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Conserved domains on  [gi|767980726|ref|XP_011535137|]
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ankyrin repeat and SOCS box protein 2 isoform X5 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
63-298 8.05e-47

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 165.13  E-value: 8.05e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  63 IDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHE 142
Cdd:COG0666   47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 143 SVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLL 222
Cdd:COG0666  127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767980726 223 SQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIR-RSGVSPLHLAAERNHDEVLEALLSARFDVNTPLA 298
Cdd:COG0666  207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKdKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
SOCS super family cl02533
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
 489-533 2.40e-23

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


The actual alignment was detected with superfamily member cd03721:

Pssm-ID: 470605  Cd Length: 45  Bit Score: 92.62  E-value: 2.40e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767980726 489 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ 533
Cdd:cd03721    1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ 45
Ank_2 pfam12796
Ankyrin repeats (3 copies);
271-367 9.39e-12

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 9.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  271 LHLAAERNHDEVLEALLSARFDVNtplaperarLYEDRRSSALYFAVVNNNVYATELLLQHgADPNRDVI--SPLLVAIR 348
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNgrTALHYAAR 70

                          90
                  ....*....|....*....
gi 767980726  349 HGCLRTMQLLLDHGANIDA 367
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
7-100 1.15e-11

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.90  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726    7 LIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGCLKVLQRAYPGtidQRTLQEETAVYLATCRGHLDCL 86
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 767980726   87 LSLLQAGAEPDISN 100
Cdd:pfam12796  78 KLLLEKGADINVKD 91
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
63-298 8.05e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 165.13  E-value: 8.05e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  63 IDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHE 142
Cdd:COG0666   47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 143 SVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLL 222
Cdd:COG0666  127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767980726 223 SQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIR-RSGVSPLHLAAERNHDEVLEALLSARFDVNTPLA 298
Cdd:COG0666  207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKdKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 96-330 1.27e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 108.98  E-value: 1.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  96 PDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALH-----ESVSRNDLEVMQILVSGGAKVESKNAYGI 170
Cdd:PHA03100  28 NDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGI 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 171 TPLFVAAQ--SGQLEALRFLAKYGADINTQASDNASALYEACKNEHE--EVVEFLLSQGADANKTNK-DGLL-------- 237
Cdd:PHA03100 108 TPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRvNYLLsygvpini 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 238 -------PLHIASKKGNYRIVQMLLPVTSRTRIR-RSGVSPLHLAAERNHDEVLEALLSARFDVNTplaperarlyedRR 309
Cdd:PHA03100 188 kdvygftPLHYAVYNNNPEFVKYLLDLGANPNLVnKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT------------II 255

                        250       260
                 ....*....|....*....|..
gi 767980726 310 SSALYFAVVN-NNVYATELLLQ 330
Cdd:PHA03100 256 ETLLYFKDKDlNTITKIKMLKK 277
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
 489-533 2.40e-23

SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ASB2 targets specific proteins to destruction by the proteasome in leukemia cells that have been induced to differentiate. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239691  Cd Length: 45  Bit Score: 92.62  E-value: 2.40e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767980726 489 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ 533
Cdd:cd03721    1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ 45
Ank_2 pfam12796
Ankyrin repeats (3 copies);
107-198 1.12e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  107 LYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSgGAKVESKNaYGITPLFVAAQSGQLEALR 186
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 767980726  187 FLAKYGADINTQ 198
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
271-367 9.39e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 9.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  271 LHLAAERNHDEVLEALLSARFDVNtplaperarLYEDRRSSALYFAVVNNNVYATELLLQHgADPNRDVI--SPLLVAIR 348
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNgrTALHYAAR 70

                          90
                  ....*....|....*....
gi 767980726  349 HGCLRTMQLLLDHGANIDA 367
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
7-100 1.15e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.90  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726    7 LIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGCLKVLQRAYPGtidQRTLQEETAVYLATCRGHLDCL 86
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 767980726   87 LSLLQAGAEPDISN 100
Cdd:pfam12796  78 KLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 38-255 2.71e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 66.19  E-value: 2.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  38 LPLHEAAYYGQVGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHLDCLLSLLQAGaePDISNKSRETPLYKacerknae 117
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAA--PELVNEPMTSDLYQ-------- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 118 avkilvqhnadtnhrcnrGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLE 183
Cdd:cd22192   89 ------------------GETALHIAVVNQNLNLVRELIARGADVVSPRAtgtffrpgpknliyYGEHPLSFAACVGNEE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 184 ALRFLAKYGADINTQASDNASALY----EACKNEHEEVVEFLLSQGADANK------TNKDGLLPLHIASKKGNYRIVQM 253
Cdd:cd22192  151 IVRLLIEHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQH 230


                 ..
gi 767980726 254 LL 255
Cdd:cd22192  231 LV 232
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 490-528 3.60e-11

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


Pssm-ID: 462192  Cd Length: 39  Bit Score: 57.95  E-value: 3.60e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 767980726  490 PPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLK 528
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
 492-530 3.40e-08

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


Pssm-ID: 198037  Cd Length: 34  Bit Score: 49.33  E-value: 3.40e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 767980726   492 RPLAHLCRLRVRKAIGKyriklLDTLPLPGRLIRYLKYE 530
Cdd:smart00969   1 RSLQHLCRLAIRRSLGG-----IDKLPLPPRLKDYLLYY 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 237-384 1.29e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 54.25  E-value: 1.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 237 LPLHIASKKGNYRIVQMLLpVTSRTRIRRSGV---SPLHLAAERNHDEVLEALL-SARFDVNTPLAPErarLYEDRrsSA 312
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLL-KCPSCDLFQRGAlgeTALHVAALYDNLEAAVVLMeAAPELVNEPMTSD---LYQGE--TA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 313 LYFAVVNNNVYATELLLQHGAD------------PNRDVI-----SPLLVAIRHGCLRTMQLLLDHGANIDA-------- 367
Cdd:cd22192   93 LHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIRAqdslgntv 172

                        170
                 ....*....|....*....
gi 767980726 368 --YIATHPTAFPATIMFAM 384
Cdd:cd22192  173 lhILVLQPNKTFACQMYDL 191
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 135-255 3.28e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 53.16  E-value: 3.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  135 RGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAKYGADINTQAS 200
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767980726  201 -----DNASALYEACKNEHEEVV----EFLLSQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 255
Cdd:TIGR00870 207 lgntlLHLLVMENEFKAEYEELScqmyNFALSLLDKLRDSkelevilNHQGLTPLKLAAKEGRIVLFRLKL 277
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 251-401 1.11e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 50.37  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 251 VQMLLPVTSRTRIRRSGVspLHLAAERNHDEVLEALLSARFDVNTPLAperarLYEDRRSSALYFAVVNNNVYATELLLQ 330
Cdd:PHA02884  19 IIFYIAIKKKNKICIANI--LYSSIKFHYTDIIDAILKLGADPEAPFP-----LSENSKTNPLIYAIDCDNDDAAKLLIR 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767980726 331 HGADPNR----DVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAFPATIMFamkCLSLLKFLMdlgCDGE 401
Cdd:PHA02884  92 YGADVNRyaeeAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALMI---CNNFLAFMI---CDNE 160
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 168-196 3.43e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 3.43e-04
                           10        20
                   ....*....|....*....|....*....
gi 767980726   168 YGITPLFVAAQSGQLEALRFLAKYGADIN 196
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
63-298 8.05e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 165.13  E-value: 8.05e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  63 IDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHE 142
Cdd:COG0666   47 LALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 143 SVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLL 222
Cdd:COG0666  127 AAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLL 206

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767980726 223 SQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIR-RSGVSPLHLAAERNHDEVLEALLSARFDVNTPLA 298
Cdd:COG0666  207 EAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKdKDGLTALLLAAAAGAALIVKLLLLALLLLAAALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-255 4.21e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 160.50  E-value: 4.21e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726   4 ADPLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHL 83
Cdd:COG0666   21 LALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDL 100

