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Conserved domains on  [gi|24586688|ref|NP_543139|]
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ankyrin repeat and SOCS box protein 16 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
108-327 3.80e-31

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.21  E-value: 3.80e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688 108 KTKQTAPLAIATARGYTDCARHLIRQGAELDARV-GGRAALHEACARAQFDCVRLLLTFGAKANVLTEEGTTPLHLCTIP 186
Cdd:COG0666  51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDdGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688 187 ESLQCAKLLLEAGATVNlAAGESQETPLHVAAARGLEQHVALYLEHGADVGLRTSQGETALNTACAgaegpgscRRHQAA 266
Cdd:COG0666 131 GNLEIVKLLLEAGADVN-AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE--------NGHLEI 201

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24586688 267 ARRLLEAGADARAAGRKRHTPLHNACANGCGGLAELLLRYGARAEVPNGAGHTPMDCALQA 327
Cdd:COG0666 202 VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAA 262
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
 406-447 5.95e-12

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: 59.82  E-value: 5.95e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24586688 406 NQPRQLQHLARLAVRARLGSRCRQGATRLPLPPLLRDYLLLR 447
Cdd:cd03716   1 STPRSLQHLCRLAIRRCLGRRRLELIKKLPLPPRLKDYLLYE 42
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
108-327 3.80e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.21  E-value: 3.80e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688 108 KTKQTAPLAIATARGYTDCARHLIRQGAELDARV-GGRAALHEACARAQFDCVRLLLTFGAKANVLTEEGTTPLHLCTIP 186
Cdd:COG0666  51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDdGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688 187 ESLQCAKLLLEAGATVNlAAGESQETPLHVAAARGLEQHVALYLEHGADVGLRTSQGETALNTACAgaegpgscRRHQAA 266
Cdd:COG0666 131 GNLEIVKLLLEAGADVN-AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE--------NGHLEI 201

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24586688 267 ARRLLEAGADARAAGRKRHTPLHNACANGCGGLAELLLRYGARAEVPNGAGHTPMDCALQA 327
Cdd:COG0666 202 VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAA 262
Ank_2 pfam12796
Ankyrin repeats (3 copies);
147-239 9.65e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 9.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688   147 LHEACARAQFDCVRLLLTFGAKANVLTEEGTTPLHLCTIPESLQCAKLLLEagaTVNLAAGESQETPLHVAAARGLEQHV 226
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 24586688   227 ALYLEHGADVGLR 239
Cdd:pfam12796  78 KLLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 147-332 4.85e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 70.76  E-value: 4.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  147 LHEACARAQFDCVRLLLTFGAKANVLTEEGTTPLHLCTIPESLQCAKLLLEAGATVNLaAGESQETPLHVAAARGLEQHV 226
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV-KDNNGESPLHNAAEYGDYACI 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  227 ALYLEHGADVGLRTSQGETALNTACAgaegpgscrrHQAAARRLLEAGADARAAGRKRHTPLHNACANGCG-GLAELLLR 305
Cdd:PHA02874 207 KLLIDHGNHIMNKCKNGFTPLHNAII----------HNRSAIELLINNASINDQDIDGSTPLHHAINPPCDiDIIDILLY 276

                        170       180
                 ....*....|....*....|....*..
gi 24586688  306 YGARAEVPNGAGHTPMDCALQAVQDSP 332
Cdd:PHA02874 277 HKADISIKDNKGENPIDTAFKYINKDP 303
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
 406-447 5.95e-12

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: 59.82  E-value: 5.95e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24586688 406 NQPRQLQHLARLAVRARLGSRCRQGATRLPLPPLLRDYLLLR 447
Cdd:cd03716   1 STPRSLQHLCRLAIRRCLGRRRLELIKKLPLPPRLKDYLLYE 42
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 407-445 1.19e-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: 53.32  E-value: 1.19e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 24586688   407 QPRQLQHLARLAVRARLGSRCRQGATRLPLPPLLRDYLL 445
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 143-248 5.14e-08

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: 55.47  E-value: 5.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688   143 GRAALHEA---CARAQFDCVRLLLTFGAKANVLTE----------EGTTPLHLCTIPESLQCAKLLLEAGATVNLAAG-- 207
Cdd:TIGR00870  82 GDTLLHAIsleYVDAVEAILLHLLAAFRKSGPLELandqytseftPGITALHLAAHRQNYEIVKLLLERGASVPARACgd 161

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 24586688   208 ---ESQ--------ETPLHVAAARGLEQHVALYLEHGADVGLRTSQGETALN 248
Cdd:TIGR00870 162 ffvKSQgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLH 213
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 122-248 3.39e-07

