NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|1622956760|ref|XP_028707612|]
View 

ankyrin repeat and SOCS box protein 2 isoform X1 [Macaca mulatta]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
280-555 7.66e-51

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 179.76  E-value: 7.66e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 280 IKEGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKS 359
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 360 RETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAKVESKNAYGITPLFVAAQSGQL 439
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 440 EALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSR-T 518
Cdd:COG0666   167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADlN 246
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1622956760 519 RVRRSGVSPLHLAAERNNDAVLEALLSARFDVNAPLA 555
Cdd:COG0666   247 AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
SOCS super family cl02533
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
746-790 4.65e-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: 92.24  E-value: 4.65e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1622956760 746 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ 790
Cdd:cd03721     1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ 45
Ank_2 pfam12796
Ankyrin repeats (3 copies);
528-624 2.40e-12

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 2.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 528 LHLAAERNNDAVLEALLSARFDVNaplaperarLYEDRRSSALYFAVVNNNVYATELLLEHgADPNRDVI--SPLLVAIR 605
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNgrTALHYAAR 70
                          90
                  ....*....|....*....
gi 1622956760 606 HGCLRTMQLLLDHGANIDA 624
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
280-555 7.66e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 179.76  E-value: 7.66e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 280 IKEGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKS 359
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 360 RETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAKVESKNAYGITPLFVAAQSGQL 439
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 440 EALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSR-T 518
Cdd:COG0666   167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADlN 246
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1622956760 519 RVRRSGVSPLHLAAERNNDAVLEALLSARFDVNAPLA 555
Cdd:COG0666   247 AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
PHA02876 PHA02876
ankyrin repeat protein; Provisional
320-624 4.52e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 107.84  E-value: 4.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 320 IDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVqhnaDTNHRCNRGWTALHE 399
Cdd:PHA02876  171 VNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII----DNRSNINKNDLSLLK 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 400 SVSRNDLEVMEILVNGGAKVESKNAYGITPLFVAAQSGQLEAL-RFLAKYGADINTQASDSASALYEACKNEHE-EVVEF 477
Cdd:PHA02876  247 AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRT 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 478 LLLQGADANKTNKDGLLPLHIASKKGNYR-IVQMLLPVTSRTRVRR-SGVSPLHLAAERNNDAVLEALLSARFDVNApla 555
Cdd:PHA02876  327 LIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDyCDKTPIHYAAVRNNVVIINTLLDYGADIEA--- 403
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622956760 556 perarlYEDRRSSALYFAVVNNNVY-ATELLLEHGAD---PNRDVISPLLVAIRHGC-LRTMQLLLDHGANIDA 624
Cdd:PHA02876  404 ------LSQKIGTALHFALCGTNPYmSVKTLIDRGANvnsKNKDLSTPLHYACKKNCkLDVIEMLLDNGADVNA 471
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
746-790 4.65e-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: 92.24  E-value: 4.65e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1622956760 746 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ 790
Cdd:cd03721     1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ 45
Ank_2 pfam12796
Ankyrin repeats (3 copies);
364-455 3.59e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 3.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 364 LYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNgGAKVESKNaYGITPLFVAAQSGQLEALR 443
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|..
gi 1622956760 444 FLAKYGADINTQ 455
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
528-624 2.40e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 2.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 528 LHLAAERNNDAVLEALLSARFDVNaplaperarLYEDRRSSALYFAVVNNNVYATELLLEHgADPNRDVI--SPLLVAIR 605
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNgrTALHYAAR 70
                          90
                  ....*....|....*....
gi 1622956760 606 HGCLRTMQLLLDHGANIDA 624
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
747-785 7.79e-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: 57.56  E-value: 7.79e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622956760 747 PPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLK 785
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
295-512 7.31e-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: 7.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 295 LPLHEAAYYGQLGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHLDCLLSLLQAGaePDISNKSRETPLYKacerknae 374
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAA--PELVNEPMTSDLYQ-------- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 375 avkilvqhnadtnhrcnrGWTALHESVSRNDLEVMEILVNGGAKVESKNA--------------YGITPLFVAAQSGQLE 440
Cdd:cd22192    89 ------------------GETALHIAVVNQNLNLVRELIARGADVVSPRAtgtffrpgpknliyYGEHPLSFAACVGNEE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 441 ALRFLAKYGADINTQASDSASALY----EACKNEHEEVVEFLLLQGADANK------TNKDGLLPLHIASKKGNYRIVQM 510
Cdd:cd22192   151 IVRLLIEHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQH 230

                  ..
gi 1622956760 511 LL 512
Cdd:cd22192   231 LV 232
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
749-787 5.31e-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: 5.31e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1622956760  749 RPLAHLCRLRVRKAIGKyriklLDTLPLPGRLIRYLKYE 787
Cdd:smart00969   1 RSLQHLCRLAIRRSLGG-----IDKLPLPPRLKDYLLYY 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
494-641 9.19e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.32  E-value: 9.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 494 LPLHIASKKGNYRIVQMLLpVTSRTRVRRSGV---SPLHLAAERNNDAVLEALL-SARFDVNAPLAPErarLYEDRrsSA 569
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLL-KCPSCDLFQRGAlgeTALHVAALYDNLEAAVVLMeAAPELVNEPMTSD---LYQGE--TA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 570 LYFAVVNNNVYATELLLEHGAD------------PNRDVI-----SPLLVAIRHGCLRTMQLLLDHGANIDA-------- 624
Cdd:cd22192    93 LHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIRAqdslgntv 172
                         170
                  ....*....|....*....
gi 1622956760 625 --YIATHPTAFPATIMFAM 641
Cdd:cd22192   173 lhILVLQPNKTFACQMYDL 191
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
392-512 1.10e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 52.39  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 392 RGWTALHESVSRNDLEVMEILVNGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAKYGADINTQAS 457
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622956760 458 DS-----ASALYEACKNEHEEVV----EFLLLQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 512
Cdd:TIGR00870 207 LGntllhLLVMENEFKAEYEELScqmyNFALSLLDKLRDSkelevilNHQGLTPLKLAAKEGRIVLFRLKL 277
PHA02884 PHA02884
ankyrin repeat protein; Provisional
539-658 3.28e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 49.60  E-value: 3.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 539 VLEALLSARFDVNAPLAperarLYEDRRSSALYFAVVNNNVYATELLLEHGADPNR----DVISPLLVAIRHGCLRTMQL 614
Cdd:PHA02884   48 IIDAILKLGADPEAPFP-----LSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRyaeeAKITPLYISVLHGCLKCLEI 122
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622956760 615 LLDHGANIDAYIATHPTAFPATIMFamkCLSLLKFLMdlgCDGE 658
Cdd:PHA02884  123 LLSYGADINIQTNDMVTPIELALMI---CNNFLAFMI---CDNE 160
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
425-453 1.41e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 1.41e-04
                           10        20
                   ....*....|....*....|....*....
gi 1622956760  425 YGITPLFVAAQSGQLEALRFLAKYGADIN 453
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
598-624 7.25e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 7.25e-03
                           10        20
                   ....*....|....*....|....*..
gi 1622956760  598 SPLLVAIRHGCLRTMQLLLDHGANIDA 624
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
280-555 7.66e-51

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 179.76  E-value: 7.66e-51
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 280 IKEGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKS 359
Cdd:COG0666     7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 360 RETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAKVESKNAYGITPLFVAAQSGQL 439
Cdd:COG0666    87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNL 166
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 440 EALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSR-T 518
Cdd:COG0666   167 EIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADlN 246
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 1622956760 519 RVRRSGVSPLHLAAERNNDAVLEALLSARFDVNAPLA 555
Cdd:COG0666   247 AKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
264-512 3.52e-50

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 177.84  E-value: 3.52e-50
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 264 LIKAIKNGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHLDCL 343
Cdd:COG0666    24 LLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 344 LSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAKVESKN 423
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARD 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 424 AYGITPLFVAAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKG 503
Cdd:COG0666   184 NDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAG 263

