23956122 590 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ 634
Cdd:cd03721   1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ 45
PHA03100 PHA03100
ankyrin repeat protein; Provisional
176-397 1.89e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.43  E-value: 1.89e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  176 LYLATCREHLDCLLSLLQAGAEPDISNKSRETPL-----YKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSR-- 248
Cdd:PHA03100  39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKks 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  249 NDLEVMEILVSGGAKVEAKNVYSITPLFVAAQSGQ--LEALRFLAKHGADINTqasdsasalyeasknehEDVVEFLLSQ 326
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINA-----------------KNRVNYLLSY 181
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23956122  327 GADANKANKDGLLPLHVASKKGNYRIVQMLLPVTSRTRVR-RSGISPLHLAAERNHDAVLEALLAARFDVNA 397
Cdd:PHA03100 182 GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVnKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
284-501 3.11e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 94.25  E-value: 3.11e-21
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 284 LEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLL-PVTSR 362
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLaAGADI 80
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 363 TRVRRSGISPLHLAAERNHDAVLEALLAARFDVNAPlaperarlyEDRRSSALYFAVVNNNVYATELLLLAGADPN---R 439
Cdd:COG0666  81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNAR---------DKDGETPLHLAAYNGNLEIVKLLLEAGADVNaqdN 151
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23956122 440 DVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAfpatIMFAMKC--LSLLKFLMDLGCD 501
Cdd:COG0666 152 DGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETP----LHLAAENghLEIVKLLLEAGAD 211
Ank_2 pfam12796
Ankyrin repeats (3 copies);
176-268 3.63e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.77  E-value: 3.63e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122   176 LYLATCREHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYnADANHRCNrGWTALHESVSRNDLEVME 255
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 23956122   256 ILVSGGAKVEAKN 268
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
92-406 6.47e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 86.56  E-value: 6.47e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122   92 KYSSNLFKTSQMAAMDPVLKAIKEGDEEALKIMIQDGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLqqaypgtIDQRTlq 171
Cdd:PHA02874  22 KNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLL-------IDNGV-- 92
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  172 eETALYLATCREHlDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRNDL 251
Cdd:PHA02874  93 -DTSILPIPCIEK-DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFF 170
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  252 EVMEILVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNeHEDVVEFLLSQgADAN 331
Cdd:PHA02874 171 DIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIH-NRSAIELLINN-ASIN 248
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 23956122  332 KANKDGLLPLHVA-SKKGNYRIVQMLLPVTSRTRVR-RSGISPLHLAAER-NHDAVLEALLAarfdvNAPLAPERARL 406
Cdd:PHA02874 249 DQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKdNKGENPIDTAFKYiNKDPVIKDIIA-----NAVLIKEADKL 321
PHA02878 PHA02878
ankyrin repeat protein; Provisional
184-463 2.11e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 85.32  E-value: 2.11e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  184 HLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVR-YNadanhRCNRGWT--ALHESVSRNDLEVMEILVSG 260
Cdd:PHA02878  49 NLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRsIN-----KCSVFYTlvAIKDAFNNRNVEIFKIILTN 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  261 gakvEAKNVYSITPLFVAAQSG----QLEALRFLAKHGADINTQASDS-ASALYEASKNEHEDVVEFLLSQGADANKANK 335
Cdd:PHA02878 124 ----RYKNIQTIDLVYIDKKSKddiiEAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDK 199
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  336 DGLLPLHVASKKGNYRIVQMLLPVTSRTRVRRS-GISPLHLAAERNHD-AVLEALLAARFDVNAPLAPerarlyedRRSS 413
Cdd:PHA02878 200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKcGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYI--------LGLT 271
                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....
gi 23956122  414 ALYFAVVNNNVyaTELLLLAGADPNR---DVISPLLVAIR-HGCLRTMQLLLDH 463
Cdd:PHA02878 272 ALHSSIKSERK--LKLLLEYGADINSlnsYKLTPLSSAVKqYLCINIGRILISN 323
Ank_2 pfam12796
Ankyrin repeats (3 copies);
308-397 2.89e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.08  E-value: 2.89e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122   308 LYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLLPvTSRTRVRRSGISPLHLAAERNHDAVLEA 387
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKL 79
                          90
                  ....*....|
gi 23956122   388 LLAARFDVNA 397
Cdd:pfam12796  80 LLEKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
267-473 1.26e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.41  E-value: 1.26e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  267 KNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEH--EDVVE---FLLSQGADANKANKDGLLPL 341
Cdd:PHA03100  31 SYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnlTDVKEivkLLLEYGANVNAPDNNGITPL 110
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  342 HVAS--KKGNYRIVQMLLPVTSRTRVRRS-GISPLHLAAERNHD--AVLEALLAARFDVNA------------PLapera 404
Cdd:PHA03100 111 LYAIskKSNSYSIVEYLLDNGANVNIKNSdGENLLHLYLESNKIdlKILKLLIDKGVDINAknrvnyllsygvPI----- 185
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 23956122  405 rLYEDRR-SSALYFAVVNNNVYATELLLLAGADPN-RDVI--SPLLVAIRHGCLRTMQLLLDHGANIDAYIAT 473
