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Conserved domains on  [gi|22507369|ref|NP_683755|]
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ankyrin repeat and SOCS box protein 16 [Mus musculus]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
108-327 7.20e-36

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.93  E-value: 7.20e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369 108 KTKQTAPLTIAVARGYTDCARHLILQGAELDAR-IGGRAALHEACAQAHPDCVRLLLTFGAKANVSSEEGMTPLHLCTSP 186
Cdd:COG0666  51 DALGALLLLAAALAGDLLVALLLLAAGADINAKdDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369 187 ESLQCAKLLLEAGASVNVASQESEvTPLHVAAARGLEQHVALYLQNGADVALRTSQGETALNAACagaegpgsSRQHEAA 266
Cdd:COG0666 131 GNLEIVKLLLEAGADVNAQDNDGN-TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA--------ENGHLEI 201
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22507369 267 ARQLLEAGADPQAAGRKRHTPLHNACANGCGGLAELLLRHGASPGVTNGAGHTPMDCALQA 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 ...
406-446 4.89e-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: 60.20  E-value: 4.89e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 22507369 406 NQPRQLQHLARLAVRAQLGSHCRQAAAQLPLPPLLRDYLLL 446
Cdd:cd03716   1 STPRSLQHLCRLAIRRCLGRRRLELIKKLPLPPRLKDYLLY 41
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
108-327 7.20e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.93  E-value: 7.20e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369 108 KTKQTAPLTIAVARGYTDCARHLILQGAELDAR-IGGRAALHEACAQAHPDCVRLLLTFGAKANVSSEEGMTPLHLCTSP 186
Cdd:COG0666  51 DALGALLLLAAALAGDLLVALLLLAAGADINAKdDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369 187 ESLQCAKLLLEAGASVNVASQESEvTPLHVAAARGLEQHVALYLQNGADVALRTSQGETALNAACagaegpgsSRQHEAA 266
Cdd:COG0666 131 GNLEIVKLLLEAGADVNAQDNDGN-TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA--------ENGHLEI 201
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22507369 267 ARQLLEAGADPQAAGRKRHTPLHNACANGCGGLAELLLRHGASPGVTNGAGHTPMDCALQA 327
Cdd:COG0666 202 VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAA 262
Ank_2 pfam12796
Ankyrin repeats (3 copies);
147-236 2.11e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.30  E-value: 2.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369   147 LHEACAQAHPDCVRLLLTFGAKANVSSEEGMTPLHLCTSPESLQCAKLLLEagaSVNVASQESEVTPLHVAAARGLEQHV 226
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|
gi 22507369   227 ALYLQNGADV 236
Cdd:pfam12796  78 KLLLEKGADI 87
PHA03095 PHA03095
ankyrin-like protein; Provisional
123-320 3.22e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.37  E-value: 3.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  123 YTDCARHLILQGAELDAR-IGGRAALH-EACAQAHPDCVRLLLTFGAKANVSSEEGMTPLHLCTSPESLQ--CAKLLLEA 198
Cdd:PHA03095  62 VKDIVRLLLEAGADVNAPeRCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRK 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  199 GASVNvASQESEVTPLHVAaargLEQH------VALYLQNGADVALRTSQGETALNAACAgaegpgSSRQHEAAARQLLE 272
Cdd:PHA03095 142 GADVN-ALDLYGMTPLAVL----LKSRnanvelLRLLIDAGADVYAVDDRFRSLLHHHLQ------SFKPRARIVRELIR 210
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 22507369  273 AGADPQAAGRKRHTPLHNAcANGCGGLAEL---LLRHGASPGVTNGAGHTP 320
Cdd:PHA03095 211 AGCDPAATDMLGNTPLHSM-ATGSSCKRSLvlpLLIAGISINARNRYGQTP 260
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
406-446 4.89e-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: 60.20  E-value: 4.89e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 22507369 406 NQPRQLQHLARLAVRAQLGSHCRQAAAQLPLPPLLRDYLLL 446
Cdd:cd03716   1 STPRSLQHLCRLAIRRCLGRRRLELIKKLPLPPRLKDYLLY 41
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
407-445 3.93e-10

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: 54.86  E-value: 3.93e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 22507369   407 QPRQLQHLARLAVRAQLGSHCRQAAAQLPLPPLLRDYLL 445
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
122-356 4.76e-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: 52.19  E-value: 4.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369 122 GYTDCARHLILQGAELDARIGgRAALHEACAQAHP---DCVRLLLTFGAKANVSSE-----------EGMTPLHLCTSPE 187
Cdd:cd21882   6 GLLECLRWYLTDSAYQRGATG-KTCLHKAALNLNDgvnEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENR 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369 188 SLQCAKLLLEAGASVNVAS-----QESEVT-------PLHVAAARGLEQHVALYLQNGADVA---LRTSQGETALNAAca 252
Cdd:cd21882  85 NLNLVRLLVENGADVSARAtgrffRKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQPAaleAQDSLGNTVLHAL-- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369 253 gAEGPGSSRQHEAAARQ----LLEAGA--DP-----QAAGRKRHTPLHNACANG-CGGLAELLLRHGASPGVTNGAGHT- 319
Cdd:cd21882 163 -VLQADNTPENSAFVCQmynlLLSYGAhlDPtqqleEIPNHQGLTPLKLAAVEGkIVMFQHILQREFSGPYQPLSRKFTe 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 22507369 320 ----PMDCALQAVQDAPNWEPEVLFAALLDYGAQPVHPEML 356
Cdd:cd21882 242 wtygPVTSSLYDLSEIDSWEKNSVLELIAFSKKREARHQML 282
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
143-250 1.13e-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: 50.85  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369   143 GRAALH----------EACA----QAHPDCVRLLLtfgAKANVSSEE--GMTPLHLCTSPESLQCAKLLLEAGASVNVA- 205
Cdd:TIGR00870  82 GDTLLHaisleyvdavEAILlhllAAFRKSGPLEL---ANDQYTSEFtpGITALHLAAHRQNYEIVKLLLERGASVPARa 158
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 22507369   206 -------SQESEV-----TPLHVAAARGLEQHVALYLQNGADVALRTSQGETALNAA 250
Cdd:TIGR00870 159 cgdffvkSQGVDSfyhgeSPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLL 215
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
409-446 6.66e-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: 42.78  E-value: 6.66e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 22507369    409 RQLQHLARLAVRAQLGshcrqAAAQLPLPPLLRDYLLL 446
Cdd:smart00969   1 RSLQHLCRLAIRRSLG-----GIDKLPLPPRLKDYLLY 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
143-171 5.52e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 5.52e-03
                           10        20
                   ....*....|....*....|....*....
gi 22507369    143 GRAALHEACAQAHPDCVRLLLTFGAKANV 171
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
108-327 7.20e-36