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  84 DCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVE 163
Cdd:COG0666  101 EIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVN 180

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 164 SKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIAS 243
Cdd:COG0666  181 ARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260

                        250
                 ....*....|..
gi 767980726 244 KKGNYRIVQMLL 255
Cdd:COG0666  261 AAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
63-317 1.71e-42

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 153.57  E-value: 1.71e-42
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  63 IDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHE 142
Cdd:COG0666   14 ALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHA 93

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 143 SVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLL 222
Cdd:COG0666   94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLL 173

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 223 SQGADANKTNKDGLLPLHIASKKGNYRIVQMLL----PVTSRTrirRSGVSPLHLAAERNHDEVLEALLSARFDVNTPLA 298
Cdd:COG0666  174 EAGADVNARDNDGETPLHLAAENGHLEIVKLLLeagaDVNAKD---NDGKTALDLAAENGNLEIVKLLLEAGADLNAKDK 250

                        250
                 ....*....|....*....
gi 767980726 299 PERARLYEDRRSSALYFAV 317
Cdd:COG0666  251 DGLTALLLAAAAGAALIVK 269
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
4-239 1.37e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 150.87  E-value: 1.37e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726   4 ADPLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGCLKVLQRAyPGTIDQRTLQEETAVYLATCRGHL 83
Cdd:COG0666   55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEA-GADVNARDKDGETPLHLAAYNGNL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  84 DCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVE 163
Cdd:COG0666  134 EIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN 213

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767980726 164 SKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPL 239
Cdd:COG0666  214 AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
86-376 7.40e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 148.95  E-value: 7.40e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  86 LLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESK 165
Cdd:COG0666    4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 166 NAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKK 245
Cdd:COG0666   84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 246 GNYRIVQMLL----PVTSRTrirRSGVSPLHLAAERNHDEVLEALLSARFDVNTPlaperarlyEDRRSSALYFAVVNNN 321
Cdd:COG0666  164 GNLEIVKLLLeagaDVNARD---NDGETPLHLAAENGHLEIVKLLLEAGADVNAK---------DNDGKTALDLAAENGN 231

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 767980726 322 VYATELLLQHGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAF 376
Cdd:COG0666  232 LEIVKLLLEAGADLNakdKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
116-375 1.29e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 134.70  E-value: 1.29e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 116 AEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADI 195
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 196 NTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL----PVTSRTrirRSGVSPL 271
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLeagaDVNAQD---NDGNTPL 157

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 272 HLAAERNHDEVLEALLSARFDVNTPlaperarlyEDRRSSALYFAVVNNNVYATELLLQHGADPN---RDVISPLLVAIR 348
Cdd:COG0666  158 HLAAANGNLEIVKLLLEAGADVNAR---------DNDGETPLHLAAENGHLEIVKLLLEAGADVNakdNDGKTALDLAAE 228

                        250       260
                 ....*....|....*....|....*..
gi 767980726 349 HGCLRTMQLLLDHGANIDAYIATHPTA 375
Cdd:COG0666  229 NGNLEIVKLLLEAGADLNAKDKDGLTA 255
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 96-330 1.27e-25

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 108.98  E-value: 1.27e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  96 PDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALH-----ESVSRNDLEVMQILVSGGAKVESKNAYGI 170
Cdd:PHA03100  28 NDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGI 107

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 171 TPLFVAAQ--SGQLEALRFLAKYGADINTQASDNASALYEACKNEHE--EVVEFLLSQGADANKTNK-DGLL-------- 237
Cdd:PHA03100 108 TPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRvNYLLsygvpini 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 238 -------PLHIASKKGNYRIVQMLLPVTSRTRIR-RSGVSPLHLAAERNHDEVLEALLSARFDVNTplaperarlyedRR 309
Cdd:PHA03100 188 kdvygftPLHYAVYNNNPEFVKYLLDLGANPNLVnKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT------------II 255

                        250       260
                 ....*....|....*....|..
gi 767980726 310 SSALYFAVVN-NNVYATELLLQ 330
Cdd:PHA03100 256 ETLLYFKDKDlNTITKIKMLKK 277
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
 489-533 2.40e-23

SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ASB2 targets specific proteins to destruction by the proteasome in leukemia cells that have been induced to differentiate. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239691  Cd Length: 45  Bit Score: 92.62  E-value: 2.40e-23
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767980726 489 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ 533
Cdd:cd03721    1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ 45
PHA03095 PHA03095
ankyrin-like protein; Provisional
 97-378 1.10e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 100.87  E-value: 1.10e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  97 DISNKSRETPLYK---ACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRN---DLEVMQILVSGGAKVESKNAYGI 170
Cdd:PHA03095   5 ESVDIIMEAALYDyllNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGF 84

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 171 TPLFVAAQSGQ-LEALRFLAKYGADINTQ--ASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHI--ASKK 245
Cdd:PHA03095  85 TPLHLYLYNATtLDVIKLLIKAGADVNAKdkVGRTPLHVYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVllKSRN 164

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 246 GNYRIVQMLLPVTSRTRIRRS-GVSPLHLAAE--RNHDEVLEALLSARFDV-------NTPLaPERARLYEDRRS----- 310
Cdd:PHA03095 165 ANVELLRLLIDAGADVYAVDDrFRSLLHHHLQsfKPRARIVRELIRAGCDPaatdmlgNTPL-HSMATGSSCKRSlvlpl 243

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 311 ---------------SALYFAVVNNNVYATELLLQHGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATH 372
Cdd:PHA03095 244 liagisinarnrygqTPLHYAAVFNNPRACRRLIALGADINavsSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATL 323


                 ....*.
gi 767980726 373 PTAFPA 378
Cdd:PHA03095 324 NTASVA 329
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 63-367 1.54e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 101.68  E-value: 1.54e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  63 IDQRTLQEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVqhnaDTNHRCNRGWTALHE 142
Cdd:PHA02876 171 VNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAII----DNRSNINKNDLSLLK 246

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 143 SVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEAL-RFLAKYGADINTQASDNASALYEACKNEHE-EVVEF 220
Cdd:PHA02876 247 AIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYDtENIRT 326

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 221 LLSQGADANKTNKDGLLPLHIASKKGNYR-IVQMLLPVTSRTRIRR-SGVSPLHLAAERNHDEVLEALLSARFDVNTpla 298
Cdd:PHA02876 327 LIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDyCDKTPIHYAAVRNNVVIINTLLDYGADIEA--- 403

                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767980726 299 perarlYEDRRSSALYFAVVNNNVY-ATELLLQHGAD---PNRDVISPLLVAIRHGC-LRTMQLLLDHGANIDA 367
Cdd:PHA02876 404 ------LSQKIGTALHFALCGTNPYmSVKTLIDRGANvnsKNKDLSTPLHYACKKNCkLDVIEMLLDNGADVNA 471
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 75-255 1.62e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.04  E-value: 1.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  75 YLATCRGHLDCLLSLLQAGAEPDISNKSRETPL-----YKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSR--N 147
Cdd:PHA03100  40 YLAKEARNIDVVKILLDNGADINSSTKNNSTPLhylsnIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksN 119

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 148 DLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQ--LEALRFLAKYGADIN--------------TQASDN--ASALYEA 209
Cdd:PHA03100 120 SYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINaknrvnyllsygvpINIKDVygFTPLHYA 199