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: 52.57  E-value: 3.39e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688 122 GYTDCARHLIRQGAELDARVGgRAALHEAC---ARAQFDCVRLLLTFGAKANVLTE-----------EGTTPLHLCTIPE 187
Cdd:cd21882   6 GLLECLRWYLTDSAYQRGATG-KTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENR 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24586688 188 SLQCAKLLLEAGATVNLAAG-----ESQ-------ETPLHVAAARGLEQHVALYLEHGAD---VGLRTSQGETALN 248
Cdd:cd21882  85 NLNLVRLLVENGADVSARATgrffrKSPgnlfyfgELPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLH 160
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
 409-447 8.76e-06

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: 42.40  E-value: 8.76e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 24586688    409 RQLQHLARLAVRARLGSRCRqgatrLPLPPLLRDYLLLR 447
Cdd:smart00969   1 RSLQHLCRLAIRRSLGGIDK-----LPLPPRLKDYLLYY 34
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
108-327 3.80e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.21  E-value: 3.80e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688 108 KTKQTAPLAIATARGYTDCARHLIRQGAELDARV-GGRAALHEACARAQFDCVRLLLTFGAKANVLTEEGTTPLHLCTIP 186
Cdd:COG0666  51 DALGALLLLAAALAGDLLVALLLLAAGADINAKDdGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688 187 ESLQCAKLLLEAGATVNlAAGESQETPLHVAAARGLEQHVALYLEHGADVGLRTSQGETALNTACAgaegpgscRRHQAA 266
Cdd:COG0666 131 GNLEIVKLLLEAGADVN-AQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE--------NGHLEI 201

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24586688 267 ARRLLEAGADARAAGRKRHTPLHNACANGCGGLAELLLRYGARAEVPNGAGHTPMDCALQA 327
Cdd:COG0666 202 VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAA 262
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
112-326 4.01e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 107.35  E-value: 4.01e-26
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688 112 TAPLAIATARGYTDCARHLIRQGAELDARVGGRAALHEACARAQFDCVRLLLTFGAKANVLTEEGTTPLHLCTIPESLQC 191
Cdd:COG0666  23 LLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEI 102

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688 192 AKLLLEAGATVNlAAGESQETPLHVAAARGLEQHVALYLEHGADVGLRTSQGETALNTACAgaegpgscRRHQAAARRLL 271
Cdd:COG0666 103 VKLLLEAGADVN-ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA--------NGNLEIVKLLL 173

                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 24586688 272 EAGADARAAGRKRHTPLHNACANGCGGLAELLLRYGARAEVPNGAGHTPMDCALQ 326
Cdd:COG0666 174 EAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
58-252 2.13e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.34  E-value: 2.13e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  58 DPAVHQALFSGNLQQVQALfqdeeaanmivetvsnqlawsAEQGFWVLTPKTKQTAPLAIATARGYTDCARHLIRQGAEL 137
Cdd:COG0666  88 NTLLHAAARNGDLEIVKLL---------------------LEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADV 146

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688 138 DAR-VGGRAALHEACARAQFDCVRLLLTFGAKANVLTEEGTTPLHLCTIPESLQCAKLLLEAGATVNlAAGESQETPLHV 216
Cdd:COG0666 147 NAQdNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN-AKDNDGKTALDL 225

                       170       180       190
                ....*....|....*....|....*....|....*.
gi 24586688 217 AAARGLEQHVALYLEHGADVGLRTSQGETALNTACA 252
Cdd:COG0666 226 AAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA 261
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
130-350 6.63e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 89.63  E-value: 6.63e-20
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688 130 LIRQGAELDARVGGRAALHEACARAQFDCVRLLLTFGAKANVLTEEGTTPLHLCTIPESLQCAKLLLEAGATVNLAAGES 209
Cdd:COG0666   7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688 210 QETPLHVAAARGLEQHVALYLEHGADVGLRTSQGETALNTACAgaegpgscRRHQAAARRLLEAGADARAAGRKRHTPLH 289
Cdd:COG0666  87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAY--------NGNLEIVKLLLEAGADVNAQDNDGNTPLH 158

                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 24586688 290 NACANGCGGLAELLLRYGARAEVPNGAGHTPMDCALQavqdspNWEPEVLfAALLDYGAQP 350
Cdd:COG0666 159 LAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE------NGHLEIV-KLLLEAGADV 212
Ank_2 pfam12796
Ankyrin repeats (3 copies);
147-239 9.65e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 9.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688   147 LHEACARAQFDCVRLLLTFGAKANVLTEEGTTPLHLCTIPESLQCAKLLLEagaTVNLAAGESQETPLHVAAARGLEQHV 226
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEIV 77