                  ....*....
gi 1622956760 504 NYRIVQMLL 512
Cdd:COG0666   264 AALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
262-496 8.88e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 168.59  E-value: 8.88e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 262 DPLIKAIKNGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQRAyPGTIDQRTLQEETAVYLATCRGHLD 341
Cdd:COG0666    56 LLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNLE 134
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 342 CLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAKVES 421
Cdd:COG0666   135 IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA 214
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622956760 422 KNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPL 496
Cdd:COG0666   215 KDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
343-633 1.84e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 164.74  E-value: 1.84e-45
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 343 LLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAKVESK 422
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 423 NAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKK 502
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 503 GNYRIVQMLL----PVTSRTrvrRSGVSPLHLAAERNNDAVLEALLSARFDVNAPlaperarlyEDRRSSALYFAVVNNN 578
Cdd:COG0666   164 GNLEIVKLLLeagaDVNARD---NDGETPLHLAAENGHLEIVKLLLEAGADVNAK---------DNDGKTALDLAAENGN 231
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1622956760 579 VYATELLLEHGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAF 633
Cdd:COG0666   232 LEIVKLLLEAGADLNakdKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
373-632 1.29e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.87  E-value: 1.29e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 373 AEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADI 452
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 453 NTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLL----PVTSRTrvrRSGVSPL 528
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLeagaDVNAQD---NDGNTPL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 529 HLAAERNNDAVLEALLSARFDVNAPlaperarlyEDRRSSALYFAVVNNNVYATELLLEHGADPN---RDVISPLLVAIR 605
Cdd:COG0666   158 HLAAANGNLEIVKLLLEAGADVNAR---------DNDGETPLHLAAENGHLEIVKLLLEAGADVNakdNDGKTALDLAAE 228
                         250       260
                  ....*....|....*....|....*..
gi 1622956760 606 HGCLRTMQLLLDHGANIDAYIATHPTA 632
Cdd:COG0666   229 NGNLEIVKLLLEAGADLNAKDKDGLTA 255
PHA02876 PHA02876
ankyrin repeat protein; Provisional
320-624 4.52e-24

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 107.84  E-value: 4.52e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 320 IDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVqhnaDTNHRCNRGWTALHE 399
Cdd:PHA02876  171 VNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII----DNRSNINKNDLSLLK 246
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 400 SVSRNDLEVMEILVNGGAKVESKNAYGITPLFVAAQSGQLEAL-RFLAKYGADINTQASDSASALYEACKNEHE-EVVEF 477
Cdd:PHA02876  247 AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRT 326
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 478 LLLQGADANKTNKDGLLPLHIASKKGNYR-IVQMLLPVTSRTRVRR-SGVSPLHLAAERNNDAVLEALLSARFDVNApla 555
Cdd:PHA02876  327 LIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDyCDKTPIHYAAVRNNVVIINTLLDYGADIEA--- 403
                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622956760 556 perarlYEDRRSSALYFAVVNNNVY-ATELLLEHGAD---PNRDVISPLLVAIRHGC-LRTMQLLLDHGANIDA 624
Cdd:PHA02876  404 ------LSQKIGTALHFALCGTNPYmSVKTLIDRGANvnsKNKDLSTPLHYACKKNCkLDVIEMLLDNGADVNA 471
PHA03100 PHA03100
ankyrin repeat protein; Provisional
353-552 4.76e-24

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 105.52  E-value: 4.76e-24
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 353 PDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALH-----ESVSRNDLEVMEILVNGGAKVESKNAYGI 427
Cdd:PHA03100   28 NDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 428 TPLFVAAQ--SGQLEALRFLAKYGADINTQASDSASALYEACKNEHE--EVVEFLLLQGADANKTNK-DGLL-------- 494
Cdd:PHA03100  108 TPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRvNYLLsygvpini 187
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622956760 495 -------PLHIASKKGNYRIVQMLLPVTSRTRVR-RSGVSPLHLAAERNNDAVLEALLSARFDVNA 552
Cdd:PHA03100  188 kdvygftPLHYAVYNNNPEFVKYLLDLGANPNLVnKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
PHA03095 PHA03095
ankyrin-like protein; Provisional
354-635 4.04e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 103.57  E-value: 4.04e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 354 DISNKSRETPLYK---ACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRN---DLEVMEILVNGGAKVESKNAYGI 427
Cdd:PHA03095    5 ESVDIIMEAALYDyllNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGF 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 428 TPLFVAAQSGQ-LEALRFLAKYGADINTQ--ASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHI--ASKK 502
Cdd:PHA03095   85 TPLHLYLYNATtLDVIKLLIKAGADVNAKdkVGRTPLHVYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVllKSRN 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 503 GNYRIVQMLLPVTSRTRVRRS-GVSPLHLAAE--RNNDAVLEALLSARFDVNAPLAPERARLYED------RRS------ 567
Cdd:PHA03095  165 ANVELLRLLIDAGADVYAVDDrFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMatgsscKRSlvlpll 244
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 568 --------------SALYFAVVNNNVYATELLLEHGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHP 630
Cdd:PHA03095  245 iagisinarnrygqTPLHYAAVFNNPRACRRLIALGADINavsSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLN 324

                  ....*
gi 1622956760 631 TAFPA 635
Cdd:PHA03095  325 TASVA 329
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
746-790 4.65e-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: 92.24  E-value: 4.65e-23
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1622956760 746 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ 790
Cdd:cd03721     1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ 45
PHA03100 PHA03100
ankyrin repeat protein; Provisional
332-512 2.96e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.04  E-value: 2.96e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 332 YLATCRGHLDCLLSLLQAGAEPDISNKSRETPL-----YKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSR--N 404
Cdd:PHA03100   40 YLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksN 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 405 DLEVMEILVNGGAKVESKNAYGITPLFVAAQSGQ--LEALRFLAKYGADINtqASDSA------------------SALY 464
Cdd:PHA03100  120 SYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDIN--AKNRVnyllsygvpinikdvygfTPLH 197
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*...
gi 1622956760 465 EACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 512
Cdd:PHA03100  198 YAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
Ank_2 pfam12796
Ankyrin repeats (3 copies);
364-455 3.59e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.63  E-value: 3.59e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 364 LYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNgGAKVESKNaYGITPLFVAAQSGQLEALR 443
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|..
gi 1622956760 444 FLAKYGADINTQ 455
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
333-423 1.88e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 1.88e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 333 LATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHnADTNHRCNrGWTALHESVSRNDLEVMEIL 412
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLL 80
                          90
                  ....*....|.
gi 1622956760 413 VNGGAKVESKN 423
Cdd:pfam12796  81 LEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
463-552 4.18e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 4.18e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 463 LYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPvTSRTRVRRSGVSPLHLAAERNNDAVLEA 542
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKL 79
                          90
                  ....*....|
gi 1622956760 543 LLSARFDVNA 552
Cdd:pfam12796  80 LLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
397-489 6.48e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.09  E-value: 6.48e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 397 LHESVSRNDLEVMEILVNGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYgADINTQASDSaSALYEACKNEHEEVVE 476
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 1622956760 477 FLLLQGADANKTN 489
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
261-561 9.36e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 89.64  E-value: 9.36e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 261 VDPLIKAIKNGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLqraypgtIDQRTlqeETAVYLATCRGHl 340
Cdd:PHA02874   36 TTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLL-------IDNGV---DTSILPIPCIEK- 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 341 DCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAKVE 420
Cdd:PHA02874  105 DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 421 SKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDSASALYEACKneHEEVVEFLLLQGADANKTNKDGLLPLHIA- 499
Cdd:PHA02874  185 VKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAi 262
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622956760 500 SKKGNYRIVQMLLPVTSRTRVR-RSGVSPLHLAAER-NNDAVLEALLSarfdvNAPLAPERARL 561
Cdd:PHA02874  263 NPPCDIDIIDILLYHKADISIKdNKGENPIDTAFKYiNKDPVIKDIIA-----NAVLIKEADKL 321
PHA02874 PHA02874
ankyrin repeat protein; Provisional
354-539 1.56e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 88.87  E-value: 1.56e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 354 DISNKSRETPLYKACERKNAEAVKILVQHNADTNHRC----NRGWTALheSVSRNDL---------------------EV 408
Cdd:PHA02874   29 NISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINtkipHPLLTAI--KIGAHDIikllidngvdtsilpipciekDM 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 409 MEILVNGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKT 488
Cdd:PHA02874  107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622956760 489 NKDGLLPLHIASKKGNYRIVQMLLPVTSRTRVR-RSGVSPLHLAAERNNDAV 539
Cdd:PHA02874  187 DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKcKNGFTPLHNAIIHNRSAI 238
Ank_2 pfam12796
Ankyrin repeats (3 copies);
430-512 3.08e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 3.08e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 430 LFVAAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEHEEVVEfLLLQGADANKTNkDGLLPLHIASKKGNYRIVQ 509
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVK-LLLEHADVNLKD-NGRTALHYAARSGHLEIVK 78

