NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|119606841|gb|EAW86435|]
View 

ankyrin repeat and SOCS box-containing 13, isoform CRA_a [Homo sapiens]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-221 2.80e-47

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 159.35  E-value: 2.80e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  20 RTPVHEAAQRGESLQLQQLIESGACVNQVTVDSITPLHAASLQGQARCVQLLLAAGAQVDARNIDGSTPLCDACASGSIE 99
Cdd:COG0666   55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLE 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 100 CVKLLLSYGAKVNPP-LYTASPLHEACMSGSSECVRLLIDVGANLEAHDCHFGTPLHVACAREHLDCVKVLLNAGANVNA 178
Cdd:COG0666  135 IVKLLLEAGADVNAQdNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA 214

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 119606841 179 A-KLHETALHHAAKVKNVDLIEMLIEFGGNIYARDNRGKKPSDY 221
Cdd:COG0666  215 KdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
SOCS_ASB13 cd03729
SOCS (suppressors of cytokine signaling) box of ASB13-like proteins. ASB family members have a ...
 237-278 1.62e-21

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: 84.84  E-value: 1.62e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 119606841 237 KTPLTLSQLCRVNLRKATGVRGLEKIAKLNIPPRLIDYLSYN 278
Cdd:cd03729    1 STPLSLQQLCRINLRKALGTRALEKIAKLNIPNRIIDYLSYN 42
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-221 2.80e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 159.35  E-value: 2.80e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  20 RTPVHEAAQRGESLQLQQLIESGACVNQVTVDSITPLHAASLQGQARCVQLLLAAGAQVDARNIDGSTPLCDACASGSIE 99
Cdd:COG0666   55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLE 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 100 CVKLLLSYGAKVNPP-LYTASPLHEACMSGSSECVRLLIDVGANLEAHDCHFGTPLHVACAREHLDCVKVLLNAGANVNA 178
Cdd:COG0666  135 IVKLLLEAGADVNAQdNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA 214

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 119606841 179 A-KLHETALHHAAKVKNVDLIEMLIEFGGNIYARDNRGKKPSDY 221
Cdd:COG0666  215 KdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
SOCS_ASB13 cd03729
SOCS (suppressors of cytokine signaling) box of ASB13-like proteins. ASB family members have a ...
 237-278 1.62e-21

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: 84.84  E-value: 1.62e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 119606841 237 KTPLTLSQLCRVNLRKATGVRGLEKIAKLNIPPRLIDYLSYN 278
Cdd:cd03729    1 STPLSLQQLCRINLRKALGTRALEKIAKLNIPNRIIDYLSYN 42
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 23-221 4.93e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 92.43  E-value: 4.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  23 VHEAAQRGESLQLQQLIESGACVNQVTVDSITPLHAASLQGQARCVQLLLAAGAQVDARNIDGSTPLCDACASGSIECVK 102
Cdd:PHA02876 149 IKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 103 -----------------------------LLLSYGAKVNP-PLYTASPLHEACMSGS-SECVRLLIDVGANLEAHDCHFG 151
Cdd:PHA02876 229 aiidnrsninkndlsllkairnedletslLLYDAGFSVNSiDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGE 308

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119606841 152 TPLHVAcAREHLDC--VKVLLNAGANVNAA-KLHETALHHAAKV-KNVDLIEMLIEFGGNIYARDNRGKKPSDY 221
Cdd:PHA02876 309 TPLYLM-AKNGYDTenIRTLIMLGADVNAAdRLYITPLHQASTLdRNKDIVITLLELGANVNARDYCDKTPIHY 381
Ank_2 pfam12796
Ankyrin repeats (3 copies);
56-147 5.73e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.78  E-value: 5.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841   56 LHAASLQGQARCVQLLLAAGAQVDARNIDGSTPLCDACASGSIECVKLLLSYgAKVNPPLYTASPLHEACMSGSSECVRL 135
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 119606841  136 LIDVGANLEAHD 147
Cdd:pfam12796  80 LLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 21-156 8.86e-10

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 58.87  E-value: 8.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  21 TPVHEAAQRGESLQLQQLIESGAC-VNQVTVDSITPLHAASLQGQARCVQLLLAAGAQVDARNI-----DGSTPLCDACA 94
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCPSCdLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMtsdlyQGETALHIAVV 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119606841  95 SGSIECVKLLLSYGAKVNPPLYTAS---------------PLHEACMSGSSECVRLLIDVGANLEAHDCHFGTPLHV 156
Cdd:cd22192   99 NQNLNLVRELIARGADVVSPRATGTffrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 238-275 6.65e-09

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: 50.63  E-value: 6.65e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 119606841  238 TPLTLSQLCRVNLRKATGVRGLEKIAKLNIPPRLIDYL 275
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYL 38
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 152-215 5.04e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.38  E-value: 5.04e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119606841  152 TPLHVACAREHLDCVKVLLNAGANVNAA--------KLHETALHH-------AAKVKNVDLIEMLIEFGGNIYARDNRG 215
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPARacgdffvkSQGVDSFYHgesplnaAACLGSPSIVALLSEDPADILTADSLG 208
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 152-178 5.57e-06

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: 42.19  E-value: 5.57e-06
                           10        20
                   ....*....|....*....|....*..
gi 119606841   152 TPLHVACAREHLDCVKVLLNAGANVNA 178
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
 240-277 1.13e-05

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: 41.24  E-value: 1.13e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 119606841   240 LTLSQLCRVNLRKATGvrgleKIAKLNIPPRLIDYLSY 277
Cdd:smart00969   1 RSLQHLCRLAIRRSLG-----GIDKLPLPPRLKDYLLY 33
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-221 2.80e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 159.35  E-value: 2.80e-47
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  20 RTPVHEAAQRGESLQLQQLIESGACVNQVTVDSITPLHAASLQGQARCVQLLLAAGAQVDARNIDGSTPLCDACASGSIE 99
Cdd:COG0666   55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLE 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 100 CVKLLLSYGAKVNPP-LYTASPLHEACMSGSSECVRLLIDVGANLEAHDCHFGTPLHVACAREHLDCVKVLLNAGANVNA 178
Cdd:COG0666  135 IVKLLLEAGADVNAQdNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA 214

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 119606841 179 A-KLHETALHHAAKVKNVDLIEMLIEFGGNIYARDNRGKKPSDY 221
Cdd:COG0666  215 KdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLL 258
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-217 7.58e-43