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.93  E-value: 7.20e-36
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369 108 KTKQTAPLTIAVARGYTDCARHLILQGAELDAR-IGGRAALHEACAQAHPDCVRLLLTFGAKANVSSEEGMTPLHLCTSP 186
Cdd:COG0666  51 DALGALLLLAAALAGDLLVALLLLAAGADINAKdDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYN 130
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369 187 ESLQCAKLLLEAGASVNVASQESEvTPLHVAAARGLEQHVALYLQNGADVALRTSQGETALNAACagaegpgsSRQHEAA 266
Cdd:COG0666 131 GNLEIVKLLLEAGADVNAQDNDGN-TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAA--------ENGHLEI 201
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22507369 267 ARQLLEAGADPQAAGRKRHTPLHNACANGCGGLAELLLRHGASPGVTNGAGHTPMDCALQA 327
Cdd:COG0666 202 VKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAA 262
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
127-326 1.00e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 122.76  E-value: 1.00e-31
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369 127 ARHLILQGAELDARIGGRAALHEACAQAHPDCVRLLLTFGAKANVSSEEGMTPLHLCTSPESLQCAKLLLEAGASVNVAS 206
Cdd:COG0666  38 LLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD 117
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369 207 QESEvTPLHVAAARGLEQHVALYLQNGADVALRTSQGETALNAACAgaegpgssRQHEAAARQLLEAGADPQAAGRKRHT 286
Cdd:COG0666 118 KDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA--------NGNLEIVKLLLEAGADVNARDNDGET 188
                       170       180       190       200
                ....*....|....*....|....*....|....*....|
gi 22507369 287 PLHNACANGCGGLAELLLRHGASPGVTNGAGHTPMDCALQ 326
Cdd:COG0666 189 PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
130-350 1.39e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 103.11  E-value: 1.39e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369 130 LILQGAELDARIGGRAALHEACAQAHPDCVRLLLTFGAKANVSSEEGMTPLHLCTSPESLQCAKLLLEAGASVNVASQES 209
Cdd:COG0666   7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369 210 EVTPLHVAAARGLEQHVALYLQNGADVALRTSQGETALNAACAgaegpgssRQHEAAARQLLEAGADPQAAGRKRHTPLH 289
Cdd:COG0666  87 GNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAY--------NGNLEIVKLLLEAGADVNAQDNDGNTPLH 158
                       170       180       190       200       210       220
                ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 22507369 290 NACANGCGGLAELLLRHGASPGVTNGAGHTPMDCALQavqdapNWEPEVLfAALLDYGAQP 350
Cdd:COG0666 159 LAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE------NGHLEIV-KLLLEAGADV 212
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
58-288 1.91e-24

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 102.72  E-value: 1.91e-24
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  58 DPAVHNALFSGDLQQLQILFQDEDAANMIVETVSNQLAWSA------------EQGFWVLTPKTKQTAPLTIAVARGYTD 125
Cdd:COG0666  55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAArngdleivklllEAGADVNARDKDGETPLHLAAYNGNLE 134
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369 126 CARHLILQGAELDAR-IGGRAALHEACAQAHPDCVRLLLTFGAKANVSSEEGMTPLHLCTSPESLQCAKLLLEAGASVNV 204
Cdd:COG0666 135 IVKLLLEAGADVNAQdNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNA 214
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369 205 ASQESEvTPLHVAAARGLEQHVALYLQNGADVALRTSQGETALNAACAgaegpgssRQHEAAARQLLEAGADPQAAGRKR 284
Cdd:COG0666 215 KDNDGK-TALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAA--------AGAALIVKLLLLALLLLAAALLDL 285

                ....
gi 22507369 285 HTPL 288
Cdd:COG0666 286 LTLL 289
Ank_2 pfam12796
Ankyrin repeats (3 copies);
147-236 2.11e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 71.30  E-value: 2.11e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369   147 LHEACAQAHPDCVRLLLTFGAKANVSSEEGMTPLHLCTSPESLQCAKLLLEagaSVNVASQESEVTPLHVAAARGLEQHV 226
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE---HADVNLKDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|
gi 22507369   227 ALYLQNGADV 236
Cdd:pfam12796  78 KLLLEKGADI 87
PHA03095 PHA03095
ankyrin-like protein; Provisional
123-320 3.22e-15

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 77.37  E-value: 3.22e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  123 YTDCARHLILQGAELDAR-IGGRAALH-EACAQAHPDCVRLLLTFGAKANVSSEEGMTPLHLCTSPESLQ--CAKLLLEA 198
Cdd:PHA03095  62 VKDIVRLLLEAGADVNAPeRCGFTPLHlYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFNINpkVIRLLLRK 141
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  199 GASVNvASQESEVTPLHVAaargLEQH------VALYLQNGADVALRTSQGETALNAACAgaegpgSSRQHEAAARQLLE 272
Cdd:PHA03095 142 GADVN-ALDLYGMTPLAVL----LKSRnanvelLRLLIDAGADVYAVDDRFRSLLHHHLQ------SFKPRARIVRELIR 210
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 22507369  273 AGADPQAAGRKRHTPLHNAcANGCGGLAEL---LLRHGASPGVTNGAGHTP 320
Cdd:PHA03095 211 AGCDPAATDMLGNTPLHSM-ATGSSCKRSLvlpLLIAGISINARNRYGQTP 260
Ank_2 pfam12796
Ankyrin repeats (3 copies);
115-204 5.96e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.14  E-value: 5.96e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369   115 LTIAVARGYTDCARHLILQGAELDARIG-GRAALHEACAQAHPDCVRLLLTFGAKANVssEEGMTPLHLCTSPESLQCAK 193
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKnGRTALHLAAKNGHLEIVKLLLEHADVNLK--DNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|.
gi 22507369   194 LLLEAGASVNV 204
Cdd:pfam12796  79 LLLEKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
147-332 3.81e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 73.84  E-value: 3.81e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  147 LHEACAQAHPDCVRLLLTFGAKANVSSEEGMTPLHLCTSPESLQCAKLLLEAGASVNVASQESEvTPLHVAAARGLEQHV 226
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGE-SPLHNAAEYGDYACI 206
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  227 ALYLQNGADVALRTSQGETALNAACAgaegpgssrqHEAAARQLLEAGADPQAAGRKRHTPLHNACANGCG-GLAELLLR 305
Cdd:PHA02874 207 KLLIDHGNHIMNKCKNGFTPLHNAII----------HNRSAIELLINNASINDQDIDGSTPLHHAINPPCDiDIIDILLY 276
                        170       180
                 ....*....|....*....|....*..
gi 22507369  306 HGASPGVTNGAGHTPMDCALQAVQDAP 332
Cdd:PHA02874 277 HKADISIKDNKGENPIDTAFKYINKDP 303
PHA03095 PHA03095
ankyrin-like protein; Provisional
159-325 1.43e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.36  E-value: 1.43e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  159 VRLLLTFGAKANVSSEEGMTPLHLCTSPESLQCAK---LLLEAGASVNVASQeSEVTPLHvaaargleqhvaLYLQNGAD 235
Cdd:PHA03095  30 VRRLLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDivrLLLEAGADVNAPER-CGFTPLH------------LYLYNATT 96
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  236 VALrtsqgetalnaacagaegpgssrqheaaARQLLEAGADPQAAGRKRHTPLHNACANGC--GGLAELLLRHGASPGVT 313
Cdd:PHA03095  97 LDV----------------------------IKLLIKAGADVNAKDKVGRTPLHVYLSGFNinPKVIRLLLRKGADVNAL 148
                        170
                 ....*....|..
gi 22507369  314 NGAGHTPMDCAL 325
Cdd:PHA03095 149 DLYGMTPLAVLL 160
PHA02876 PHA02876
ankyrin repeat protein; Provisional
99-349 5.13e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 71.25  E-value: 5.13e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369   99 EQGFWVLTPKTKQTAPLTIAV-ARGYTDCARHLILQGAELDAR-IGGRAALHEACAQAH-PDCVRLLLTFGAKANVSSEE 175
Cdd:PHA02876 261 DAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKnIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRL 340
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  176 GMTPLHLCTSPESLQCAKL-LLEAGASVNvASQESEVTPLHVAAARGLEQHVALYLQNGADVALRTSQGETALNAACAGA 254
Cdd:PHA02876 341 YITPLHQASTLDRNKDIVItLLELGANVN-ARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGT 419
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  255 EgPGSSrqheaaARQLLEAGADPQAAGRKRHTPLHNACANGCG-GLAELLLRHGASPGVTNGAGHTPMDCALqavqdapn 333
Cdd:PHA02876 420 N-PYMS------VKTLIDRGANVNSKNKDLSTPLHYACKKNCKlDVIEMLLDNGADVNAINIQNQYPLLIAL-------- 484
                        250
                 ....*....|....*.
gi 22507369  334 wEPEVLFAALLDYGAQ 349
Cdd:PHA02876 485 -EYHGIVNILLHYGAE 499
PHA02875 PHA02875
ankyrin repeat protein; Provisional
113-322 4.85e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 67.32  E-value: 4.85e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  113 APLTIAVARGYTDCARHLILQGAELDARIGG-RAALHEACAQAHPDCVRLLLTFGAKAN-VSSEEGMTPLHLCTSPESLQ 190
Cdd:PHA02875  37 SPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDiESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLD 116
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  191 CAKLLLEAGASVNVASQEsEVTPLHVAAARGLEQHVALYLQNGADVALRTSQGETALNAACagaegpgsSRQHEAAARQL 270
Cdd:PHA02875 117 IMKLLIARGADPDIPNTD-KFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAM--------AKGDIAICKML 187
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 22507369  271 LEAGADPQAAGRKRH-TPLHNACANGCGGLAELLLRHGASPGVT---NGAGHTPMD 322
Cdd:PHA02875 188 LDSGANIDYFGKNGCvAALCYAIENNKIDIVRLFIKRGADCNIMfmiEGEECTILD 243
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
406-446 4.89e-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: 60.20  E-value: 4.89e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 22507369 406 NQPRQLQHLARLAVRAQLGSHCRQAAAQLPLPPLLRDYLLL 446
Cdd:cd03716   1 STPRSLQHLCRLAIRRCLGRRRLELIKKLPLPPRLKDYLLY 41
Ank_2 pfam12796
Ankyrin repeats (3 copies);
214-314 6.59e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.29  E-value: 6.59e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369   214 LHVAAARGLEQHVALYLQNGADVALRTSQGETALNAACagaegpgsSRQHEAAARQLLE-AGADPQAAGRkrhTPLHNAC 292
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAA--------KNGHLEIVKLLLEhADVNLKDNGR---TALHYAA 69
                          90       100
                  ....*....|....*....|..
gi 22507369   293 ANGCGGLAELLLRHGASPGVTN 314
Cdd:pfam12796  70 RSGHLEIVKLLLEKGADINVKD 91
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
407-446 6.80e-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: 59.79  E-value: 6.80e-12
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 22507369 407 QPRQLQHLARLAVRAQLGSHCRQAAAQLPLPPLLRDYLLL 446
Cdd:cd03587   1 NPRSLQHLCRLAIRRCLGKRRLDLIDKLPLPPRLKDYLLY 40
PHA03095 PHA03095
ankyrin-like protein; Provisional
130-325 2.78e-11

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 65.43  E-value: 2.78e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  130 LILQGAELDARIG-GRAALHeACAQ---AHPDCVRLLLTFGAKANVSSEEGMTPLHLCT-----SPESLqcaKLLLEAGA 200
Cdd:PHA03095 103 LIKAGADVNAKDKvGRTPLH-VYLSgfnINPKVIRLLLRKGADVNALDLYGMTPLAVLLksrnaNVELL---RLLIDAGA 178
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  201 SVnVASQESEVTPLHVAA--ARGLEQHVALYLQNGADVALRTSQGETALNAACAGaegpgsSRQHEAAARQLLEAGADPQ 278
Cdd:PHA03095 179 DV-YAVDDRFRSLLHHHLqsFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATG------SSCKRSLVLPLLIAGISIN 251
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 22507369  279 AAGRKRHTPLHNACANGCGGLAELLLRHGASPGVTNGAGHTPMDCAL 325
Cdd:PHA03095 252 ARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMV 298
PHA02878 PHA02878
ankyrin repeat protein; Provisional
124-323 4.83e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 64.52  E-value: 4.83e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  124 TDCARHLILQGAELDA--RIGGRAALHEACAQAHPDCVRLLLTFGAKANVSSEEGMTPLHLCTSPESLQCAKLLLEAGAS 201
Cdd:PHA02878 147 AEITKLLLSYGADINMkdRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAS 226
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  202 VNVASQESEvTPLHVAAARGLEQHV-ALYLQNGADVALRTS-QGETALNaacagaegpgSSRQHEAAARQLLEAGADPQA 279
Cdd:PHA02878 227 TDARDKCGN-TPLHISVGYCKDYDIlKLLLEHGVDVNAKSYiLGLTALH----------SSIKSERKLKLLLEYGADINS 295
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 22507369  280 AGRKRHTPLHNA-----CANGCGGL-AELLLRHGASPGVTNGAGHTP-MDC 323
Cdd:PHA02878 296 LNSYKLTPLSSAvkqylCINIGRILiSNICLLKRIKPDIKNSEGFIDnMDC 346
PHA02878 PHA02878
ankyrin repeat protein; Provisional
159-325 1.24e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 63.36  E-value: 1.24e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  159 VRLLLTFGAKANVSSEE-GMTPLHLCTSPESLQCAKLLLEAGASVNVASQESEvTPLHVAAARGLEQHVALYLQNGADVA 237
Cdd:PHA02878 150 TKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVNIPDKTNN-SPLHHAVKHYNKPIVHILLENGASTD 228
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  238 LRTSQGETALNAACagaegpGSSRQHEAAaRQLLEAGADPQAAGRKRH-TPLHNACANGcgGLAELLLRHGASPGVTNGA 316
Cdd:PHA02878 229 ARDKCGNTPLHISV------GYCKDYDIL-KLLLEHGVDVNAKSYILGlTALHSSIKSE--RKLKLLLEYGADINSLNSY 299

                 ....*....
gi 22507369  317 GHTPMDCAL 325
Cdd:PHA02878 300 KLTPLSSAV 308
PHA02875 PHA02875
ankyrin repeat protein; Provisional
144-350 1.26e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.09  E-value: 1.26e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  144 RAALHEACAQAHPDCVRLLLTFGAKANVSSEEGMTPLHLCTSPESLQCAKLLLEAGASVNVASQESEvTPLHVAAARGLE 223
Cdd:PHA02875   3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIE-SELHDAVEEGDV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  224 QHVALYLQNGA---DVALRtsQGETALNAAcagaegpgSSRQHEAAARQLLEAGADPQAAGRKRHTPLHNACANGCGGLA 300
Cdd:PHA02875  82 KAVEELLDLGKfadDVFYK--DGMTPLHLA--------TILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGI 151
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 22507369  301 ELLLRHGASPGVTNGAGHTPMDCALQAVQDApnwepevLFAALLDYGAQP 350
Cdd:PHA02875 152 ELLIDHKACLDIEDCCGCTPLIIAMAKGDIA-------ICKMLLDSGANI 194
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
406-452 2.20e-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: 55.91  E-value: 2.20e-10
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*..
gi 22507369 406 NQPRQLQHLARLAVRAQLGSHCRQAAAQLPLPPLLRDYLLLGVEGRI 452
Cdd:cd03723   1 GTPRSLQHLCRCAIRKLLGSRCHKLVPQLSLPTSLKNYLLLEPEGVL 47
PHA02876 PHA02876
ankyrin repeat protein; Provisional
127-349 3.52e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.00  E-value: 3.52e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  127 ARHLILQGAELDAR-IGGRAALHEACAQAHPDCVRLLLTFGAKANVSSEEGMTPLHLCT--------------------- 184
Cdd:PHA02876 161 AEMLLEGGADVNAKdIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVdsknidtikaiidnrsninkn 240
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  185 --------SPESLQCAKLLLEAGASVNvASQESEVTPLHVAA-ARGLEQHVALYLQNGADVALRTSQGETALNAACAGae 255
Cdd:PHA02876 241 dlsllkaiRNEDLETSLLLYDAGFSVN-SIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPLYLMAKN-- 317
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  256 gpGSSRQHeaaARQLLEAGADPQAAGRKRHTPLHNACA-NGCGGLAELLLRHGASPGVTNGAGHTPMDCAlqAVQDAPnw 334
Cdd:PHA02876 318 --GYDTEN---IRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYA--AVRNNV-- 388
                        250
                 ....*....|....*
gi 22507369  335 epeVLFAALLDYGAQ 349
Cdd:PHA02876 389 ---VIINTLLDYGAD 400
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
407-445 3.93e-10

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: 54.86  E-value: 3.93e-10
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 22507369   407 QPRQLQHLARLAVRAQLGSHCRQAAAQLPLPPLLRDYLL 445
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
PHA03100 PHA03100
ankyrin repeat protein; Provisional
147-320 4.70e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 58.14  E-value: 4.70e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  147 LHEACAQAHPDCVRLLLTFGAKANVSSEEGMTPLHLCT-----SPESLQCAKLLLEAGASVNVASQESeVTPLHVAAARG 221
Cdd:PHA03100  39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSnikynLTDVKEIVKLLLEYGANVNAPDNNG-ITPLLYAISKK 117
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  222 LEQH--VALYLQNGADVALRTSQGETALNAACAgaegpgSSRQHEAAARQLLEAGADPQAAGR----------------K 283
Cdd:PHA03100 118 SNSYsiVEYLLDNGANVNIKNSDGENLLHLYLE------SNKIDLKILKLLIDKGVDINAKNRvnyllsygvpinikdvY 191
                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 22507369  284 RHTPLHNACANGCGGLAELLLRHGASPGVTNGAGHTP 320
Cdd:PHA03100 192 GFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTP 228
PHA03100 PHA03100
ankyrin repeat protein; Provisional
156-309 1.50e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 56.60  E-value: 1.50e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  156 PDCVRLLLTFGAKANVSSEEGMTPLHLC--TSPESLQCAKLLLEAGASVNVASQESEvTPLHVAA---------ARGLEQ 224
Cdd:PHA03100  86 KEIVKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGE-NLLHLYLesnkidlkiLKLLID 164
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  225 H---------VALYLQNGADVALRTSQGETALNAACagaegpgsSRQHEAAARQLLEAGADPQAAGRKRHTPLHNACANG 295
Cdd:PHA03100 165 KgvdinaknrVNYLLSYGVPINIKDVYGFTPLHYAV--------YNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNN 236
                        170
                 ....*....|....
gi 22507369  296 CGGLAELLLRHGAS 309
Cdd:PHA03100 237 NKEIFKLLLNNGPS 250
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
267-324 4.86e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 4.86e-08
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 22507369  267 ARQLLEAGADPQAAGRKRHTPLHNACANGCGGLAELLLRHGASPGVTNGAGHTPMDCA 324
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
Ank_2 pfam12796
Ankyrin repeats (3 copies);
114-171 4.87e-08

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 50.50  E-value: 4.87e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 22507369   114 PLTIAVARGYTDCARHLiLQGAELDARIGGRAALHEACAQAHPDCVRLLLTFGAKANV 171
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLL-LEHADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINV 89
PHA02874 PHA02874
ankyrin repeat protein; Provisional
109-326 7.76e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 54.20  E-value: 7.76e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  109 TKQTAPLTIAVARGYTDCARHLILQGAEldariggRAALHEACAQAhpDCVRLLLTFGAKANVSSEEGMTPLHLCTSPES 188
Cdd:PHA02874  66 TKIPHPLLTAIKIGAHDIIKLLIDNGVD-------TSILPIPCIEK--DMIKTILDCGIDVNIKDAELKTFLHYAIKKGD 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  189 LQCAKLLLEAGASVNVaSQESEVTPLHVAAARGLEQHVALYLQNGADVALRTSQGETAL-NAACAGaegpgssrqHEAAA 267
Cdd:PHA02874 137 LESIKMLFEYGADVNI-EDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLhNAAEYG---------DYACI 206
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 22507369  268 RQLLEAGADPQAAGRKRHTPLHNACANGCGGLAelLLRHGASPGVTNGAGHTPMDCALQ 326
Cdd:PHA02874 207 KLLIDHGNHIMNKCKNGFTPLHNAIIHNRSAIE--LLINNASINDQDIDGSTPLHHAIN 263
PHA03100 PHA03100
ankyrin repeat protein; Provisional
159-236 1.51e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 53.52  E-value: 1.51e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22507369  159 VRLLLTFGAKANVSSEEGMTPLHLCTSPESLQCAKLLLEAGASVNVASqESEVTPLHVAAARGLEQHVALYLQNGADV 236
Cdd:PHA03100 175 VNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVN-KYGDTPLHIAILNNNKEIFKLLLNNGPSI 251
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
195-309 1.58e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 53.72  E-value: 1.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  195 LLEAGASVNVASQESEvTPLHVAAARGLEQHVALYLQNGADVALRTSQGETALNAA--------------CAGAEGP--- 257
Cdd:PLN03192 544 LLKAKLDPDIGDSKGR-TPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAisakhhkifrilyhFASISDPhaa 622
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 22507369  258 ------GSSRQHEAAARQLLEAGADPQAAGRKRHTPLHNACANGCGGLAELLLRHGAS 309
Cdd:PLN03192 623 gdllctAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
Ank_4 pfam13637
Ankyrin repeats (many copies);
143-196 2.97e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.88  E-value: 2.97e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 22507369   143 GRAALHEACAQAHPDCVRLLLTFGAKANVSSEEGMTPLHLCTSPESLQCAKLLL 196
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
218-306 4.58e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.21  E-value: 4.58e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  218 AARGLEQHVALYLQNGADVALRTSQGETALNAACAGAegpgssrqHEAAARQLLEAGADPQAAGRKRHTPLHNACANGCG 297
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANG--------HVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFR 161

                 ....*....
gi 22507369  298 GLAELLLRH 306
Cdd:PTZ00322 162 EVVQLLSRH 170
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
122-356 4.76e-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: 52.19  E-value: 4.76e-07
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369 122 GYTDCARHLILQGAELDARIGgRAALHEACAQAHP---DCVRLLLTFGAKANVSSE-----------EGMTPLHLCTSPE 187
Cdd:cd21882   6 GLLECLRWYLTDSAYQRGATG-KTCLHKAALNLNDgvnEAIMLLLEAAPDSGNPKElvnapctdefyQGQTALHIAIENR 84
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369 188 SLQCAKLLLEAGASVNVAS-----QESEVT-------PLHVAAARGLEQHVALYLQNGADVA---LRTSQGETALNAAca 252
Cdd:cd21882  85 NLNLVRLLVENGADVSARAtgrffRKSPGNlfyfgelPLSLAACTNQEEIVRLLLENGAQPAaleAQDSLGNTVLHAL-- 162
                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369 253 gAEGPGSSRQHEAAARQ----LLEAGA--DP-----QAAGRKRHTPLHNACANG-CGGLAELLLRHGASPGVTNGAGHT- 319
Cdd:cd21882 163 -VLQADNTPENSAFVCQmynlLLSYGAhlDPtqqleEIPNHQGLTPLKLAAVEGkIVMFQHILQREFSGPYQPLSRKFTe 241
                       250       260       270       280
                ....*....|....*....|....*....|....*....|.
gi 22507369 320 ----PMDCALQAVQDAPNWEPEVLFAALLDYGAQPVHPEML 356
Cdd:cd21882 242 wtygPVTSSLYDLSEIDSWEKNSVLELIAFSKKREARHQML 282
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
143-250 1.13e-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: 50.85  E-value: 1.13e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369   143 GRAALH----------EACA----QAHPDCVRLLLtfgAKANVSSEE--GMTPLHLCTSPESLQCAKLLLEAGASVNVA- 205
Cdd:TIGR00870  82 GDTLLHaisleyvdavEAILlhllAAFRKSGPLEL---ANDQYTSEFtpGITALHLAAHRQNYEIVKLLLERGASVPARa 158
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 22507369   206 -------SQESEV-----TPLHVAAARGLEQHVALYLQNGADVALRTSQGETALNAA 250
Cdd:TIGR00870 159 cgdffvkSQGVDSfyhgeSPLNAAACLGSPSIVALLSEDPADILTADSLGNTLLHLL 215
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
109-236 1.49e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.64  E-value: 1.49e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  109 TKQTAPLTIAVARGYTDCARHLILQGAELDAR-IGGRAALHEACAQAHPDCVRLLLTFGAKANVSSEEGMtplhLCTSPE 187
Cdd:PLN03192 556 SKGRTPLHIAASKGYEDCVLVLLKHACNVHIRdANGNTALWNAISAKHHKIFRILYHFASISDPHAAGDL----LCTAAK 631
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|..
gi 22507369  188 --SLQCAKLLLEAGasVNVASQESE-VTPLHVAAARGLEQHVALYLQNGADV 236
Cdd:PLN03192 632 rnDLTAMKELLKQG--LNVDSEDHQgATALQVAMAEDHVDMVRLLIMNGADV 681
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
176-289 4.19e-06

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 49.24  E-value: 4.19e-06
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369 176 GMTPLHLCTSPESLQCAKLLLEAGAS-VNVA--SQESE-VTPLHVAAARGLEQHVALYLQNGADVA--------LRTSQ- 242
Cdd:cd22192  51 GETALHVAALYDNLEAAVVLMEAAPElVNEPmtSDLYQgETALHIAVVNQNLNLVRELIARGADVVspratgtfFRPGPk 130
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|...
gi 22507369 243 -----GETALN-AACAGaegpgssrqHEAAARQLLEAGADPQAAGRKRHTPLH 289
Cdd:cd22192 131 nliyyGEHPLSfAACVG---------NEEIVRLLIEHGADIRAQDSLGNTVLH 174
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
409-446 6.66e-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: 42.78  E-value: 6.66e-06
                           10        20        30
                   ....*....|....*....|....*....|....*...
gi 22507369    409 RQLQHLARLAVRAQLGshcrqAAAQLPLPPLLRDYLLL 446
Cdd:smart00969   1 RSLQHLCRLAIRRSLG-----GIDKLPLPPRLKDYLLY 33
PHA02875 PHA02875
ankyrin repeat protein; Provisional
110-251 6.67e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.06  E-value: 6.67e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  110 KQTAPLTIAVARGYTDCARHLILQGAELDARIGGR-AALHEACAQAHPDCVRLLLTFGAKANVSSEEGMTPLHLCTSPES 188
Cdd:PHA02875 101 DGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKfSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGD 180
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22507369  189 LQCAKLLLEAGASVNVASQESEVTPLHVAAARGLEQHVALYLQNGADVALRTS-QGE--TALNAAC 251
Cdd:PHA02875 181 IAICKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNIMFMiEGEecTILDMIC 246
Ank_5 pfam13857
Ankyrin repeats (many copies);
270-324 7.28e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 43.10  E-value: 7.28e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 22507369   270 LLEAG-ADPQAAGRKRHTPLHNACANGCGGLAELLLRHGASPGVTNGAGHTPMDCA 324
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
120-196 8.40e-06

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 8.40e-06
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 22507369  120 ARGYTDCARHLILQGAELDAR-IGGRAALHEACAQAHPDCVRLLLTFGAKANVSSEEGMTPLHLCTSPESLQCAKLLL 196
Cdd:PTZ00322  91 ASGDAVGARILLTGGADPNCRdYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
406-445 1.05e-05

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: 42.20  E-value: 1.05e-05
                        10        20        30        40
                ....*....|....*....|....*....|....*....|
gi 22507369 406 NQPRQLQHLARLAVRAQLGshcRQAAAQLPLPPLLRDYLL 445
Cdd:cd03717   1 TSVRSLQHLCRFVIRQCTR---RDLIDQLPLPRRLKDYLK 37
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
126-255 3.18e-05

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 46.33  E-value: 3.18e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369 126 CARHLILQGAELDARIGGRAALHEACAQAHP---DCVRLLLTFGAKAN-----VSSE------EGMTPLHLCTSPESLQC 191
Cdd:cd22193  12 CRRRKDLTDSEFTESSTGKTCLMKALLNLNPgtnDTIRILLDIAEKTDnlkrfINAEytdeyyEGQTALHIAIERRQGDI 91
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369 192 AKLLLEAGASVNVASQ--------ESEV-----TPLHVAAARGLEQHVALYLQNG---ADVALRTSQGETALNAACAGAE 255
Cdd:cd22193  92 VALLVENGADVHAHAKgrffqpkyQGEGfyfgeLPLSLAACTNQPDIVQYLLENEhqpADIEAQDSRGNTVLHALVTVAD 171
Ank_2 pfam12796
Ankyrin repeats (3 copies);
263-326 3.38e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.41  E-value: 3.38e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 22507369   263 HEAAARQLLEAGADPQAAGRKRHTPLHNACANGCGGLAELLLRHGASPGVTNgaGHTPMDCALQ 326
Cdd:pfam12796   9 NLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNLKDN--GRTALHYAAR 70
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
159-230 4.93e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 4.93e-05
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 22507369  159 VRLLLTFGAKANVSSEEGMTPLHLCTSPESLQCAKLLLEAGASVNVASQESEvTPLHVAAARGLEQHVALYL 230
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK-TPLELAEENGFREVVQLLS 168
PHA02878 PHA02878
ankyrin repeat protein; Provisional
147-330 7.92e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.87  E-value: 7.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  147 LHEACAQAHPDCVRLLLTFGAKANVSSEEGMTPLHL-CTSPESLQCAKLLLEAGA-----------------SVNVAS-- 206
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIiCKEPNKLGMKEMIRSINKcsvfytlvaikdafnnrNVEIFKii 120
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  207 --------QESEVTPL-HVAAARGLEQH-VALYLQNGADVALRT-SQGETALNAAcagaegpgSSRQHEAAARQLLEAGA 275
Cdd:PHA02878 121 ltnrykniQTIDLVYIdKKSKDDIIEAEiTKLLLSYGADINMKDrHKGNTALHYA--------TENKDQRLTELLLSYGA 192
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 22507369  276 DPQAAGRKRHTPLHNACANGCGGLAELLLRHGASPGVTNGAGHTPMDCALQAVQD 330
Cdd:PHA02878 193 NVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKD 247
PHA02876 PHA02876
ankyrin repeat protein; Provisional
187-321 1.57e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.28  E-value: 1.57e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  187 ESLQCAKLLLEAGASVNvASQESEVTPLHVAAARGLEQHVALYLQNGADVALRTSQGETALNAAC---------AGAEGP 257
Cdd:PHA02876 156 DELLIAEMLLEGGADVN-AKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVdsknidtikAIIDNR 234
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 22507369  258 GSSRQHEAAARQ------------LLEAGADPQAAGRKRHTPLHNAC-ANGCGGLAELLLRHGASPGVTNGAGHTPM 321
Cdd:PHA02876 235 SNINKNDLSLLKairnedletsllLYDAGFSVNSIDDCKNTPLHHASqAPSLSRLVPKLLERGADVNAKNIKGETPL 311
PHA03100 PHA03100
ankyrin repeat protein; Provisional
130-204 1.79e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 43.50  E-value: 1.79e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 22507369  130 LILQGAELDAR-IGGRAALHEACAQAHPDCVRLLLTFGAKANVSSEEGMTPLHLCTSPESLQCAKLLLEAGASVNV 204
Cdd:PHA03100 178 LLSYGVPINIKdVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT 253
SOCS_SSB2 cd03719
SOCS (suppressors of cytokine signaling) box of SSB2 (SPRY domain-containing SOCS box proteins) ...
407-445 2.50e-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: 38.46  E-value: 2.50e-04
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 22507369 407 QPRQLQHLARLAVRAQLGSHCRQAAAQLPLPPLLRDYLL 445
Cdd:cd03719   2 EPHSLLHLSRLCVRHALGDTRLGQVSALPLPPAMKRYLL 40
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
408-445 5.21e-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: 37.89  E-value: 5.21e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 22507369 408 PRQLQHLARLAVRAQLGSH--CRQAAAQ-LPLPPLLRDYLL 445
Cdd:cd03731   3 PRPLKHLCRLKIRKLMGLQklQQPSSMKkLPLPPALKRYIL 43
SOCS_ASB8 cd03727
SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a ...
407-446 5.23e-04

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: 37.51  E-value: 5.23e-04
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 22507369 407 QPRQLQHLARLAVRAQLG-SHCRQAAAQLPLPPLLRDYLLL 446
Cdd:cd03727   2 APGTLKALARYAVRRSLGvQYLPEAVKQLPLPRSVKEYLLL 42
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
143-247 5.69e-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: 42.31  E-value: 5.69e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369 143 GRAALHEA-------CAQAHPDCVRLLLtfgaKANVSSE--EGMTPLHLCTSPESLQCAKLLLEAGASVNVAsqesEVT- 212
Cdd:cd22192  51 GETALHVAalydnleAAVVLMEAAPELV----NEPMTSDlyQGETALHIAVVNQNLNLVRELIARGADVVSP----RATg 122
                        90       100       110       120       130
                ....*....|....*....|....*....|....*....|....*....|.
gi 22507369 213 ----------------PLHVAAARGLEQHVALYLQNGADVALRTSQGETAL 247
Cdd:cd22192 123 tffrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
SOCS smart00253
suppressors of cytokine signalling; suppressors of cytokine signalling
407-445 6.28e-04

suppressors of cytokine signalling; suppressors of cytokine signalling


Pssm-ID: 128549  Cd Length: 43  Bit Score: 37.28  E-value: 6.28e-04
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 22507369    407 QPRQLQHLARLAVRAQLGSHcrqAAAQLPLPPLLRDYLL 445
Cdd:smart00253   6 NVPSLQHLCRFTIRRCTRTD---QIKTLPLPPKLKDYLS 41
SOCS_SSB1_4 cd03718
SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box ...
407-445 6.68e-04

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: 37.28  E-value: 6.68e-04
                        10        20        30
                ....*....|....*....|....*....|....*....
gi 22507369 407 QPRQLQHLARLAVRAQLGSHCRQAAAQLPLPPLLRDYLL 445
Cdd:cd03718   2 EPLPLMDLCRRRVRVALGRDRLEEIEQLPLPPSLKNYLL 40
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
175-204 8.70e-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: 8.70e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 22507369   175 EGMTPLHL-CTSPESLQCAKLLLEAGASVNV 204
Cdd:pfam00023   1 DGNTPLHLaAGRRGNLEIVKLLLSKGADVNA 31
SOCS_ASB3 cd03722
SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a ...
411-445 1.19e-03

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


Pssm-ID: 239692  Cd Length: 51  Bit Score: 36.69  E-value: 1.19e-03
                        10        20        30
                ....*....|....*....|....*....|....*...
gi 22507369 411 LQHLARLAVRAQLGS-HCRQAA--AQLPLPPLLRDYLL 445
Cdd:cd03722   6 LTHLCRLEIRSSLKSeRLRSDSfiCQLPLPRSLQDYLL 43
Ank_4 pfam13637
Ankyrin repeats (many copies);
210-253 1.61e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 1.61e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 22507369   210 EVTPLHVAAARGLEQHVALYLQNGADVALRTSQGETALNAACAG 253
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASN 44
SOCS_ASB14 cd03730
SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a ...
408-445 2.77e-03

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: 35.98  E-value: 2.77e-03
                        10        20        30        40
                ....*....|....*....|....*....|....*....|.
gi 22507369 408 PRQLQHLARLAVRAQLGS---HCRQAAAQLPLPPLLRDYLL 445
Cdd:cd03730   3 PRSLKHLCRLKIRACMGRlrlRCPVFMSFLPLPNRLKAYIL 43
Ank_5 pfam13857
Ankyrin repeats (many copies);
195-247 4.95e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 4.95e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 22507369   195 LLEAGASVNVASQESEVTPLHVAAARGLEQHVALYLQNGADVALRTSQGETAL 247
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
143-171 5.52e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.49  E-value: 5.52e-03
                           10        20
                   ....*....|....*....|....*....
gi 22507369    143 GRAALHEACAQAHPDCVRLLLTFGAKANV 171
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
408-444 5.89e-03

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: 34.84  E-value: 5.89e-03
                        10        20        30
                ....*....|....*....|....*....|....*..
gi 22507369 408 PRQLQHLARLAVRAQLGSHCRQAAAQLPLPPLLRDYL 444
Cdd:cd03721   3 PRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYL 39
PHA02884 PHA02884
ankyrin repeat protein; Provisional
157-250 6.60e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 38.43  E-value: 6.60e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  157 DCVRLLLTFGAKANV----SSEEGMTPLHLCTSPESLQCAKLLLEAGASVNVASQESEVTPLHVAAARGLEQHVALYLQN 232
Cdd:PHA02884  47 DIIDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYISVLHGCLKCLEILLSY 126
                         90
                 ....*....|....*...
gi 22507369  233 GADVALRTSQGETALNAA 250
Cdd:PHA02884 127 GADINIQTNDMVTPIELA 144
Ank_5 pfam13857
Ankyrin repeats (many copies);
146-183 7.42e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 34.63  E-value: 7.42e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 22507369   146 ALHEACAQAHPDCVRLLLTFGAKANVSSEEGMTPLHLC 183
Cdd:pfam13857  19 PLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
87-255 8.76e-03

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 38.59  E-value: 8.76e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369  87 VETVSNQLAWSAEQGFWVLTPKTKqtapLTIAVARGYTDCARHLILQGAELDARIGGRAA----LHEACAQAH------- 155
Cdd:cd22194  25 DDTPSNPNSPSAELAKEEQRDKKK----RLKKVSEAAVEELGELLKELKDLSRRRRKTDVpdflMHKLTASDTgktclmk 100
                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 22507369 156 ---------PDCVRLLLTFgAKAN------VSSE------EGMTPLHLCTSPESLQCAKLLLEAGASVNVASQESEV--- 211
Cdd:cd22194 101 allninentKEIVRILLAF-AEENgildrfINAEyteeayEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVFFnpk 179
                       170       180       190       200       210
                ....*....|....*....|....*....|....*....|....*....|....*
gi 22507369 212 ----------TPLHVAAARGLEQHVALYLQNGAD-VALRTSQGETALNAACAGAE 255
Cdd:cd22194 180 ykhegfyfgeTPLALAACTNQPEIVQLLMEKESTdITSQDSRGNTVLHALVTVAE 234
 
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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