                  ...
gi 1622956760 510 MLL 512
Cdd:pfam12796  79 LLL 81
PHA02875 PHA02875
ankyrin repeat protein; Provisional
334-551 3.19e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 87.74  E-value: 3.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 334 ATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILV 413
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 414 NGGAKVES---KNayGITPLFVAAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNK 490
Cdd:PHA02875   89 DLGKFADDvfyKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622956760 491 DGLLPLHIASKKGNYRIVQMLLPVTSRTRV--RRSGVSPLHLAAERNNDAVLEALLSARFDVN 551
Cdd:PHA02875  167 CGCTPLIIAMAKGDIAICKMLLDSGANIDYfgKNGCVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02878 PHA02878
ankyrin repeat protein; Provisional
339-618 1.30e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 86.47  E-value: 1.30e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 339 HLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQhnadTNHRCNRGWT--ALHESVSRNDLEVME-ILVNg 415
Cdd:PHA02878   49 NLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR----SINKCSVFYTlvAIKDAFNNRNVEIFKiILTN- 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 416 gakvESKNAYGITPLFVAAQSG----QLEALRFLAKYGADINTQASDS-ASALYEACKNEHEEVVEFLLLQGADANKTNK 490
Cdd:PHA02878  124 ----RYKNIQTIDLVYIDKKSKddiiEAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDK 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 491 DGLLPLHIASKKGNYRIVQMLLPVTSRTRVRRS-GVSPLHLAAERNND-AVLEALLSARFDVNAPLAPerarlyedRRSS 568
Cdd:PHA02878  200 TNNSPLHHAVKHYNKPIVHILLENGASTDARDKcGNTPLHISVGYCKDyDILKLLLEHGVDVNAKSYI--------LGLT 271
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622956760 569 ALYFAVVNNNVyaTELLLEHGADPNR---DVISPLLVAIR-HGCLRTMQLLLDH 618
Cdd:PHA02878  272 ALHSSIKSERK--LKLLLEYGADINSlnsYKLTPLSSAVKqYLCINIGRILISN 323
PHA02875 PHA02875
ankyrin repeat protein; Provisional
261-453 1.52e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 85.81  E-value: 1.52e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 261 VDPLIKAIKNGDEEALKTMIKEGK--NLAEPNKEGwlPLHEAAYYGQLGCLKVLQRAYPGTIDQRTLQEETAVYLATCRG 338
Cdd:PHA02875   36 ISPIKLAMKFRDSEAIKLLMKHGAipDVKYPDIES--ELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILK 113
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 339 HLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAK 418
Cdd:PHA02875  114 KLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622956760 419 VE--SKNAyGITPLFVAAQSGQLEALRFLAKYGADIN 453
Cdd:PHA02875  194 IDyfGKNG-CVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02876 PHA02876
ankyrin repeat protein; Provisional
264-522 9.19e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 84.73  E-value: 9.19e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 264 LIKAIKNGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQLGCL--KVLQRAypGTIDQRTLQEETAVYLATCRGH-L 340
Cdd:PHA02876  244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvpKLLERG--ADVNAKNIKGETPLYLMAKNGYdT 321
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 341 DCLLSLLQAGAEPDISNKSRETPLYKACE-RKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAKV 419
Cdd:PHA02876  322 ENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 420 ES-KNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEHE-EVVEFLLLQGADANKTNKDGLLPLH 497
Cdd:PHA02876  402 EAlSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLL 481
                         250       260
                  ....*....|....*....|....*
gi 1622956760 498 IAskKGNYRIVQMLLPVTSRTRVRR 522
Cdd:PHA02876  482 IA--LEYHGIVNILLHYGAELRDSR 504
PHA02878 PHA02878
ankyrin repeat protein; Provisional
329-468 1.02e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 83.78  E-value: 1.02e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 329 TAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSR-NDLE 407
Cdd:PHA02878  170 TALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYD 249
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1622956760 408 VMEILVNGGAKVESKNA-YGITPLFVAAQSGQleALRFLAKYGADINTQASDSASALYEACK 468
Cdd:PHA02878  250 ILKLLLEHGVDVNAKSYiLGLTALHSSIKSER--KLKLLLEYGADINSLNSYKLTPLSSAVK 309
PHA03100 PHA03100
ankyrin repeat protein; Provisional
399-628 1.15e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 83.18  E-value: 1.15e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 399 ESVSRNDLEVMEILVNGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEH-----EE 473
Cdd:PHA03100    8 TKSRIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKE 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 474 VVEFLLLQGADANKTNKDGLLPLHIAS--KKGNYRIVQMLLPVTSRTRVRRS-GVSPLHLAAERNND--AVLEALLSARF 548
Cdd:PHA03100   88 IVKLLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNIKNSdGENLLHLYLESNKIdlKILKLLIDKGV 167
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 549 DVNA------------PLaperarLYEDRR-SSALYFAVVNNNVYATELLLEHGADPN-RDVI--SPLLVAIRHGCLRTM 612
Cdd:PHA03100  168 DINAknrvnyllsygvPI------NIKDVYgFTPLHYAVYNNNPEFVKYLLDLGANPNlVNKYgdTPLHIAILNNNKEIF 241
                         250
                  ....*....|....*.
gi 1622956760 613 QLLLDHGANIDAYIAT 628
Cdd:PHA03100  242 KLLLNNGPSIKTIIET 257
PHA02878 PHA02878
ankyrin repeat protein; Provisional
246-502 4.07e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 81.85  E-value: 4.07e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 246 QKYSSSLfqtsQLAPVDPLIKAIKNGDEEALKTMIKEGKNLAEPNKEGWLPLH--------------------------- 298
Cdd:PHA02878   27 ENYSTSA----SLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHiickepnklgmkemirsinkcsvfytl 102
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 299 ----EAAYYGQLGCLK-VLQRAYPGTIDQRTLQEETAVYLATCRGHLDCLLslLQAGAEPDISNKSR-ETPLYKACERKN 372
Cdd:PHA02878  103 vaikDAFNNRNVEIFKiILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLL--LSYGADINMKDRHKgNTALHYATENKD 180
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 373 AEAVKILVQHNADTN--HRCNRgwTALHESVSRNDLEVMEILVNGGAKVESKNAYGITPLFVAAQS-GQLEALRFLAKYG 449
Cdd:PHA02878  181 QRLTELLLSYGANVNipDKTNN--SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHG 258
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622956760 450 ADINTQAS-DSASALYEACKNEheEVVEFLLLQGADANKTNKDGLLPLHIASKK 502
Cdd:PHA02878  259 VDVNAKSYiLGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA03095 PHA03095
ankyrin-like protein; Provisional
272-513 9.26e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.37  E-value: 9.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 272 DEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQ-LGCLKVLQRA-----YPGTIDQRTLQeetaVYLATCRGHLDCLLS 345
Cdd:PHA03095   62 VKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAgadvnAKDKVGRTPLH----VYLSGFNINPKVIRL 137
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 346 LLQAGAEPDISNKSRETPLYKACERKNA--EAVKILVQHNADTNHRCNRGWTALH---ESVsRNDLEVMEILVNGGAKVE 420
Cdd:PHA03095  138 LLRKGADVNALDLYGMTPLAVLLKSRNAnvELLRLLIDAGADVYAVDDRFRSLLHhhlQSF-KPRARIVRELIRAGCDPA 216
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 421 SKNAYGITPLFVAAQSGQLEALR---FLAKyGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLH 497
Cdd:PHA03095  217 ATDMLGNTPLHSMATGSSCKRSLvlpLLIA-GISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLS 295
                         250
                  ....*....|....*.
gi 1622956760 498 IASKKGNYRIVQMLLP 513
Cdd:PHA03095  296 LMVRNNNGRAVRAALA 311
PHA02876 PHA02876
ankyrin repeat protein; Provisional
397-656 1.19e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.80  E-value: 1.19e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 397 LHESVSRNDLEVMEILVNGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDSASA-------------- 462
Cdd:PHA02876  149 IKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVlecavdsknidtik 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 463 ------------------------------LYEA---------CKNE--HEEV--------VEFLLLQGADANKTNKDGL 493
Cdd:PHA02876  229 aiidnrsninkndlsllkairnedletsllLYDAgfsvnsiddCKNTplHHASqapslsrlVPKLLERGADVNAKNIKGE 308
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 494 LPLHIASKKG----NYRIVQMLLPVTSRTrvRRSGVSPLHLAA--ERNNDAVLeALLSARFDVNaplaperARLYEDRrs 567
Cdd:PHA02876  309 TPLYLMAKNGydteNIRTLIMLGADVNAA--DRLYITPLHQAStlDRNKDIVI-TLLELGANVN-------ARDYCDK-- 376
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 568 SALYFAVVNNNVYATELLLEHGADPnrDVISPLLVAIRHGCL------RTMQLLLDHGANIDA---YIAThptafPATIM 638
Cdd:PHA02876  377 TPIHYAAVRNNVVIINTLLDYGADI--EALSQKIGTALHFALcgtnpyMSVKTLIDRGANVNSknkDLST-----PLHYA 449
                         330
                  ....*....|....*....
gi 1622956760 639 FAMKC-LSLLKFLMDLGCD 656
Cdd:PHA02876  450 CKKNCkLDVIEMLLDNGAD 468
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
343-491 1.23e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 77.99  E-value: 1.23e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 343 LLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGgAKVESK 422
Cdd:PLN03192  541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-ASISDP 619
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622956760 423 NAYGiTPLFVAAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKD 491
Cdd:PLN03192  620 HAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
PHA02875 PHA02875
ankyrin repeat protein; Provisional
433-630 1.30e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 76.57  E-value: 1.30e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 433 AAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 512
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 513 PVTSRTR--VRRSGVSPLHLAAERNNDAVLEALLSARFDVNAPlaperarlyEDRRSSALYFAVVNNNVYATELLLEHGA 590
Cdd:PHA02875   89 DLGKFADdvFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP---------NTDKFSPLHLAVMMGDIKGIELLIDHKA 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 1622956760 591 DPNRDV---ISPLLVAIRHGCLRTMQLLLDHGANIDaYIATHP 630
Cdd:PHA02875  160 CLDIEDccgCTPLIIAMAKGDIAICKMLLDSGANID-YFGKNG 201
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
746-787 1.75e-13