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 767980726 210 CKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 255
Cdd:PHA03100 200 VYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
Ank_2 pfam12796
Ankyrin repeats (3 copies);
107-198 1.12e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 83.63  E-value: 1.12e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  107 LYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSgGAKVESKNaYGITPLFVAAQSGQLEALR 186
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 767980726  187 FLAKYGADINTQ 198
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
206-295 2.39e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.86  E-value: 2.39e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  206 LYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPvTSRTRIRRSGVSPLHLAAERNHDEVLEA 285
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|
gi 767980726  286 LLSARFDVNT 295
Cdd:pfam12796  80 LLEKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 97-297 6.87e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 89.25  E-value: 6.87e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  97 DISNKSRETPLYKACERKNAEAVKILVQHNADTNHRC----NRGWTALheSVSRNDL---------------------EV 151
Cdd:PHA02874  29 NISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINtkipHPLLTAI--KIGAHDIikllidngvdtsilpipciekDM 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 152 MQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKT 231
Cdd:PHA02874 107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767980726 232 NKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIR-RSGVSPLHLAAERNHdEVLEALLSARF----DVN--TPL 297
Cdd:PHA02874 187 DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKcKNGFTPLHNAIIHNR-SAIELLINNASindqDIDgsTPL 258
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 77-294 1.05e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 88.51  E-value: 1.05e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  77 ATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILV 156
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 157 SGGAKVES---KNayGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNK 233
Cdd:PHA02875  89 DLGKFADDvfyKD--GMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDC 166

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767980726 234 DGLLPLHIASKKGNYRIVQMLLPVTSRTRI--RRSGVSPLHLAAERNHDEVLEALLSARFDVN 294
Cdd:PHA02875 167 CGCTPLIIAMAKGDIAICKMLLDSGANIDYfgKNGCVAALCYAIENNKIDIVRLFIKRGADCN 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
140-232 1.99e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 80.16  E-value: 1.99e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  140 LHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYgADINTQaSDNASALYEACKNEHEEVVE 219
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 767980726  220 FLLSQGADANKTN 232
Cdd:pfam12796  79 LLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
76-166 3.24e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.39  E-value: 3.24e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726   76 LATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHnADTNHRCNrGWTALHESVSRNDLEVMQIL 155
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVKLL 80

                          90
                  ....*....|.
gi 767980726  156 VSGGAKVESKN 166
Cdd:pfam12796  81 LEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 6-196 3.42e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 86.97  E-value: 3.42e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726   6 PLIKAIKDGDEEALKTMIKEGK--NLAEPNKEGwlPLHEAAYYGQVGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHL 83
Cdd:PHA02875  38 PIKLAMKFRDSEAIKLLMKHGAipDVKYPDIES--ELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKL 115

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  84 DCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVE 163
Cdd:PHA02875 116 DIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANID 195

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 767980726 164 --SKNAyGITPLFVAAQSGQLEALRFLAKYGADIN 196
Cdd:PHA02875 196 yfGKNG-CVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 6-288 4.20e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 86.56  E-value: 4.20e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726   6 PLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAyygQVGCLKVLQRAYPGTIDqrtlqeeTAVYLATCRGHlDC 85
Cdd:PHA02874  38 PLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAI---KIGAHDIIKLLIDNGVD-------TSILPIPCIEK-DM 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  86 LLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESK 165
Cdd:PHA02874 107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVK 186

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 166 NAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKneHEEVVEFLLSQGADANKTNKDGLLPLHIA-SK 244
Cdd:PHA02874 187 DNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAiNP 264

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|....*.
gi 767980726 245 KGNYRIVQMLLPVTSRTRIR-RSGVSPLHLAAER-NHDEVLEALLS 288
Cdd:PHA02874 265 PCDIDIIDILLYHKADISIKdNKGENPIDTAFKYiNKDPVIKDIIA 310
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 82-361 1.48e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 85.32  E-value: 1.48e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  82 HLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQhnadTNHRCNRGWT--ALHESVSRNDLEVMQILVSGg 159
Cdd:PHA02878  49 NLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIR----SINKCSVFYTlvAIKDAFNNRNVEIFKIILTN- 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 160 akvESKNAYGITPLFVAAQSG----QLEALRFLAKYGADINTQASDN-ASALYEACKNEHEEVVEFLLSQGADANKTNKD 234
Cdd:PHA02878 124 ---RYKNIQTIDLVYIDKKSKddiiEAEITKLLLSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 235 GLLPLHIASKKGNYRIVQMLLPVTSRTRIRRS-GVSPLHLAAERNHD-EVLEALLSARFDVNtplaperARLYeDRRSSA 312
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKcGNTPLHISVGYCKDyDILKLLLEHGVDVN-------AKSY-ILGLTA 272

                        250       260       270       280       290
                 ....*....|....*....|....*....|....*....|....*....|...
gi 767980726 313 LYFAVVNNNVyaTELLLQHGADPNR---DVISPLLVAIR-HGCLRTMQLLLDH 361
Cdd:PHA02878 273 LHSSIKSERK--LKLLLEYGADINSlnsYKLTPLSSAVKqYLCINIGRILISN 323
Ank_2 pfam12796
Ankyrin repeats (3 copies);
173-255 1.70e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 1.70e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  173 LFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQgADANKTNkDGLLPLHIASKKGNYRIVQ 252
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78


                  ...
gi 767980726  253 MLL 255
Cdd:pfam12796  79 LLL 81
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 3-245 2.12e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 81.85  E-value: 2.12e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726   3 PADPLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLH-------------------------------EAAYYGQVGC 51
Cdd:PHA02878  37 PFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHiickepnklgmkemirsinkcsvfytlvaikDAFNNRNVEI 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  52 LK-VLQRAYPGTIDQRTLQEETAVYLATCRGHLDCLLslLQAGAEPDISNKSR-ETPLYKACERKNAEAVKILVQHNADT 129
Cdd:PHA02878 117 FKiILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLL--LSYGADINMKDRHKgNTALHYATENKDQRLTELLLSYGANV 194

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 130 N--HRCNRgwTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQS-GQLEALRFLAKYGADINTQAS-DNASA 205
Cdd:PHA02878 195 NipDKTNN--SPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYiLGLTA 272

                        250       260       270       280
                 ....*....|....*....|....*....|....*....|
gi 767980726 206 LYEACKNEheEVVEFLLSQGADANKTNKDGLLPLHIASKK 245
Cdd:PHA02878 273 LHSSIKSE--RKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 176-373 4.66e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.42  E-value: 4.66e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 176 AAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 255
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 256 PVTSRTR--IRRSGVSPLHLAAERNHDEVLEALLSARFDVNTPlaperarlyEDRRSSALYFAVVNNNVYATELLLQHGA 333
Cdd:PHA02875  89 DLGKFADdvFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP---------NTDKFSPLHLAVMMGDIKGIELLIDHKA 159

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767980726 334 DPNRDV---ISPLLVAIRHGCLRTMQLLLDHGANIDaYIATHP 373
Cdd:PHA02875 160 CLDIEDccgCTPLIIAMAKGDIAICKMLLDSGANID-YFGKNG 201
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 7-265 5.20e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 81.26  E-value: 5.20e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726   7 LIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGCL--KVLQRAypGTIDQRTLQEETAVYLATCRGH-L 83
Cdd:PHA02876 244 LLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvpKLLERG--ADVNAKNIKGETPLYLMAKNGYdT 321

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  84 DCLLSLLQAGAEPDISNKSRETPLYKACE-RKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKV 162
Cdd:PHA02876 322 ENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADI 401

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 163 ES-KNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHE-EVVEFLLSQGADANKTNKDGLLPLH 240
Cdd:PHA02876 402 EAlSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLL 481

                        250       260
                 ....*....|....*....|....*
gi 767980726 241 IAskKGNYRIVQMLLPVTSRTRIRR 265
Cdd:PHA02876 482 IA--LEYHGIVNILLHYGAELRDSR 504
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 86-234 1.27e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 76.83  E-value: 1.27e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  86 LLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGgAKVESK 165
Cdd:PLN03192 541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHF-ASISDP 619