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 147.79  E-value: 7.58e-43
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  20 RTPVHEAAQRGESLQLQQLIESGACVNQVTVDSITPLHAASLQGQARCVQLLLAAGAQVDARNIDGSTPLCDACASGSIE 99
Cdd:COG0666   88 NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLE 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 100 CVKLLLSYGAKVN-PPLYTASPLHEACMSGSSECVRLLIDVGANLEAHDCHFGTPLHVACAREHLDCVKVLLNAGANVNA 178
Cdd:COG0666  168 IVKLLLEAGADVNaRDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 119606841 179 A-KLHETALHHAAKVKNVDLIEMLIEFGGNIYARDNRGKK 217
Cdd:COG0666  248 KdKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
21-221 1.51e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.71  E-value: 1.51e-41
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  21 TPVHEAAQRGESLQLQQLIESGACVNQVTVDSITPLHAASLQGQARCVQLLLAAGAQVDARNIDGSTPLCDACASGSIEC 100
Cdd:COG0666   23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 101 VKLLLSYGAKVNPP-LYTASPLHEACMSGSSECVRLLIDVGANLEAHDCHFGTPLHVACAREHLDCVKVLLNAGANVNAA 179
Cdd:COG0666  103 VKLLLEAGADVNARdKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNAR 182

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 119606841 180 -KLHETALHHAAKVKNVDLIEMLIEFGGNIYARDNRGKKPSDY 221
Cdd:COG0666  183 dNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDL 225
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
20-187 3.02e-32

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 120.06  E-value: 3.02e-32
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  20 RTPVHEAAQRGESLQLQQLIESGACVNQVTVDSITPLHAASLQGQARCVQLLLAAGAQVDARNIDGSTPLCDACASGSIE 99
Cdd:COG0666  121 ETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLE 200

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 100 CVKLLLSYGAKVNPP-LYTASPLHEACMSGSSECVRLLIDVGANLEAHDCHFGTPLHVACAREHLDCVKVLLNAGANVNA 178
Cdd:COG0666  201 IVKLLLEAGADVNAKdNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAA 280


                 ....*....
gi 119606841 179 AKLHETALH 187
Cdd:COG0666  281 ALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
33-218 9.83e-29

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 110.81  E-value: 9.83e-29
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  33 LQLQQLIESGACVNQVTVDSITPLHAASLQGQARCVQLLLAAGAQVDARNIDGSTPLCDACASGSIECVKLLLSYGAKVN 112
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 113 PP-LYTASPLHEACMSGSSECVRLLIDVGANLEAHDCHFGTPLHVACAREHLDCVKVLLNAGANVNAA-KLHETALHHAA 190
Cdd:COG0666   82 AKdDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQdNDGNTPLHLAA 161

                        170       180
                 ....*....|....*....|....*...
gi 119606841 191 KVKNVDLIEMLIEFGGNIYARDNRGKKP 218
Cdd:COG0666  162 ANGNLEIVKLLLEAGADVNARDNDGETP 189
SOCS_ASB13 cd03729
SOCS (suppressors of cytokine signaling) box of ASB13-like proteins. ASB family members have a ...
 237-278 1.62e-21

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: 84.84  E-value: 1.62e-21
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 119606841 237 KTPLTLSQLCRVNLRKATGVRGLEKIAKLNIPPRLIDYLSYN 278
Cdd:cd03729    1 STPLSLQQLCRINLRKALGTRALEKIAKLNIPNRIIDYLSYN 42
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 23-221 4.93e-21

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 92.43  E-value: 4.93e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  23 VHEAAQRGESLQLQQLIESGACVNQVTVDSITPLHAASLQGQARCVQLLLAAGAQVDARNIDGSTPLCDACASGSIECVK 102
Cdd:PHA02876 149 IKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 103 -----------------------------LLLSYGAKVNP-PLYTASPLHEACMSGS-SECVRLLIDVGANLEAHDCHFG 151
Cdd:PHA02876 229 aiidnrsninkndlsllkairnedletslLLYDAGFSVNSiDDCKNTPLHHASQAPSlSRLVPKLLERGADVNAKNIKGE 308

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119606841 152 TPLHVAcAREHLDC--VKVLLNAGANVNAA-KLHETALHHAAKV-KNVDLIEMLIEFGGNIYARDNRGKKPSDY 221
Cdd:PHA02876 309 TPLYLM-AKNGYDTenIRTLIMLGADVNAAdRLYITPLHQASTLdRNKDIVITLLELGANVNARDYCDKTPIHY 381
Ank_2 pfam12796
Ankyrin repeats (3 copies);
56-147 5.73e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.78  E-value: 5.73e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841   56 LHAASLQGQARCVQLLLAAGAQVDARNIDGSTPLCDACASGSIECVKLLLSYgAKVNPPLYTASPLHEACMSGSSECVRL 135
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 119606841  136 LIDVGANLEAHD 147
Cdd:pfam12796  80 LLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 37-218 9.08e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 91.24  E-value: 9.08e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  37 QLIESGACVNQVTVDSITPLHA---ASLQGQARCVQLLLAAGAQVDARNIDGSTPL-CDACASGSIECVKLLLSYGAKVN 112
Cdd:PHA03095  32 RLLAAGADVNFRGEYGKTPLHLylhYSSEKVKDIVRLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVN 111

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 113 PP-LYTASPLHeACMSGSS---ECVRLLIDVGANLEAHDCHFGTPLHV--ACAREHLDCVKVLLNAGANVNAAKL-HETA 185
Cdd:PHA03095 112 AKdKVGRTPLH-VYLSGFNinpKVIRLLLRKGADVNALDLYGMTPLAVllKSRNANVELLRLLIDAGADVYAVDDrFRSL 190

                        170       180       190
                 ....*....|....*....|....*....|....*
gi 119606841 186 LHHAAKV--KNVDLIEMLIEFGGNIYARDNRGKKP 218
Cdd:PHA03095 191 LHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTP 225
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 27-218 1.78e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 90.89  E-value: 1.78e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  27 AQRGESLQLQQLI-ESGACVNQVTVDSITPLHAAS-LQGQARCVQLLLAAGAQVDARNIDGSTPLCDACASG-SIECVKL 103
Cdd:PHA02876 247 AIRNEDLETSLLLyDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRT 326