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: 64.82  E-value: 1.75e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1622956760 746 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 787
Cdd:cd03716     1 STPRSLQHLCRLAIRRCLGRRRLELIKKLPLPPRLKDYLLYE 42
Ank_2 pfam12796
Ankyrin repeats (3 copies);
264-357 2.70e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.91  E-value: 2.70e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 264 LIKAIKNGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQRAYPGtidQRTLQEETAVYLATCRGHLDCL 343
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 1622956760 344 LSLLQAGAEPDISN 357
Cdd:pfam12796  78 KLLLEKGADINVKD 91
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
748-787 2.86e-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: 64.41  E-value: 2.86e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622956760 748 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 787
Cdd:cd03587     2 PRSLQHLCRLAIRRCLGKRRLDLIDKLPLPPRLKDYLLYK 41
Ank_2 pfam12796
Ankyrin repeats (3 copies);
528-624 2.40e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 2.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 528 LHLAAERNNDAVLEALLSARFDVNaplaperarLYEDRRSSALYFAVVNNNVYATELLLEHgADPNRDVI--SPLLVAIR 605
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNgrTALHYAAR 70
                          90
                  ....*....|....*....
gi 1622956760 606 HGCLRTMQLLLDHGANIDA 624
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
436-630 1.83e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.91  E-value: 1.83e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 436 SGQLEALRFLAKYGAD-INTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPv 514
Cdd:PHA02874   11 SGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 515 tsrtrvrrSGVSPLHLAAERNNDAVLEALLSARFDVNAplaperarlyEDRRSSA-LYFAVVNNNVYATELLLEHGADPN 593
Cdd:PHA02874   90 --------NGVDTSILPIPCIEKDMIKTILDCGIDVNI----------KDAELKTfLHYAIKKGDLESIKMLFEYGADVN 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 1622956760 594 RDVIS---PLLVAIRHGCLRTMQLLLDHGA--NIDAYIATHP 630
Cdd:PHA02874  152 IEDDNgcyPIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGESP 193
Ank_4 pfam13637
Ankyrin repeats (many copies);
461-512 2.34e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.21  E-value: 2.34e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622956760 461 SALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 512
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
329-470 3.54e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.82  E-value: 3.54e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 329 TAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCnrGWTALHESVSRNDLEV 408
Cdd:PLN03192  560 TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKRNDLTA 637
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622956760 409 MEILVNGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADI---NTQASDSASALYEACKNE 470
Cdd:PLN03192  638 MKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVdkaNTDDDFSPTELRELLQKR 702
PHA02859 PHA02859
ankyrin repeat protein; Provisional
357-503 4.91e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 62.91  E-value: 4.91e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 357 NKSRETPLYKACERKNA--EAVKILVQHNADTNHRC-NRGWTALHESVSRN---DLEVMEILVNGGAKVESKNAYGITPL 430
Cdd:PHA02859   48 NDLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTrDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLL 127
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622956760 431 --FVAAQSGQLEALRFLAKYGADINTQASDSASALYEACK-NEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKG 503
Cdd:PHA02859  128 hmYMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILfHSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
747-785 7.79e-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: 57.56  E-value: 7.79e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622956760 747 PPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLK 785
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
Ank_4 pfam13637
Ankyrin repeats (many copies);
428-479 2.15e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 56.51  E-value: 2.15e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1622956760 428 TPLFVAAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLL 479
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02878 PHA02878
ankyrin repeat protein; Provisional
455-656 5.39e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.59  E-value: 5.39e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 455 QASDSASA-----LYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRVRRSGVSpLH 529
Cdd:PHA02878   28 NYSTSASLipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVA-IK 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 530 LAAERNNDAVLEALLSARFDVN--------------APLAPERARLY-----------EDRRSSALYFAVVNNNVYATEL 584
Cdd:PHA02878  107 DAFNNRNVEIFKIILTNRYKNIqtidlvyidkkskdDIIEAEITKLLlsygadinmkdRHKGNTALHYATENKDQRLTEL 186
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622956760 585 LLEHGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAFPATIMFaMKCLSLLKFLMDLGCD 656
Cdd:PHA02878  187 LLSYGANVNipdKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY-CKDYDILKLLLEHGVD 260
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
295-512 7.31e-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: 7.31e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 295 LPLHEAAYYGQLGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHLDCLLSLLQAGaePDISNKSRETPLYKacerknae 374
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAA--PELVNEPMTSDLYQ-------- 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 375 avkilvqhnadtnhrcnrGWTALHESVSRNDLEVMEILVNGGAKVESKNA--------------YGITPLFVAAQSGQLE 440
Cdd:cd22192    89 ------------------GETALHIAVVNQNLNLVRELIARGADVVSPRAtgtffrpgpknliyYGEHPLSFAACVGNEE 150
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 441 ALRFLAKYGADINTQASDSASALY----EACKNEHEEVVEFLLLQGADANK------TNKDGLLPLHIASKKGNYRIVQM 510
Cdd:cd22192   151 IVRLLIEHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQH 230