Cdd:PHA03100 186 -NIKDVYgFTPLHYAVYNNNPEFVKYLLDLGANPNlVNKYgdTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA02878 PHA02878
ankyrin repeat protein; Provisional
174-313 3.23e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 81.85  E-value: 3.23e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  174 TALYLATCREHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSR-NDLE 252
Cdd:PHA02878 170 TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYD 249
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23956122  253 VMEILVSGGAKVEAKN-VYSITPLFVAAQSGQleALRFLAKHGADINTQASDSASALYEASK 313
Cdd:PHA02878 250 ILKLLLEHGVDVNAKSyILGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVK 309
Ank_2 pfam12796
Ankyrin repeats (3 copies);
242-334 3.46e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.00  E-value: 3.46e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122   242 LHESVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHgADINTQASDSaSALYEASKNEHEDVVE 321
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 23956122   322 FLLSQGADANKAN 334
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
275-357 5.21e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.61  E-value: 5.21e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122   275 LFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQgADANKANkDGLLPLHVASKKGNYRIVQ 354
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                  ...
gi 23956122   355 MLL 357
Cdd:pfam12796  79 LLL 81
PHA02875 PHA02875
ankyrin repeat protein; Provisional
108-298 6.42e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.42  E-value: 6.42e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  108 PVLKAIKEGDEEALKIMIQDGK--NLAEPNKEGwlPLHEAAYYGQLGCLKVLQQAYPGTIDQRTLQEETALYLATCREHL 185
Cdd:PHA02875  38 PIKLAMKFRDSEAIKLLMKHGAipDVKYPDIES--ELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKL 115
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  186 DCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVE 265
Cdd:PHA02875 116 DIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 23956122  266 --AKNVySITPLFVAAQSGQLEALRFLAKHGADIN 298
Cdd:PHA02875 196 yfGKNG-CVAALCYAIENNKIDIVRLFIKRGADCN 229
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
188-336 3.01e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 79.53  E-value: 3.01e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  188 LLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAkveAK 267
Cdd:PLN03192 541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS---IS 617
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  268 NVYSITPLF-VAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKD 336
Cdd:PLN03192 618 DPHAAGDLLcTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
PHA02875 PHA02875
ankyrin repeat protein; Provisional
185-396 3.11e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 78.11  E-value: 3.11e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  185 LDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKv 264
Cdd:PHA02875  15 LDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKF- 93
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  265 eAKNVY---SITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPL 341
Cdd:PHA02875  94 -ADDVFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPL 172
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 23956122  342 HVASKKGNYRIVQMLLPVTSRTRV--RRSGISPLHLAAERNHDAVLEALLAARFDVN 396
Cdd:PHA02875 173 IIAMAKGDIAICKMLLDSGANIDYfgKNGCVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02876 PHA02876
ankyrin repeat protein; Provisional
242-501 2.14e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.64  E-value: 2.14e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  242 LHESVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEA--SKN----- 314
Cdd:PHA02876 149 IKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAvdSKNidtik 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  315 --------------------EHED------------------------------------VVEFLLSQGADANKANKDGL 338
Cdd:PHA02876 229 aiidnrsninkndlsllkaiRNEDletslllydagfsvnsiddckntplhhasqapslsrLVPKLLERGADVNAKNIKGE 308
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  339 LPLHVASKKG----NYRIVQMLLPVTSRTrvRRSGISPLHLAA--ERNHDAVLeALLAARFDVNaplaperARLYEDRrs 412
Cdd:PHA02876 309 TPLYLMAKNGydteNIRTLIMLGADVNAA--DRLYITPLHQAStlDRNKDIVI-TLLELGANVN-------ARDYCDK-- 376
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  413 SALYFAVVNNNVYATELLLLAGADPnrDVISPLLVAIRHGCL------RTMQLLLDHGANIDA---YIAThptafPATIM 483
Cdd:PHA02876 377 TPIHYAAVRNNVVIINTLLDYGADI--EALSQKIGTALHFALcgtnpyMSVKTLIDRGANVNSknkDLST-----PLHYA 449
                        330
                 ....*....|....*....
gi 23956122  484 FAMKC-LSLLKFLMDLGCD 501
Cdd:PHA02876 450 CKKNCkLDVIEMLLDNGAD 468
PHA02876 PHA02876
ankyrin repeat protein; Provisional
109-367 2.93e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.26  E-value: 2.93e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  109 VLKAIKEGDEEALKIMIQDGKNLAEPNKEGWLPLHEAAYYGQLGCL--KVLQQAypGTIDQRTLQEETALYL-ATCREHL 185
Cdd:PHA02876 244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvpKLLERG--ADVNAKNIKGETPLYLmAKNGYDT 321
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  186 DCLLSLLQAGAEPDISNKSRETPLYKACE-RKNAEAVRILVRYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKV 264
Cdd:PHA02876 322 ENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  265 EAKNVYSITPL-FVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHE-DVVEFLLSQGADANKANKDGLLPLH 342
Cdd:PHA02876 402 EALSQKIGTALhFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLL 481
                        250       260
                 ....*....|....*....|....*
gi 23956122  343 VAskKGNYRIVQMLLPVTSRTRVRR 367
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 ...
590-631 9.59e-14