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767980726 166 NAYGiTPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKD 234
Cdd:PLN03192 620 HAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 140-399 1.65e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 76.26  E-value: 1.65e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 140 LHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNAS--------------- 204
Cdd:PHA02876 149 IKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSvlecavdsknidtik 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 205 --------------ALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNY-RIVQMLLPVTSRTRIRR-SGV 268
Cdd:PHA02876 229 aiidnrsninkndlSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNiKGE 308

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 269 SPLHLAAERNHD-EVLEALLSARFDVN-------TPL--------------------APERARLYEDRrsSALYFAVVNN 320
Cdd:PHA02876 309 TPLYLMAKNGYDtENIRTLIMLGADVNaadrlyiTPLhqastldrnkdivitllelgANVNARDYCDK--TPIHYAAVRN 386

                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 321 NVYATELLLQHGADPnrDVISPLLVAIRHGCL------RTMQLLLDHGANIDA---YIAThptafPATIMFAMKC-LSLL 390
Cdd:PHA02876 387 NVVIINTLLDYGADI--EALSQKIGTALHFALcgtnpyMSVKTLIDRGANVNSknkDLST-----PLHYACKKNCkLDVI 459


                 ....*....
gi 767980726 391 KFLMDLGCD 399
Cdd:PHA02876 460 EMLLDNGAD 468
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
 489-530 8.90e-14

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


Pssm-ID: 239686  Cd Length: 42  Bit Score: 65.21  E-value: 8.90e-14
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 767980726 489 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 530
Cdd:cd03716    1 STPRSLQHLCRLAIRRCLGRRRLELIKKLPLPPRLKDYLLYE 42
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
 491-530 1.46e-13

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


Pssm-ID: 239641  Cd Length: 41  Bit Score: 64.80  E-value: 1.46e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 767980726 491 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 530
Cdd:cd03587    2 PRSLQHLCRLAIRRCLGKRRLDLIDKLPLPPRLKDYLLYK 41
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 100-246 3.90e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 68.31  E-value: 3.90e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 100 NKSRETPLYKACERKNA--EAVKILVQHNADTNHRC-NRGWTALHESVSRN---DLEVMQILVSGGAKVESKNAYGITPL 173
Cdd:PHA02859  48 NDLYETPIFSCLEKDKVnvEILKFLIENGADVNFKTrDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLL 127

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 767980726 174 --FVAAQSGQLEALRFLAKYGADINTQASDNASALYEACK-NEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKG 246
Cdd:PHA02859 128 hmYMCNFNVRINVIKLLIDSGVSFLNKDFDNNNILYSYILfHSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 179-373 2.36e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.84  E-value: 2.36e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 179 SGQLEALRFLAKYGAD-INTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPv 257
Cdd:PHA02874  11 SGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID- 89

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 258 tsrtrirrSGVSPLHLAAERNHDEVLEALLSARFDVNTplaperarlyEDRRSSA-LYFAVVNNNVYATELLLQHGADPN 336
Cdd:PHA02874  90 --------NGVDTSILPIPCIEKDMIKTILDCGIDVNI----------KDAELKTfLHYAIKKGDLESIKMLFEYGADVN 151

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 767980726 337 RDVIS---PLLVAIRHGCLRTMQLLLDHGA--NIDAYIATHP 373
Cdd:PHA02874 152 IEDDNgcyPIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGESP 193
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 72-202 7.43e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.97  E-value: 7.43e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  72 TAVYLATCRGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCnrGWTALHESVSRNDLEV 151
Cdd:PLN03192 560 TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHA--AGDLLCTAAKRNDLTA 637

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 767980726 152 MQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDN 202
Cdd:PLN03192 638 MKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDD 688
Ank_2 pfam12796
Ankyrin repeats (3 copies);
271-367 9.39e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 9.39e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  271 LHLAAERNHDEVLEALLSARFDVNtplaperarLYEDRRSSALYFAVVNNNVYATELLLQHgADPNRDVI--SPLLVAIR 348
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNgrTALHYAAR 70

                          90
                  ....*....|....*....
gi 767980726  349 HGCLRTMQLLLDHGANIDA 367
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
7-100 1.15e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.90  E-value: 1.15e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726    7 LIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGCLKVLQRAYPGtidQRTLQEETAVYLATCRGHLDCL 86
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV---NLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|....
gi 767980726   87 LSLLQAGAEPDISN 100
Cdd:pfam12796  78 KLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 38-255 2.71e-11

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 66.19  E-value: 2.71e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  38 LPLHEAAYYGQVGCLKVLQRAYPGTIDQRTLQEETAVYLATCRGHLDCLLSLLQAGaePDISNKSRETPLYKacerknae 117
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAA--PELVNEPMTSDLYQ-------- 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 118 avkilvqhnadtnhrcnrGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLE 183
Cdd:cd22192   89 ------------------GETALHIAVVNQNLNLVRELIARGADVVSPRAtgtffrpgpknliyYGEHPLSFAACVGNEE 150

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 184 ALRFLAKYGADINTQASDNASALY----EACKNEHEEVVEFLLSQGADANK------TNKDGLLPLHIASKKGNYRIVQM 253
Cdd:cd22192  151 IVRLLIEHGADIRAQDSLGNTVLHilvlQPNKTFACQMYDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQH 230


                 ..
gi 767980726 254 LL 255
Cdd:cd22192  231 LV 232
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 490-528 3.60e-11

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


Pssm-ID: 462192  Cd Length: 39  Bit Score: 57.95  E-value: 3.60e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 767980726  490 PPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLK 528
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
Ank_4 pfam13637
Ankyrin repeats (many copies);
204-255 3.61e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.44  E-value: 3.61e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767980726  204 SALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 255
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 170-365 6.47e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.60  E-value: 6.47e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 170 ITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANktnkdgLLPLHIASKKGNYR 249
Cdd:PHA02874  36 TTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTS------ILPIPCIEKDMIKT 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 250 IVQMLLPVTSRTRIRRSGvspLHLAAERNHDEVLEALLSARFDVNtplaperarLYEDRRSSALYFAVVNNNVYATELLL 329
Cdd:PHA02874 110 ILDCGIDVNIKDAELKTF---LHYAIKKGDLESIKMLFEYGADVN---------IEDDNGCYPIHIAIKHNFFDIIKLLL 177

                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 767980726 330 QHGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANI 365
Cdd:PHA02874 178 EKGAYANvkdNNGESPLHNAAEYGDYACIKLLIDHGNHI 216
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 206-371 7.40e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 64.30  E-value: 7.40e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 206 LYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIAS----------------------------------------KK 245
Cdd:PHA03100  39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynltdvkeivkllleyganvnapdnngitpllyaiskKS 118

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 246 GNYRIVQMLLPVTSRTRIRRS-GVSPLHLAAERNHD--EVLEALLSARFDVNtplAPERARLY----------EDRRSSA 312
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSdGENLLHLYLESNKIdlKILKLLIDKGVDIN---AKNRVNYLlsygvpinikDVYGFTP 195

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767980726 313 LYFAVVNNNVYATELLLQHGADPN-RDVI--SPLLVAIRHGCLRTMQLLLDHGANIDAYIAT 371
Cdd:PHA03100 196 LHYAVYNNNPEFVKYLLDLGANPNlVNKYgdTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
PHA03095 PHA03095
ankyrin-like protein; Provisional
 15-214 2.85e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.35  E-value: 2.85e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  15 DEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQV-GCLKVLQRA-----YPGTIDQRTLQeetaVYLATCRGHLDCLLS 88
Cdd:PHA03095  62 VKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVIKLLIKAgadvnAKDKVGRTPLH----VYLSGFNINPKVIRL 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  89 LLQAGAEPDISNKSRETPLYKACERKNA--EAVKILVQHNADTNHRCNRGWTALH---------ESVSRNDLE------- 150
Cdd:PHA03095 138 LLRKGADVNALDLYGMTPLAVLLKSRNAnvELLRLLIDAGADVYAVDDRFRSLLHhhlqsfkprARIVRELIRagcdpaa 217