                  ..
gi 1622956760 511 LL 512
Cdd:cd22192   231 LV 232
PHA02798 PHA02798
ankyrin-like protein; Provisional
376-605 2.18e-09

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 60.62  E-value: 2.18e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 376 VKILVQHNADTNHRCNRGWTALHESVSR---NDLEVMEILVNGGAKVESKNAYGITPLFVAAQSG---QLEALRFLAKYG 449
Cdd:PHA02798   92 VKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKG 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 450 ADINTQAS----DSASALYEACKNEHE-EVVEFLLLQGADANKTNK-------DGLLPLHIASKKGNYRIVQMLLPVTSR 517
Cdd:PHA02798  172 VDINTHNNkekyDTLHCYFKYNIDRIDaDILKLFVDNGFIINKENKshkkkfmEYLNSLLYDNKRFKKNILDFIFSYIDI 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 518 TRVRRSGVSPLHLAAERNNDAVLEALLSARFDVNaplaperarLYEDRRSSALYFAVVNNNVYATELLLEHgaDPNRDVI 597
Cdd:PHA02798  252 NQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDIN---------IITELGNTCLFTAFENESKFIFNSILNK--KPNKNTI 320

                  ....*...
gi 1622956760 598 SPLLVAIR 605
Cdd:PHA02798  321 SYTYYKLR 328
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
263-447 1.32e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 58.49  E-value: 1.32e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 263 PLIKAIKNGDEEALKTMIK-EGKNLAEPNKEGWLPLHEAAYYGQLGCLKVLQRAYPGTIDQRTLQE----ETAVYLATCR 337
Cdd:cd22192    20 PLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDlyqgETALHIAVVN 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 338 GHLDCLLSLLQAGAepDISN---------KSR-------ETPL-YKACErKNAEAVKILVQHNADTNHRCNRGWTALHES 400
Cdd:cd22192   100 QNLNLVRELIARGA--DVVSpratgtffrPGPknliyygEHPLsFAACV-GNEEIVRLLIEHGADIRAQDSLGNTVLHIL 176
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1622956760 401 VSRND----LEVMEILVNGGAKVES------KNAYGITPLFVAAQSGQLEALRFLAK 447
Cdd:cd22192   177 VLQPNktfaCQMYDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
749-787 5.31e-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: 5.31e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1622956760  749 RPLAHLCRLRVRKAIGKyriklLDTLPLPGRLIRYLKYE 787
Cdd:smart00969   1 RSLQHLCRLAIRRSLGG-----IDKLPLPPRLKDYLLYY 34
PHA02946 PHA02946
ankyin-like protein; Provisional
346-530 6.08e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 55.83  E-value: 6.08e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 346 LLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHeSVSRNDLEVME---ILVNGGAKVE-S 421
Cdd:PHA02946   58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY-YLSGTDDEVIErinLLVQYGAKINnS 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 422 KNAYGITPLFVAAQSGQLEALRFLA-KYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIAS 500
Cdd:PHA02946  137 VDEEGCGPLLACTDPSERVFKKIMSiGFEARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVC 216
                         170       180       190
                  ....*....|....*....|....*....|..
gi 1622956760 501 KK--GNYRIVQMLLPVTSRTRVRRSGVSPLHL 530
Cdd:PHA02946  217 SKtvKNVDIINLLLPSTDVNKQNKFGDSPLTL 248
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
434-512 7.78e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.06  E-value: 7.78e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622956760 434 AQSGQLEALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 512
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_4 pfam13637
Ankyrin repeats (many copies);
360-413 9.69e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 9.69e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622956760 360 RETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILV 413
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SOCS_SSB1_4 cd03718
SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box ...
748-787 1.15e-07

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: 48.45  E-value: 1.15e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622956760 748 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 787
Cdd:cd03718     3 PLPLMDLCRRRVRVALGRDRLEEIEQLPLPPSLKNYLLYQ 42
PHA03100 PHA03100
ankyrin repeat protein; Provisional
263-425 1.20e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.67  E-value: 1.20e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 263 PLIKAI--KNGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQLGcLKVLQraypgtidqrTLQEETAVYLATCRghL 340
Cdd:PHA03100  109 PLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKID-LKILK----------LLIDKGVDINAKNR--V 175
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 341 DCLLSLlqaGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAKVE 420
Cdd:PHA03100  176 NYLLSY---GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252

                  ....*
gi 1622956760 421 SKNAY 425
Cdd:PHA03100  253 TIIET 257
Ank_4 pfam13637
Ankyrin repeats (many copies);
262-312 1.74e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.74e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1622956760 262 DPLIKAIKNGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQLGCLKVL 312
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
360-547 2.12e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 54.63  E-value: 2.12e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 360 RETPLYKACERKNAEAVK-ILVQHNADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAK-----VESKNAYGITPLFVA 433
Cdd:cd22192    17 SESPLLLAAKENDVQAIKkLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElvnepMTSDLYQGETALHIA 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 434 AQSGQLEALRFLAKYGADINTQA------SDSASAL---------YEACKNeHEEVVEFLLLQGADANKTNKDGLLPLHI 498
Cdd:cd22192    97 VVNQNLNLVRELIARGADVVSPRatgtffRPGPKNLiyygehplsFAACVG-NEEIVRLLIEHGADIRAQDSLGNTVLHI 175
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 499 ----ASKKGNYRIVQMLL-------PVTSRTRVRRSGVSPLHLAAERNNDAVLEALLSAR 547
Cdd:cd22192   176 lvlqPNKTFACQMYDLILsydkeddLQPLDLVPNNQGLTPFKLAAKEGNIVMFQHLVQKR 235
SOCS_ASB14 cd03730
SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a ...
746-787 3.61e-07

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


Pssm-ID: 239700  Cd Length: 57  Bit Score: 47.53  E-value: 3.61e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1622956760 746 EPPRPLAHLCRLRVRKAIGKYRIK---LLDTLPLPGRLIRYLKYE 787
Cdd:cd03730     1 TNPRSLKHLCRLKIRACMGRLRLRcpvFMSFLPLPNRLKAYILYK 45
SOCS_ASB1 cd03720
SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a ...
748-787 3.99e-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: 47.03  E-value: 3.99e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622956760 748 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 787
Cdd:cd03720     3 PRSLLSLCRIAVRRALGKQRLSLICSLPLPDPIKKFLLHE 42
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
748-786 5.30e-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: 46.44  E-value: 5.30e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622956760 748 PRPLAHLCRLRVRKAIGKYRIkllDTLPLPGRLIRYLKY 786
Cdd:cd03717     3 VRSLQHLCRFVIRQCTRRDLI---DQLPLPRRLKDYLKE 38
SOCS_SOCS7 cd03741
SOCS (suppressors of cytokine signaling) box of SOCS7-like proteins. Together with CIS1, the ...
749-788 5.84e-07