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 104 LLSYGAKVNP-------PLYTAS----------------------------PLHEACMSGSSECVRLLIDVGANLEAHDC 148
Cdd:PHA02876 327 LIMLGADVNAadrlyitPLHQAStldrnkdivitllelganvnardycdktPIHYAAVRNNVVIINTLLDYGADIEALSQ 406

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119606841 149 HFGTPLHVA-CAREHLDCVKVLLNAGANVNAA-KLHETALHHAAKvKN--VDLIEMLIEFGGNIYARDNRGKKP 218
Cdd:PHA02876 407 KIGTALHFAlCGTNPYMSVKTLIDRGANVNSKnKDLSTPLHYACK-KNckLDVIEMLLDNGADVNAINIQNQYP 479
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 11-222 2.98e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 89.34  E-value: 2.98e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  11 LGDVGFWVERTPVHEAAQRGESLQLQQLIESGACVNQVTVDSITPLHAASLQGQA-----RCVQLLLAAGAQVDARNIDG 85
Cdd:PHA03100  27 LNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNG 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  86 STPL--CDACASGSIECVKLLLSYGAKVNPPLYTA-SPLHEA--CMSGSSECVRLLIDVGANLEAhdchfgtplhvacar 160
Cdd:PHA03100 107 ITPLlyAISKKSNSYSIVEYLLDNGANVNIKNSDGeNLLHLYleSNKIDLKILKLLIDKGVDINA--------------- 171

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119606841 161 ehLDCVKVLLNAGANVNAAKLH-ETALHHAAKVKNVDLIEMLIEFGGNIYARDNRGKKPSDYT 222
Cdd:PHA03100 172 --KNRVNYLLSYGVPINIKDVYgFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIA 232
PHA03095 PHA03095
ankyrin-like protein; Provisional
 68-215 3.16e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 89.70  E-value: 3.16e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  68 VQLLLAAGAQVDARNIDGSTPLCDACASGSIEC---VKLLLSYGAKVN-PPLYTASPLHEACMSGSSE-CVRLLIDVGAN 142
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVkdiVRLLLEAGADVNaPERCGFTPLHLYLYNATTLdVIKLLIKAGAD 109

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119606841 143 LEA-HDCHFgTPLHVACA--REHLDCVKVLLNAGANVNAAKLHE-TALHHAAKVKNVD--LIEMLIEFGGNIYARDNRG 215
Cdd:PHA03095 110 VNAkDKVGR-TPLHVYLSgfNINPKVIRLLLRKGADVNALDLYGmTPLAVLLKSRNANveLLRLLIDAGADVYAVDDRF 187
Ank_2 pfam12796
Ankyrin repeats (3 copies);
121-212 4.15e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 82.47  E-value: 4.15e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  121 LHEACMSGSSECVRLLIDVGANLEAHDCHFGTPLHVACAREHLDCVKVLLNaGANVNAAKLHETALHHAAKVKNVDLIEM 200
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 119606841  201 LIEFGGNIYARD 212
Cdd:pfam12796  80 LLEKGADINVKD 91
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 21-207 5.14e-20

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 88.89  E-value: 5.14e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  21 TPVHEAAQRGESLQLQQLIESGACVNQVTVDSITPLHAASLQGQARCVQLLLAAGAQV-DARNIDGSTPLCDACASGSIE 99
Cdd:PHA02875  37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFAdDVFYKDGMTPLHLATILKKLD 116

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 100 CVKLLLSYGAKVN-PPLYTASPLHEACMSGSSECVRLLIDVGANLEAHDCHFGTPLHVACAREHLDCVKVLLNAGANVN- 177
Cdd:PHA02875 117 IMKLLIARGADPDiPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDy 196

                        170       180       190
                 ....*....|....*....|....*....|.
gi 119606841 178 -AAKLHETALHHAAKVKNVDLIEMLIEFGGN 207
Cdd:PHA02875 197 fGKNGCVAALCYAIENNKIDIVRLFIKRGAD 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 35-255 1.64e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 87.33  E-value: 1.64e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  35 LQQLIESGACVNQVTVDSITPLHAASLQGQARCVQLLLAAGAQVDARNIDGSTPLCDACASGSIECVKLLLSYGAKVN-P 113
Cdd:PHA02874 107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANvK 186

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 114 PLYTASPLHEACMSGSSECVRLLIDVGANLeAHDCHFG-TPLHVACAREHlDCVKVLLNaGANVNAAKLH-ETALHHAAK 191
Cdd:PHA02874 187 DNNGESPLHNAAEYGDYACIKLLIDHGNHI-MNKCKNGfTPLHNAIIHNR-SAIELLIN-NASINDQDIDgSTPLHHAIN 263

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119606841 192 VK-NVDLIEMLIEFGGNIYARDNRGKKPSDYTwsssapakcFEYYEKTPLTLSQLCRVNLRKATG 255
Cdd:PHA02874 264 PPcDIDIIDILLYHKADISIKDNKGENPIDTA---------FKYINKDPVIKDIIANAVLIKEAD 319
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 38-178 1.50e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 84.72  E-value: 1.50e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  38 LIESGACVNQVTVDSITPLHAASLQ--GQARCVQLLLAAGAQVDARNIDGSTPLCDACASGSI--ECVKLLLSYGAKVN- 112
Cdd:PHA03100  92 LLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINa 171

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 113 ----------------PPLYTASPLHEACMSGSSECVRLLIDVGANLEAHDCHFGTPLHVACAREHLDCVKVLLNAGANV 176
Cdd:PHA03100 172 knrvnyllsygvpiniKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSI 251


                 ..
gi 119606841 177 NA 178
Cdd:PHA03100 252 KT 253
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 21-214 1.96e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 84.73  E-value: 1.96e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  21 TPVHEAAQRG-ESLQLQQLIESGACVNQVTVDSITPLHAAS-LQGQARCVQLLLAAGAQVDARNIDGSTPLCDACASGSI 98
Cdd:PHA02876 309 TPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNV 388

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  99 ECVKLLLSYGAKVNP-PLYTASPLHEA-CMSGSSECVRLLIDVGANLEAHDCHFGTPLHVACARE-HLDCVKVLLNAGAN 175
Cdd:PHA02876 389 VIINTLLDYGADIEAlSQKIGTALHFAlCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGAD 468