                          90
                  ....*....|...
gi 24586688   227 ALYLEHGADVGLR 239
Cdd:pfam12796  78 KLLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 147-332 4.85e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 70.76  E-value: 4.85e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  147 LHEACARAQFDCVRLLLTFGAKANVLTEEGTTPLHLCTIPESLQCAKLLLEAGATVNLaAGESQETPLHVAAARGLEQHV 226
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV-KDNNGESPLHNAAEYGDYACI 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  227 ALYLEHGADVGLRTSQGETALNTACAgaegpgscrrHQAAARRLLEAGADARAAGRKRHTPLHNACANGCG-GLAELLLR 305
Cdd:PHA02874 207 KLLIDHGNHIMNKCKNGFTPLHNAII----------HNRSAIELLINNASINDQDIDGSTPLHHAINPPCDiDIIDILLY 276

                        170       180
                 ....*....|....*....|....*..
gi 24586688  306 YGARAEVPNGAGHTPMDCALQAVQDSP 332
Cdd:PHA02874 277 HKADISIKDNKGENPIDTAFKYINKDP 303
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 108-262 2.23e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 68.75  E-value: 2.23e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  108 KTKQTAPLAIATARGYTDCARHLIRQGAELDA-RVGGRAALHEACARAQFDCVRLLLTFGAKANVLTEEGTTPLHLCT-I 185
Cdd:PHA02878 165 RHKGNTALHYATENKDQRLTELLLSYGANVNIpDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVgY 244

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 24586688  186 PESLQCAKLLLEAGATVNLAAGESQETPLHVAAARglEQHVALYLEHGADVGLRTSQGETALNTACAGAEGPGSCRR 262
Cdd:PHA02878 245 CKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLCINIGRI 319
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
 406-447 5.95e-12

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: 59.82  E-value: 5.95e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24586688 406 NQPRQLQHLARLAVRARLGSRCRQGATRLPLPPLLRDYLLLR 447
Cdd:cd03716   1 STPRSLQHLCRLAIRRCLGRRRLELIKKLPLPPRLKDYLLYE 42
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
 407-447 1.03e-11

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: 1.03e-11
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24586688 407 QPRQLQHLARLAVRARLGSRCRQGATRLPLPPLLRDYLLLR 447
Cdd:cd03587   1 NPRSLQHLCRLAIRRCLGKRRLDLIDKLPLPPRLKDYLLYK 41
Ank_2 pfam12796
Ankyrin repeats (3 copies);
214-314 5.21e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 58.97  E-value: 5.21e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688   214 LHVAAARGLEQHVALYLEHGADVGLRTSQGETALNTACagaegpgsCRRHQAAARRLLEagADARAAGRKRHTPLHNACA 293
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAA--------KNGHLEIVKLLLE--HADVNLKDNGRTALHYAAR 70

                          90       100
                  ....*....|....*....|.
gi 24586688   294 NGCGGLAELLLRYGARAEVPN 314
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINVKD 91
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
 406-452 1.39e-10

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: 56.29  E-value: 1.39e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 24586688 406 NQPRQLQHLARLAVRARLGSRCRQGATRLPLPPLLRDYLLLRVEGCI 452
Cdd:cd03723   1 GTPRSLQHLCRCAIRKLLGSRCHKLVPQLSLPTSLKNYLLLEPEGVL 47
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 64-349 3.55e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.00  E-value: 3.55e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688   64 ALFSGNLQQVQALFQDEEAANM----IVETVSNQLAWSA----EQGFWVLTPKTKQTAPLAIAT-ARGYTDCARHLIRQG 134
Cdd:PHA02876 218 AVDSKNIDTIKAIIDNRSNINKndlsLLKAIRNEDLETSlllyDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERG 297

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  135 AELDAR-VGGRAALHeACARAQFDC--VRLLLTFGAKANVLTEEGTTPLH-LCTIPESLQCAKLLLEAGATVNlAAGESQ 210
Cdd:PHA02876 298 ADVNAKnIKGETPLY-LMAKNGYDTenIRTLIMLGADVNAADRLYITPLHqASTLDRNKDIVITLLELGANVN-ARDYCD 375

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  211 ETPLHVAAARGLEQHVALYLEHGADVGLRTSQGETALNTACAGAEGPGScrrhqaaARRLLEAGADARAAGRKRHTPLHN 290
Cdd:PHA02876 376 KTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYMS-------VKTLIDRGANVNSKNKDLSTPLHY 448

                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  291 ACANGCG-GLAELLLRYGARAEVPNGAGHTPMDCALqavqdspnwEPEVLFAALLDYGAQ 349
Cdd:PHA02876 449 ACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAL---------EYHGIVNILLHYGAE 499
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 407-445 1.19e-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: 53.32  E-value: 1.19e-09
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 24586688   407 QPRQLQHLARLAVRARLGSRCRQGATRLPLPPLLRDYLL 445
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 124-250 5.14e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.97  E-value: 5.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  124 TDCARHLIRQGAELDA--RVGGRAALHEACARAQFDCVRLLLTFGAKANVLTEEGTTPLHLCTIPESLQCAKLLLEAGAT 201
Cdd:PHA02878 147 AEITKLLLSYGADINMkdRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 24586688  202 VNlAAGESQETPLHVAAARGLEQHV-ALYLEHGADVGLRTS-QGETALNTA 250
Cdd:PHA02878 227 TD-ARDKCGNTPLHISVGYCKDYDIlKLLLEHGVDVNAKSYiLGLTALHSS 276
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 127-349 2.76e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 56.23  E-value: 2.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  127 ARHLIRQGAELDAR-VGGRAALHEACARAQFDCVRLLLTFGAKANVLTEEGTTPL-------HLCTIP------------ 186
Cdd:PHA02876 161 AEMLLEGGADVNAKdIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLecavdskNIDTIKaiidnrsninkn 240

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  187 ----------ESLQCAKLLLEAGATVNlAAGESQETPLHVAA-ARGLEQHVALYLEHGADVGLRTSQGETALNTACAGAE 255
Cdd:PHA02876 241 dlsllkairnEDLETSLLLYDAGFSVN-SIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKNGY 319

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  256 GPGSCrrhqaaaRRLLEAGADARAAGRKRHTPLHNACA-NGCGGLAELLLRYGARAEVPNGAGHTPMDCAlqAVQDSPnw 334
Cdd:PHA02876 320 DTENI-------RTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYA--AVRNNV-- 388

                        250
                 ....*....|....*
gi 24586688  335 epeVLFAALLDYGAQ 349
Cdd:PHA02876 389 ---VIINTLLDYGAD 400
PHA03095 PHA03095
ankyrin-like protein; Provisional
 149-365 3.52e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.42  E-value: 3.52e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  149 EACARAQFDCVRLLLTFGAKANVLTEEGTTPLHLC---TIPESLQCAKLLLEAGATVNlAAGESQETPLHVAAARGLEQH 225
Cdd:PHA03095  20 LNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYlhySSEKVKDIVRLLLEAGADVN-APERCGFTPLHLYLYNATTLD 98

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  226 V-ALYLEHGADVGLRTSQGETALntacagaegpgscrrhqaaarrlleagadaraagrkrHTPLHNACANGcgGLAELLL 304
Cdd:PHA03095  99 ViKLLIKAGADVNAKDKVGRTPL-------------------------------------HVYLSGFNINP--KVIRLLL 139

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24586688  305 RYGARAEVPNGAGHTPMDCALQavqdSPNWEPEVLfAALLDYGAQP-----VRPEMLKHCANFPRA 365
Cdd:PHA03095 140 RKGADVNALDLYGMTPLAVLLK----SRNANVELL-RLLIDAGADVyavddRFRSLLHHHLQSFKP 200
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 143-248 5.14e-08

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: 55.47  E-value: 5.14e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688   143 GRAALHEA---CARAQFDCVRLLLTFGAKANVLTE----------EGTTPLHLCTIPESLQCAKLLLEAGATVNLAAG-- 207
Cdd:TIGR00870  82 GDTLLHAIsleYVDAVEAILLHLLAAFRKSGPLELandqytseftPGITALHLAAHRQNYEIVKLLLERGASVPARACgd 161

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 24586688   208 ---ESQ--------ETPLHVAAARGLEQHVALYLEHGADVGLRTSQGETALN 248
Cdd:TIGR00870 162 ffvKSQgvdsfyhgESPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLH 213
Ank_2 pfam12796
Ankyrin repeats (3 copies);
62-171 5.69e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.11  E-value: 5.69e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688    62 HQALFSGNLQQVQALFQDEEAANmivetvsnqlawsaeqgfwvLTPKTKQTaPLAIATARGYTDCARHLIRQgAELDARV 141
Cdd:pfam12796   2 HLAAKNGNLELVKLLLENGADAN--------------------LQDKNGRT-ALHLAAKNGHLEIVKLLLEH-ADVNLKD 59

                          90       100       110
                  ....*....|....*....|....*....|
gi 24586688   142 GGRAALHEACARAQFDCVRLLLTFGAKANV 171
Cdd:pfam12796  60 NGRTALHYAARSGHLEIVKLLLEKGADINV 89
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 159-325 9.50e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.12  E-value: 9.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  159 VRLLLTFGAKANVLTEE-GTTPLHLCTIPESLQCAKLLLEAGATVNLAaGESQETPLHVAAARGLEQHVALYLEHGADVG 237
Cdd:PHA02878 150 TKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIP-DKTNNSPLHHAVKHYNKPIVHILLENGASTD 228

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  238 LRTSQGETALNTACagaegpGSCRRHQAAaRRLLEAGADARAAGRKRH-TPLHNACANGcgGLAELLLRYGARAEVPNGA 316
Cdd:PHA02878 229 ARDKCGNTPLHISV------GYCKDYDIL-KLLLEHGVDVNAKSYILGlTALHSSIKSE--RKLKLLLEYGADINSLNSY 299


                 ....*....
gi 24586688  317 GHTPMDCAL 325
Cdd:PHA02878 300 KLTPLSSAV 308
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 122-248 3.39e-07

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: 52.57  E-value: 3.39e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688 122 GYTDCARHLIRQGAELDARVGgRAALHEAC---ARAQFDCVRLLLTFGAKANVLTE-----------EGTTPLHLCTIPE 187
Cdd:cd21882   6 GLLECLRWYLTDSAYQRGATG-KTCLHKAAlnlNDGVNEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENR 84

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24586688 188 SLQCAKLLLEAGATVNLAAG-----ESQ-------ETPLHVAAARGLEQHVALYLEHGAD---VGLRTSQGETALN 248
Cdd:cd21882  85 NLNLVRLLVENGADVSARATgrffrKSPgnlfyfgELPLSLAACTNQEEIVRLLLENGAQpaaLEAQDSLGNTVLH 160
PHA03095 PHA03095
ankyrin-like protein; Provisional
 130-305 6.37e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.56  E-value: 6.37e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  130 LIRQGAELDARVG-GRAALHeACAR---AQFDCVRLLLTFGAKANVLTEEGTTPLHL------CTIpESLqcaKLLLEAG 199
Cdd:PHA03095 103 LIKAGADVNAKDKvGRTPLH-VYLSgfnINPKVIRLLLRKGADVNALDLYGMTPLAVllksrnANV-ELL---RLLIDAG 177

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  200 ATV---------------------------NLAAG-------ESQETPLHVAAARGLEQ--HVALYLEHGADVGLRTSQG 243
Cdd:PHA03095 178 ADVyavddrfrsllhhhlqsfkprarivreLIRAGcdpaatdMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYG 257

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 24586688  244 ETALNTAcagaegpgSCRRHQAAARRLLEAGADARAAGRKRHTPLHNACANGCGGLAELLLR 305
Cdd:PHA03095 258 QTPLHYA--------AVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALA 311
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 113-247 1.88e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 49.99  E-value: 1.88e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  113 APLAIATARGYTDCARHLIRQGAELDARV--GGRAALHEACARAQFDCVRLLLTFGAKANVLTEEGTTPLHLCTIPESLQ 190
Cdd:PHA02875  70 SELHDAVEEGDVKAVEELLDLGKFADDVFykDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIK 149

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 24586688  191 CAKLLLEAGATVNLAAGESQeTPLHVAAARGLEQHVALYLEHGADVGLRTSQGETAL 247
Cdd:PHA02875 150 GIELLIDHKACLDIEDCCGC-TPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA 205
Ank_4 pfam13637
Ankyrin repeats (many copies);
143-196 5.59e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 5.59e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 24586688   143 GRAALHEACARAQFDCVRLLLTFGAKANVLTEEGTTPLHLCTIPESLQCAKLLL 196
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
 406-445 8.07e-06

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: 42.58  E-value: 8.07e-06
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24586688 406 NQPRQLQHLARLAVRARLGsrcRQGATRLPLPPLLRDYLL 445
Cdd:cd03717   1 TSVRSLQHLCRFVIRQCTR---RDLIDQLPLPRRLKDYLK 37
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
 409-447 8.76e-06

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: 42.40  E-value: 8.76e-06
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 24586688    409 RQLQHLARLAVRARLGSRCRqgatrLPLPPLLRDYLLLR 447
Cdd:smart00969   1 RSLQHLCRLAIRRSLGGIDK-----LPLPPRLKDYLLYY 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 120-182 9.01e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 9.01e-06
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24586688  120 ARGYTDCARHLIRQGAELDAR-VGGRAALHEACARAQFDCVRLLLTFGAKANVLTEEGTTPLHL 182
Cdd:PTZ00322  91 ASGDAVGARILLTGGADPNCRdYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 159-232 1.06e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.97  E-value: 1.06e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24586688  159 VRLLLTFGAKANVLTEEGTTPLHLCTIPESLQCAKLLLEAGATVNLAAGESQeTPLHVAAARGLEQHVALYLEH 232
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK-TPLELAEENGFREVVQLLSRH 170
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 159-236 1.26e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 47.35  E-value: 1.26e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24586688  159 VRLLLTFGAKANVLTEEGTTPLHLCTIPESLQCAKLLLEAGATVNLAAgESQETPLHVAAARGLEQHVALYLEHGADV 236
Cdd:PHA03100 175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVN-KYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 153-252 2.82e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.20  E-value: 2.82e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  153 RAQFDCVRLLLTFGAKANVLTEEGTTPLHL----CTIpeSLQCAKLLLEAGATVNL---------------AAGESQETP 213
Cdd:PHA03100 118 SNSYSIVEYLLDNGANVNIKNSDGENLLHLylesNKI--DLKILKLLIDKGVDINAknrvnyllsygvpinIKDVYGFTP 195

                         90       100       110
                 ....*....|....*....|....*....|....*....
gi 24586688  214 LHVAAARGLEQHVALYLEHGADVGLRTSQGETALNTACA 252
Cdd:PHA03100 196 LHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAIL 234
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 195-252 4.78e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.01  E-value: 4.78e-05
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 24586688  195 LLEAGATVNLaaGESQ-ETPLHVAAARGLEQHVALYLEHGADVGLRTSQGETALNTACA 252
Cdd:PLN03192 544 LLKAKLDPDI--GDSKgRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAIS 600
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 144-357 8.19e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.60  E-value: 8.19e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  144 RAALHEACARAQFDCVRLLLTFGAKANVLTEEGTTPLHLCTIPESLQCAKLLLEAGATVNLAAgESQETPLHVAAARGLE 223
Cdd:PHA02875   3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKY-PDIESELHDAVEEGDV 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  224 QHVALYLEHGA---DVGLRtsQGETALNTAcagaegpgSCRRHQAAARRLLEAGADARAAGRKRHTPLHNACANGCGGLA 300
Cdd:PHA02875  82 KAVEELLDLGKfadDVFYK--DGMTPLHLA--------TILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 24586688  301 ELLLRYGARAEVPNGAGHTPMDCAL--------QAVQDS---PNWEPEVLFAALLDYGAQPVRPEMLK 357
Cdd:PHA02875 152 ELLIDHKACLDIEDCCGCTPLIIAMakgdiaicKMLLDSganIDYFGKNGCVAALCYAIENNKIDIVR 219
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 157-255 1.11e-04

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 44.40  E-value: 1.11e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688 157 DCVRLLLTFGAKANVLTE-----------EGTTPLHLCTIPESLQCAKLLLEAGATVNLAA----------GES---QET 212
Cdd:cd22193  46 DTIRILLDIAEKTDNLKRfinaeytdeyyEGQTALHIAIERRQGDIVALLVENGADVHAHAkgrffqpkyqGEGfyfGEL 125

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*.
gi 24586688 213 PLHVAAARGLEQHVALYLEHG---ADVGLRTSQGETALNTACAGAE 255
Cdd:cd22193 126 PLSLAACTNQPDIVQYLLENEhqpADIEAQDSRGNTVLHALVTVAD 171
SOCS_ASB14 cd03730
SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a ...
 408-447 1.81e-04

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


Pssm-ID: 239700  Cd Length: 57  Bit Score: 39.44  E-value: 1.81e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 24586688 408 PRQLQHLARLAVRA---RLGSRCRQGATRLPLPPLLRDYLLLR 447
Cdd:cd03730   3 PRSLKHLCRLKIRAcmgRLRLRCPVFMSFLPLPNRLKAYILYK 45
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 187-250 2.05e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 43.90  E-value: 2.05e-04
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 24586688  187 ESLQCAKLLLEAGATVNlAAGESQETPLHVAAARGLEQHVALYLEHGADVGLRTSQGETALNTA 250
Cdd:PHA02876 156 DELLIAEMLLEGGADVN-AKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECA 218
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 110-251 2.32e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.44  E-value: 2.32e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  110 KQTAPLAIATARGYTDCARHLIRQGAELDARVGGR-AALHEACARAQFDCVRLLLTFGAKANVLTEEGTTPLHLCTIPES 188
Cdd:PHA02875 101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKfSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 24586688  189 LQCAKLLLEAGATVNLAAGESQETPLHVAAARGLEQHVALYLEHGADVGLRTS-QGE--TALNTAC 251
Cdd:PHA02875 181 IAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNIMFMiEGEecTILDMIC 246
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 145-247 3.05e-04

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: 43.08  E-value: 3.05e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688 145 AALHEACARAQF--DCVRLLLTfgakaNVLTEE---GTTPLHLCTIPESLQCAKLLLEAGATVNLAAGESQ--------- 210
Cdd:cd22192  58 AALYDNLEAAVVlmEAAPELVN-----EPMTSDlyqGETALHIAVVNQNLNLVRELIARGADVVSPRATGTffrpgpknl 132

                        90       100       110       120
                ....*....|....*....|....*....|....*....|.
gi 24586688 211 ----ETPLHVAAARGLEQHVALYLEHGADVGLRTSQGETAL 247
Cdd:cd22192 133 iyygEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 135-252 3.31e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 43.32  E-value: 3.31e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  135 AELDARVG---GRAALHEACARAQFDCVRLLLTFGAKANVLTEEGTTPLHLCTIPESLQCAKLLLE-AGATVNLAAGESq 210
Cdd:PLN03192 547 AKLDPDIGdskGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHfASISDPHAAGDL- 625

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|..
gi 24586688  211 etpLHVAAARGLEQHVALYLEHGADVGLRTSQGETALNTACA 252
Cdd:PLN03192 626 ---LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMA 664
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 130-203 3.39e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 42.73  E-value: 3.39e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 24586688  130 LIRQGAELDAR-VGGRAALHEACARAQFDCVRLLLTFGAKANVLTEEGTTPLHLCTIPESLQCAKLLLEAGATVN 203
Cdd:PHA03100 178 LLSYGVPINIKdVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
SOCS_SSB2 cd03719
SOCS (suppressors of cytokine signaling) box of SSB2 (SPRY domain-containing SOCS box proteins) ...
 407-447 4.16e-04

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


Pssm-ID: 239689  Cd Length: 42  Bit Score: 37.69  E-value: 4.16e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 24586688 407 QPRQLQHLARLAVRARLGSRCRQGATRLPLPPLLRDYLLLR 447
Cdd:cd03719   2 EPHSLLHLSRLCVRHALGDTRLGQVSALPLPPAMKRYLLYQ 42
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 109-236 4.88e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.55  E-value: 4.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  109 TKQTAPLAIATARGYTDCARHLIRQGAELDAR-VGGRAALHEACARAQFDCVRLLLTFGAKANVLTEEGTtplhLCTIPE 187
Cdd:PLN03192 556 SKGRTPLHIAASKGYEDCVLVLLKHACNVHIRdANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL----LCTAAK 631

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 24586688  188 --SLQCAKLLLEAGATVNlAAGESQETPLHVAAARGLEQHVALYLEHGADV 236
Cdd:PLN03192 632 rnDLTAMKELLKQGLNVD-SEDHQGATALQVAMAEDHVDMVRLLIMNGADV 681
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 159-312 5.73e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.96  E-value: 5.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  159 VRLLLTFGAKANVLTEEGTTPLHLCTIP--ESLQCAKLLLEAGATVNLAAGESqETPLHVAA---------ARGLEQH-- 225
Cdd:PHA03100  89 VKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVNIKNSDG-ENLLHLYLesnkidlkiLKLLIDKgv 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  226 -------VALYLEHGADVGLRTSQGETALNTACAgaegpgscRRHQAAARRLLEAGADARAAGRKRHTPLHNACANGCGG 298
Cdd:PHA03100 168 dinaknrVNYLLSYGVPINIKDVYGFTPLHYAVY--------NNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKE 239

                        170
                 ....*....|....
gi 24586688  299 LAELLLRYGARAEV 312
Cdd:PHA03100 240 IFKLLLNNGPSIKT 253
Ank_5 pfam13857
Ankyrin repeats (many copies);
195-250 5.84e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.71  E-value: 5.84e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 24586688   195 LLEAGATVNLAAGESQETPLHVAAARGLEQHVALYLEHGADVGLRTSQGETALNTA 250
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
 408-447 8.79e-04

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: 37.50  E-value: 8.79e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|...
gi 24586688 408 PRQLQHLARLAVRARLG-SRCRQGAT--RLPLPPLLRDYLLLR 447
Cdd:cd03731   3 PRPLKHLCRLKIRKLMGlQKLQQPSSmkKLPLPPALKRYILYK 45
SOCS_ASB8 cd03727
SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a ...
 407-447 1.15e-03

SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. Human ASB8 is highly transcribed in skeletal muscle and in lung carcinoma cell lines. 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: 239697  Cd Length: 43  Bit Score: 36.74  E-value: 1.15e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|..
gi 24586688 407 QPRQLQHLARLAVRARLGSRCRQGA-TRLPLPPLLRDYLLLR 447
Cdd:cd03727   2 APGTLKALARYAVRRSLGVQYLPEAvKQLPLPRSVKEYLLLL 43
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 192-250 1.46e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 41.04  E-value: 1.46e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 24586688  192 AKLLLEAGATVNLAAGESQeTPLHVAAARGLEQHVALYLEHGADVGLRTSQGETALNTA 250
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGR-TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
SOCS smart00253
suppressors of cytokine signalling; suppressors of cytokine signalling
 407-445 1.49e-03

suppressors of cytokine signalling; suppressors of cytokine signalling


Pssm-ID: 128549  Cd Length: 43  Bit Score: 36.12  E-value: 1.49e-03
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 24586688    407 QPRQLQHLARLAVRARLGsrcRQGATRLPLPPLLRDYLL 445
Cdd:smart00253   6 NVPSLQHLCRFTIRRCTR---TDQIKTLPLPPKLKDYLS 41
PHA02798 PHA02798
ankyrin-like protein; Provisional
 156-247 2.13e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 40.20  E-value: 2.13e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  156 FDCVRLLLTFGAKANVLTEEGTTPlhLCTI-------PESLQCAKLLLEAGATVNlAAGESQETPLHVAAARGL---EQH 225
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTP--LCTIlsnikdyKHMLDIVKILIENGADIN-KKNSDGETPLYCLLSNGYinnLEI 127

                         90       100
                 ....*....|....*....|..
gi 24586688  226 VALYLEHGADVGLRTSQGETAL 247
Cdd:PHA02798 128 LLFMIENGADTTLLDKDGFTML 149
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 286-324 2.57e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 40.27  E-value: 2.57e-03
                         10        20        30
                 ....*....|....*....|....*....|....*....
gi 24586688  286 TPLHNACANGCGGLAELLLRYGARAEVPNGAGHTPMDCA 324
Cdd:PTZ00322 117 TPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 114-197 3.49e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 39.59  E-value: 3.49e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688  114 PLAIATARGYTDCARHLIRQGAELD--ARVGGRAALHEACARAQFDCVRLLLTFGAKANVLT----EEGTT---PLHLCT 184
Cdd:PHA02875 171 PLIIAMAKGDIAICKMLLDSGANIDyfGKNGCVAALCYAIENNKIDIVRLFIKRGADCNIMFmiegEECTIldmICNMCT 250

                         90
                 ....*....|...
gi 24586688  185 IPESLQCAKLLLE 197
Cdd:PHA02875 251 NLESEAIDALIAD 263
SOCS_ASB7 cd03726
SOCS (suppressors of cytokine signaling) box of ASB7-like proteins. ASB family members have a ...
 407-444 3.75e-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: 35.21  E-value: 3.75e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 24586688 407 QPRQLQHLARLAVRARLGSRCRQGATRLPLPPLLRDYL 444
Cdd:cd03726   2 QPRTLQDLCRIKIRHCIGLQNLKLLDELPIAKVMKDYL 39
Ank_4 pfam13637
Ankyrin repeats (many copies);
212-253 3.80e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 35.33  E-value: 3.80e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 24586688   212 TPLHVAAARGLEQHVALYLEHGADVGLRTSQGETALNTACAG 253
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASN 44
Ank_2 pfam12796
Ankyrin repeats (3 copies);
263-352 4.05e-03

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 36.63  E-value: 4.05e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 24586688   263 HQAA-------ARRLLEAGADARAAGRKRHTPLHNACANGCGGLAELLLRYGARAEVPNgaGHTPMDCAlqAVQDSPNwe 335
Cdd:pfam12796   2 HLAAkngnlelVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYA--ARSGHLE-- 75

                          90
                  ....*....|....*..
gi 24586688   336 pevLFAALLDYGAQPVR 352
Cdd:pfam12796  76 ---IVKLLLEKGADINV 89
Ank_5 pfam13857
Ankyrin repeats (many copies);
283-324 5.10e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 5.10e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 24586688   283 KRHTPLHNACANGCGGLAELLLRYGARAEVPNGAGHTPMDCA 324
Cdd:pfam13857  15 EGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SOCS_ASB13 cd03729
SOCS (suppressors of cytokine signaling) box of ASB13-like proteins. ASB family members have a ...
 408-447 7.67e-03

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: 34.38  E-value: 7.67e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 24586688 408 PRQLQHLARLAVRARLGSRCRQGATRLPLPPLLRDYLLLR 447
Cdd:cd03729   3 PLSLQQLCRINLRKALGTRALEKIAKLNIPNRIIDYLSYN 42
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 175-204 8.97e-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: 33.80  E-value: 8.97e-03
                          10        20        30
                  ....*....|....*....|....*....|.
gi 24586688   175 EGTTPLHL-CTIPESLQCAKLLLEAGATVNL 204
Cdd:pfam00023   1 DGNTPLHLaAGRRGNLEIVKLLLSKGADVNA 31
Ank_5 pfam13857
Ankyrin repeats (many copies);
146-183 9.50e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 34.24  E-value: 9.50e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 24586688   146 ALHEACARAQFDCVRLLLTFGAKANVLTEEGTTPLHLC 183
Cdd:pfam13857  19 PLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

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