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 151 ---------------------VMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEA 209
Cdd:PHA03095 218 tdmlgntplhsmatgssckrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLM 297


                 ....*
gi 767980726 210 CKNEH 214
Cdd:PHA03095 298 VRNNN 302
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 198-367 5.58e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 61.43  E-value: 5.58e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 198 QASDNASA-----LYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIRRSGVSpLH 272
Cdd:PHA02878  28 NYSTSASLipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVA-IK 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 273 LAAERNHDEVLEALLSARFDVN--------------TPLAPERARLY-----------EDRRSSALYFAVVNNNVYATEL 327
Cdd:PHA02878 107 DAFNNRNVEIFKIILTNRYKNIqtidlvyidkkskdDIIEAEITKLLlsygadinmkdRHKGNTALHYATENKDQRLTEL 186

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 767980726 328 LLQHGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDA 367
Cdd:PHA02878 187 LLSYGANVNipdKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
Ank_4 pfam13637
Ankyrin repeats (many copies);
171-222 7.48e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 54.59  E-value: 7.48e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 767980726  171 TPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLL 222
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 2-190 6.33e-09

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: 6.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726   2 RPAD-PLIKAIKDGDEEALKTMIK-EGKNLAEPNKEGWLPLHEAAYYGQVGCLKVLQRAYPGTIDQRTLQE----ETAVY 75
Cdd:cd22192   15 RISEsPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMTSDlyqgETALH 94

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  76 LATCRGHLDCLLSLLQAGAepDISN---------KSR-------ETPL-YKACErKNAEAVKILVQHNADTNHRCNRGWT 138
Cdd:cd22192   95 IAVVNQNLNLVRELIARGA--DVVSpratgtffrPGPknliyygEHPLsFAACV-GNEEIVRLLIEHGADIRAQDSLGNT 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 767980726 139 ALHESVSRND----LEVMQILVSGGAKVES------KNAYGITPLFVAAQSGQLEALRFLAK 190
Cdd:cd22192  172 VLHILVLQPNktfaCQMYDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLVQ 233
PHA02946 PHA02946
ankyin-like protein; Provisional
 89-273 1.18e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 57.37  E-value: 1.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  89 LLQAGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRND--LEVMQILVSGGAKVE-SK 165
Cdd:PHA02946  58 LLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKINnSV 137

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 166 NAYGITPLFVAAQSGQLEALRFLA-KYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASK 244
Cdd:PHA02946 138 DEEGCGPLLACTDPSERVFKKIMSiGFEARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCS 217

                        170       180       190
                 ....*....|....*....|....*....|.
gi 767980726 245 K--GNYRIVQMLLPVTSRTRIRRSGVSPLHL 273
Cdd:PHA02946 218 KtvKNVDIINLLLPSTDVNKQNKFGDSPLTL 248
PHA02798 PHA02798
ankyrin-like protein; Provisional
 119-348 1.77e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 56.77  E-value: 1.77e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 119 VKILVQHNADTNHRCNRGWTALHESVSR---NDLEVMQILVSGGAKVESKNAYGITPLFVAAQSG---QLEALRFLAKYG 192
Cdd:PHA02798  92 VKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKG 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 193 ADINTQASDNA-SALYEACKNEHE----EVVEFLLSQGADANKTNK-------DGLLPLHIASKKGNYRIVQMLLPVTSR 260
Cdd:PHA02798 172 VDINTHNNKEKyDTLHCYFKYNIDridaDILKLFVDNGFIINKENKshkkkfmEYLNSLLYDNKRFKKNILDFIFSYIDI 251

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 261 TRIRRSGVSPLHLAAERNHDEVLEALLSARFDVN--TPLAperarlyedrrSSALYFAVVNNNVYATELLLQHgaDPNRD 338
Cdd:PHA02798 252 NQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINiiTELG-----------NTCLFTAFENESKFIFNSILNK--KPNKN 318

                        250
                 ....*....|
gi 767980726 339 VISPLLVAIR 348
Cdd:PHA02798 319 TISYTYYKLR 328
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 177-255 2.12e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 2.12e-08
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 767980726 177 AQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 255
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
 492-530 3.40e-08

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


Pssm-ID: 198037  Cd Length: 34  Bit Score: 49.33  E-value: 3.40e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 767980726   492 RPLAHLCRLRVRKAIGKyriklLDTLPLPGRLIRYLKYE 530
Cdd:smart00969   1 RSLQHLCRLAIRRSLGG-----IDKLPLPPRLKDYLLYY 34
SOCS_SSB1_4 cd03718
SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box ...
 491-530 4.86e-08

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


Pssm-ID: 239688  Cd Length: 42  Bit Score: 49.22  E-value: 4.86e-08
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 767980726 491 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 530
Cdd:cd03718    3 PLPLMDLCRRRVRVALGRDRLEEIEQLPLPPSLKNYLLYQ 42
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 6-168 1.01e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 54.29  E-value: 1.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726   6 PLIKAI--KDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGcLKVLQraypgtidqrTLQEETAVYLATCRghL 83
Cdd:PHA03100 109 PLLYAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKID-LKILK----------LLIDKGVDINAKNR--V 175

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  84 DCLLSLlqaGAEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVE 163
Cdd:PHA03100 176 NYLLSY---GVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252


                 ....*
gi 767980726 164 SKNAY 168
Cdd:PHA03100 253 TIIET 257
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 237-384 1.29e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 54.25  E-value: 1.29e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 237 LPLHIASKKGNYRIVQMLLpVTSRTRIRRSGV---SPLHLAAERNHDEVLEALL-SARFDVNTPLAPErarLYEDRrsSA 312
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLL-KCPSCDLFQRGAlgeTALHVAALYDNLEAAVVLMeAAPELVNEPMTSD---LYQGE--TA 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 313 LYFAVVNNNVYATELLLQHGAD------------PNRDVI-----SPLLVAIRHGCLRTMQLLLDHGANIDA-------- 367
Cdd:cd22192   93 LHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIRAqdslgntv 172

                        170
                 ....*....|....*....
gi 767980726 368 --YIATHPTAFPATIMFAM 384
Cdd:cd22192  173 lhILVLQPNKTFACQMYDL 191
SOCS_ASB1 cd03720
SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a ...
 491-530 1.34e-07

SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239690  Cd Length: 42  Bit Score: 47.80  E-value: 1.34e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 767980726 491 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 530
Cdd:cd03720    3 PRSLLSLCRIAVRRALGKQRLSLICSLPLPDPIKKFLLHE 42
Ank_4 pfam13637
Ankyrin repeats (many copies);
103-156 1.51e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 1.51e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767980726  103 RETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILV 156
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
5-55 1.63e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.04  E-value: 1.63e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 767980726    5 DPLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGCLKVL 55
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
SOCS_ASB14 cd03730
SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a ...
 489-530 1.70e-07

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


Pssm-ID: 239700  Cd Length: 57  Bit Score: 47.92  E-value: 1.70e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767980726 489 EPPRPLAHLCRLRVRKAIGKYRIK---LLDTLPLPGRLIRYLKYE 530
Cdd:cd03730    1 TNPRSLKHLCRLKIRACMGRLRLRcpvFMSFLPLPNRLKAYILYK 45
SOCS_SSB4 cd03743
SOCS (suppressors of cytokine signaling) box of SSB4 (SPRY domain-containing SOCS box ...
 491-530 2.41e-07