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 119606841 176 VNAAKLHET-----ALHHAAkvknvdLIEMLIEFGGNIyaRDNR 214
Cdd:PHA02876 469 VNAINIQNQyplliALEYHG------IVNILLHYGAEL--RDSR 504
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 20-267 4.08e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 83.50  E-value: 4.08e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  20 RTPVHEAAQRGESLQLQQLIESGACVNQVTV-DSITPLHAASLQGQARCVQLLLAAGAQVDARNIDGSTPLCDACASGSI 98
Cdd:PHA02875  69 ESELHDAVEEGDVKAVEELLDLGKFADDVFYkDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  99 ECVKLLLSYGAKVN-PPLYTASPLHEACMSGSSECVRLLIDVGANLEahdcHFG-----TPLHVACAREHLDCVKVLLNA 172
Cdd:PHA02875 149 KGIELLIDHKACLDiEDCCGCTPLIIAMAKGDIAICKMLLDSGANID----YFGkngcvAALCYAIENNKIDIVRLFIKR 224

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 173 GANVNAAKLHETALHHAAKV-KNVDL------IEMLI-EFGGNIYAR-DNRGKKPSDYTWSSSAPAKCFEYYEKtpltls 243
Cdd:PHA02875 225 GADCNIMFMIEGEECTILDMiCNMCTnleseaIDALIaDIAIRIHKKtIRRDEGFKNNMSTIEDKEEFKDVFEK------ 298

                        250       260
                 ....*....|....*....|....
gi 119606841 244 qlCRVNLRKATGvrglEKIAKLNI 267
Cdd:PHA02875 299 --CIIELRRIKS----EKIGKKNI 316
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 35-218 5.32e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 83.09  E-value: 5.32e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  35 LQQLIES-GACVNQVTVDSITPLHAASLQGQARCVQLLLAAGAQVDARNIDGSTPLCDACASGSIECVKLL--------- 104
Cdd:PHA02874  17 IEKIIKNkGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLidngvdtsi 96

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 105 --------------LSYGAKVN-PPLYTASPLHEACMSGSSECVRLLIDVGANLEAHDCHFGTPLHVACAREHLDCVKVL 169
Cdd:PHA02874  97 lpipciekdmiktiLDCGIDVNiKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLL 176

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 119606841 170 LNAGANVNAAKLH-ETALHHAAKVKNVDLIEMLIEFGGNIYARDNRGKKP 218
Cdd:PHA02874 177 LEKGAYANVKDNNgESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTP 226
Ank_2 pfam12796
Ankyrin repeats (3 copies);
24-112 5.13e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 5.13e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841   24 HEAAQRGESLQLQQLIESGACVNQVTVDSITPLHAASLQGQARCVQLLLaAGAQVDARNiDGSTPLCDACASGSIECVKL 103
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLKD-NGRTALHYAARSGHLEIVKL 79


                  ....*....
gi 119606841  104 LLSYGAKVN 112
Cdd:pfam12796  80 LLEKGADIN 88
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 26-183 1.47e-15

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 76.45  E-value: 1.47e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  26 AAQRGESLQLQQLIESGACVNQVTVDSITPLHAASLQGQARCVQLLLAAGAQVDARNIDGSTPLCDACASGSIECVKLLL 105
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119606841 106 SYGAKVNPplYTASP-LHEACMSGSSECVRLLIDVGANLEAHDCHFGTPLHVACAREHLDCVKVLLNAGANVNAAKLHE 183
Cdd:PLN03192 612 HFASISDP--HAAGDlLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDD 688
PHA03095 PHA03095
ankyrin-like protein; Provisional
 97-220 1.28e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 70.44  E-value: 1.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  97 SIECVKLLLSYGAKVN---PPLYTasPLHeACMSGSS----ECVRLLIDVGANLEAHDCHFGTPLHV-ACAREHLDCVKV 168
Cdd:PHA03095  26 TVEEVRRLLAAGADVNfrgEYGKT--PLH-LYLHYSSekvkDIVRLLLEAGADVNAPERCGFTPLHLyLYNATTLDVIKL 102

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 119606841 169 LLNAGANVNAA-KLHETALHHAAKVKNVD--LIEMLIEFGGNIYARDNRGKKPSD 220
Cdd:PHA03095 103 LIKAGADVNAKdKVGRTPLHVYLSGFNINpkVIRLLLRKGADVNALDLYGMTPLA 157
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
 237-278 1.33e-13

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


Pssm-ID: 239686  Cd Length: 42  Bit Score: 63.67  E-value: 1.33e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 119606841 237 KTPLTLSQLCRVNLRKATGVRGLEKIAKLNIPPRLIDYLSYN 278
Cdd:cd03716    1 STPRSLQHLCRLAIRRCLGRRRLELIKKLPLPPRLKDYLLYE 42
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 22-225 1.71e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 69.91  E-value: 1.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  22 PVHEAAQRGESLQLQQLIESGACVNQVTVDSITPLHAASLQGQARCVQLLLAAGAQVDARNidGSTPLCDACASGSIECV 101
Cdd:PHA02878  40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFY--TLVAIKDAFNNRNVEIF 117

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 102 KLLLSYGAKVNpplYTaSPLHEACMSG-----SSECVRLLIDVGANLEAHDCHFG-TPLHVACAREHLDCVKVLLNAGAN 175
Cdd:PHA02878 118 KIILTNRYKNI---QT-IDLVYIDKKSkddiiEAEITKLLLSYGADINMKDRHKGnTALHYATENKDQRLTELLLSYGAN 193

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 119606841 176 VNAA-KLHETALHHAAKVKNVDLIEMLIEFGGNIYARDNRGKKPSDYTWSS 225
Cdd:PHA02878 194 VNIPdKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGY 244
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
 238-277 4.92e-12

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: 59.41  E-value: 4.92e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 119606841 238 TPLTLSQLCRVNLRKATGVRGLEKIAKLNIPPRLIDYLSY 277
Cdd:cd03587    1 NPRSLQHLCRLAIRRCLGKRRLDLIDKLPLPPRLKDYLLY 40
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 20-157 5.01e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.59  E-value: 5.01e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  20 RTPVHEAAQRGESLQLQQLIESGACVNQVTVDSITPLHAASLQGQARCVQLLLAAGAQVDARNIDGSTPLCDACAS-GSI 98
Cdd:PHA02878 169 NTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDY 248