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


Pssm-ID: 239686  Cd Length: 42  Bit Score: 65.59  E-value: 9.59e-14
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 23956122 590 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 631
Cdd:cd03716   1 STPRSLQHLCRLAIRRCLGRRRLELIKKLPLPPRLKDYLLYE 42
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
592-631 1.44e-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: 1.44e-13
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 23956122 592 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 631
Cdd:cd03587   2 PRSLQHLCRLAIRRCLGKRRLDLIDKLPLPPRLKDYLLYK 41
PHA03095 PHA03095
ankyrin-like protein; Provisional
110-358 1.83e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.14  E-value: 1.83e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  110 LKAIKEGDEEALKIMIQDGKNLAEPNKEGWLPLHEAAYYGQ-LGCLKVLQQA-----YPGTIDQRTLQeetaLYLATCRE 183
Cdd:PHA03095  55 LHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAgadvnAKDKVGRTPLH----VYLSGFNI 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  184 HLDCLLSLLQAGAEPDISNKSRETPLYKACERKNA--EAVRILVRYNADANHRCNRGWTALH---ESVsRNDLEVMEILV 258
Cdd:PHA03095 131 NPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNAnvELLRLLIDAGADVYAVDDRFRSLLHhhlQSF-KPRARIVRELI 209
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  259 SGGAKVEAKNVYSITPLFVAAQSGQLEA--LRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKD 336
Cdd:PHA03095 210 RAGCDPAATDMLGNTPLHSMATGSSCKRslVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSD 289
                        250       260
                 ....*....|....*....|..
gi 23956122  337 GLLPLHVASKKGNYRIVQMLLP 358
Cdd:PHA03095 290 GNTPLSLMVRNNNGRAVRAALA 311
PHA02875 PHA02875
ankyrin repeat protein; Provisional
278-475 1.08e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 70.41  E-value: 1.08e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  278 AAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLL 357
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  358 PVTSRTR--VRRSGISPLHLAAERNHDAVLEALLAARFDVNAPlaperarlyEDRRSSALYFAVVNNNVYATELLLLAGA 435
Cdd:PHA02875  89 DLGKFADdvFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP---------NTDKFSPLHLAVMMGDIKGIELLIDHKA 159
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 23956122  436 DPNRD---VISPLLVAIRHGCLRTMQLLLDHGANIDaYIATHP 475
Cdd:PHA02875 160 CLDIEdccGCTPLIIAMAKGDIAICKMLLDSGANID-YFGKNG 201
Ank_2 pfam12796
Ankyrin repeats (3 copies);
112-202 1.56e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.90  E-value: 1.56e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122   112 AIKEGDEEALKIMIQDGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQQAYPGtidQRTLQEETALYLATCREHLDCLLSL 191
Cdd:pfam12796   4 AAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEIVKLL 80
                          90
                  ....*....|.
gi 23956122   192 LQAGAEPDISN 202
Cdd:pfam12796  81 LEKGADINVKD 91
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
591-629 3.70e-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: 3.70e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 23956122   591 PPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLK 629
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
PHA02874 PHA02874
ankyrin repeat protein; Provisional
271-467 1.39e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.83  E-value: 1.39e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  271 SITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANkankdgLLPLHVASKKGNY 350
Cdd:PHA02874  35 TTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTS------ILPIPCIEKDMIK 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  351 RIVQMLLPVTSRTRVRRSGispLHLAAERNHDAVLEALLAARFDVNaplaperarLYEDRRSSALYFAVVNNNVYATELL 430
Cdd:PHA02874 109 TILDCGIDVNIKDAELKTF---LHYAIKKGDLESIKMLFEYGADVN---------IEDDNGCYPIHIAIKHNFFDIIKLL 176
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 23956122  431 LLAGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANI 467
Cdd:PHA02874 177 LEKGAYANvkdNNGESPLHNAAEYGDYACIKLLIDHGNHI 216
Ank_2 pfam12796
Ankyrin repeats (3 copies);
373-469 5.22e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 56.28  E-value: 5.22e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122   373 LHLAAERNHDAVLEALLAARFDVNaplaperarLYEDRRSSALYFAVVNNNVYATELLLlAGADPNRDVI--SPLLVAIR 450
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKDNgrTALHYAAR 70
                          90
                  ....*....|....*....
gi 23956122   451 HGCLRTMQLLLDHGANIDA 469
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
140-357 5.49e-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: 62.34  E-value: 5.49e-10
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 140 LPLHEAAYYGQLGCLKVLQQAYPGTIDQRTLQEETALYLATCREHLDCLLSLLQAGaePDISNKSRETPLYKacerknae 219
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAA--PELVNEPMTSDLYQ-------- 88
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 220 avrilvrynadanhrcnrGWTALHESVSRNDLEVMEILVSGGAKV------------EAKNV--YSITPLFVAAQSGQLE 285
Cdd:cd22192  89 ------------------GETALHIAVVNQNLNLVRELIARGADVvspratgtffrpGPKNLiyYGEHPLSFAACVGNEE 150
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 286 ALRFLAKHGADINTQASDSASALY----EASKNEHEDVVEFLLSQGADANKA------NKDGLLPLHVASKKGNYRIVQM 355
Cdd:cd22192 151 IVRLLIEHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILSYDKEDDLQpldlvpNNQGLTPFKLAAKEGNIVMFQH 230