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


Pssm-ID: 239710  Cd Length: 49  Bit Score: 46.63  E-value: 5.84e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622956760 749 RPLAHLCRLRVRKAIgkyRIKLLDTLPLPGRLIRYLKYEN 788
Cdd:cd03741     4 QSLQHLCRFVIRKLV---RRDHIPALPLPRRLIDYLREKH 40
SOCS_SSB4 cd03743
SOCS (suppressors of cytokine signaling) box of SSB4 (SPRY domain-containing SOCS box ...
748-787 5.90e-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: 5.90e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622956760 748 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 787
Cdd:cd03743     3 PLPLMDLCRRSARQALGRHRLHHIQSLPLPQTLKNYLQYQ 42
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
494-641 9.19e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 52.32  E-value: 9.19e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 494 LPLHIASKKGNYRIVQMLLpVTSRTRVRRSGV---SPLHLAAERNNDAVLEALL-SARFDVNAPLAPErarLYEDRrsSA 569
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLL-KCPSCDLFQRGAlgeTALHVAALYDNLEAAVVLMeAAPELVNEPMTSD---LYQGE--TA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 570 LYFAVVNNNVYATELLLEHGAD------------PNRDVI-----SPLLVAIRHGCLRTMQLLLDHGANIDA-------- 624
Cdd:cd22192    93 LHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIRAqdslgntv 172
                         170
                  ....*....|....*....
gi 1622956760 625 --YIATHPTAFPATIMFAM 641
Cdd:cd22192   173 lhILVLQPNKTFACQMYDL 191
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
392-512 1.10e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 52.39  E-value: 1.10e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 392 RGWTALHESVSRNDLEVMEILVNGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAKYGADINTQAS 457
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622956760 458 DS-----ASALYEACKNEHEEVV----EFLLLQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 512
Cdd:TIGR00870 207 LGntllhLLVMENEFKAEYEELScqmyNFALSLLDKLRDSkelevilNHQGLTPLKLAAKEGRIVLFRLKL 277
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
383-512 1.96e-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: 51.30  E-value: 1.96e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 383 NADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAKY 448
Cdd:cd22194   131 NAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPEIVQLLMEK 210
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1622956760 449 GADINTqASDSAS-----ALYEACKNEHE------EVVEFLLLQGADAN---KTNKDGLLPLHIASKKGNYRIVQMLL 512
Cdd:cd22194   211 ESTDIT-SQDSRGntvlhALVTVAEDSKTqndfvkRMYDMILLKSENKNletIRNNEGLTPLQLAAKMGKAEILKYIL 287
PHA02884 PHA02884
ankyrin repeat protein; Provisional
539-658 3.28e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 49.60  E-value: 3.28e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 539 VLEALLSARFDVNAPLAperarLYEDRRSSALYFAVVNNNVYATELLLEHGADPNR----DVISPLLVAIRHGCLRTMQL 614
Cdd:PHA02884   48 IIDAILKLGADPEAPFP-----LSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRyaeeAKITPLYISVLHGCLKCLEI 122
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622956760 615 LLDHGANIDAYIATHPTAFPATIMFamkCLSLLKFLMdlgCDGE 658
Cdd:PHA02884  123 LLSYGADINIQTNDMVTPIELALMI---CNNFLAFMI---CDNE 160
Ank_5 pfam13857
Ankyrin repeats (many copies);
346-398 3.62e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 3.62e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622956760 346 LLQAG-AEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALH 398
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
393-445 5.35e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 5.35e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622956760 393 GWTALHESVSRNDLEVMEILVNGGAKVESKNAYGITPLFVAAQSGQLEALRFL 445
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
SOCS smart00253
suppressors of cytokine signalling; suppressors of cytokine signalling
742-786 5.53e-06

suppressors of cytokine signalling; suppressors of cytokine signalling


Pssm-ID: 128549  Cd Length: 43  Bit Score: 43.82  E-value: 5.53e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1622956760  742 KEKAEPPRPLAHLCRLRVRKAIGKYRIKlldTLPLPGRLIRYLKY 786
Cdd:smart00253   1 LPRPSNVPSLQHLCRFTIRRCTRTDQIK---TLPLPPKLKDYLSY 42
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
392-512 6.55e-06

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 49.49  E-value: 6.55e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 392 RGWTALHESVSRNDLEVMEILVNGGAKVESKNA-------------YGITPLFVAAQSGQLEALRFLAKYGADI-NTQAS 457
Cdd:cd21882    72 QGQTALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQPaALEAQ 151
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622956760 458 DSAS-----ALYEACKNEHE------EVVEFLLLQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 512
Cdd:cd21882   152 DSLGntvlhALVLQADNTPEnsafvcQMYNLLLSYGAHLDPTqqleeipNHQGLTPLKLAAVEGKIVMFQHIL 224
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
397-591 7.13e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 49.87  E-value: 7.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 397 LHESVSRNDLEVMEILV-NGGAKVESKNAYGITPLFVAAQSGQLEALrFLAKYGADINTqaSDSASALYEACKNEHEEVV 475
Cdd:PLN03192  498 LQHHKELHDLNVGDLLGdNGGEHDDPNMASNLLTVASTGNAALLEEL-LKAKLDPDIGD--SKGRTPLHIAASKGYEDCV 574
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 476 EFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRVRRSGvSPLHLAAERNNDAVLEALLSARFDVNApla 555
Cdd:PLN03192  575 LVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDS--- 650
                         170       180       190
                  ....*....|....*....|....*....|....*..
gi 1622956760 556 perarlyEDRR-SSALYFAVVNNNVYATELLLEHGAD 591
Cdd:PLN03192  651 -------EDHQgATALQVAMAEDHVDMVRLLIMNGAD 680
Ank_2 pfam12796
Ankyrin repeats (3 copies);
263-312 1.19e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 44.34  E-value: 1.19e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622956760 263 PLIKAIKNGDEEALKTMIKegKNLAEPNKEGWLPLHEAAYYGQLGCLKVL 312
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVKLL 80
Ank_4 pfam13637
Ankyrin repeats (many copies);
337-380 1.33e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 1.33e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1622956760 337 RGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILV 380
Cdd:pfam13637  11 SGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SOCS_SSB2 cd03719
SOCS (suppressors of cytokine signaling) box of SSB2 (SPRY domain-containing SOCS box proteins) ...
746-787 1.62e-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: 42.70  E-value: 1.62e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1622956760 746 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 787
Cdd:cd03719     1 AEPHSLLHLSRLCVRHALGDTRLGQVSALPLPPAMKRYLLYQ 42
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
746-787 2.21e-05

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


Pssm-ID: 239701  Cd Length: 56  Bit Score: 42.51  E-value: 2.21e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 1622956760 746 EPPRPLAHLCRLRVRKAIGKYRIKLLDT---LPLPGRLIRYLKYE 787
Cdd:cd03731     1 ENPRPLKHLCRLKIRKLMGLQKLQQPSSmkkLPLPPALKRYILYK 45
SOCS_SSB1 cd03744
SOCS (suppressors of cytokine signaling) box of SSB1 (SPRY domain-containing SOCS box proteins) ...
748-787 2.28e-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: 2.28e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622956760 748 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 787
Cdd:cd03744     3 PLPLMDLCRRSVRLALGRERLSEIHTLPLPASLKNYLLYQ 42
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
392-512 2.51e-05

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: 47.87  E-value: 2.51e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 392 RGWTALHESVSRNDLEVMEILVNGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFL---AKYGADINT 454
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKgrffqpkyqgegfyFGELPLSLAACTNQPDIVQYLlenEHQPADIEA 154
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622956760 455 QASDSAS---ALYEACKNEHEE------VVEFLLLQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 512
Cdd:cd22193   155 QDSRGNTvlhALVTVADNTKENtkfvtrMYDMILIRGAKLCPTveleeirNNDGLTPLQLAAKMGKIEILKYIL 228
SOCS_ASB7 cd03726
SOCS (suppressors of cytokine signaling) box of ASB7-like proteins. ASB family members have a ...
748-787 3.74e-05

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


Pssm-ID: 239696  Cd Length: 45  Bit Score: 41.76  E-value: 3.74e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1622956760 748 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 787
Cdd:cd03726     3 PRTLQDLCRIKIRHCIGLQNLKLLDELPIAKVMKDYLKHK 42
Ank_5 pfam13857
Ankyrin repeats (many copies);
445-499 4.26e-05