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119606841  99 ECVKLLLSYGAKVNPPLYTA--SPLHEACMsgSSECVRLLIDVGANLEAHDCHFGTPLHVA 157
Cdd:PHA02878 249 DILKLLLEHGVDVNAKSYILglTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSA 307
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 21-156 8.86e-10

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 58.87  E-value: 8.86e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  21 TPVHEAAQRGESLQLQQLIESGAC-VNQVTVDSITPLHAASLQGQARCVQLLLAAGAQVDARNI-----DGSTPLCDACA 94
Cdd:cd22192   19 SPLLLAAKENDVQAIKKLLKCPSCdLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEPMtsdlyQGETALHIAVV 98

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 119606841  95 SGSIECVKLLLSYGAKVNPPLYTAS---------------PLHEACMSGSSECVRLLIDVGANLEAHDCHFGTPLHV 156
Cdd:cd22192   99 NQNLNLVRELIARGADVVSPRATGTffrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHI 175
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 8-142 2.72e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.31  E-value: 2.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841   8 GCFLGDVGFWVERTPVHEAAQRGESLQLQQLIESGACVNQVTVDSITPLHAASLQGQARCVQLLLAAGAQVDARNIDGST 87
Cdd:PHA02875  91 GKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 119606841  88 PLCDACASGSIECVKLLLSYGAkvNPPLYTASP----LHEACMSGSSECVRLLIDVGAN 142
Cdd:PHA02875 171 PLIIAMAKGDIAICKMLLDSGA--NIDYFGKNGcvaaLCYAIENNKIDIVRLFIKRGAD 227
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 25-120 3.42e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 3.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  25 EAAQRGESLQLQQLIESGACVNQVTVDSITPLHAASLQGQARCVQLLLAAGAQVDARNIDGSTPLCDACASGSIECVKLL 104
Cdd:PTZ00322  88 QLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167

                         90       100
                 ....*....|....*....|...
gi 119606841 105 LSY-------GAKVNPPLYTASP 120
Cdd:PTZ00322 168 SRHsqchfelGANAKPDSFTGKP 190
Ank_4 pfam13637
Ankyrin repeats (many copies);
152-202 4.32e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.51  E-value: 4.32e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119606841  152 TPLHVACAREHLDCVKVLLNAGANVNAA-KLHETALHHAAKVKNVDLIEMLI 202
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVdGNGETALHFAASNGNVEVLKLLL 54
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 238-275 6.65e-09

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: 50.63  E-value: 6.65e-09
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 119606841  238 TPLTLSQLCRVNLRKATGVRGLEKIAKLNIPPRLIDYL 275
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYL 38
Ank_4 pfam13637
Ankyrin repeats (many copies);
54-105 2.05e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 2.05e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119606841   54 TPLHAASLQGQARCVQLLLAAGAQVDARNIDGSTPLCDACASGSIECVKLLL 105
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
 239-277 6.87e-08

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: 47.94  E-value: 6.87e-08
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 119606841 239 PLTLSQLCRVNLRKATGVRGLEKIAKLNIPPRLIDYLSY 277
Cdd:cd03721    3 PRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNH 41
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 86-175 9.79e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 9.79e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  86 STPLCDACASGSIECVKLLLSYGAKVNPPLYTAS-PLHEACMSGSSECVRLLIDVGANLEAHDCHFGTPLHVACAREHLD 164
Cdd:PTZ00322  83 TVELCQLAASGDAVGARILLTGGADPNCRDYDGRtPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFRE 162

                         90
                 ....*....|....*...
gi 119606841 165 CVKVLL-------NAGAN 175
Cdd:PTZ00322 163 VVQLLSrhsqchfELGAN 180
Ank_4 pfam13637
Ankyrin repeats (many copies);
119-170 1.14e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.65  E-value: 1.14e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 119606841  119 SPLHEACMSGSSECVRLLIDVGANLEAHDCHFGTPLHVACAREHLDCVKVLL 170
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 17-143 1.47e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.37  E-value: 1.47e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  17 WVERTPVHEAAQRGESLQLQQLIESGACVNQVTVDSITPLHAAsLQGQA--RCVQLLLAAGAQVDARNIDGSTPLCDACA 94
Cdd:PHA02876 373 YCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFA-LCGTNpyMSVKTLIDRGANVNSKNKDLSTPLHYACK 451

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119606841  95 SG-SIECVKLLLSYGAKVNP-------PLYTASPLHeacmsgssECVRLLIDVGANL 143
Cdd:PHA02876 452 KNcKLDVIEMLLDNGADVNAiniqnqyPLLIALEYH--------GIVNILLHYGAEL 500
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 86-215 1.53e-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: 51.94  E-value: 1.53e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  86 STPLCDACASGSIECVKLLLSYgAKVNP----PL-YTAspLHEACMSGSSECVRLLIDVG---ANLEA-HDCHFG-TPLH 155
Cdd:cd22192   18 ESPLLLAAKENDVQAIKKLLKC-PSCDLfqrgALgETA--LHVAALYDNLEAAVVLMEAApelVNEPMtSDLYQGeTALH 94

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 119606841 156 VACAREHLDCVKVLLNAGANVNAA-------------KLH--ETALHHAAKVKNVDLIEMLIEFGGNIYARDNRG 215
Cdd:cd22192   95 IAVVNQNLNLVRELIARGADVVSPratgtffrpgpknLIYygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLG 169
PHA03095 PHA03095
ankyrin-like protein; Provisional
 21-203 2.72e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.18  E-value: 2.72e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  21 TPVHEAAQRGESLQ-LQQLIESGACVNQVTVDSITPLHA--ASLQGQARCVQLLLAAGAQVDARNIDGSTPLcdAC---- 93
Cdd:PHA03095  85 TPLHLYLYNATTLDvIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPL--AVllks 162

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  94 ASGSIECVKLLLSYGAKVnpplYTA-----SPLHEACMS--GSSECVRLLIDVGANLEAHDCHFGTPLHVA-----CARE 161
Cdd:PHA03095 163 RNANVELLRLLIDAGADV----YAVddrfrSLLHHHLQSfkPRARIVRELIRAGCDPAATDMLGNTPLHSMatgssCKRS 238

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 119606841 162 HLD-------------------------------CVKvLLNAGANVNAAKLH-ETALHHAAKVKNVDLIEMLIE 203
Cdd:PHA03095 239 LVLplliagisinarnrygqtplhyaavfnnpraCRR-LIALGADINAVSSDgNTPLSLMVRNNNGRAVRAALA 311
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 127-244 3.98e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 51.05  E-value: 3.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 127 SGSSECVRLLIDVGANLEAHDCHFGTPLHVACAREHLDCVKVLLNAGANVNAA-KLHETALHHAAKVKNVDLIEMLIEFG 205
Cdd:PTZ00322  92 SGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLdKDGKTPLELAEENGFREVVQLLSRHS 171

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 119606841 206 GNIYARDNRGkKPSDYTWSSSApakcfeyYEKTPLTLSQ 244
Cdd:PTZ00322 172 QCHFELGANA-KPDSFTGKPPS-------LEDSPISSHH 202
PHA03095 PHA03095
ankyrin-like protein; Provisional
 20-117 1.95e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.48  E-value: 1.95e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  20 RTPVHEAAQRG--ESLQLQQLIESGACVNQVTVDSITPLHAASLQGQARCVQLLLAAGAQVDARNIDGSTPLCDACASGS 97
Cdd:PHA03095 223 NTPLHSMATGSscKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNN 302

                         90       100
                 ....*....|....*....|
gi 119606841  98 IECVKLLLsygaKVNPPLYT 117
Cdd:PHA03095 303 GRAVRAAL----AKNPSAET 318
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 110-240 2.53e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.52  E-value: 2.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 110 KVNPPLYTASPLHEACMSGSSECVRLLIDVGANLEAHDCHFGTPLHVACAREHLDCVKVLLNAGANVNAAKLHE-TALHH 188
Cdd:PHA02876 138 KINESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDlSVLEC 217

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 189 AAKVKNVDLIEMLIEFGGNIYARD--------NRGKKPSDYTWSSSAPAKCFEYYEKTPL 240
Cdd:PHA02876 218 AVDSKNIDTIKAIIDNRSNINKNDlsllkairNEDLETSLLLYDAGFSVNSIDDCKNTPL 277
Ank_4 pfam13637
Ankyrin repeats (many copies);
19-72 3.71e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 3.71e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 119606841   19 ERTPVHEAAQRGESLQLQQLIESGACVNQVTVDSITPLHAASLQGQARCVQLLL 72
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 152-215 5.04e-06

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 47.38  E-value: 5.04e-06
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 119606841  152 TPLHVACAREHLDCVKVLLNAGANVNAA--------KLHETALHH-------AAKVKNVDLIEMLIEFGGNIYARDNRG 215
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPARacgdffvkSQGVDSFYHgesplnaAACLGSPSIVALLSEDPADILTADSLG 208
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 152-178 5.57e-06

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: 42.19  E-value: 5.57e-06
                           10        20
                   ....*....|....*....|....*..
gi 119606841   152 TPLHVACAREHLDCVKVLLNAGANVNA 178
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 152-178 1.05e-05

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: 41.51  E-value: 1.05e-05
                          10        20
                  ....*....|....*....|....*...
gi 119606841  152 TPLHVACARE-HLDCVKVLLNAGANVNA 178
Cdd:pfam00023   4 TPLHLAAGRRgNLEIVKLLLSKGADVNA 31
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
 240-277 1.13e-05

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: 41.24  E-value: 1.13e-05
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 119606841   240 LTLSQLCRVNLRKATGvrgleKIAKLNIPPRLIDYLSY 277
Cdd:smart00969   1 RSLQHLCRLAIRRSLG-----GIDKLPLPPRLKDYLLY 33
PHA02946 PHA02946
ankyin-like protein; Provisional
 35-229 1.20e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.20  E-value: 1.20e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  35 LQQLIESGACVNQVTVDSITPLHAASLQGQARCVQLLLAAGAQVDARNIDGSTPLCDACASGS--IECVKLLLSYGAKVN 112
Cdd:PHA02946  55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERINLLVQYGAKIN 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 113 PPL--YTASPLHeACMSGSSECVRLLIDVGANLEAHDcHFGTP---LHVACAREHLDCVKVLLNAGANVNAAKlHE--TA 185
Cdd:PHA02946 135 NSVdeEGCGPLL-ACTDPSERVFKKIMSIGFEARIVD-KFGKNhihRHLMSDNPKASTISWMMKLGISPSKPD-HDgnTP 211

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 119606841 186 LH--HAAKVKNVDLIEMLIEfGGNIYARDNRGKKPSDYTWSSSAPA 229
Cdd:PHA02946 212 LHivCSKTVKNVDIINLLLP-STDVNKQNKFGDSPLTLLIKTLSPA 256
Ank_2 pfam12796
Ankyrin repeats (3 copies);
20-82 1.46e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.80  E-value: 1.46e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 119606841   20 RTPVHEAAQRGESLQLQQLIESGACvnQVTVDSITPLHAASLQGQARCVQLLLAAGAQVDARN 82
Cdd:pfam12796  31 RTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 84-112 2.30e-05

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: 40.65  E-value: 2.30e-05
                           10        20
                   ....*....|....*....|....*....
gi 119606841    84 DGSTPLCDACASGSIECVKLLLSYGAKVN 112
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 108-216 2.36e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 45.63  E-value: 2.36e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 108 GAKVNPPLytASPLHEACMSGSSECVRLLIDVGANLEAHDCHFGTPLHVACAREHLDCVKVLLNAGANVN---------- 177
Cdd:PLN03192 518 GEHDDPNM--ASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHirdangntal 595

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 119606841 178 ----AAKLHE--TALHH----------------AAKVKNVDLIEMLIEFGGNIYARDNRGK 216
Cdd:PLN03192 596 wnaiSAKHHKifRILYHfasisdphaagdllctAAKRNDLTAMKELLKQGLNVDSEDHQGA 656
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 131-215 2.68e-05

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: 45.13  E-value: 2.68e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 131 ECVRLLID-----------VGANLEAHDCHFGTPLHVACAREHLDCVKVLLNAGANVNA-AK--------------LHET 184
Cdd:cd22194  111 EIVRILLAfaeengildrfINAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAhAKgvffnpkykhegfyFGET 190

                         90       100       110
                 ....*....|....*....|....*....|..
gi 119606841 185 ALHHAAKVKNVDLIEMLIEFGGNIYA-RDNRG 215
Cdd:cd22194  191 PLALAACTNQPEIVQLLMEKESTDITsQDSRG 222
SOCS_SSB1_4 cd03718
SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box ...
 239-277 3.59e-05