                ..
gi 23956122 356 LL 357
Cdd:cd22192 231 LV 232
Ank_4 pfam13637
Ankyrin repeats (many copies);
273-324 7.48e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.97  E-value: 7.48e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 23956122   273 TPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLL 324
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
306-357 1.24e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.20  E-value: 1.24e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 23956122   306 SALYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLL 357
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
300-469 5.21e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.74  E-value: 5.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  300 QASDSASA-----LYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLLPVTSRTRV--------- 365
Cdd:PHA02878  28 NYSTSASLipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVfytlvaikd 107
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  366 ----------------RRSGISPLHLAA--ERNHDAVLEA-----LLAARFDVNaplaperaRLYEDRRSSALYFAVVNN 422
Cdd:PHA02878 108 afnnrnveifkiiltnRYKNIQTIDLVYidKKSKDDIIEAeitklLLSYGADIN--------MKDRHKGNTALHYATENK 179
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 23956122  423 NVYATELLLLAGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDA 469
Cdd:PHA02878 180 DQRLTELLLSYGANVNipdKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
PHA03100 PHA03100
ankyrin repeat protein; Provisional
111-299 1.11e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 57.75  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  111 KAIKEGDEEALKIMIQDGKNLAEPNKEGWLPLHEAAYY--GQLGCLKVLQQaYPGTIDQRTLQEETAL--YLATCREHLD 186
Cdd:PHA03100  79 KYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLD-NGANVNIKNSDGENLLhlYLESNKIDLK 157
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  187 CLLSLLQAGAepDISNKSRetplykacerknaeaVRILVRYNADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEA 266
Cdd:PHA03100 158 ILKLLIDKGV--DINAKNR---------------VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNL 220
                        170       180       190
                 ....*....|....*....|....*....|...
gi 23956122  267 KNVYSITPLFVAAQSGQLEALRFLAKHGADINT 299
Cdd:PHA03100 221 VNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA03095 PHA03095
ankyrin-like protein; Provisional
118-326 2.59e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 56.57  E-value: 2.59e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  118 EEALKIMIQDGKNLAEPNKEGWLPLHEaayygqlgCLKVLQqAYPGTIdqRTLQEETA------LYLATcreHLDCLLS- 190
Cdd:PHA03095  97 LDVIKLLIKAGADVNAKDKVGRTPLHV--------YLSGFN-INPKVI--RLLLRKGAdvnaldLYGMT---PLAVLLKs 162
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  191 ----------LLQAGAEPDISNKSRETPLYKACE--RKNAEAVRILVRYNADANHRCNRGWTALHE--SVSRNDLEVMEI 256
Cdd:PHA03095 163 rnanvellrlLIDAGADVYAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSmaTGSSCKRSLVLP 242
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  257 LVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQ 326
Cdd:PHA03095 243 LLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
PHA02859 PHA02859
ankyrin repeat protein; Provisional
202-348 3.16e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 54.44  E-value: 3.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  202 NKSRETPLYKACERKNA--EAVRILVRYNADANHRC-NRGWTALHESVSRN---DLEVMEILVSGGAKVEAKNVYSITPL 275
Cdd:PHA02859  48 NDLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTrDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLL 127
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956122  276 --FVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHED-VVEFLLSQGADANKANKDGLLPLHVASKKG 348
Cdd:PHA02859 128 hmYMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILFHSDKkIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
593-631 4.03e-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: 4.03e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 23956122    593 RPLAHLCRLRVRKAIGKyriklLDTLPLPGRLIRYLKYE 631
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 ...
592-631 7.76e-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: 48.84  E-value: 7.76e-08
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 23956122 592 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 631
Cdd:cd03718   3 PLPLMDLCRRRVRVALGRDRLEEIEQLPLPPSLKNYLLYQ 42
SOCS_ASB14 cd03730
SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a ...
590-631 1.48e-07

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


Pssm-ID: 239700  Cd Length: 57  Bit Score: 48.30  E-value: 1.48e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 23956122 590 EPPRPLAHLCRLRVRKAIGKYRIK---LLDTLPLPGRLIRYLKYE 631
Cdd:cd03730   1 TNPRSLKHLCRLKIRACMGRLRLRcpvFMSFLPLPNRLKAYILYK 45
SOCS_ASB1 cd03720
SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a ...
592-631 1.54e-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: 1.54e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 23956122 592 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 631
Cdd:cd03720   3 PRSLLSLCRIAVRRALGKQRLSLICSLPLPDPIKKFLLHE 42
PHA02798 PHA02798
ankyrin-like protein; Provisional
221-450 2.44e-07

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 53.69  E-value: 2.44e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  221 VRILVRYNADANHRCNRGWTALHESVSR---NDLEVMEILVSGGAKVEAKNVYSITPLFVAAQSG---QLEALRFLAKHG 294
Cdd:PHA02798  92 VKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKG 171
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  295 ADINTQAS----DSASALYEASKNEHE-DVVEFLLSQGADANKANK-------DGLLPLHVASKKGNYRIVQMLLPVTSR 362
Cdd:PHA02798 172 VDINTHNNkekyDTLHCYFKYNIDRIDaDILKLFVDNGFIINKENKshkkkfmEYLNSLLYDNKRFKKNILDFIFSYIDI 251
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  363 TRVRRSGISPLHLAAERNHDAVLEALLAARFDVNaplaperarLYEDRRSSALYFAVVNNNVYATELLLlaGADPNRDVI 442
Cdd:PHA02798 252 NQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDIN---------IITELGNTCLFTAFENESKFIFNSIL--NKKPNKNTI 320

                 ....*...
gi 23956122  443 SPLLVAIR 450
Cdd:PHA02798 321 SYTYYKLR 328
Ank_4 pfam13637
Ankyrin repeats (many copies);
106-157 2.97e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 2.97e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 23956122   106 MDPVLKAIKEGDEEALKIMIQDGKNLAEPNKEGWLPLHEAAYYGQLGCLKVL 157
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
592-630 3.21e-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: 3.21e-07
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 23956122 592 PRPLAHLCRLRVRKAIGKYRIkllDTLPLPGRLIRYLKY 630
Cdd:cd03717   3 VRSLQHLCRFVIRQCTRRDLI---DQLPLPRRLKDYLKE 38
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
279-357 4.20e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 4.20e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 23956122  279 AQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLL 357
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
237-357 4.41e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 53.16  E-value: 4.41e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122   237 RGWTALHESVSRNDLEVMEILVSGGAKVEAKNV--------------YSITPLFVAAQSGQLEALRFLAKHGADINTQAS 302
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 23956122   303 DS-----ASALYEASKNEHEDVV----EFLLSQGADANKA-------NKDGLLPLHVASKKGNYRIVQMLL 357
Cdd:TIGR00870 207 LGntllhLLVMENEFKAEYEELScqmyNFALSLLDKLRDSkelevilNHQGLTPLKLAAKEGRIVLFRLKL 277
SOCS_SSB4 cd03743
SOCS (suppressors of cytokine signaling) box of SSB4 (SPRY domain-containing SOCS box ...
592-631 4.73e-07

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


Pssm-ID: 239712  Cd Length: 42  Bit Score: 46.49  E-value: 4.73e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 23956122 592 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 631
Cdd:cd03743   3 PLPLMDLCRRSARQALGRHRLHHIQSLPLPQTLKNYLQYQ 42
SOCS_SOCS7 cd03741
SOCS (suppressors of cytokine signaling) box of SOCS7-like proteins. Together with CIS1, the ...
593-632 8.18e-07

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


Pssm-ID: 239710  Cd Length: 49  Bit Score: 46.24  E-value: 8.18e-07
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 23956122 593 RPLAHLCRLRVRKAIgkyRIKLLDTLPLPGRLIRYLKYEN 632
Cdd:cd03741   4 QSLQHLCRFVIRKLV---RRDHIPALPLPRRLIDYLREKH 40
Ank_5 pfam13857
Ankyrin repeats (many copies);
191-243 1.10e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 45.80  E-value: 1.10e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 23956122   191 LLQAG-AEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALH 243
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
151-357 1.10e-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: 51.80  E-value: 1.10e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 151 LGCLKVLQQAYPGTIDQRTLQEETALYLATCREH---LDCLLSLLQAGaepdisnksretplykacerKNAEAVRILVry 227
Cdd:cd21882   5 LGLLECLRWYLTDSAYQRGATGKTCLHKAALNLNdgvNEAIMLLLEAA--------------------PDSGNPKELV-- 62
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 228 NADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKNV-------------YSITPLFVAAQSGQLEALRFLAKHG 294
Cdd:cd21882  63 NAPCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENG 142
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 295 ADI-NTQASDSAS-----ALYEASKNEHED------VVEFLLSQGADANK-------ANKDGLLPLHVASKKGNYRIVQM 355
Cdd:cd21882 143 AQPaALEAQDSLGntvlhALVLQADNTPENsafvcqMYNLLLSYGAHLDPtqqleeiPNHQGLTPLKLAAVEGKIVMFQH 222

                ..
gi 23956122 356 LL 357
Cdd:cd21882 223 IL 224
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
242-436 1.77e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.02  E-value: 1.77e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  242 LHESVSRNDLEVMEILVSGGAkvEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVE 321
Cdd:PLN03192 498 LQHHKELHDLNVGDLLGDNGG--EHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVL 575
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  322 FLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLLPVTSRTRVRRSGiSPLHLAAERNHDAVLEALLAARFDVNAplap 401
Cdd:PLN03192 576 VLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDS---- 650
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 23956122  402 erarlyEDRR-SSALYFAVVNNNVYATELLLLAGAD 436
Cdd:PLN03192 651 ------EDHQgATALQVAMAEDHVDMVRLLIMNGAD 680
Ank_4 pfam13637
Ankyrin repeats (many copies);
205-258 2.35e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.96  E-value: 2.35e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 23956122   205 RETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHESVSRNDLEVMEILV 258
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SOCS smart00253
suppressors of cytokine signalling; suppressors of cytokine signalling
586-630 2.86e-06

suppressors of cytokine signalling; suppressors of cytokine signalling


Pssm-ID: 128549  Cd Length: 43  Bit Score: 44.21  E-value: 2.86e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 23956122    586 KEKAEPPRPLAHLCRLRVRKAIGKYRIKlldTLPLPGRLIRYLKY 630
Cdd:smart00253   1 LPRPSNVPSLQHLCRFTIRRCTRTDQIK---TLPLPPKLKDYLSY 42
PHA02946 PHA02946
ankyin-like protein; Provisional
191-375 5.99e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 49.28  E-value: 5.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  191 LLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRGWTALHeSVSRNDLEVME---ILVSGGAKVE-A 266
Cdd:PHA02946  58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY-YLSGTDDEVIErinLLVQYGAKINnS 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  267 KNVYSITPLFVAAQSGQLEALRFLA-KHGADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVAS 345
Cdd:PHA02946 137 VDEEGCGPLLACTDPSERVFKKIMSiGFEARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVC 216
                        170       180       190
                 ....*....|....*....|....*....|..
gi 23956122  346 KK--GNYRIVQMLLPVTSRTRVRRSGISPLHL 375
Cdd:PHA02946 217 SKtvKNVDIINLLLPSTDVNKQNKFGDSPLTL 248
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
219-357 6.33e-06

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 49.37  E-value: 6.33e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 219 EAVRILVRY-----------NADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKN--------------VYSIT 273
Cdd:cd22194 111 EIVRILLAFaeengildrfiNAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAkgvffnpkykhegfYFGET 190
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 274 PLFVAAQSGQLEALRFLAKHGADINTqASDSAS-----ALYEASKN--EHEDVV----EFLLSQGADAN---KANKDGLL 339
Cdd:cd22194 191 PLALAACTNQPEIVQLLMEKESTDIT-SQDSRGntvlhALVTVAEDskTQNDFVkrmyDMILLKSENKNletIRNNEGLT 269
                       170
                ....*....|....*...
gi 23956122 340 PLHVASKKGNYRIVQMLL 357
Cdd:cd22194 270 PLQLAAKMGKAEILKYIL 287
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
339-486 8.07e-06

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: 48.86  E-value: 8.07e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 339 LPLHVASKKGNYRIVQMLLpVTSRTRVRRSGI---SPLHLAAERNHDAVLEALL-AARFDVNAPLAPErarLYEDRrsSA 414
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLL-KCPSCDLFQRGAlgeTALHVAALYDNLEAAVVLMeAAPELVNEPMTSD---LYQGE--TA 92
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 415 LYFAVVNNNVYATELLLLAGAD------------PNRDVI-----SPLLVAIRHGCLRTMQLLLDHGANIDA-------- 469
Cdd:cd22192  93 LHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIRAqdslgntv 172
                       170
                ....*....|....*....
gi 23956122 470 --YIATHPTAFPATIMFAM 486
Cdd:cd22192 173 lhILVLQPNKTFACQMYDL 191
SOCS_SSB1 cd03744
SOCS (suppressors of cytokine signaling) box of SSB1 (SPRY domain-containing SOCS box proteins) ...
592-631 1.40e-05

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: 42.28  E-value: 1.40e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 23956122 592 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 631
Cdd:cd03744   3 PLPLMDLCRRSVRLALGRERLSEIHTLPLPASLKNYLLYQ 42
SOCS_SSB2 cd03719
SOCS (suppressors of cytokine signaling) box of SSB2 (SPRY domain-containing SOCS box proteins) ...
590-631 1.40e-05

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: 42.32  E-value: 1.40e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 23956122 590 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 631
Cdd:cd03719   1 AEPHSLLHLSRLCVRHALGDTRLGQVSALPLPPAMKRYLLYQ 42
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
590-631 1.47e-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: 42.90  E-value: 1.47e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*
gi 23956122 590 EPPRPLAHLCRLRVRKAIGKYRIKLLDT---LPLPGRLIRYLKYE 631
Cdd:cd03731   1 ENPRPLKHLCRLKIRKLMGLQKLQQPSSmkkLPLPPALKRYILYK 45
PHA02884 PHA02884
ankyrin repeat protein; Provisional
384-503 1.57e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 47.29  E-value: 1.57e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  384 VLEALLAARFDVNAPLAperarLYEDRRSSALYFAVVNNNVYATELLLLAGADPNR----DVISPLLVAIRHGCLRTMQL 459
Cdd:PHA02884  48 IIDAILKLGADPEAPFP-----LSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRyaeeAKITPLYISVLHGCLKCLEI 122
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 23956122  460 LLDHGANIDAYIATHPTAFPATIMFamkCLSLLKFLMdlgCDGE 503
Cdd:PHA02884 123 LLSYGADINIQTNDMVTPIELALMI---CNNFLAFMI---CDNE 160
SOCS_ASB13 cd03729
SOCS (suppressors of cytokine signaling) box of ASB13-like proteins. ASB family members have a ...
592-630 3.70e-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: 3.70e-05
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 23956122 592 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKY 630
Cdd:cd03729   3 PLSLQQLCRINLRKALGTRALEKIAKLNIPNRIIDYLSY 41
SOCS_ASB5 cd03724
SOCS (suppressors of cytokine signaling) box of ASB5-like proteins. ASB family members have a ...
592-630 4.31e-05

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


Pssm-ID: 239694  Cd Length: 42  Bit Score: 41.02  E-value: 4.31e-05
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 23956122 592 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKY 630
Cdd:cd03724   3 PSSLCQLCRLCIRNYIGRSRLHLIPQLQLPTLLKNFLQY 41
SOCS_ASB7 cd03726
SOCS (suppressors of cytokine signaling) box of ASB7-like proteins. ASB family members have a ...
592-631 5.10e-05

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


Pssm-ID: 239696  Cd Length: 45  Bit Score: 40.99  E-value: 5.10e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 23956122 592 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 631
Cdd:cd03726   3 PRTLQDLCRIKIRHCIGLQNLKLLDELPIAKVMKDYLKHK 42
PHA02878 PHA02878
ankyrin repeat protein; Provisional
108-225 5.80e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.03  E-value: 5.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  108 PVLKAIKEGDEEALKIMIQDGKNLAEPNKEGWLPLHEA-AYYGQLGCLKVLQQAYPGTIDQRTLQEETALYLATCREhlD 186
Cdd:PHA02878 204 PLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSE--R 281
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 23956122  187 CLLSLLQAGAEPDISNKSRETPLYKAC-ERKNAEAVRILV 225
Cdd:PHA02878 282 KLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRILI 321
Ank_4 pfam13637
Ankyrin repeats (many copies);
238-290 7.25e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 7.25e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 23956122   238 GWTALHESVSRNDLEVMEILVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFL 290
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
PHA02859 PHA02859
ankyrin repeat protein; Provisional
268-352 7.71e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.42  E-value: 7.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  268 NVYSITPLF--VAAQSGQLEALRFLAKHGADINTQASD---SASALYEA-SKNEHEDVVEFLLSQGADANKANKDGLLPL 341
Cdd:PHA02859  48 NDLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRDnnlSALHHYLSfNKNVEPEILKILIDSGSSITEEDEDGKNLL 127
                         90
                 ....*....|.
gi 23956122  342 HVASKKGNYRI 352
Cdd:PHA02859 128 HMYMCNFNVRI 138
PHA02798 PHA02798
ankyrin-like protein; Provisional
222-438 1.63e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.44  E-value: 1.63e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  222 RILVRYNADANHRcnrGWTALHESVSRND--LEVMEILVSGGAKVEAKNVYSITPLF-----VAAQSGQLEALRFLAKHG 294
Cdd:PHA02798  23 LLIKSCNPNEIVN---EYSIFQKYLQRDSpsTDIVKLFINLGANVNGLDNEYSTPLCtilsnIKDYKHMLDIVKILIENG 99
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  295 ADINTQASDSASALYEASKNEH---EDVVEFLLSQGADANKANKDGLLPLHVASKKGNY---RIVQMLLP--VTSRTRVR 366
Cdd:PHA02798 100 ADINKKNSDGETPLYCLLSNGYinnLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEkgVDINTHNN 179
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  367 RSGISPLHLAAERNHDA----VLEALLAARFDVNAPLAPERAR--------LYEDRRS---------------------- 412
Cdd:PHA02798 180 KEKYDTLHCYFKYNIDRidadILKLFVDNGFIINKENKSHKKKfmeylnslLYDNKRFkknildfifsyidinqvdelgf 259
                        250       260
                 ....*....|....*....|....*.
gi 23956122  413 SALYFAVVNNNVYATELLLLAGADPN 438
Cdd:PHA02798 260 NPLYYSVSHNNRKIFEYLLQLGGDIN 285
Ank_4 pfam13637
Ankyrin repeats (many copies);
174-225 1.71e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 1.71e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 23956122   174 TALYLATCREHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILV 225
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
237-357 2.46e-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: 2.46e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 237 RGWTALHESVSRNDLEVMEILVSGGAKVEAKN--------------VYSITPLFVAAQSGQLEALRFLAKH---GADINt 299
Cdd:cd22196  93 KGQTALHIAIERRNMHLVELLVQNGADVHARAsgeffkkkkggpgfYFGELPLSLAACTNQLDIVKFLLENphsPADIS- 171
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 23956122 300 qASDSAS-----ALYEASKNEHEDvVEF-------LLSQGADANK-------ANKDGLLPLHVASKKGNYRIVQMLL 357
Cdd:cd22196 172 -ARDSMGntvlhALVEVADNTPEN-TKFvtkmyneILILGAKIRPllkleeiTNKKGLTPLKLAAKTGKIGIFAYIL 246
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
237-357 2.62e-04

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 44.02  E-value: 2.62e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 237 RGWTALHESVSRNDLEVMEILVSGGAKVEAKN--------------VYSITPLFVAAQSGQLEALRFLAKHG-ADINTQA 301
Cdd:cd22193  75 EGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfYFGELPLSLAACTNQPDIVQYLLENEhQPADIEA 154
                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 23956122 302 SDSAS-----ALYEASKNEHED------VVEFLLSQGADANKA-------NKDGLLPLHVASKKGNYRIVQMLL 357
Cdd:cd22193 155 QDSRGntvlhALVTVADNTKENtkfvtrMYDMILIRGAKLCPTveleeirNNDGLTPLQLAAKMGKIEILKYIL 228
PHA02884 PHA02884
ankyrin repeat protein; Provisional
176-278 2.76e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 43.43  E-value: 2.76e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  176 LYLATCREHLDCLLSLLQAGAEPDI----SNKSRETPLYKACERKNAEAVRILVRYNADANHRCNRG-WTALHESVSRND 250
Cdd:PHA02884  37 LYSSIKFHYTDIIDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAkITPLYISVLHGC 116
                         90       100
                 ....*....|....*....|....*...
gi 23956122  251 LEVMEILVSGGAKVEAKNVYSITPLFVA 278
Cdd:PHA02884 117 LKCLEILLSYGADINIQTNDMVTPIELA 144
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
592-632 4.36e-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: 4.36e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 23956122 592 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYEN 632
Cdd:cd03723   3 PRSLQHLCRCAIRKLLGSRCHKLVPQLSLPTSLKNYLLLEP 43
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
337-469 4.96e-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: 43.15  E-value: 4.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122   337 GLLPLHVASKKGNYRIVQMLLPVTSRtRVRrSGISPLHLAAERNHDAVLEALL----AARFDVNAPLAPERA--RLYEDR 410
Cdd:TIGR00870  52 GRSALFVAAIENENLELTELLLNLSC-RGA-VGDTLLHAISLEYVDAVEAILLhllaAFRKSGPLELANDQYtsEFTPGI 129
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 23956122   411 rsSALYFAVVNNNVYATELLLLAGAD-PNRD-----VISPLLVAIRHGCLR-----------TMQLLLDHGANIDA 469
Cdd:TIGR00870 130 --TALHLAAHRQNYEIVKLLLERGASvPARAcgdffVKSQGVDSFYHGESPlnaaaclgspsIVALLSEDPADILT 203
PHA02946 PHA02946
ankyin-like protein; Provisional
309-357 5.70e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 42.73  E-value: 5.70e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*....
gi 23956122  309 YEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLL 357
Cdd:PHA02946  44 YCGIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLL 92
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
256-325 9.66e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 9.66e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  256 ILVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEFLLS 325
Cdd:PTZ00322 100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
273-298 1.47e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 1.47e-03
                           10        20
                   ....*....|....*....|....*.
gi 23956122    273 TPLFVAAQSGQLEALRFLAKHGADIN 298
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
228-357 2.13e-03

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 40.99  E-value: 2.13e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 228 NADANHRCNRGWTALHESVSRNDLEVMEILVSGGAKVEAKN-------------VYSITPLFVAAQSGQLEALRFLAKHG 294
Cdd:cd22197  84 NAQCTDEYYRGHSALHIAIEKRSLQCVKLLVENGADVHARAcgrffqkkqgtcfYFGELPLSLAACTKQWDVVNYLLENP 163
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 295 ADI-NTQASDSAS-----ALYEASKNEHED---VVEF---LLSQGADANKA-------NKDGLLPLHVASKKGNYRIVQM 355
Cdd:cd22197 164 HQPaSLQAQDSLGntvlhALVMIADNSPENsalVIKMydgLLQAGARLCPTvqleeisNHEGLTPLKLAAKEGKIEIFRH 243

                ..
gi 23956122 356 LL 357
Cdd:cd22197 244 IL 245
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
108-209 2.35e-03

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 40.32  E-value: 2.35e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122 108 PVLKAIKEGDEEALKIMIQDGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQQAYpGTIDQRTLQEETALYLATCREHLDC 187
Cdd:COG0666 189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAG-ADLNAKDKDGLTALLLAAAAGAALI 267
                        90       100
                ....*....|....*....|..
gi 23956122 188 LLSLLQAGAEPDISNKSRETPL 209
Cdd:COG0666 268 VKLLLLALLLLAAALLDLLTLL 289
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
273-299 2.43e-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: 35.70  E-value: 2.43e-03
                          10        20
                  ....*....|....*....|....*..
gi 23956122   273 TPLFVAAQSGQLEALRFLAKHGADINT 299
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
250-341 2.60e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.59  E-value: 2.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  250 DLEVMEILVSGGAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHE-----DVVEFLL 324
Cdd:PHA02798  17 KLSTVKLLIKSCNPNEIVNEYSIFQKYLQRDSPSTDIVKLFINLGANVNGLDNEYSTPLCTILSNIKDykhmlDIVKILI 96
                         90
                 ....*....|....*..
gi 23956122  325 SQGADANKANKDGLLPL 341
Cdd:PHA02798  97 ENGADINKKNSDGETPL 113
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
311-397 2.70e-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: 40.83  E-value: 2.70e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122   311 ASKNEHEDVVEFLLSQGADAnkANKDGLLplHVASKkGNYRIVQMLL------------------PVTSRTRVrrsGISP 372
Cdd:TIGR00870  60 AIENENLELTELLLNLSCRG--AVGDTLL--HAISL-EYVDAVEAILlhllaafrksgplelandQYTSEFTP---GITA 131
                          90       100
                  ....*....|....*....|....*
gi 23956122   373 LHLAAERNHDAVLEALLAARFDVNA 397
Cdd:TIGR00870 132 LHLAAHRQNYEIVKLLLERGASVPA 156
Ank_5 pfam13857
Ankyrin repeats (many copies);
290-344 3.18e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 3.18e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 23956122   290 LAKHG-ADINTQASDSASALYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVA 344
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
369-397 3.23e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 3.23e-03
                           10        20
                   ....*....|....*....|....*....
gi 23956122    369 GISPLHLAAERNHDAVLEALLAARFDVNA 397
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
323-376 3.24e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 3.24e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 23956122   323 LLSQG-ADANKANKDGLLPLHVASKKGNYRIVQMLL-PVTSRTRVRRSGISPLHLA 376
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLaYGVDLNLKDEEGLTALDLA 56
PHA03100 PHA03100
ankyrin repeat protein; Provisional
308-469 4.06e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 40.03  E-value: 4.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  308 LYEASKNEHEDVVEFLLSQGADANKANKDGLLPLHVASKKGNYRIVQMLLPVTSRTRVRRSGIS-PLHLAAERNHDA--- 383
Cdd:PHA03100   6 VLTKSRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNStPLHYLSNIKYNLtdv 85
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  384 --VLEALLAARFDVNAplaperarlYEDRRSSALYFAVVN--NNVYATELLLLAGADPN---RDVISPLLVAIRHGC--L 454
Cdd:PHA03100  86 keIVKLLLEYGANVNA---------PDNNGITPLLYAISKksNSYSIVEYLLDNGANVNiknSDGENLLHLYLESNKidL 156
                        170
                 ....*....|....*
gi 23956122  455 RTMQLLLDHGANIDA 469
Cdd:PHA03100 157 KILKLLIDKGVDINA 171
SOCS_WSB_SWIP cd03733
SOCS (suppressors of cytokine signaling) box of WSB/SWiP-like proteins. This subfamily ...
595-630 5.88e-03

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


Pssm-ID: 239702  Cd Length: 39  Bit Score: 35.09  E-value: 5.88e-03
                        10        20        30
                ....*....|....*....|....*....|....*.
gi 23956122 595 LAHLCRLRVRKAIGKYRIKlldTLPLPGRLIRYLKY 630
Cdd:cd03733   6 LQHLCRMALRRVMTTQQVL---ALPIPKKMKEFLTY 38
PHA02989 PHA02989
ankyrin repeat protein; Provisional
243-324 6.50e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 39.34  E-value: 6.50e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 23956122  243 HESVSRNDLEVMEILVSGgAKVEAKNVYSITPLFVAAQSGQLEALRFLAKHGADINTQASDSASALYEASKNEHEDVVEF 322
Cdd:PHA02989 229 NKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNR 307

                 ..
gi 23956122  323 LL 324
Cdd:PHA02989 308 IL 309
PHA03100 PHA03100
ankyrin repeat protein; Provisional
165-236 6.83e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 39.26  E-value: 6.83e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 23956122  165 IDQRTLQEETALYLATCREHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVRILVRYNADANHRCN 236
Cdd:PHA03100 185 INIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIE 256
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
237-266 7.46e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 7.46e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 23956122    237 RGWTALHESVSRNDLEVMEILVSGGAKVEA 266
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
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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