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


Pssm-ID: 239712  Cd Length: 42  Bit Score: 47.26  E-value: 2.41e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 767980726 491 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 530
Cdd:cd03743    3 PLPLMDLCRRSARQALGRHRLHHIQSLPLPQTLKNYLQYQ 42
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 135-255 3.28e-07

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 53.16  E-value: 3.28e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  135 RGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAKYGADINTQAS 200
Cdd:TIGR00870 127 PGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADS 206

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767980726  201 -----DNASALYEACKNEHEEVV----EFLLSQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 255
Cdd:TIGR00870 207 lgntlLHLLVMENEFKAEYEELScqmyNFALSLLDKLRDSkelevilNHQGLTPLKLAAKEGRIVLFRLKL 277
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
 491-529 3.41e-07

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


Pssm-ID: 239687  Cd Length: 39  Bit Score: 46.82  E-value: 3.41e-07
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 767980726 491 PRPLAHLCRLRVRKAIGKYRIkllDTLPLPGRLIRYLKY 529
Cdd:cd03717    3 VRSLQHLCRFVIRQCTRRDLI---DQLPLPRRLKDYLKE 38
SOCS_SOCS7 cd03741
SOCS (suppressors of cytokine signaling) box of SOCS7-like proteins. Together with CIS1, the ...
 492-531 7.50e-07

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


Pssm-ID: 239710  Cd Length: 49  Bit Score: 45.86  E-value: 7.50e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 767980726 492 RPLAHLCRLRVRKAIgkyRIKLLDTLPLPGRLIRYLKYEN 531
Cdd:cd03741    4 QSLQHLCRFVIRKLV---RRDHIPALPLPRRLIDYLREKH 40
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 251-401 1.11e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 50.37  E-value: 1.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 251 VQMLLPVTSRTRIRRSGVspLHLAAERNHDEVLEALLSARFDVNTPLAperarLYEDRRSSALYFAVVNNNVYATELLLQ 330
Cdd:PHA02884  19 IIFYIAIKKKNKICIANI--LYSSIKFHYTDIIDAILKLGADPEAPFP-----LSENSKTNPLIYAIDCDNDDAAKLLIR 91

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 767980726 331 HGADPNR----DVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAFPATIMFamkCLSLLKFLMdlgCDGE 401
Cdd:PHA02884  92 YGADVNRyaeeAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALMI---CNNFLAFMI---CDNE 160
SOCS smart00253
suppressors of cytokine signalling; suppressors of cytokine signalling
 485-529 2.20e-06

suppressors of cytokine signalling; suppressors of cytokine signalling


Pssm-ID: 128549  Cd Length: 43  Bit Score: 44.59  E-value: 2.20e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 767980726   485 KEKAEPPRPLAHLCRLRVRKAIGKYRIKlldTLPLPGRLIRYLKY 529
Cdd:smart00253   1 LPRPSNVPSLQHLCRFTIRRCTRTDQIK---TLPLPPKLKDYLSY 42
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 135-255 3.18e-06

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 49.88  E-value: 3.18e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 135 RGWTALHESVSRNDLEVMQILVSGGAKVESKNA-------------YGITPLFVAAQSGQLEALRFLAKYGADI-NTQAS 200
Cdd:cd21882   72 QGQTALHIAIENRNLNLVRLLVENGADVSARATgrffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQPaALEAQ 151

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767980726 201 DNAS-----ALYEACKNEHE------EVVEFLLSQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 255
Cdd:cd21882  152 DSLGntvlhALVLQADNTPEnsafvcQMYNLLLSYGAHLDPTqqleeipNHQGLTPLKLAAVEGKIVMFQHIL 224
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 126-255 3.88e-06

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 49.76  E-value: 3.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 126 NADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAKY 191
Cdd:cd22194  131 NAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnpkykhegfyFGETPLALAACTNQPEIVQLLMEK 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 192 GADI--------NT------QASDNASA-------LYE----ACKNEHEEVVefllsqgadankTNKDGLLPLHIASKKG 246
Cdd:cd22194  211 ESTDitsqdsrgNTvlhalvTVAEDSKTqndfvkrMYDmillKSENKNLETI------------RNNEGLTPLQLAAKMG 278


                 ....*....
gi 767980726 247 NYRIVQMLL 255
Cdd:cd22194  279 KAEILKYIL 287
SOCS_SSB2 cd03719
SOCS (suppressors of cytokine signaling) box of SSB2 (SPRY domain-containing SOCS box proteins) ...
 489-530 6.81e-06

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


Pssm-ID: 239689  Cd Length: 42  Bit Score: 43.09  E-value: 6.81e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 767980726 489 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 530
Cdd:cd03719    1 AEPHSLLHLSRLCVRHALGDTRLGQVSALPLPPAMKRYLLYQ 42
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 140-334 7.42e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.71  E-value: 7.42e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 140 LHESVSRNDLEVMQILVSGGAkvESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVE 219
Cdd:PLN03192 498 LQHHKELHDLNVGDLLGDNGG--EHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVL 575

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 220 FLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIRRSGvSPLHLAAERNHDEVLEALLSARFDVNTplap 299
Cdd:PLN03192 576 VLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDS---- 650

                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 767980726 300 erarlyEDRR-SSALYFAVVNNNVYATELLLQHGAD 334
Cdd:PLN03192 651 ------EDHQgATALQVAMAEDHVDMVRLLIMNGAD 680
SOCS_SSB1 cd03744
SOCS (suppressors of cytokine signaling) box of SSB1 (SPRY domain-containing SOCS box proteins) ...
 491-530 8.11e-06

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


Pssm-ID: 239713  Cd Length: 42  Bit Score: 43.05  E-value: 8.11e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 767980726 491 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 530
Cdd:cd03744    3 PLPLMDLCRRSVRLALGRERLSEIHTLPLPASLKNYLLYQ 42
Ank_4 pfam13637
Ankyrin repeats (many copies);
136-188 9.58e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.03  E-value: 9.58e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767980726  136 GWTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFL 188
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
89-141 9.67e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 9.67e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767980726   89 LLQAG-AEPDISNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNRGWTALH 141
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALD 54
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
 489-530 1.32e-05

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


Pssm-ID: 239701  Cd Length: 56  Bit Score: 42.51  E-value: 1.32e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 767980726 489 EPPRPLAHLCRLRVRKAIGKYRIKLLDT---LPLPGRLIRYLKYE 530
Cdd:cd03731    1 ENPRPLKHLCRLKIRKLMGLQKLQQPSSmkkLPLPPALKRYILYK 45
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 162-294 1.76e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.97  E-value: 1.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 162 VESKNAYGITPLF--VAAQSGQLEALRFLAKYGADINTQASD-NASALYEAC---KNEHEEVVEFLLSQGADANKTNKDG 235
Cdd:PHA02859  44 VNDCNDLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRDnNLSALHHYLsfnKNVEPEILKILIDSGSSITEEDEDG 123

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 236 LLPLHIASKKGNYRIVQMLLpvtsrtrIRRSGVSPLHLAAERNH-----------DEVLEALLSARFDVN 294
Cdd:PHA02859 124 KNLLHMYMCNFNVRINVIKL-------LIDSGVSFLNKDFDNNNilysyilfhsdKKIFDFLTSLGIDIN 186
PHA02946 PHA02946
ankyin-like protein; Provisional
 198-255 1.79e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 47.36  E-value: 1.79e-05
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 198 QASDNASALYEAC--KNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 255
Cdd:PHA02946  33 EPSGNYHILHAYCgiKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLL 92
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 153-223 2.10e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 2.10e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 767980726 153 QILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLS 223
Cdd:PTZ00322  99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
80-123 2.66e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 2.66e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 767980726   80 RGHLDCLLSLLQAGAEPDISNKSRETPLYKACERKNAEAVKILV 123
Cdd:pfam13637  11 SGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SOCS_ASB13 cd03729
SOCS (suppressors of cytokine signaling) box of ASB13-like proteins. ASB family members have a ...
 491-529 3.43e-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: 40.92  E-value: 3.43e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 767980726 491 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKY 529
Cdd:cd03729    3 PLSLQQLCRINLRKALGTRALEKIAKLNIPNRIIDYLSY 41
SOCS_ASB5 cd03724
SOCS (suppressors of cytokine signaling) box of ASB5-like proteins. ASB family members have a ...
 491-529 3.62e-05

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


Pssm-ID: 239694  Cd Length: 42  Bit Score: 41.02  E-value: 3.62e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 767980726 491 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKY 529
Cdd:cd03724    3 PSSLCQLCRLCIRNYIGRSRLHLIPQLQLPTLLKNFLQY 41
SOCS_ASB7 cd03726
SOCS (suppressors of cytokine signaling) box of ASB7-like proteins. ASB family members have a ...
 491-530 6.60e-05

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


Pssm-ID: 239696  Cd Length: 45  Bit Score: 40.22  E-value: 6.60e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 767980726 491 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 530
Cdd:cd03726    3 PRTLQDLCRIKIRHCIGLQNLKLLDELPIAKVMKDYLKHK 42
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 141-222 1.28e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 44.73  E-value: 1.28e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 141 HESVSRNDLEVMQILVSGgAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEF 220
Cdd:PHA02989 229 NKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNR 307


                 ..
gi 767980726 221 LL 222
Cdd:PHA02989 308 IL 309
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 135-255 1.42e-04

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 44.40  E-value: 1.42e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 135 RGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFL---AKYGADINT 197
Cdd:cd22193   75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKgrffqpkyqgegfyFGELPLSLAACTNQPDIVQYLlenEHQPADIEA 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767980726 198 QASDNAS---ALYEACKNEHEE------VVEFLLSQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 255
Cdd:cd22193  155 QDSRGNTvlhALVTVADNTKENtkfvtrMYDMILIRGAKLCPTveleeirNNDGLTPLQLAAKMGKIEILKYIL 228
Ank_5 pfam13857
Ankyrin repeats (many copies);
188-242 2.02e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 2.02e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 767980726  188 LAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIA 242
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
 135-255 2.85e-04

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 43.64  E-value: 2.85e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 135 RGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAK---YGADINT 197
Cdd:cd22196   93 KGQTALHIAIERRNMHLVELLVQNGADVHARASgeffkkkkggpgfyFGELPLSLAACTNQLDIVKFLLEnphSPADISA 172

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767980726 198 QASDNAS---ALYEACKNEHE------EVVEFLLSQGADANK-------TNKDGLLPLHIASKKGNYRIVQMLL 255
Cdd:cd22196  173 RDSMGNTvlhALVEVADNTPEntkfvtKMYNEILILGAKIRPllkleeiTNKKGLTPLKLAAKTGKIGIFAYIL 246
Ank_2 pfam12796
Ankyrin repeats (3 copies);
6-55 2.87e-04

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 40.10  E-value: 2.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 767980726    6 PLIKAIKDGDEEALKTMIKegKNLAEPNKEGWLPLHEAAYYGQVGCLKVL 55
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEIVKLL 80
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 168-197 3.08e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.01  E-value: 3.08e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 767980726  168 YGITPLFVAAQSGQLEALRFLAKYGADINT 197
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 168-196 3.43e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.95  E-value: 3.43e-04
                           10        20
                   ....*....|....*....|....*....
gi 767980726   168 YGITPLFVAAQSGQLEALRFLAKYGADIN 196
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
 491-531 4.08e-04

SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. Asb4 was identified as imprinted gene in mice. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239693  Cd Length: 48  Bit Score: 38.19  E-value: 4.08e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 767980726 491 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYEN 531
Cdd:cd03723    3 PRSLQHLCRCAIRKLLGSRCHKLVPQLSLPTSLKNYLLLEP 43
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 267-294 6.55e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 6.55e-04
                           10        20
                   ....*....|....*....|....*...
gi 767980726   267 GVSPLHLAAERNHDEVLEALLSARFDVN 294
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 162-336 7.43e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.38  E-value: 7.43e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  162 VESKNAYGITPLFVAAQSGQLEALRFLAKYgadINTQASDNASALYEACKNEHEeVVEFLLSQGADANKtnKDGLLPLHI 241
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISLEYVD-AVEAILLHLLAAFR--KSGPLELAN 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  242 ASKKGNYrivqmllpvtsrTRirrsGVSPLHLAAERNHDEVLEALLSARFDVNTP-------LAPERARLYEDRRSSALY 314
Cdd:TIGR00870 119 DQYTSEF------------TP----GITALHLAAHRQNYEIVKLLLERGASVPARacgdffvKSQGVDSFYHGESPLNAA 182

                         170       180
                  ....*....|....*....|..
gi 767980726  315 FAVVNNNVYAteLLLQHGADPN 336
Cdd:TIGR00870 183 ACLGSPSIVA--LLSEDPADIL 202
PHA02716 PHA02716
CPXV016; CPX019; EVM010; Provisional
 83-173 9.73e-04

CPXV016; CPX019; EVM010; Provisional


Pssm-ID: 165089 [Multi-domain]  Cd Length: 764  Bit Score: 41.82  E-value: 9.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  83 LDCLLSLLQAGAEPDISNKSRETPLYKACERKN--AEAVKILVQHNADTNHRCNRGWTALHESVSR------------ND 148
Cdd:PHA02716 297 ISVVYSFLQPGVKLHYKDSAGRTCLHQYILRHNisTDIIKLLHEYGNDLNEPDNIGNTVLHTYLSMlsvvnildpetdND 376

                         90       100
                 ....*....|....*....|....*..
gi 767980726 149 --LEVMQILVSGGAKVESKNAYGITPL 173
Cdd:PHA02716 377 irLDVIQCLISLGADITAVNCLGYTPL 403
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 308-399 1.35e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.19  E-value: 1.35e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 308 RRSSALYFAVVNNNVYATELLLQHGADPNRDV-----ISPLLVAIRHGC---LRTMQLLLDHGANIDAYIATHPTAFPAT 379
Cdd:PHA03100  34 KPVLPLYLAKEARNIDVVKILLDNGADINSSTknnstPLHYLSNIKYNLtdvKEIVKLLLEYGANVNAPDNNGITPLLYA 113

                         90       100
                 ....*....|....*....|
gi 767980726 380 IMFAMKCLSLLKFLMDLGCD 399
Cdd:PHA03100 114 ISKKSNSYSIVEYLLDNGAN 133
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 84-201 1.83e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 40.35  E-value: 1.83e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  84 DCLLSLLQAGAEPDI----SNKSRETPLYKACERKNAEAVKILVQHNADTNHRCNrgwtalhesvsrndlevmqilvsgg 159
Cdd:PHA02884  47 DIIDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAE------------------------- 101

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767980726 160 akvESKnaygITPLFVAAQSGQLEALRFLAKYGADINTQASD 201
Cdd:PHA02884 102 ---EAK----ITPLYISVLHGCLKCLEILLSYGADINIQTND 136
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
 135-255 1.85e-03

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 40.99  E-value: 1.85e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 135 RGWTALHESVSRNDLEVMQILVSGGAKVESKNA-------------YGITPLFVAAQSGQLEALRFLAKYGADI-NTQAS 200
Cdd:cd22197   93 RGHSALHIAIEKRSLQCVKLLVENGADVHARACgrffqkkqgtcfyFGELPLSLAACTKQWDVVNYLLENPHQPaSLQAQ 172

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767980726 201 DNAS-----ALYEACKN--EHEEVV----EFLLSQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 255
Cdd:cd22197  173 DSLGntvlhALVMIADNspENSALVikmyDGLLQAGARLCPTvqleeisNHEGLTPLKLAAKEGKIEIFRHIL 245
Ank_4 pfam13637
Ankyrin repeats (many copies);
309-359 2.02e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 2.02e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 767980726  309 RSSALYFAVVNNNVYATELLLQHGADPNR---DVISPLLVAIRHGCLRTMQLLL 359
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAvdgNGETALHFAASNGNVEVLKLLL 54
Ank_5 pfam13857
Ankyrin repeats (many copies);
122-173 2.69e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 2.69e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 767980726  122 LVQH-NADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPL 173
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 40-188 2.87e-03

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 40.25  E-value: 2.87e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  40 LHEAAYY---GQVGCLKVLQRAYPGTIDQRTL----------QEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSR--- 103
Cdd:cd21882   30 LHKAALNlndGVNEAIMLLLEAAPDSGNPKELvnapctdefyQGQTALHIAIENRNLNLVRLLVENGADVSARATGRffr 109

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 104 ----------ETPLYKACERKNAEAVKILVQHNADTNHRCNR---GWTALHESVSRND---------LEVMQILVSGGAK 161
Cdd:cd21882  110 kspgnlfyfgELPLSLAACTNQEEIVRLLLENGAQPAALEAQdslGNTVLHALVLQADntpensafvCQMYNLLLSYGAH 189

                        170       180       190
                 ....*....|....*....|....*....|....
gi 767980726 162 V-------ESKNAYGITPLFVAAQSGQLEALRFL 188
Cdd:cd21882  190 LdptqqleEIPNHQGLTPLKLAAVEGKIVMFQHI 223
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 69-188 3.36e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.16  E-value: 3.36e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  69 QEETAVYLATCRGHLDCLLSLLQAGAEPDISNKSR--------------ETPLYKACERKNAEAVKILVQH---NADTNH 131
Cdd:cd22193   75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGRffqpkyqgegfyfgELPLSLAACTNQPDIVQYLLENehqPADIEA 154

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767980726 132 RCNRGWTALH-------ESVSRNDL--EVMQILVSGGAKV-------ESKNAYGITPLFVAAQSGQLEALRFL 188
Cdd:cd22193  155 QDSRGNTVLHalvtvadNTKENTKFvtRMYDMILIRGAKLcptveleEIRNNDGLTPLQLAAKMGKIEILKYI 227
Ank_5 pfam13857
Ankyrin repeats (many copies);
221-274 3.47e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.79  E-value: 3.47e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 767980726  221 LLSQG-ADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIR-RSGVSPLHLA 274
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKdEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
267-329 3.47e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.71  E-value: 3.47e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 767980726  267 GVSPLHLAAERNHDEVLEALLSARFDVNtplaperARLYEDRrsSALYFAVVNNNVYATELLL 329
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADIN-------AVDGNGE--TALHFAASNGNVEVLKLLL 54
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 183-254 3.48e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 38.32  E-value: 3.48e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 767980726 183 EALRFLAKYGADINTQASDNA-SALYEACKNEHEEVVEFLLSQ-GADANKTNKDGLLPLHIASKKGNYRIVQML 254
Cdd:PHA02736  72 EKLKLLMEWGADINGKERVFGnTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNIL 145
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 105-130 3.96e-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: 3.96e-03
                           10        20
                   ....*....|....*....|....*.
gi 767980726   105 TPLYKACERKNAEAVKILVQHNADTN 130
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
SOCS_WSB_SWIP cd03733
SOCS (suppressors of cytokine signaling) box of WSB/SWiP-like proteins. This subfamily ...
 494-529 4.10e-03

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


Pssm-ID: 239702  Cd Length: 39  Bit Score: 35.09  E-value: 4.10e-03
                         10        20        30
                 ....*....|....*....|....*....|....*.
gi 767980726 494 LAHLCRLRVRKAIGKYRIKlldTLPLPGRLIRYLKY 529
Cdd:cd03733    6 LQHLCRMALRRVMTTQQVL---ALPIPKKMKEFLTY 38
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 50-188 6.79e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 39.36  E-value: 6.79e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726  50 GCLKVL------QRAYPGtidqrtlqeETAVYLATCRGHLDCLLSLLQAGAEPDISNKSR--------------ETPLYK 109
Cdd:cd22194  124 GILDRFinaeytEEAYEG---------QTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLAL 194

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 110 ACERKNAEAVKILVQhNADTNHRC--NRGWTALH-------ESVSRNDLEV----MQILVSGGAKVES-KNAYGITPLFV 175
Cdd:cd22194  195 AACTNQPEIVQLLME-KESTDITSqdSRGNTVLHalvtvaeDSKTQNDFVKrmydMILLKSENKNLETiRNNEGLTPLQL 273

                        170
                 ....*....|...
gi 767980726 176 AAQSGQLEALRFL 188
Cdd:cd22194  274 AAKMGKAEILKYI 286
SOCS_ASB3 cd03722
SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a ...
 494-531 6.79e-03

SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ABS3 has been shown to be negative regulator of TNF-R2-mediated cellular responses to TNF-alpha by direct targeting of tumor necrosis factor receptor II (TNF-R2) for ubiquitination and proteasome-mediated degradation. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239692  Cd Length: 51  Bit Score: 34.77  E-value: 6.79e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 767980726 494 LAHLCRLRVRKAIGKYRIK---LLDTLPLPGRLIRYLKYEN 531
Cdd:cd03722    6 LTHLCRLEIRSSLKSERLRsdsFICQLPLPRSLQDYLLYSD 46
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 115-191 7.02e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.11  E-value: 7.02e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 767980726 115 NAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKY 191
Cdd:PTZ00322  94 DAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 164-244 7.58e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 38.43  E-value: 7.58e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726 164 SKNAYgITPLFVAAQSGQLEALRFLAKYGADINTQASD-NASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIA 242
Cdd:PHA02884  66 SENSK-TNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEaKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELA 144


                 ..
gi 767980726 243 SK 244
Cdd:PHA02884 145 LM 146
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 6-125 7.78e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 38.71  E-value: 7.78e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 767980726   6 PLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEA-AYYGQVGCLKVLQRAYPGTIDQRTLQEETAVYLATcrGHLD 84
Cdd:PHA02878 204 PLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYILGLTALHSSI--KSER 281

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 767980726  85 CLLSLLQAGAEPDISNKSRETPLYKAC-ERKNAEAVKILVQH 125
Cdd:PHA02878 282 KLKLLLEYGADINSLNSYKLTPLSSAVkQYLCINIGRILISN 323
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 267-294 8.08e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.19  E-value: 8.08e-03
                          10        20
                  ....*....|....*....|....*....
gi 767980726  267 GVSPLHLAAER-NHDEVLEALLSARFDVN 294
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
SOCS_CIS1 cd03734
SOCS (suppressors of cytokine signaling) box of CIS (cytokine-inducible SH2 protein) 1-like ...
 492-528 9.78e-03

SOCS (suppressors of cytokine signaling) box of CIS (cytokine-inducible SH2 protein) 1-like proteins. Together with the SOCS proteins, the CIS/SOCS family of proteins is characterized by the presence of a C-terminal SOCS box and a central SH2 domain. CIS1, like SOCS1 and SOCS3, is involved in the down-regulation of the JAK/STAT pathway. CIS1 binds to cytokine receptors at STAT5-docking sites, which prohibits recruitment of STAT5 to the receptor signaling complex and results in the down-regulation of activation by STAT5.


Pssm-ID: 239703  Cd Length: 41  Bit Score: 34.17  E-value: 9.78e-03
                         10        20        30
                 ....*....|....*....|....*....|....*..
gi 767980726 492 RPLAHLCRLRVRKAIGKyriklLDTLPLPGRLIRYLK 528
Cdd:cd03734    4 RSLQHLCRLVINRLVTD-----VDCLPLPRRMADYLR 35
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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