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 41.56  E-value: 4.26e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1622956760 445 LAKYGADINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIA 499
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
419-593 4.36e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.00  E-value: 4.36e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 419 VESKNAYGITPLFVAAQSGQLEALRFLAKYgadINTQASDSASALYEACKNEHEEVVEFLLLQGADANKTnkdGLLPLHI 498
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISLEYVDAVEAILLHLLAAFRKS---GPLELAN 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 499 ASKKGNYrivqmllpvtsrTRvrrsGVSPLHLAAERNNDAVLEALLSARFDVNAP-------LAPERARLYEDRRSSALY 571
Cdd:TIGR00870 119 DQYTSEF------------TP----GITALHLAAHRQNYEIVKLLLERGASVPARacgdffvKSQGVDSFYHGESPLNAA 182
                         170       180
                  ....*....|....*....|..
gi 1622956760 572 FAVVNNNVYAteLLLEHGADPN 593
Cdd:TIGR00870 183 ACLGSPSIVA--LLSEDPADIL 202
SOCS_ASB13 cd03729
SOCS (suppressors of cytokine signaling) box of ASB13-like proteins. ASB family members have a ...
748-786 4.75e-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: 4.75e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622956760 748 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKY 786
Cdd:cd03729     3 PLSLQQLCRINLRKALGTRALEKIAKLNIPNRIIDYLSY 41
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
392-512 5.67e-05

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: 46.72  E-value: 5.67e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 392 RGWTALHESVSRNDLEVMEILVNGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAK---YGADINt 454
Cdd:cd22196    93 KGQTALHIAIERRNMHLVELLVQNGADVHARASgeffkkkkggpgfyFGELPLSLAACTNQLDIVKFLLEnphSPADIS- 171
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1622956760 455 qASDSAS-----ALYEACKNEHE------EVVEFLLLQGADANK-------TNKDGLLPLHIASKKGNYRIVQMLL 512
Cdd:cd22196   172 -ARDSMGntvlhALVEVADNTPEntkfvtKMYNEILILGAKIRPllkleeiTNKKGLTPLKLAAKTGKIGIFAYIL 246
PHA02946 PHA02946
ankyin-like protein; Provisional
464-512 8.54e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.82  E-value: 8.54e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1622956760 464 YEACKNEHEEVVEFLLLQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 512
Cdd:PHA02946   44 YCGIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLL 92
SOCS_ASB5 cd03724
SOCS (suppressors of cytokine signaling) box of ASB5-like proteins. ASB family members have a ...
748-786 9.31e-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: 40.25  E-value: 9.31e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1622956760 748 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKY 786
Cdd:cd03724     3 PSSLCQLCRLCIRNYIGRSRLHLIPQLQLPTLLKNFLQY 41
PHA02798 PHA02798
ankyrin-like protein; Provisional
403-593 9.71e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.60  E-value: 9.71e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 403 RND--LEVMEILVNGGAKVESKNAYGITPLF-----VAAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEH---E 472
Cdd:PHA02798   46 RDSpsTDIVKLFINLGANVNGLDNEYSTPLCtilsnIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnL 125
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 473 EVVEFLLLQGADANKTNKDGLLPLHIASKKGNY---RIVQMLLP--VTSRTRVRRSGVSPLHLAAERNNDA----VLEAL 543
Cdd:PHA02798  126 EILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEkgVDINTHNNKEKYDTLHCYFKYNIDRidadILKLF 205
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 544 LSARFDVNAPLAPERAR--------LYEDRRS----------------------SALYFAVVNNNVYATELLLEHGADPN 593
Cdd:PHA02798  206 VDNGFIINKENKSHKKKfmeylnslLYDNKRFkknildfifsyidinqvdelgfNPLYYSVSHNNRKIFEYLLQLGGDIN 285
PHA02859 PHA02859
ankyrin repeat protein; Provisional
419-536 1.19e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 44.04  E-value: 1.19e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 419 VESKNAYGITPLF--VAAQSGQLEALRFLAKYGADINTQASDSA-SALYEAC---KNEHEEVVEFLLLQGADANKTNKDG 492
Cdd:PHA02859   44 VNDCNDLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRDNNlSALHHYLsfnKNVEPEILKILIDSGSSITEEDEDG 123
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1622956760 493 LLPLHIASKKGNYRIVQMLLPVtsrtrvrRSGVSPLHLAAERNN 536
Cdd:PHA02859  124 KNLLHMYMCNFNVRINVIKLLI-------DSGVSFLNKDFDNNN 160
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
425-453 1.41e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 39.49  E-value: 1.41e-04
                           10        20
                   ....*....|....*....|....*....
gi 1622956760  425 YGITPLFVAAQSGQLEALRFLAKYGADIN 453
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
425-454 1.54e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.55  E-value: 1.54e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 1622956760 425 YGITPLFVAAQSGQLEALRFLAKYGADINT 454
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
411-479 2.02e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 2.02e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1622956760 411 ILVNGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDSASALYEACKNEHEEVVEFLL 479
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
Ank_5 pfam13857
Ankyrin repeats (many copies);
379-430 3.10e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 3.10e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1622956760 379 LVQH-NADTNHRCNRGWTALHESVSRNDLEVMEILVNGGAKVESKNAYGITPL 430
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02989 PHA02989
ankyrin repeat protein; Provisional
372-597 5.89e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 43.19  E-value: 5.89e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 372 NAEAVKILVQHNADTNHRCN-RGWTALH---ESVSRNdLEVMEILVNGGAKV-ESKNAYGITPLFVAAQSG----QLEAL 442
Cdd:PHA02989  123 NCDMLRFLLSKGINVNDVKNsRGYNLLHmylESFSVK-KDVIKILLSFGVNLfEKTSLYGLTPMNIYLRNDidviSIKVI 201
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 443 RFLAKYGADINTQasdsasalyeacKNEHEEVVEFLLlqgaDANKtnkdgllplhIASKKgNYRIVQMLLPVTSRTRVRR 522
Cdd:PHA02989  202 KYLIKKGVNIETN------------NNGSESVLESFL----DNNK----------ILSKK-EFKVLNFILKYIKINKKDK 254
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1622956760 523 SGVSPLHLAAERNNDAVLEALLSARFDVNAplaperarlYEDRRSSALYFAVVNNNVYATELLLehGADPNRDVI 597
Cdd:PHA02989  255 KGFNPLLISAKVDNYEAFNYLLKLGDDIYN---------VSKDGDTVLTYAIKHGNIDMLNRIL--QLKPGKYLI 318
Ank_4 pfam13637
Ankyrin repeats (many copies);
566-616 7.98e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 7.98e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1622956760 566 RSSALYFAVVNNNVYATELLLEHGADPNR---DVISPLLVAIRHGCLRTMQLLL 616
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAvdgNGETALHFAASNGNVEVLKLLL 54
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
748-788 8.65e-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: 37.81  E-value: 8.65e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 1622956760 748 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYEN 788
Cdd:cd03723     3 PRSLQHLCRCAIRKLLGSRCHKLVPQLSLPTSLKNYLLLEP 43
PHA03100 PHA03100
ankyrin repeat protein; Provisional
565-656 8.70e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.34  E-value: 8.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 565 RRSSALYFAVVNNNVYATELLLEHGADPNRDV-----ISPLLVAIRHGC---LRTMQLLLDHGANIDAYIATHPTAFPAT 636
Cdd:PHA03100   34 KPVLPLYLAKEARNIDVVKILLDNGADINSSTknnstPLHYLSNIKYNLtdvKEIVKLLLEYGANVNAPDNNGITPLLYA 113
                          90       100
                  ....*....|....*....|
gi 1622956760 637 IMFAMKCLSLLKFLMDLGCD 656
Cdd:PHA03100  114 ISKKSNSYSIVEYLLDNGAN 133
Ank_5 pfam13857
Ankyrin repeats (many copies);
483-531 1.08e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 1.08e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1622956760 483 ADANKTNKDGLLPLHIASKKGNYRIVQMLL-PVTSRTRVRRSGVSPLHLA 531
Cdd:pfam13857   7 IDLNRLDGEGYTPLHVAAKYGALEIVRVLLaYGVDLNLKDEEGLTALDLA 56
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
362-387 1.83e-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: 1.83e-03
                           10        20
                   ....*....|....*....|....*.
gi 1622956760  362 TPLYKACERKNAEAVKILVQHNADTN 387
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
524-552 1.92e-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: 1.92e-03
                           10        20
                   ....*....|....*....|....*....
gi 1622956760  524 GVSPLHLAAERNNDAVLEALLSARFDVNA 552
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
392-512 2.65e-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: 41.38  E-value: 2.65e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 392 RGWTALHESVSRNDLEVMEILVNGGAKVESKNA-------------YGITPLFVAAQSGQLEALRFLAKYGADI-NTQAS 457
Cdd:cd22197    93 RGHSALHIAIEKRSLQCVKLLVENGADVHARACgrffqkkqgtcfyFGELPLSLAACTKQWDVVNYLLENPHQPaSLQAQ 172
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622956760 458 DSAS-----ALYEACKN--EHEEVV----EFLLLQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 512
Cdd:cd22197   173 DSLGntvlhALVMIADNspENSALVikmyDGLLQAGARLCPTvqleeisNHEGLTPLKLAAKEGKIEIFRHIL 245
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
326-445 2.77e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 41.32  E-value: 2.77e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 326 QEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSR--------------ETPLYKACERKNAEAVKILVQH---NADTNH 388
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRffqpkyqgegfyfgELPLSLAACTNQPDIVQYLLENehqPADIEA 154
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1622956760 389 RCNRGWTALH-------ESVSRNDL--EVMEILVNGGAKV-------ESKNAYGITPLFVAAQSGQLEALRFL 445
Cdd:cd22193   155 QDSRGNTVLHalvtvadNTKENTKFvtRMYDMILIRGAKLcptveleEIRNNDGLTPLQLAAKMGKIEILKYI 227
PHA02884 PHA02884
ankyrin repeat protein; Provisional
341-458 2.99e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.35  E-value: 2.99e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 341 DCLLSLLQAGAEPDI----SNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNrgwtalhesvsrndlevmeilvngg 416
Cdd:PHA02884   47 DIIDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAE------------------------- 101
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1622956760 417 akvESKnaygITPLFVAAQSGQLEALRFLAKYGADINTQASD 458
Cdd:PHA02884  102 ---EAK----ITPLYISVLHGCLKCLEILLSYGADINIQTND 136
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
297-445 3.42e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 41.02  E-value: 3.42e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 297 LHEAAYY---GQLGCLKVLQRAYPGTIDQRTL----------QEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSR--- 360
Cdd:cd21882    30 LHKAALNlndGVNEAIMLLLEAAPDSGNPKELvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSARATGRffr 109
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 361 ----------ETPLYKACERKNAEAVKILVQHNADTNHRCNR---GWTALHESVSRND---------LEVMEILVNGGAK 418
Cdd:cd21882   110 kspgnlfyfgELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHALVLQADntpensafvCQMYNLLLSYGAH 189
                         170       180       190
                  ....*....|....*....|....*....|....
gi 1622956760 419 V-------ESKNAYGITPLFVAAQSGQLEALRFL 445
Cdd:cd21882   190 LdptqqleEIPNHQGLTPLKLAAVEGKIVMFQHI 223
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
392-420 4.39e-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: 4.39e-03
                           10        20
                   ....*....|....*....|....*....
gi 1622956760  392 RGWTALHESVSRNDLEVMEILVNGGAKVE 420
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02878 PHA02878
ankyrin repeat protein; Provisional
263-382 5.06e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.25  E-value: 5.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 263 PLIKAIKNGDEEALKTMIKEGKNLAEPNKEGWLPLHEA-AYYGQLGCLKVLQRAYPGTIDQRTLQEETAVYLATcrGHLD 341
Cdd:PHA02878  204 PLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSI--KSER 281
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|..
gi 1622956760 342 CLLSLLQAGAEPDISNKSRETPLYKAC-ERKNAEAVKILVQH 382
Cdd:PHA02878  282 KLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRILISN 323
PHA02736 PHA02736
Viral ankyrin protein; Provisional
440-520 5.50e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 38.32  E-value: 5.50e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 440 EALRFLAKYGADINTQAS-DSASALYEACKNEHEEVVEFLLLQ-GADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSR 517
Cdd:PHA02736   72 EKLKLLMEWGADINGKERvFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGAQ 151