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: 40.36  E-value: 3.59e-05
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 119606841 239 PLTLSQLCRVNLRKATGVRGLEKIAKLNIPPRLIDYLSY 277
Cdd:cd03718    3 PLPLMDLCRRRVRVALGRDRLEEIEQLPLPPSLKNYLLY 41
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 18-147 1.01e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 43.53  E-value: 1.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841   18 VERTPVHEAAQRGESLQLQQLIESgaCVNQVTVDsITPLHAASLQGQARCVQLLLAAGAQVDARnidgstPLCDACASGS 97
Cdd:TIGR00870  97 VEAILLHLLAAFRKSGPLELANDQ--YTSEFTPG-ITALHLAAHRQNYEIVKLLLERGASVPAR------ACGDFFVKSQ 167

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 119606841   98 iecVKLLLSYGakvnpplytASPLHEACMSGSSECVRLLIDVGANLEAHD 147
Cdd:TIGR00870 168 ---GVDSFYHG---------ESPLNAAACLGSPSIVALLSEDPADILTAD 205
PHA02859 PHA02859
ankyrin repeat protein; Provisional
 97-220 1.03e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 42.50  E-value: 1.03e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  97 SIECVKLLLSYGAKVN--PPLYTASPLHEACMSG---SSECVRLLIDVGANLEAHDCHFGTPLHVACAR--EHLDCVKVL 169
Cdd:PHA02859  65 NVEILKFLIENGADVNfkTRDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHMYMCNfnVRINVIKLL 144

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 119606841 170 LNAGANV------NAAKLHETALHHAAKvknvDLIEMLIEFGGNIYARDNRGKKPSD 220
Cdd:PHA02859 145 IDSGVSFlnkdfdNNNILYSYILFHSDK----KIFDFLTSLGIDINETNKSGYNCYD 197
Ank_5 pfam13857
Ankyrin repeats (many copies);
45-89 1.68e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 1.68e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 119606841   45 VNQVTVDSITPLHAASLQGQARCVQLLLAAGAQVDARNIDGSTPL 89
Cdd:pfam13857   9 LNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 128-215 1.75e-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: 42.86  E-value: 1.75e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 128 GSSECVRLLIDVG---------ANLEAHDCHF--GTPLHVACAREHLDCVKVLLNAGANVNAAK---------------L 181
Cdd:cd22193   43 GTNDTIRILLDIAektdnlkrfINAEYTDEYYegQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqgegfyF 122

                         90       100       110
                 ....*....|....*....|....*....|....*..
gi 119606841 182 HETALHHAAKVKNVDLIEMLIEFG---GNIYARDNRG 215
Cdd:cd22193  123 GELPLSLAACTNQPDIVQYLLENEhqpADIEAQDSRG 159
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 54-82 4.46e-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. 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: 36.88  E-value: 4.46e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 119606841   54 TPLH-AASLQGQARCVQLLLAAGAQVDARN 82
Cdd:pfam00023   4 TPLHlAAGRRGNLEIVKLLLSKGADVNARD 33
SOCS_SSB4 cd03743
SOCS (suppressors of cytokine signaling) box of SSB4 (SPRY domain-containing SOCS box ...
 239-277 5.41e-04

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: 36.86  E-value: 5.41e-04
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 119606841 239 PLTLSQLCRVNLRKATGVRGLEKIAKLNIPPRLIDYLSY 277
Cdd:cd03743    3 PLPLMDLCRRSARQALGRHRLHHIQSLPLPQTLKNYLQY 41
SOCS_ASB1 cd03720
SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a ...
 239-278 5.42e-04

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: 37.01  E-value: 5.42e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 119606841 239 PLTLSQLCRVNLRKATGVRGLEKIAKLNIPPRLIDYLSYN 278
Cdd:cd03720    3 PRSLLSLCRIAVRRALGKQRLSLICSLPLPDPIKKFLLHE 42
Ank_5 pfam13857
Ankyrin repeats (many copies);
183-221 5.64e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 5.64e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 119606841  183 ETALHHAAKVKNVDLIEMLIEFGGNIYARDNRGKKPSDY 221
Cdd:pfam13857  17 YTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDL 55
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 184-210 7.60e-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: 36.03  E-value: 7.60e-04
                           10        20
                   ....*....|....*....|....*..
gi 119606841   184 TALHHAAKVKNVDLIEMLIEFGGNIYA 210
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 129-215 9.19e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.20  E-value: 9.19e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 129 SSECVRLLIDVGANLEAHDCHFGTPL-----HVACAREHLDCVKVLLNAGANVNAAKLH-ETALH---HAAKVKNVDLIE 199
Cdd:PHA02798  50 STDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIENGADINKKNSDgETPLYcllSNGYINNLEILL 129

                         90
                 ....*....|....*.
gi 119606841 200 MLIEFGGNIYARDNRG 215
Cdd:PHA02798 130 FMIENGADTTLLDKDG 145
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 119-145 9.91e-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: 36.03  E-value: 9.91e-04
                           10        20
                   ....*....|....*....|....*..
gi 119606841   119 SPLHEACMSGSSECVRLLIDVGANLEA 145
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 152-178 1.27e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.70  E-value: 1.27e-03
                          10        20
                  ....*....|....*....|....*..
gi 119606841  152 TPLHVACAREHLDCVKVLLNAGANVNA 178
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
SOCS_ASB7 cd03726
SOCS (suppressors of cytokine signaling) box of ASB7-like proteins. ASB family members have a ...
 237-277 1.64e-03

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: 35.59  E-value: 1.64e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 119606841 237 KTPLTLSQLCRVNLRKATGVRGLEKIAKLNIPPRLIDYLSY 277
Cdd:cd03726    1 RQPRTLQDLCRIKIRHCIGLQNLKLLDELPIAKVMKDYLKH 41
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 84-112 1.91e-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: 35.34  E-value: 1.91e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 119606841   84 DGSTPLCDACAS-GSIECVKLLLSYGAKVN 112
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
 239-277 2.02e-03

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: 35.58  E-value: 2.02e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 119606841 239 PLTLSQLCRVNLRKATGVRGLEKIA---KLNIPPRLIDYLSY 277
Cdd:cd03731    3 PRPLKHLCRLKIRKLMGLQKLQQPSsmkKLPLPPALKRYILY 44
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 119-145 2.12e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.93  E-value: 2.12e-03
                          10        20
                  ....*....|....*....|....*..
gi 119606841  119 SPLHEACMSGSSECVRLLIDVGANLEA 145
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADINA 30
SOCS_ASB_9_11 cd03728
SOCS (suppressors of cytokine signaling) box of ASB9 and 11 proteins. ASB family members have ...
 239-277 2.44e-03

SOCS (suppressors of cytokine signaling) box of ASB9 and 11 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: 239698  Cd Length: 42  Bit Score: 35.15  E-value: 2.44e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 119606841 239 PLTLSQLCRVNLRKATGVRGLEKIAKLNIPPRLIDYLSY 277
Cdd:cd03728    3 PPSLMQLCRLCIRKCFGRKQHHKIHKLHLPEPLKHFLLY 41
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 182-210 2.90e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 34.54  E-value: 2.90e-03
                          10        20
                  ....*....|....*....|....*....
gi 119606841  182 HETALHHAAKVKNVDLIEMLIEFGGNIYA 210
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 183-213 2.98e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.57  E-value: 2.98e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 119606841  183 ETALHHAA-KVKNVDLIEMLIEFGGNIYARDN 213
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
 239-277 3.08e-03

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: 34.49  E-value: 3.08e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 119606841 239 PLTLSQLCRVNLRKATGVrglEKIAKLNIPPRLIDYLSY 277
Cdd:cd03717    3 VRSLQHLCRFVIRQCTRR---DLIDQLPLPRRLKDYLKE 38
Ank_5 pfam13857
Ankyrin repeats (many copies);
152-189 3.10e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 3.10e-03
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 119606841  152 TPLHVACAREHLDCVKVLLNAGANVNAAKLH-ETALHHA 189
Cdd:pfam13857  18 TPLHVAAKYGALEIVRVLLAYGVDLNLKDEEgLTALDLA 56
SOCS smart00253
suppressors of cytokine signalling; suppressors of cytokine signalling
 239-277 3.77e-03

suppressors of cytokine signalling; suppressors of cytokine signalling


Pssm-ID: 128549  Cd Length: 43  Bit Score: 34.58  E-value: 3.77e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 119606841   239 PLTLSQLCRVNLRKATGVrglEKIAKLNIPPRLIDYLSY 277
Cdd:smart00253   7 VPSLQHLCRFTIRRCTRT---DQIKTLPLPPKLKDYLSY 42
SOCS_ASB5 cd03724
SOCS (suppressors of cytokine signaling) box of ASB5-like proteins. ASB family members have a ...
 238-277 3.79e-03

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: 34.47  E-value: 3.79e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 119606841 238 TPLTLSQLCRVNLRKATGVRGLEKIAKLNIPPRLIDYLSY 277
Cdd:cd03724    2 TPSSLCQLCRLCIRNYIGRSRLHLIPQLQLPTLLKNFLQY 41
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
 238-275 4.33e-03

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: 34.72  E-value: 4.33e-03
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 119606841 238 TPLTLSQLCRVNLRKATGVRGLEKIAKLNIPPRLIDYL 275
Cdd:cd03723    2 TPRSLQHLCRCAIRKLLGSRCHKLVPQLSLPTSLKNYL 39
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 119-147 4.46e-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: 4.46e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 119606841  119 SPLHEAC-MSGSSECVRLLIDVGANLEAHD 147
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 121-215 4.94e-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: 38.32  E-value: 4.94e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 121 LHEACM---SGSSECVRLLIDVG---------ANLEAHDCHF--GTPLHVACAREHLDCVKVLLNAGANVNAAK------ 180
Cdd:cd21882   30 LHKAALnlnDGVNEAIMLLLEAApdsgnpkelVNAPCTDEFYqgQTALHIAIENRNLNLVRLLVENGADVSARAtgrffr 109

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 119606841 181 --------LHETALHHAAKVKNVDLIEMLIEFGGNI---YARDNRG 215
Cdd:cd21882  110 kspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQPaalEAQDSLG 155
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 97-213 7.09e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 37.80  E-value: 7.09e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  97 SIECVKLLLSYGAKVNPPLYTASPL------HEACMSGSSECVRLLIDVGANLEAHDCHFGTPLHVACAREH---LDCVK 167
Cdd:PHA02989  49 KIKIVKLLIDNGADVNYKGYIETPLcavlrnREITSNKIKKIVKLLLKFGADINLKTFNGVSPIVCFIYNSNinnCDMLR 128

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 119606841 168 VLLNAGANVNAAKLHE--TALHHAAKVKNV--DLIEMLIEFGGNIYARDN 213
Cdd:PHA02989 129 FLLSKGINVNDVKNSRgyNLLHMYLESFSVkkDVIKILLSFGVNLFEKTS 178
PHA02736 PHA02736
Viral ankyrin protein; Provisional
 98-174 7.59e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 36.39  E-value: 7.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  98 IECVKLLLSYGAKVNPP--LYTASPLHEACMSGSSECVRLLIDV-GANLEAHDCHFGTPLHVACAREHLDCVKVLLNAGA 174
Cdd:PHA02736  71 QEKLKLLMEWGADINGKerVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
PHA02791 PHA02791
ankyrin-like protein; Provisional
 38-210 9.65e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 36.94  E-value: 9.65e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841  38 LIESGACVNqvTVDSITPLHAASLQGQARCVQLLLAAGAQVDARNIDGSTPLCDACASGSIECVKL-------LLSYGAK 110
Cdd:PHA02791  49 LLNAGALKN--LLENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQTVKLfvkknwrLMFYGKT 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 119606841 111 VnpplYTASPLHEACMSGSSECVRLLIDVGANLEAhdCHFGTPLHVACAREHLDCVKVLLN--AGANVNAAKLHETALHH 188
Cdd:PHA02791 127 G----WKTSFYHAVMLNDVSIVSYFLSEIPSTFDL--AILLSCIHITIKNGHVDMMILLLDymTSTNTNNSLLFIPDIKL 200

                        170       180
                 ....*....|....*....|..
gi 119606841 189 AAKVKNVDLIEMLIEFGGNIYA 210
Cdd:PHA02791 201 AIDNKDLEMLQALFKYDINIYS 222
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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