                  ...
gi 1622956760 518 TRV 520
Cdd:PHA02736  152 CKV 154
PHA02884 PHA02884
ankyrin repeat protein; Provisional
458-605 7.22e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.20  E-value: 7.22e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 458 DSASALYEACKNEHEEVVEFLLLQGADANKTNkdgllPLHIASKkgnyrivqmllpvtsrtrvrrsgVSPLHLAAERNND 537
Cdd:PHA02884   32 CIANILYSSIKFHYTDIIDAILKLGADPEAPF-----PLSENSK-----------------------TNPLIYAIDCDND 83
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1622956760 538 AVLEALLSARFDVNaplaperaRLYEDRRSSALYFAVVNNNVYATELLLEHGADPN---RDVISPLLVAIR 605
Cdd:PHA02884   84 DAAKLLIRYGADVN--------RYAEEAKITPLYISVLHGCLKCLEILLSYGADINiqtNDMVTPIELALM 146
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
598-624 7.25e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 7.25e-03
                           10        20
                   ....*....|....*....|....*..
gi 1622956760  598 SPLLVAIRHGCLRTMQLLLDHGANIDA 624
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV4 cd22195
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed ...
392-512 7.25e-03

Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 4; TRPV4 is expressed broadly in neuronal and non-neuronal cells. It is activated by various stimuli, including hypo-osmolarity, warm temperature, and chemical ligands. TRPV4 acts in physiological functions such as osmoregulation and thermoregulation. It also has a role in mechanosensation in the vascular endothelium and urinary tract, and in cell barrier formation in vascular and epidermal tissues. Knockout mice studies suggested the functional importance of TRPV4 in the central nervous system, nociception, and bone formation. TRPV4 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: 411979 [Multi-domain]  Cd Length: 733  Bit Score: 39.83  E-value: 7.25e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 392 RGWTALHESVSRNDLEVMEILVNGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAKYG---ADINT 454
Cdd:cd22195   136 RGQTALHIAIERRCKHYVELLVEKGADVHAQARgrffqpkdeggyfyFGELPLSLAACTNQPDIVHYLTENAhkkADLRR 215
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1622956760 455 QASDSAS---ALYEACKNEHE------EVVEFLLLQGA----DANKT---NKDGLLPLHIASKKGNYRIVQMLL 512
Cdd:cd22195   216 QDSRGNTvlhALVAIADNTREntkfvtKMYDLLLIKCAklypDCNLEailNNDGMSPLMMAAKLGKIGIFQHII 289
SOCS_WSB_SWIP cd03733
SOCS (suppressors of cytokine signaling) box of WSB/SWiP-like proteins. This subfamily ...
751-786 8.01e-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: 34.71  E-value: 8.01e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 1622956760 751 LAHLCRLRVRKAIGKYRIKlldTLPLPGRLIRYLKY 786
Cdd:cd03733     6 LQHLCRMALRRVMTTQQVL---ALPIPKKMKEFLTY 38
PHA02792 PHA02792
ankyrin-like protein; Provisional
405-492 8.06e-03

ankyrin-like protein; Provisional


Pssm-ID: 165155 [Multi-domain]  Cd Length: 631  Bit Score: 39.55  E-value: 8.06e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1622956760 405 DLEVME-ILVNGGAKVES-KNAYGITPLFVAAQSGQLEALRFLA---KYGADINTQASDSASALYEACKNEHEEVVEFLL 479
Cdd:PHA02792  351 DPKVVEyILKNGNVVVEDdDNIINIMPLFPTLSIHESDVLSILKlckPYIDDINKIDKHGRSILYYCIESHSVSLVEWLI 430
                          90
                  ....*....|...
gi 1622956760 480 LQGADANKTNKDG 492
Cdd:PHA02792  431 DNGADINITTKYG 443
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH