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Conserved domains on  [gi|255982572|ref|NP_001157637|]
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GPR75-ASB3 protein [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];
54-307 6.18e-46

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 163.20  E-value: 6.18e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  54 LAAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLQMLINADsseNYIKMKTFEGFCALHLAASQGHWKIV 133
Cdd:COG0666   27 AAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAG---ADINAKDDGGNTLLHAAARNGDLEIV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 134 QILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLQHGANVNGSHSMcGWNSLHQASFQENAEIIKLLLRKGANKECQ 213
Cdd:COG0666  104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNAR 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 214 DDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGADPDLYCNEDSwqLPIHAAA 293
Cdd:COG0666  183 DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGL--TALLLAA 260
                        250
                 ....*....|....
gi 255982572 294 QMGHTKILDLLIPL 307
Cdd:COG0666  261 AAGAALIVKLLLLA 274
SOCS_ASB3 cd03722
SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a ...
495-545 1.00e-25

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: 99.48  E-value: 1.00e-25
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 255982572 495 ATVPSLTHLCRLEIRSSLKSERLRSDSYISQLPLPRSLHNYLLYEDVLRMY 545
Cdd:cd03722    1 ASVPSLTHLCRLEIRSSLKSERLRSDSFICQLPLPRSLQDYLLYSDVLRMY 51
ANKYR super family cl34000
Ankyrin repeat [Signal transduction mechanisms];
230-406 1.42e-05

Ankyrin repeat [Signal transduction mechanisms];


The actual alignment was detected with superfamily member COG0666:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 47.26  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 230 LESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGADPDLycNEDSWQLPIHAAAQMGHTKILDLLIPLTN 309
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALAL--ADALGALLLLAAALAGDLLVALLLLAAGA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 310 RACDTGLNKVSPVYSAVFGGHEDCLEILLRNGYSPDAQAclVFGFSSPVCMAFQKDCEffgIVNILLKYGAQINE----- 384
Cdd:COG0666   79 DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD--KDGETPLHLAAYNGNLE---IVKLLLEAGADVNAqdndg 153
                        170       180
                 ....*....|....*....|....*
gi 255982572 385 ---LHLAYCLKYEKfsIFRYFLRKG 406
Cdd:COG0666  154 ntpLHLAAANGNLE--IVKLLLEAG 176
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-307 6.18e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 163.20  E-value: 6.18e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  54 LAAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLQMLINADsseNYIKMKTFEGFCALHLAASQGHWKIV 133
Cdd:COG0666   27 AAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAG---ADINAKDDGGNTLLHAAARNGDLEIV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 134 QILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLQHGANVNGSHSMcGWNSLHQASFQENAEIIKLLLRKGANKECQ 213
Cdd:COG0666  104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNAR 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 214 DDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGADPDLYCNEDSwqLPIHAAA 293
Cdd:COG0666  183 DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGL--TALLLAA 260
                        250
                 ....*....|....
gi 255982572 294 QMGHTKILDLLIPL 307
Cdd:COG0666  261 AAGAALIVKLLLLA 274
SOCS_ASB3 cd03722
SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a ...
495-545 1.00e-25

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: 99.48  E-value: 1.00e-25
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 255982572 495 ATVPSLTHLCRLEIRSSLKSERLRSDSYISQLPLPRSLHNYLLYEDVLRMY 545
Cdd:cd03722    1 ASVPSLTHLCRLEIRSSLKSERLRSDSFICQLPLPRSLQDYLLYSDVLRMY 51
PHA03095 PHA03095
ankyrin-like protein; Provisional
34-279 8.89e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 101.25  E-value: 8.89e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  34 RLVKQ---MDFTEAYADTCSTVGLAAREGNVK-VLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVE-CLQMLI--NADss 106
Cdd:PHA03095  32 RLLAAgadVNFRGEYGKTPLHLYLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIkaGAD-- 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 107 enyIKMKTFEGFCALH--LAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDV--LRLLLQHGANVNGShSM 182
Cdd:PHA03095 110 ---VNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV-DD 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 183 CGWNSLHQ--ASFQENAEIIKLLLRKGANKECQDDFGITPLFVAAQYGKLESLSI--LISSGANVNCQALDKATPLFIAA 258
Cdd:PHA03095 186 RFRSLLHHhlQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAA 265
                        250       260
                 ....*....|....*....|.
gi 255982572 259 QEGHTKCVELLLSSGADPDLY 279
Cdd:PHA03095 266 VFNNPRACRRLIALGADINAV 286
Ank_2 pfam12796
Ankyrin repeats (3 copies);
121-214 7.37e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 7.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  121 LHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLQHganVNGSHSMCGWNSLHQASFQENAEII 200
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 255982572  201 KLLLRKGANKECQD 214
Cdd:pfam12796  78 KLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
80-272 4.67e-15

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: 78.13  E-value: 4.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  80 RGW-MPIHEAAYHNSVECLQMLINADSSENYIKMKTFEgfCALHLAASQGHWKIVQILLEAgaDPNATTLEET------- 151
Cdd:cd22192   15 RISeSPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGE--TALHVAALYDNLEAAVVLMEA--APELVNEPMTsdlyqge 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 152 TPLFLAVENGQIDVLRLLLQHGANVN-----------GSHSMC--GWNSLHQASFQENAEIIKLLLRKGANKECQDDFGI 218
Cdd:cd22192   91 TALHIAVVNQNLNLVRELIARGADVVspratgtffrpGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255982572 219 TPLFV-AAQYGKL---ESLSILISSGANVNCQALDKA------TPLFIAAQEGHTKCVELLLSS 272
Cdd:cd22192  171 TVLHIlVLQPNKTfacQMYDLILSYDKEDDLQPLDLVpnnqglTPFKLAAKEGNIVMFQHLVQK 234
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
496-537 7.59e-11

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


Pssm-ID: 462192  Cd Length: 39  Bit Score: 57.18  E-value: 7.59e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 255982572  496 TVPSLTHLCRLEIRSSLKSERLrsdSYISQLPLPRSLHNYLL 537
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRL---GAIDKLPLPPLLKDYLL 39
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
498-539 1.07e-08

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


Pssm-ID: 198037  Cd Length: 34  Bit Score: 50.87  E-value: 1.07e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 255982572   498 PSLTHLCRLEIRSSLKSerlrsdsyISQLPLPRSLHNYLLYE 539
Cdd:smart00969   1 RSLQHLCRLAIRRSLGG--------IDKLPLPPRLKDYLLYY 34
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
152-177 9.94e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 9.94e-06
                           10        20
                   ....*....|....*....|....*.
gi 255982572   152 TPLFLAVENGQIDVLRLLLQHGANVN 177
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
230-406 1.42e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 47.26  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 230 LESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGADPDLycNEDSWQLPIHAAAQMGHTKILDLLIPLTN 309
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALAL--ADALGALLLLAAALAGDLLVALLLLAAGA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 310 RACDTGLNKVSPVYSAVFGGHEDCLEILLRNGYSPDAQAclVFGFSSPVCMAFQKDCEffgIVNILLKYGAQINE----- 384
Cdd:COG0666   79 DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD--KDGETPLHLAAYNGNLE---IVKLLLEAGADVNAqdndg 153
                        170       180
                 ....*....|....*....|....*
gi 255982572 385 ---LHLAYCLKYEKfsIFRYFLRKG 406
Cdd:COG0666  154 ntpLHLAAANGNLE--IVKLLLEAG 176
Ank_2 pfam12796
Ankyrin repeats (3 copies);
289-383 4.30e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.41  E-value: 4.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  289 IHAAAQMGHTKILDLLIPLTNRACDTGLNKVSPVYSAVFGGHEDCLEILLRNgyspdAQACLVFGFSSPVCMAFQKDCef 368
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-----ADVNLKDNGRTALHYAARSGH-- 73
                          90
                  ....*....|....*
gi 255982572  369 FGIVNILLKYGAQIN 383
Cdd:pfam12796  74 LEIVKLLLEKGADIN 88
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
152-305 4.63e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.23  E-value: 4.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  152 TPLF-LAVENGQIDVLRLLLQHGANVNgshsmCGWNSLHQAS--FQENAE-IIKLLLRKG--------ANKECQDDF--G 217
Cdd:TIGR00870  54 SALFvAAIENENLELTELLLNLSCRGA-----VGDTLLHAISleYVDAVEaILLHLLAAFrksgplelANDQYTSEFtpG 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  218 ITPLFVAAQYGKLESLSILISSGANVNCQAldkatplfiaaqeghtKCVELLLSSGADpDLYCNEdswqLPIHAAAQMGH 297
Cdd:TIGR00870 129 ITALHLAAHRQNYEIVKLLLERGASVPARA----------------CGDFFVKSQGVD-SFYHGE----SPLNAAACLGS 187

                  ....*...
gi 255982572  298 TKILDLLI 305
Cdd:TIGR00870 188 PSIVALLS 195
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-307 6.18e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 163.20  E-value: 6.18e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  54 LAAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLQMLINADsseNYIKMKTFEGFCALHLAASQGHWKIV 133
Cdd:COG0666   27 AAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAG---ADINAKDDGGNTLLHAAARNGDLEIV 103
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 134 QILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLQHGANVNGSHSMcGWNSLHQASFQENAEIIKLLLRKGANKECQ 213
Cdd:COG0666  104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNAR 182
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 214 DDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGADPDLYCNEDSwqLPIHAAA 293
Cdd:COG0666  183 DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGL--TALLLAA 260
                        250
                 ....*....|....
gi 255982572 294 QMGHTKILDLLIPL 307
Cdd:COG0666  261 AAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-283 7.67e-46

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 162.82  E-value: 7.67e-46
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  54 LAAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLQMLINADSSENYikmKTFEGFCALHLAASQGHWKIV 133
Cdd:COG0666   60 AAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA---RDKDGETPLHLAAYNGNLEIV 136
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 134 QILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLQHGANVNGSHSMcGWNSLHQASFQENAEIIKLLLRKGANKECQ 213
Cdd:COG0666  137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAK 215
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 214 DDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGADPDLYCNED 283
Cdd:COG0666  216 DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
64-341 1.53e-45

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 162.05  E-value: 1.53e-45
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  64 LRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLQMLINADSSENYIKMKTFEGFCALHLAASQGHWKIVQILLEAGADP 143
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 144 NATTLEETTPLFLAVENGQIDVLRLLLQHGANVNgSHSMCGWNSLHQASFQENAEIIKLLLRKGANKECQDDFGITPLFV 223
Cdd:COG0666   81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN-ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 224 AAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGADPDLYCNEDSWqlPIHAAAQMGHTKILDL 303
Cdd:COG0666  160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKT--ALDLAAENGNLEIVKL 237
                        250       260       270
                 ....*....|....*....|....*....|....*...
gi 255982572 304 LIPLTNRACDTGLNKVSPVYSAVFGGHEDCLEILLRNG 341
Cdd:COG0666  238 LLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
54-254 7.59e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 146.64  E-value: 7.59e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  54 LAAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLQMLINADSSENyikMKTFEGFCALHLAASQGHWKIV 133
Cdd:COG0666   93 AAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVN---AQDNDGNTPLHLAAANGNLEIV 169
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 134 QILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLQHGANVNgSHSMCGWNSLHQASFQENAEIIKLLLRKGANKECQ 213
Cdd:COG0666  170 KLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVN-AKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 255982572 214 DDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPL 254
Cdd:COG0666  249 DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
SOCS_ASB3 cd03722
SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a ...
495-545 1.00e-25

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: 99.48  E-value: 1.00e-25
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|.
gi 255982572 495 ATVPSLTHLCRLEIRSSLKSERLRSDSYISQLPLPRSLHNYLLYEDVLRMY 545
Cdd:cd03722    1 ASVPSLTHLCRLEIRSSLKSERLRSDSFICQLPLPRSLQDYLLYSDVLRMY 51
PHA03095 PHA03095
ankyrin-like protein; Provisional
34-279 8.89e-23

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 101.25  E-value: 8.89e-23
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  34 RLVKQ---MDFTEAYADTCSTVGLAAREGNVK-VLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVE-CLQMLI--NADss 106
Cdd:PHA03095  32 RLLAAgadVNFRGEYGKTPLHLYLHYSSEKVKdIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIkaGAD-- 109
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 107 enyIKMKTFEGFCALH--LAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDV--LRLLLQHGANVNGShSM 182
Cdd:PHA03095 110 ---VNAKDKVGRTPLHvyLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV-DD 185
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 183 CGWNSLHQ--ASFQENAEIIKLLLRKGANKECQDDFGITPLFVAAQYGKLESLSI--LISSGANVNCQALDKATPLFIAA 258
Cdd:PHA03095 186 RFRSLLHHhlQSFKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAA 265
                        250       260
                 ....*....|....*....|.
gi 255982572 259 QEGHTKCVELLLSSGADPDLY 279
Cdd:PHA03095 266 VFNNPRACRRLIALGADINAV 286
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
132-383 1.95e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 97.72  E-value: 1.95e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 132 IVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLQHGANVNGSHSMCGWNSLHQASFQENAEIIKLLLRKGANKE 211
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 212 CQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGADPDlycnedswqlpihA 291
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVN-------------A 148
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 292 AAQMGHTkildllipltnracdtglnkvsPVYSAVFGGHEDCLEILLRNGYSPDAQAClvfGFSSPVCMAFQKDCEffGI 371
Cdd:COG0666  149 QDNDGNT----------------------PLHLAAANGNLEIVKLLLEAGADVNARDN---DGETPLHLAAENGHL--EI 201
                        250
                 ....*....|..
gi 255982572 372 VNILLKYGAQIN 383
Cdd:COG0666  202 VKLLLEAGADVN 213
PHA03100 PHA03100
ankyrin repeat protein; Provisional
60-275 2.68e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 99.35  E-value: 2.68e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  60 NVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLQMLINadsSENYIKMKTFEGFCALHLAASQGH-----WKIVQ 134
Cdd:PHA03100  14 KVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLD---NGADINSSTKNNSTPLHYLSNIKYnltdvKEIVK 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 135 ILLEAGADPNATTLEETTPLFLAVEN--GQIDVLRLLLQHGANVNgSHSMCGWNSLHQA--SFQENAEIIKLLLRKGA-- 208
Cdd:PHA03100  91 LLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVN-IKNSDGENLLHLYleSNKIDLKILKLLIDKGVdi 169
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 209 NKECQ--------------DDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGA 274
Cdd:PHA03100 170 NAKNRvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249

                 .
gi 255982572 275 D 275
Cdd:PHA03100 250 S 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
121-214 7.37e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 87.09  E-value: 7.37e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  121 LHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLQHganVNGSHSMCGWNSLHQASFQENAEII 200
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 255982572  201 KLLLRKGANKECQD 214
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
188-278 1.13e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 86.71  E-value: 1.13e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  188 LHQASFQENAEIIKLLLRKGANKECQDDFGITPLFVAAQYGKLESLSILISSgANVNCQaLDKATPLFIAAQEGHTKCVE 267
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|.
gi 255982572  268 LLLSSGADPDL 278
Cdd:pfam12796  79 LLLEKGADINV 89
PHA03095 PHA03095
ankyrin-like protein; Provisional
61-346 7.35e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 92.40  E-value: 7.35e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  61 VKVLRKLLKKGRSVDVADNRGWMPIHeaAYhnsveclqmlinadssenyikMKTFEGFCAlhlaasqghwKIVQILLEAG 140
Cdd:PHA03095  27 VEEVRRLLAAGADVNFRGEYGKTPLH--LY---------------------LHYSSEKVK----------DIVRLLLEAG 73
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 141 ADPNATTLEETTPLFLAVENGQ-IDVLRLLLQHGANVNGSHSmCGWNSLHQ--ASFQENAEIIKLLLRKGANKECQDDFG 217
Cdd:PHA03095  74 ADVNAPERCGFTPLHLYLYNATtLDVIKLLIKAGADVNAKDK-VGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYG 152
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 218 ITPLFVaaqYGK-----LESLSILISSGANVNCQALDKATPLFIAAQEGHT--KCVELLLSSGADPDlyCNEDSWQLPIH 290
Cdd:PHA03095 153 MTPLAV---LLKsrnanVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPraRIVRELIRAGCDPA--ATDMLGNTPLH 227
                        250       260       270       280       290       300
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255982572 291 AAAQMG---HTKILDLL-----IPLTNRACDTGLNkvspvYSAVFGGHEDCLEiLLRNGYSPDA 346
Cdd:PHA03095 228 SMATGSsckRSLVLPLLiagisINARNRYGQTPLH-----YAAVFNNPRACRR-LIALGADINA 285
PHA03100 PHA03100
ankyrin repeat protein; Provisional
60-244 1.94e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.88  E-value: 1.94e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  60 NVKVLRKLLKKGRSVD--VADNRGWMPIHEAAYHNS---VECLQMLINadsSENYIKMKTFEGFCALHLAASQ--GHWKI 132
Cdd:PHA03100  47 NIDVVKILLDNGADINssTKNNSTPLHYLSNIKYNLtdvKEIVKLLLE---YGANVNAPDNNGITPLLYAISKksNSYSI 123
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 133 VQILLEAGADPNATTLEETTPLFLAVENGQID--VLRLLLQHGANVN-----------GSH----SMCGWNSLHQASFQE 195
Cdd:PHA03100 124 VEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINaknrvnyllsyGVPinikDVYGFTPLHYAVYNN 203
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 255982572 196 NAEIIKLLLRKGANKECQDDFGITPLFVAAQYGKLESLSILISSGANVN 244
Cdd:PHA03100 204 NPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
PHA02875 PHA02875
ankyrin repeat protein; Provisional
59-278 1.06e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 88.51  E-value: 1.06e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  59 GNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLQMLINADSSENYiKMKTFEGfcALHLAASQGHWKIVQILLE 138
Cdd:PHA02875  13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDV-KYPDIES--ELHDAVEEGDVKAVEELLD 89
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 139 AGADPNATTLEE-TTPLFLAVENGQIDVLRLLLQHGANVNGShSMCGWNSLHQASFQENAEIIKLLLRKGANKECQDDFG 217
Cdd:PHA02875  90 LGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGADPDIP-NTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255982572 218 ITPLFVAAQYGKLESLSILISSGANVNCQALDK-ATPLFIAAQEGHTKCVELLLSSGADPDL 278
Cdd:PHA02875 169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA03100 PHA03100
ankyrin repeat protein; Provisional
151-399 4.46e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 86.64  E-value: 4.46e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 151 TTPLFLAVENGQIDVLRLLLQHGANVNgSHSMCGWNSLH-----QASFQENAEIIKLLLRKGANKECQDDFGITPLFVAA 225
Cdd:PHA03100  36 VLPLYLAKEARNIDVVKILLDNGADIN-SSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAI 114
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 226 QyGKLESLSI---LISSGANVNCQALDKATPLFIAAQEGH--TKCVELLLSSGADPDLYCNEDSwqlpihaaaqmghtkI 300
Cdd:PHA03100 115 S-KKSNSYSIveyLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINAKNRVNY---------------L 178
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 301 LDLLIPLTNRacdtGLNKVSPVYSAVFGGHEDCLEILLRNGYSPDaqACLVFGfSSPVCMAFQKDCEFfgIVNILLKYGA 380
Cdd:PHA03100 179 LSYGVPINIK----DVYGFTPLHYAVYNNNPEFVKYLLDLGANPN--LVNKYG-DTPLHIAILNNNKE--IFKLLLNNGP 249
                        250
                 ....*....|....*....
gi 255982572 381 QINelHLAYCLKYEKFSIF 399
Cdd:PHA03100 250 SIK--TIIETLLYFKDKDL 266
Ank_2 pfam12796
Ankyrin repeats (3 copies);
54-146 9.19e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.23  E-value: 9.19e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572   54 LAAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLQMLINADSSENyikmkTFEGFCALHLAASQGHWKIV 133
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL-----KDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|...
gi 255982572  134 QILLEAGADPNAT 146
Cdd:pfam12796  78 KLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
85-177 3.81e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.69  E-value: 3.81e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572   85 IHEAAYHNSVECLQMLINADSSENyikMKTFEGFCALHLAASQGHWKIVQILLEaGADPNATTlEETTPLFLAVENGQID 164
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---LQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLE 75
                          90
                  ....*....|...
gi 255982572  165 VLRLLLQHGANVN 177
Cdd:pfam12796  76 IVKLLLEKGADIN 88
PHA02876 PHA02876
ankyrin repeat protein; Provisional
121-426 5.99e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 84.34  E-value: 5.99e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 121 LHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLQHGANVNGSHSmcgwnSLHQASFQENAEII 200
Cdd:PHA02876 182 IHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDL-----SLLKAIRNEDLETS 256
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 201 KLLLRKGANKECQDDFGITPLFVAAQYGKLESL-SILISSGANVNCQALDKATPLFIAAQEGH-TKCVELLLSSGADPDl 278
Cdd:PHA02876 257 LLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVN- 335
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 279 yCNEDSWQLPIHAAAQMGHTKilDLLIPLTNRACDTGLNKV---SPVYSAVFGGHEDCLEILLRNGYSPDAQA-----CL 350
Cdd:PHA02876 336 -AADRLYITPLHQASTLDRNK--DIVITLLELGANVNARDYcdkTPIHYAAVRNNVVIINTLLDYGADIEALSqkigtAL 412
                        250       260       270       280       290       300       310       320
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 351 VFG--------------------------FSSPVCMAFQKDC------------------------------EFFGIVNI 374
Cdd:PHA02876 413 HFAlcgtnpymsvktlidrganvnsknkdLSTPLHYACKKNCkldviemlldngadvnainiqnqypllialEYHGIVNI 492
                        330       340       350       360       370
                 ....*....|....*....|....*....|....*....|....*....|...
gi 255982572 375 LLKYGAQINELH-LAYCLKYEKFSiFRYFLRKGCslgpwnhIYEFVNHAIKAQ 426
Cdd:PHA02876 493 LLHYGAELRDSRvLHKSLNDNMFS-FRYIIAHIC-------IQDFIRHDIRNE 537
PHA02874 PHA02874
ankyrin repeat protein; Provisional
55-305 3.06e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 81.16  E-value: 3.06e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  55 AAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLQMLINADSSENYIKMKTFEGfcalhlaasqghwKIVQ 134
Cdd:PHA02874  42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSILPIPCIEK-------------DMIK 108
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 135 ILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLQHGANVNgSHSMCGWNSLHQASFQENAEIIKLLLRKGANKECQD 214
Cdd:PHA02874 109 TILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVN-IEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 215 DFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTkCVELLLSSGADPDLYCNEDSwqlPIHAAAQ 294
Cdd:PHA02874 188 NNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLINNASINDQDIDGST---PLHHAIN 263
                        250
                 ....*....|..
gi 255982572 295 MGHTK-ILDLLI 305
Cdd:PHA02874 264 PPCDIdIIDILL 275
PHA02874 PHA02874
ankyrin repeat protein; Provisional
90-340 5.89e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 80.39  E-value: 5.89e-16
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  90 YHNSVECLQMLINadSSENYIKMKTFEGFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLL 169
Cdd:PHA02874  10 YSGDIEAIEKIIK--NKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLL 87
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 170 LQHGANVNGSHSMCGWNS----------------------LHQASFQENAEIIKLLLRKGANKECQDDFGITPLFVAAQY 227
Cdd:PHA02874  88 IDNGVDTSILPIPCIEKDmiktildcgidvnikdaelktfLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKH 167
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 228 GKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGADPDLYCNEDSwqLPIHAAAqMGHTKILDLLIpl 307
Cdd:PHA02874 168 NFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGF--TPLHNAI-IHNRSAIELLI-- 242
                        250       260       270
                 ....*....|....*....|....*....|....*
gi 255982572 308 TNRAC-DTGLNKVSPVYSAV-FGGHEDCLEILLRN 340
Cdd:PHA02874 243 NNASInDQDIDGSTPLHHAInPPCDIDIIDILLYH 277
Ank_2 pfam12796
Ankyrin repeats (3 copies);
221-305 1.33e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.07  E-value: 1.33e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  221 LFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSgADPDLYCNEDSwqlPIHAAAQMGHTKI 300
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRT---ALHYAARSGHLEI 76

                  ....*
gi 255982572  301 LDLLI 305
Cdd:pfam12796  77 VKLLL 81
PHA02876 PHA02876
ankyrin repeat protein; Provisional
55-305 3.15e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 78.95  E-value: 3.15e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  55 AAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLQMLINADSSEN--------YIKMKTFE--------GF 118
Cdd:PHA02876 185 AAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINkndlsllkAIRNEDLEtslllydaGF 264
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 119 CA----------LHLAASQGHW-KIVQILLEAGADPNATTLEETTPLFLAVENG-QIDVLRLLLQHGANVNGSHSMcgWN 186
Cdd:PHA02876 265 SVnsiddckntpLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRL--YI 342
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 187 S-LHQAS-FQENAEIIKLLLRKGANKECQDDFGITPLFVAA------------QYG-KLESLS----------------- 234
Cdd:PHA02876 343 TpLHQAStLDRNKDIVITLLELGANVNARDYCDKTPIHYAAvrnnvviintllDYGaDIEALSqkigtalhfalcgtnpy 422
                        250       260       270       280       290       300       310
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 255982572 235 ----ILISSGANVNCQALDKATPLFIAAQEG-HTKCVELLLSSGADPDLYCNEDSWQLPIhaaaQMGHTKILDLLI 305
Cdd:PHA02876 423 msvkTLIDRGANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLI----ALEYHGIVNILL 494
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
80-272 4.67e-15

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: 78.13  E-value: 4.67e-15
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  80 RGW-MPIHEAAYHNSVECLQMLINADSSENYIKMKTFEgfCALHLAASQGHWKIVQILLEAgaDPNATTLEET------- 151
Cdd:cd22192   15 RISeSPLLLAAKENDVQAIKKLLKCPSCDLFQRGALGE--TALHVAALYDNLEAAVVLMEA--APELVNEPMTsdlyqge 90
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 152 TPLFLAVENGQIDVLRLLLQHGANVN-----------GSHSMC--GWNSLHQASFQENAEIIKLLLRKGANKECQDDFGI 218
Cdd:cd22192   91 TALHIAVVNQNLNLVRELIARGADVVspratgtffrpGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 255982572 219 TPLFV-AAQYGKL---ESLSILISSGANVNCQALDKA------TPLFIAAQEGHTKCVELLLSS 272
Cdd:cd22192  171 TVLHIlVLQPNKTfacQMYDLILSYDKEDDLQPLDLVpnnqglTPFKLAAKEGNIVMFQHLVQK 234
PHA02875 PHA02875
ankyrin repeat protein; Provisional
87-277 1.41e-14

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 75.80  E-value: 1.41e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  87 EAAYHNSVECLQMLINADSSENYikmKTFEGFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVL 166
Cdd:PHA02875   8 DAILFGELDIARRLLDIGINPNF---EIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAV 84
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 167 RLLLQHGANVNGSHSMCGWNSLHQASFQENAEIIKLLLRKGANKECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQ 246
Cdd:PHA02875  85 EELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIE 164
                        170       180       190
                 ....*....|....*....|....*....|.
gi 255982572 247 ALDKATPLFIAAQEGHTKCVELLLSSGADPD 277
Cdd:PHA02875 165 DCCGCTPLIIAMAKGDIAICKMLLDSGANID 195
Ank_2 pfam12796
Ankyrin repeats (3 copies);
254-347 1.51e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.37  E-value: 1.51e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  254 LFIAAQEGHTKCVELLLSSGADPDLYCNEDswQLPIHAAAQMGHTKILDLLIPltNRACDTGLNKVSPVYSAVFGGHEDC 333
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNG--RTALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHLEI 76
                          90
                  ....*....|....
gi 255982572  334 LEILLRNGYSPDAQ 347
Cdd:pfam12796  77 VKLLLEKGADINVK 90
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
495-539 2.61e-13

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


Pssm-ID: 239686  Cd Length: 42  Bit Score: 64.05  E-value: 2.61e-13
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*
gi 255982572 495 ATVPSLTHLCRLEIRSSLKSERLrsdSYISQLPLPRSLHNYLLYE 539
Cdd:cd03716    1 STPRSLQHLCRLAIRRCLGRRRL---ELIKKLPLPPRLKDYLLYE 42
PHA02878 PHA02878
ankyrin repeat protein; Provisional
62-267 3.91e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.83  E-value: 3.91e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  62 KVLRKLLKKGRSVDVAD-NRGWMPIHEAAYHNSVECLQMLINADSSENyIKMKTFEGfcALHLAASQGHWKIVQILLEAG 140
Cdd:PHA02878 148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVN-IPDKTNNS--PLHHAVKHYNKPIVHILLENG 224
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 141 ADPNATTLEETTPLFLAVEN-GQIDVLRLLLQHGANVNGSHSMCGWNSLHQASFQEnaEIIKLLLRKGANKECQDDFGIT 219
Cdd:PHA02878 225 ASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLT 302
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 255982572 220 PLFVAA-QYGKLESLSILISsgaNVNCQALDKAtplFIAAQEGHTKCVE 267
Cdd:PHA02878 303 PLSSAVkQYLCINIGRILIS---NICLLKRIKP---DIKNSEGFIDNMD 345
PHA02878 PHA02878
ankyrin repeat protein; Provisional
36-275 5.71e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.06  E-value: 5.71e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  36 VKQMDFTEAYADTCSTVGL-----AAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLQMLINAdssenYI 110
Cdd:PHA02878  20 IEYIDHTENYSTSASLIPFiplhqAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRS-----IN 94
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 111 KMKTFEGFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLQHGANVNGSHSMCGWNSLHQ 190
Cdd:PHA02878  95 KCSVFYTLVAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHKGNTALHY 174
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 191 ASFQENAEIIKLLLRKGANKECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAqeGHTKCVE--- 267
Cdd:PHA02878 175 ATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV--GYCKDYDilk 252

                 ....*...
gi 255982572 268 LLLSSGAD 275
Cdd:PHA02878 253 LLLEHGVD 260
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
496-539 1.29e-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: 62.10  E-value: 1.29e-12
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 255982572 496 TVPSLTHLCRLEIRSSLKSERLrsdSYISQLPLPRSLHNYLLYE 539
Cdd:cd03587    1 NPRSLQHLCRLAIRRCLGKRRL---DLIDKLPLPPRLKDYLLYK 41
PHA03100 PHA03100
ankyrin repeat protein; Provisional
199-408 3.78e-12

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 68.15  E-value: 3.78e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 199 IIKLLLRKGANKE-----CQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHT-----KCVEL 268
Cdd:PHA03100  12 IIKVKNIKYIIMEddlndYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKL 91
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 269 LLSSGADPDLYCNEDSWQLPIHAAAQMGHTKILDLLIpltNRACDTGLNKV---SPVYSAVFGGHED--CLEILLRNGYS 343
Cdd:PHA03100  92 LLEYGANVNAPDNNGITPLLYAISKKSNSYSIVEYLL---DNGANVNIKNSdgeNLLHLYLESNKIDlkILKLLIDKGVD 168
                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255982572 344 PDAqaclvfgfsspvcmafqKDceffgIVNILLKYGAQINE--------LHLAycLKYEKFSIFRYFLRKGCS 408
Cdd:PHA03100 169 INA-----------------KN-----RVNYLLSYGVPINIkdvygftpLHYA--VYNNNPEFVKYLLDLGAN 217
PHA02875 PHA02875
ankyrin repeat protein; Provisional
124-317 4.91e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 68.09  E-value: 4.91e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 124 AASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLQHGA--NVN--GSHSmcgwnSLHQASFQENAEI 199
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipDVKypDIES-----ELHDAVEEGDVKA 83
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 200 IKLLLRkgANKECQDDF---GITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGADP 276
Cdd:PHA02875  84 VEELLD--LGKFADDVFykdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL 161
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|..
gi 255982572 277 DLycnEDSWQL-PIHAAAQMGHTKILDLLIpltnracDTGLN 317
Cdd:PHA02875 162 DI---EDCCGCtPLIIAMAKGDIAICKMLL-------DSGAN 193
PHA03095 PHA03095
ankyrin-like protein; Provisional
155-409 9.24e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.36  E-value: 9.24e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 155 FLAVENGQIDVLRLLLQHGANVN--GSHSMCGWNSLHQASFQENAEIIKLLLRKGANKECQDDFGITPLFVAAQYG-KLE 231
Cdd:PHA03095  19 LLNASNVTVEEVRRLLAAGADVNfrGEYGKTPLHLYLHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNAtTLD 98
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 232 SLSILISSGANVNCQALDKATPLFI--AAQEGHTKCVELLLSSGADPdlyCNEDSWQL-PIHA-----AAQMghtKILDL 303
Cdd:PHA03095  99 VIKLLIKAGADVNAKDKVGRTPLHVylSGFNINPKVIRLLLRKGADV---NALDLYGMtPLAVllksrNANV---ELLRL 172
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 304 LI-----PLTNRAC-DTGLN--KVSPVYSAvfggheDCLEILLRNGYSPDAQAclVFGFSSPVCMAFQKDCEFFGIVNIL 375
Cdd:PHA03095 173 LIdagadVYAVDDRfRSLLHhhLQSFKPRA------RIVRELIRAGCDPAATD--MLGNTPLHSMATGSSCKRSLVLPLL 244
                        250       260       270       280
                 ....*....|....*....|....*....|....*....|..
gi 255982572 376 LKyGAQINE--------LHLAYClkYEKFSIFRYFLRKGCSL 409
Cdd:PHA03095 245 IA-GISINArnrygqtpLHYAAV--FNNPRACRRLIALGADI 283
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
124-277 1.15e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 67.59  E-value: 1.15e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 124 AASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLQHGANV-----NGSHSMcgWNSL---HQASFQe 195
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVhirdaNGNTAL--WNAIsakHHKIFR- 608
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 196 naeiIKLLLRKGANKECQDDFgitpLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGAD 275
Cdd:PLN03192 609 ----ILYHFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680

                 ..
gi 255982572 276 PD 277
Cdd:PLN03192 681 VD 682
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
55-221 3.02e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.43  E-value: 3.02e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  55 AAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLQMLINADSSenyIKMKTFEGFCALHLAASQGHWKIVQ 134
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACN---VHIRDANGNTALWNAISAKHHKIFR 608
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 135 IL--LEAGADPNATtleeTTPLFLAVENGQIDVLRLLLQHGANVNgSHSMCGWNSLHQASFQENAEIIKLLLRKGANKEC 212
Cdd:PLN03192 609 ILyhFASISDPHAA----GDLLCTAAKRNDLTAMKELLKQGLNVD-SEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
                        170
                 ....*....|..
gi 255982572 213 ---QDDFGITPL 221
Cdd:PLN03192 684 antDDDFSPTEL 695
PHA02874 PHA02874
ankyrin repeat protein; Provisional
55-227 7.29e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 64.21  E-value: 7.29e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  55 AAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLQMLINADSsenYIKMKTFEGFCALHLAASQGHWKIVQ 134
Cdd:PHA02874 131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA---YANVKDNNGESPLHNAAEYGDYACIK 207
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 135 ILLEAGADPNATTLEETTPLFLAVENGQiDVLRLLLQHgANVNgSHSMCGWNSLHQA-SFQENAEIIKLLLRKGANKECQ 213
Cdd:PHA02874 208 LLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLINN-ASIN-DQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIK 284
                        170
                 ....*....|....
gi 255982572 214 DDFGITPLFVAAQY 227
Cdd:PHA02874 285 DNKGENPIDTAFKY 298
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
496-537 7.59e-11

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


Pssm-ID: 462192  Cd Length: 39  Bit Score: 57.18  E-value: 7.59e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 255982572  496 TVPSLTHLCRLEIRSSLKSERLrsdSYISQLPLPRSLHNYLL 537
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRL---GAIDKLPLPPLLKDYLL 39
PHA02875 PHA02875
ankyrin repeat protein; Provisional
45-177 1.33e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 63.47  E-value: 1.33e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  45 YADTCSTVGLAAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLQMLINADSSENyikMKTFEGFCALHLA 124
Cdd:PHA02875  99 YKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD---IEDCCGCTPLIIA 175
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 255982572 125 ASQGHWKIVQILLEAGADPNATTLE-ETTPLFLAVENGQIDVLRLLLQHGANVN 177
Cdd:PHA02875 176 MAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA03100 PHA03100
ankyrin repeat protein; Provisional
59-177 1.75e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.15  E-value: 1.75e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  59 GNVKVLRKLLKKGRSVDVADNRGWMPIHEAAY--HNSVECLQMLI------NADSSENY-------IKMKTFEGFCALHL 123
Cdd:PHA03100 119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLEsnKIDLKILKLLIdkgvdiNAKNRVNYllsygvpINIKDVYGFTPLHY 198
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 255982572 124 AASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLQHGANVN 177
Cdd:PHA03100 199 AVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
96-238 4.67e-10

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: 62.47  E-value: 4.67e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  96 CLQMLINADSSEnyikmKTFEGFCALHLAASQGHWKIVQILLEAGADPNATTLEE--------------TTPLFLAVENG 161
Cdd:cd22194  125 ILDRFINAEYTE-----EAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKGVffnpkykhegfyfgETPLALAACTN 199
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 162 QIDVLRLLLQHGANVNGSHSMCGWNSLH------QASFQENAEIIKL---LLRKGANKECQ---DDFGITPLFVAAQYGK 229
Cdd:cd22194  200 QPEIVQLLMEKESTDITSQDSRGNTVLHalvtvaEDSKTQNDFVKRMydmILLKSENKNLEtirNNEGLTPLQLAAKMGK 279

                 ....*....
gi 255982572 230 LESLSILIS 238
Cdd:cd22194  280 AEILKYILS 288
PHA02989 PHA02989
ankyrin repeat protein; Provisional
131-244 7.94e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 61.30  E-value: 7.94e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 131 KIVQILLEAGADPNATTLEETTPLFLAVENGQI---DVLRLLLQHGANVNGSHSMCGWNSLHQ--ASFQENAEIIKLLLR 205
Cdd:PHA02989  89 KIVKLLLKFGADINLKTFNGVSPIVCFIYNSNInncDMLRFLLSKGINVNDVKNSRGYNLLHMylESFSVKKDVIKILLS 168
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 255982572 206 KGANK-ECQDDFGITPLFV----AAQYGKLESLSILISSGANVN 244
Cdd:PHA02989 169 FGVNLfEKTSLYGLTPMNIylrnDIDVISIKVIKYLIKKGVNIE 212
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
115-172 2.39e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 59.91  E-value: 2.39e-09
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 255982572 115 FEGFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLQH 172
Cdd:PTZ00322 113 YDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
498-539 1.07e-08

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


Pssm-ID: 198037  Cd Length: 34  Bit Score: 50.87  E-value: 1.07e-08
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 255982572   498 PSLTHLCRLEIRSSLKSerlrsdsyISQLPLPRSLHNYLLYE 539
Cdd:smart00969   1 RSLQHLCRLAIRRSLGG--------IDKLPLPPRLKDYLLYY 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
219-270 4.12e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 4.12e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 255982572  219 TPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLL 270
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
55-101 4.68e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 4.68e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 255982572   55 AAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLQMLI 101
Cdd:pfam13637   8 AAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02884 PHA02884
ankyrin repeat protein; Provisional
90-257 5.18e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 54.60  E-value: 5.18e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  90 YHNSVECLQMLINADSSENYIKMKTFEGFC---ALHLAASQGHWKIVQILLEAGADPNA----TTLEETTPLFLAVENGQ 162
Cdd:PHA02884   3 IINLIDIITLLCRIFYIIFYIAIKKKNKICianILYSSIKFHYTDIIDAILKLGADPEApfplSENSKTNPLIYAIDCDN 82
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 163 IDVLRLLLQHGANVNgshsmcgwnslhqaSFQENAEIiklllrkgankecqddfgiTPLFVAAQYGKLESLSILISSGAN 242
Cdd:PHA02884  83 DDAAKLLIRYGADVN--------------RYAEEAKI-------------------TPLYISVLHGCLKCLEILLSYGAD 129
                        170
                 ....*....|....*
gi 255982572 243 VNCQALDKATPLFIA 257
Cdd:PHA02884 130 INIQTNDMVTPIELA 144
Ank_4 pfam13637
Ankyrin repeats (many copies);
120-170 5.37e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.58  E-value: 5.37e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 255982572  120 ALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLL 170
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
252-305 5.75e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 5.75e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 255982572  252 TPLFIAAQEGHTKCVELLLSSGADPDlYCNEDSWQlPIHAAAQMGHTKILDLLI 305
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADIN-AVDGNGET-ALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
150-204 7.71e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 7.71e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 255982572  150 ETTPLFLAVENGQIDVLRLLLQHGANVNGSHSmCGWNSLHQASFQENAEIIKLLL 204
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
152-312 8.39e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 55.02  E-value: 8.39e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 152 TPLFLAV-ENGQIDVLRLLLQHGANV--NGSHsmcGWNSLHQASFQENAEIIKLLLRKG---ANKECQDDF--GITPLFV 223
Cdd:cd22192   19 SPLLLAAkENDVQAIKKLLKCPSCDLfqRGAL---GETALHVAALYDNLEAAVVLMEAApelVNEPMTSDLyqGETALHI 95
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 224 AAQYGKLESLSILISSGANVncqALDKAT-----------------PLFIAAQEGHTKCVELLLSSGADPDlycNEDSW- 285
Cdd:cd22192   96 AVVNQNLNLVRELIARGADV---VSPRATgtffrpgpknliyygehPLSFAACVGNEEIVRLLIEHGADIR---AQDSLg 169
                        170       180
                 ....*....|....*....|....*..
gi 255982572 286 QLPIHaaaqmghtkILdLLIPLTNRAC 312
Cdd:cd22192  170 NTVLH---------IL-VLQPNKTFAC 186
PHA02884 PHA02884
ankyrin repeat protein; Provisional
198-282 8.43e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 53.83  E-value: 8.43e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 198 EIIKLLLRKGANKECQDDFG----ITPLFVAAQYGKLESLSILISSGANVNCQALD-KATPLFIAAQEGHTKCVELLLSS 272
Cdd:PHA02884  47 DIIDAILKLGADPEAPFPLSenskTNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEaKITPLYISVLHGCLKCLEILLSY 126
                         90
                 ....*....|
gi 255982572 273 GADPDLYCNE 282
Cdd:PHA02884 127 GADINIQTND 136
SOCS_ASB14 cd03730
SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a ...
499-540 1.22e-07

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


Pssm-ID: 239700  Cd Length: 57  Bit Score: 48.69  E-value: 1.22e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 255982572 499 SLTHLCRLEIRSSLKSERLRSDSYISQLPLPRSLHNYLLYED 540
Cdd:cd03730    5 SLKHLCRLKIRACMGRLRLRCPVFMSFLPLPNRLKAYILYKE 46
SOCS_SSB1_4 cd03718
SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box ...
499-539 1.39e-07

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


Pssm-ID: 239688  Cd Length: 42  Bit Score: 48.07  E-value: 1.39e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 255982572 499 SLTHLCRLEIRSSLKSERLRSdsyISQLPLPRSLHNYLLYE 539
Cdd:cd03718    5 PLMDLCRRRVRVALGRDRLEE---IEQLPLPPSLKNYLLYQ 42
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
497-538 2.29e-07

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


Pssm-ID: 239687  Cd Length: 39  Bit Score: 47.21  E-value: 2.29e-07
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 255982572 497 VPSLTHLCRLEIRSSLKSERlrsdsyISQLPLPRSLHNYLLY 538
Cdd:cd03717    3 VRSLQHLCRFVIRQCTRRDL------IDQLPLPRRLKDYLKE 38
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
111-216 2.61e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 53.36  E-value: 2.61e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 111 KMKTFEgFCalHLAASqGHWKIVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLLQHGANVNGSHSMcGWNSLHQ 190
Cdd:PTZ00322  80 HMLTVE-LC--QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKD-GKTPLEL 154
                         90       100
                 ....*....|....*....|....*.
gi 255982572 191 ASFQENAEIIKLLLRkgankECQDDF 216
Cdd:PTZ00322 155 AEENGFREVVQLLSR-----HSQCHF 175
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
97-237 4.50e-07

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 52.89  E-value: 4.50e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  97 LQMLINADSSENYIKMKTfegfcALHLAASQGHWKIVQILLEAGADPNATTLEE--------------TTPLFLAVENGQ 162
Cdd:cd22196   79 LKEFVNAAYTDSYYKGQT-----ALHIAIERRNMHLVELLVQNGADVHARASGEffkkkkggpgfyfgELPLSLAACTNQ 153
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 163 IDVLRLLLQH---GANVNGSHSMcGWNSLHQA-----SFQENAEIIKL----LLRKGAN-------KECQDDFGITPLFV 223
Cdd:cd22196  154 LDIVKFLLENphsPADISARDSM-GNTVLHALvevadNTPENTKFVTKmyneILILGAKirpllklEEITNKKGLTPLKL 232
                        170
                 ....*....|....
gi 255982572 224 AAQYGKLESLSILI 237
Cdd:cd22196  233 AAKTGKIGIFAYIL 246
PHA02874 PHA02874
ankyrin repeat protein; Provisional
49-177 5.26e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 52.27  E-value: 5.26e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  49 CSTVGLAAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLQMLInadSSENYIKMKTFEGFCALHLAASqg 128
Cdd:PHA02874 158 CYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI---DHGNHIMNKCKNGFTPLHNAII-- 232
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|
gi 255982572 129 HWKIVQILLEAGADPNATTLEETTPLFLAVENG-QIDVLRLLLQHGANVN 177
Cdd:PHA02874 233 HNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADIS 282
PHA02876 PHA02876
ankyrin repeat protein; Provisional
194-383 8.08e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.99  E-value: 8.08e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 194 QENAEIIKLLLRKGANKECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVEL----- 268
Cdd:PHA02876 155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAiidnr 234
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 269 ---------LLSSGADPDLYCN-------------EDSWQLPIHAAAQmghTKILDLLIP-LTNRACDTGLNKV---SPV 322
Cdd:PHA02876 235 sninkndlsLLKAIRNEDLETSlllydagfsvnsiDDCKNTPLHHASQ---APSLSRLVPkLLERGADVNAKNIkgeTPL 311
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 255982572 323 YSAVFGGHE-DCLEILLRNGYSPDAQACLvfgFSSPVCMAFQKDcEFFGIVNILLKYGAQIN 383
Cdd:PHA02876 312 YLMAKNGYDtENIRTLIMLGADVNAADRL---YITPLHQASTLD-RNKDIVITLLELGANVN 369
PHA03095 PHA03095
ankyrin-like protein; Provisional
62-170 1.22e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 51.18  E-value: 1.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  62 KVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLQM--LINADSSENYikmKTFEGFCALHLAASQGHWKIVQILLEA 139
Cdd:PHA03095 203 RIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVlpLLIAGISINA---RNRYGQTPLHYAAVFNNPRACRRLIAL 279
                         90       100       110
                 ....*....|....*....|....*....|.
gi 255982572 140 GADPNATTLEETTPLFLAVENGQIDVLRLLL 170
Cdd:PHA03095 280 GADINAVSSDGNTPLSLMVRNNNGRAVRAAL 310
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
496-539 1.60e-06

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: 45.12  E-value: 1.60e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 255982572 496 TVPSLTHLCRLEIRSSLKSerlRSDSYISQLPLPRSLHNYLLYE 539
Cdd:cd03723    2 TPRSLQHLCRCAIRKLLGS---RCHKLVPQLSLPTSLKNYLLLE 42
PHA02798 PHA02798
ankyrin-like protein; Provisional
142-282 2.05e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 50.22  E-value: 2.05e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 142 DPNATTLEETT-PLFLAVENGQIDVLRLLLQHGANVNG-----SHSMCGWNSlHQASFQENAEIIKLLLRKGANKECQDD 215
Cdd:PHA02798  29 NPNEIVNEYSIfQKYLQRDSPSTDIVKLFINLGANVNGldneySTPLCTILS-NIKDYKHMLDIVKILIENGADINKKNS 107
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 255982572 216 FGITPLFVAAQYG---KLESLSILISSGANVNCQALDKATPLFIAAQEGHT---KCVELLLSSGADPDLYCNE 282
Cdd:PHA02798 108 DGETPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNNK 180
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
499-540 2.13e-06

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: 44.82  E-value: 2.13e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 255982572 499 SLTHLCRLEIRSSLKSERLRSDSYISQLPLPRSLHNYLLYED 540
Cdd:cd03731    5 PLKHLCRLKIRKLMGLQKLQQPSSMKKLPLPPALKRYILYKE 46
PHA02946 PHA02946
ankyin-like protein; Provisional
116-272 4.00e-06

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 49.28  E-value: 4.00e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 116 EGFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFL--AVENGQIDVLRLLLQHGANVNGSHSMCGWNSLhQASF 193
Cdd:PHA02946  71 DGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKINNSVDEEGCGPL-LACT 149
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 194 QENAEIIKLLLRKGANKECQDDFGITPL--FVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQE--GHTKCVELL 269
Cdd:PHA02946 150 DPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKtvKNVDIINLL 229

                 ...
gi 255982572 270 LSS 272
Cdd:PHA02946 230 LPS 232
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
97-238 4.94e-06

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: 49.41  E-value: 4.94e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  97 LQMLINADSSENYikmktFEGFCALHLAASQGHWKIVQILLEAGADPNAT--------TLEET------TPLFLAVENGQ 162
Cdd:cd22193   61 LKRFINAEYTDEY-----YEGQTALHIAIERRQGDIVALLVENGADVHAHakgrffqpKYQGEgfyfgeLPLSLAACTNQ 135
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 163 IDVLRLLLQHG---ANVNGSHSMcGWNSLHQA-----SFQENAEIIK----LLLRKGAN-------KECQDDFGITPLFV 223
Cdd:cd22193  136 PDIVQYLLENEhqpADIEAQDSR-GNTVLHALvtvadNTKENTKFVTrmydMILIRGAKlcptvelEEIRNNDGLTPLQL 214
                        170
                 ....*....|....*
gi 255982572 224 AAQYGKLESLSILIS 238
Cdd:cd22193  215 AAKMGKIEILKYILQ 229
SOCS_SSB1 cd03744
SOCS (suppressors of cytokine signaling) box of SSB1 (SPRY domain-containing SOCS box proteins) ...
499-539 7.30e-06

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


Pssm-ID: 239713  Cd Length: 42  Bit Score: 43.05  E-value: 7.30e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 255982572 499 SLTHLCRLEIRSSLKSERLrsdSYISQLPLPRSLHNYLLYE 539
Cdd:cd03744    5 PLMDLCRRSVRLALGRERL---SEIHTLPLPASLKNYLLYQ 42
SOCS_SSB4 cd03743
SOCS (suppressors of cytokine signaling) box of SSB4 (SPRY domain-containing SOCS box ...
500-539 7.36e-06

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


Pssm-ID: 239712  Cd Length: 42  Bit Score: 43.02  E-value: 7.36e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 255982572 500 LTHLCRLEIRSSLKSERLRsdsYISQLPLPRSLHNYLLYE 539
Cdd:cd03743    6 LMDLCRRSARQALGRHRLH---HIQSLPLPQTLKNYLQYQ 42
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
152-177 9.94e-06

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 42.19  E-value: 9.94e-06
                           10        20
                   ....*....|....*....|....*.
gi 255982572   152 TPLFLAVENGQIDVLRLLLQHGANVN 177
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
200-284 1.16e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 48.36  E-value: 1.16e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 200 IKLLLRKGANKECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSsgadpdlY 279
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR-------H 170

                 ....*
gi 255982572 280 CNEDS 284
Cdd:PTZ00322 171 SQCHF 175
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
116-147 1.35e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.89  E-value: 1.35e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 255982572  116 EGFCALHLAASQ-GHWKIVQILLEAGADPNATT 147
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
230-406 1.42e-05

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 47.26  E-value: 1.42e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 230 LESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGADPDLycNEDSWQLPIHAAAQMGHTKILDLLIPLTN 309
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALAL--ADALGALLLLAAALAGDLLVALLLLAAGA 78
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 310 RACDTGLNKVSPVYSAVFGGHEDCLEILLRNGYSPDAQAclVFGFSSPVCMAFQKDCEffgIVNILLKYGAQINE----- 384
Cdd:COG0666   79 DINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARD--KDGETPLHLAAYNGNLE---IVKLLLEAGADVNAqdndg 153
                        170       180
                 ....*....|....*....|....*
gi 255982572 385 ---LHLAYCLKYEKfsIFRYFLRKG 406
Cdd:COG0666  154 ntpLHLAAANGNLE--IVKLLLEAG 176
PHA02989 PHA02989
ankyrin repeat protein; Provisional
62-270 1.45e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 47.81  E-value: 1.45e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  62 KVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLQMLINADSSENYIK-MKTFEGFCALH--LAASQGHWKIVQILLE 138
Cdd:PHA02989  89 KIVKLLLKFGADINLKTFNGVSPIVCFIYNSNINNCDMLRFLLSKGINVNdVKNSRGYNLLHmyLESFSVKKDVIKILLS 168
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 139 AGADP-NATTLEETTPLFLAVENG----QIDVLRLLLQHGANVNGShsmcgwNSLHQA---SFQENAEI-----IKLL-- 203
Cdd:PHA02989 169 FGVNLfEKTSLYGLTPMNIYLRNDidviSIKVIKYLIKKGVNIETN------NNGSESvleSFLDNNKIlskkeFKVLnf 242
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 255982572 204 LRKGANKECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLL 270
Cdd:PHA02989 243 ILKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRIL 309
PHA02798 PHA02798
ankyrin-like protein; Provisional
132-209 1.71e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.52  E-value: 1.71e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 132 IVQILLEAGADPNATTLEETTPLFLAVENGQIDVLRLLL---QHGANVNgSHSMCGWNSLH---QASFQENAEIIKLLLR 205
Cdd:PHA02798  91 IVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfmiENGADTT-LLDKDGFTMLQvylQSNHHIDIEIIKLLLE 169

                 ....
gi 255982572 206 KGAN 209
Cdd:PHA02798 170 KGVD 173
SOCS_SOCS7 cd03741
SOCS (suppressors of cytokine signaling) box of SOCS7-like proteins. Together with CIS1, the ...
497-538 3.71e-05

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


Pssm-ID: 239710  Cd Length: 49  Bit Score: 41.24  E-value: 3.71e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|..
gi 255982572 497 VPSLTHLCRLEIRSSLkserlRSDsYISQLPLPRSLHNYLLY 538
Cdd:cd03741    3 VQSLQHLCRFVIRKLV-----RRD-HIPALPLPRRLIDYLRE 38
SOCS smart00253
suppressors of cytokine signalling; suppressors of cytokine signalling
497-538 3.99e-05

suppressors of cytokine signalling; suppressors of cytokine signalling


Pssm-ID: 128549  Cd Length: 43  Bit Score: 41.13  E-value: 3.99e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 255982572   497 VPSLTHLCRLEIRSSLKSErlrsdsYISQLPLPRSLHNYLLY 538
Cdd:smart00253   7 VPSLQHLCRFTIRRCTRTD------QIKTLPLPPKLKDYLSY 42
Ank_2 pfam12796
Ankyrin repeats (3 copies);
289-383 4.30e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.41  E-value: 4.30e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  289 IHAAAQMGHTKILDLLIPLTNRACDTGLNKVSPVYSAVFGGHEDCLEILLRNgyspdAQACLVFGFSSPVCMAFQKDCef 368
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-----ADVNLKDNGRTALHYAARSGH-- 73
                          90
                  ....*....|....*
gi 255982572  369 FGIVNILLKYGAQIN 383
Cdd:pfam12796  74 LEIVKLLLEKGADIN 88
SOCS_WSB_SWIP cd03733
SOCS (suppressors of cytokine signaling) box of WSB/SWiP-like proteins. This subfamily ...
496-538 4.45e-05

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


Pssm-ID: 239702  Cd Length: 39  Bit Score: 40.87  E-value: 4.45e-05
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 255982572 496 TVPSLTHLCRLEIRSSLKSERlrsdsyISQLPLPRSLHNYLLY 538
Cdd:cd03733    2 VVSSLQHLCRMALRRVMTTQQ------VLALPIPKKMKEFLTY 38
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
152-305 4.63e-05

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 46.23  E-value: 4.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  152 TPLF-LAVENGQIDVLRLLLQHGANVNgshsmCGWNSLHQAS--FQENAE-IIKLLLRKG--------ANKECQDDF--G 217
Cdd:TIGR00870  54 SALFvAAIENENLELTELLLNLSCRGA-----VGDTLLHAISleYVDAVEaILLHLLAAFrksgplelANDQYTSEFtpG 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  218 ITPLFVAAQYGKLESLSILISSGANVNCQAldkatplfiaaqeghtKCVELLLSSGADpDLYCNEdswqLPIHAAAQMGH 297
Cdd:TIGR00870 129 ITALHLAAHRQNYEIVKLLLERGASVPARA----------------CGDFFVKSQGVD-SFYHGE----SPLNAAACLGS 187

                  ....*...
gi 255982572  298 TKILDLLI 305
Cdd:TIGR00870 188 PSIVALLS 195
PHA02798 PHA02798
ankyrin-like protein; Provisional
61-257 6.50e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 45.60  E-value: 6.50e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  61 VKVLRKLLKKGRSVDVADNRGWMPI-----HEAAYHNSVECLQMLI--NADssenyIKMKTFEG----FCALHlAASQGH 129
Cdd:PHA02798  51 TDIVKLFINLGANVNGLDNEYSTPLctilsNIKDYKHMLDIVKILIenGAD-----INKKNSDGetplYCLLS-NGYINN 124
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 130 WKIVQILLEAGADPNATTLEETTPLFLAVENG---QIDVLRLLLQHGANVNGSHSMCGWNSLHqASFQEN-----AEIIK 201
Cdd:PHA02798 125 LEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDINTHNNKEKYDTLH-CYFKYNidridADILK 203
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 202 LLLRKG--ANKECQ-------------------------------------DDFGITPLFVAAQYGKLESLSILISSGAN 242
Cdd:PHA02798 204 LFVDNGfiINKENKshkkkfmeylnsllydnkrfkknildfifsyidinqvDELGFNPLYYSVSHNNRKIFEYLLQLGGD 283
                        250
                 ....*....|....*
gi 255982572 243 VNCQALDKATPLFIA 257
Cdd:PHA02798 284 INIITELGNTCLFTA 298
Ank_4 pfam13637
Ankyrin repeats (many copies);
184-237 1.20e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 1.20e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 255982572  184 GWNSLHQASFQENAEIIKLLLRKGANKECQDDFGITPLFVAAQYGKLESLSILI 237
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SOCS_SSB2 cd03719
SOCS (suppressors of cytokine signaling) box of SSB2 (SPRY domain-containing SOCS box proteins) ...
499-539 1.49e-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: 39.23  E-value: 1.49e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 255982572 499 SLTHLCRLEIRSSLKSERLrsdSYISQLPLPRSLHNYLLYE 539
Cdd:cd03719    5 SLLHLSRLCVRHALGDTRL---GQVSALPLPPAMKRYLLYQ 42
Ank_5 pfam13857
Ankyrin repeats (many copies);
116-157 2.09e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 39.25  E-value: 2.09e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 255982572  116 EGFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFLA 157
Cdd:pfam13857  15 EGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
288-338 2.28e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 2.28e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 255982572  288 PIHAAAQMGHTKILDLLIPLTNRACDTGLNKVSPVYSAVFGGHEDCLEILL 338
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
83-250 2.37e-04

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: 44.10  E-value: 2.37e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  83 MPIHEAAyhNSVECLQMLINADSSENYikmktFEGFCALHLAASQGHWKIVQILLEAGAD----PNATTLEETT------ 152
Cdd:cd21882   46 MLLLEAA--PDSGNPKELVNAPCTDEF-----YQGQTALHIAIENRNLNLVRLLVENGADvsarATGRFFRKSPgnlfyf 118
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 153 ---PLFLAVENGQIDVLRLLLQHGANVNGSHSM--CGWNSLHQASFQEN---------AEIIKLLLRKGAN-------KE 211
Cdd:cd21882  119 gelPLSLAACTNQEEIVRLLLENGAQPAALEAQdsLGNTVLHALVLQADntpensafvCQMYNLLLSYGAHldptqqlEE 198
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 255982572 212 CQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDK 250
Cdd:cd21882  199 IPNHQGLTPLKLAAVEGKIVMFQHILQREFSGPYQPLSR 237
SOCS_WSB2_SWIP2 cd03745
SOCS (suppressors of cytokine signaling) box of WSB2/SWiP2-like proteins. This family consists ...
496-538 2.75e-04

SOCS (suppressors of cytokine signaling) box of WSB2/SWiP2-like proteins. This family consists of WSB-2 (SOCS-box-containing WD-40 protein) and SWiP-2 (SOCS box and WD-repeats in Protein). No functional information is available for WSB2 or SWiP-2, but limited information is available for the isoforms WSB-1 and SWiP-1. 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: 239714  Cd Length: 39  Bit Score: 38.72  E-value: 2.75e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 255982572 496 TVPSLTHLCRLEIRSSLKSERlrsdsyISQLPLPRSLHNYLLY 538
Cdd:cd03745    2 VLPSLRHLCRKALRHFLTTYQ------VLALPIPKKMKEFLTY 38
SOCS_WSB1_SWIP1 cd03746
SOCS (suppressors of cytokine signaling) box of WSB1/SWiP1-like proteins. This subfamily ...
497-539 2.78e-04

SOCS (suppressors of cytokine signaling) box of WSB1/SWiP1-like proteins. This subfamily contains WSB-1 (SOCS-box-containing WD-40 protein), part of an E3 ubiquitin ligase for the thyroid-hormone-activating type 2 iodothyronine deiodinase (D2) and SWiP-1 (SOCS box and WD-repeats in Protein), a WD40-containing protein that is expressed in embryonic structures of chickens and regulated by Sonic Hedgehog (Shh). 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: 239715  Cd Length: 40  Bit Score: 38.64  E-value: 2.78e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|...
gi 255982572 497 VPSLTHLCRLEIRsslkseRLRSDSYISQLPLPRSLHNYLLYE 539
Cdd:cd03746    3 VASLQHLCRMAIR------RVMPTQQVKELPIPSKLLEFLTYR 39
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
500-540 4.63e-04

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: 37.92  E-value: 4.63e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 255982572 500 LTHLCRLEIRSSLKSERLRsdsYISQLPLPRSLHNYLLYED 540
Cdd:cd03721    6 LAHLCRLKVRTLIGINRIK---LIDTLPLPPRLIRYLNHQE 43
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
98-231 5.09e-04

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 42.92  E-value: 5.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  98 QMLINADSSENYikmktFEGFCALHLAASQGHWKIVQILLEAGADPNATTLEE-------------TTPLFLAVENGQID 164
Cdd:cd22197   80 KPLVNAQCTDEY-----YRGHSALHIAIEKRSLQCVKLLVENGADVHARACGRffqkkqgtcfyfgELPLSLAACTKQWD 154
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 165 VLRLLLQHG---ANVNGSHSMcGWNSLHQASF-----QENAEI-IKL---LLRKGAN-------KECQDDFGITPLFVAA 225
Cdd:cd22197  155 VVNYLLENPhqpASLQAQDSL-GNTVLHALVMiadnsPENSALvIKMydgLLQAGARlcptvqlEEISNHEGLTPLKLAA 233

                 ....*.
gi 255982572 226 QYGKLE 231
Cdd:cd22197  234 KEGKIE 239
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
152-177 5.35e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 37.62  E-value: 5.35e-04
                          10        20
                  ....*....|....*....|....*.
gi 255982572  152 TPLFLAVENGQIDVLRLLLQHGANVN 177
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADIN 29
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
249-278 5.89e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 5.89e-04
                           10        20        30
                   ....*....|....*....|....*....|
gi 255982572   249 DKATPLFIAAQEGHTKCVELLLSSGADPDL 278
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
SOCS_ASB5 cd03724
SOCS (suppressors of cytokine signaling) box of ASB5-like proteins. ASB family members have a ...
495-538 6.36e-04

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


Pssm-ID: 239694  Cd Length: 42  Bit Score: 37.55  E-value: 6.36e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....
gi 255982572 495 ATVPSLTHLCRLEIRSSLKSERLRsdsYISQLPLPRSLHNYLLY 538
Cdd:cd03724    1 ATPSSLCQLCRLCIRNYIGRSRLH---LIPQLQLPTLLKNFLQY 41
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
120-145 6.44e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 37.18  E-value: 6.44e-04
                           10        20
                   ....*....|....*....|....*.
gi 255982572   120 ALHLAASQGHWKIVQILLEAGADPNA 145
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
47-154 7.13e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 42.29  E-value: 7.13e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  47 DTCSTVGLAAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAYHNSVECLQMLINADSSENYIKMKTfeGFCALHLAAS 126
Cdd:PHA02875 134 DKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNG--CVAALCYAIE 211
                         90       100       110
                 ....*....|....*....|....*....|.
gi 255982572 127 QGHWKIVQILLEAGADPNATTL---EETTPL 154
Cdd:PHA02875 212 NNKIDIVRLFIKRGADCNIMFMiegEECTIL 242
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
152-177 7.70e-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: 37.27  E-value: 7.70e-04
                          10        20
                  ....*....|....*....|....*..
gi 255982572  152 TPLFLAV-ENGQIDVLRLLLQHGANVN 177
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVN 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
252-278 7.93e-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: 7.93e-04
                          10        20
                  ....*....|....*....|....*...
gi 255982572  252 TPLFIAA-QEGHTKCVELLLSSGADPDL 278
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVNA 31
SOCS_CIS1 cd03734
SOCS (suppressors of cytokine signaling) box of CIS (cytokine-inducible SH2 protein) 1-like ...
496-536 8.18e-04

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


Pssm-ID: 239703  Cd Length: 41  Bit Score: 37.25  E-value: 8.18e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 255982572 496 TVPSLTHLCRLEIrsslksERLRSDsyISQLPLPRSLHNYL 536
Cdd:cd03734    2 SARSLQHLCRLVI------NRLVTD--VDCLPLPRRMADYL 34
PHA02859 PHA02859
ankyrin repeat protein; Provisional
152-242 1.23e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.57  E-value: 1.23e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 152 TPLFLAVENGQI--DVLRLLLQHGANVNGSHSMCGWNSLHQ-ASFQENA--EIIKLLLRKGANKECQDDFGITPL--FVA 224
Cdd:PHA02859  53 TPIFSCLEKDKVnvEILKFLIENGADVNFKTRDNNLSALHHyLSFNKNVepEILKILIDSGSSITEEDEDGKNLLhmYMC 132
                         90
                 ....*....|....*...
gi 255982572 225 AQYGKLESLSILISSGAN 242
Cdd:PHA02859 133 NFNVRINVIKLLIDSGVS 150
SOCS_ASB1 cd03720
SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a ...
499-539 1.35e-03

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


Pssm-ID: 239690  Cd Length: 42  Bit Score: 36.63  E-value: 1.35e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|.
gi 255982572 499 SLTHLCRLEIRSSLKSERLrsdSYISQLPLPRSLHNYLLYE 539
Cdd:cd03720    5 SLLSLCRIAVRRALGKQRL---SLICSLPLPDPIKKFLLHE 42
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
116-145 1.76e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.08  E-value: 1.76e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 255982572  116 EGFCALHLAASQGHWKIVQILLEAGADPNA 145
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
226-278 2.66e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 40.43  E-value: 2.66e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|...
gi 255982572 226 QYGKLESLSILISSGANVNCQALDKATPLFIAAQEGHTKCVELLLSSGADPDL 278
Cdd:PHA02876 154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNI 206
Ank_4 pfam13637
Ankyrin repeats (many copies);
84-137 2.75e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 2.75e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 255982572   84 PIHEAAYHNSVECLQMLINADSSENyikMKTFEGFCALHLAASQGHWKIVQILL 137
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADIN---AVDGNGETALHFAASNGNVEVLKLLL 54
SOCS_ASB8 cd03727
SOCS (suppressors of cytokine signaling) box of ASB8-like proteins. ASB family members have a ...
498-537 3.14e-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: 35.58  E-value: 3.14e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|
gi 255982572 498 PSLTHLCRLEIRSSLkSERLRSDSyISQLPLPRSLHNYLL 537
Cdd:cd03727    4 GTLKALARYAVRRSL-GVQYLPEA-VKQLPLPRSVKEYLL 41
PHA02736 PHA02736
Viral ankyrin protein; Provisional
163-241 3.29e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 38.32  E-value: 3.29e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 163 IDVLRLLLQHGANVNGSHSMCGWNSLHQASFQENAEIIKLLLRK-GANKECQDDFGITPLFVAAQYGKLESLSILISSGA 241
Cdd:PHA02736  71 QEKLKLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
217-245 3.42e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 35.26  E-value: 3.42e-03
                           10        20
                   ....*....|....*....|....*....
gi 255982572   217 GITPLFVAAQYGKLESLSILISSGANVNC 245
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
258-339 5.55e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.50  E-value: 5.55e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 258 AQEGHTKCVELLLSSGADPDlyCNEDSWQLPIHAAAQMGHTKILDLLIPLTNRACDTGLNKVSPVYSAVFGGHEDCLEIL 337
Cdd:PTZ00322  90 AASGDAVGARILLTGGADPN--CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167

                 ..
gi 255982572 338 LR 339
Cdd:PTZ00322 168 SR 169
PHA02791 PHA02791
ankyrin-like protein; Provisional
77-204 6.42e-03

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 38.87  E-value: 6.42e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  77 ADNRGWMPIHEAAYHNSVECLQMLINADSSENYIkmktfEGFCALHLAASQGHWKIVQILLEAGADPNATTLEETTPLFL 156
Cdd:PHA02791  26 ADVHGHSALYYAIADNNVRLVCTLLNAGALKNLL-----ENEFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYY 100
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*....
gi 255982572 157 AVENGQIDVLRLLLQHGANVNgSHSMCGW-NSLHQASFQENAEIIKLLL 204
Cdd:PHA02791 101 AVDSGNMQTVKLFVKKNWRLM-FYGKTGWkTSFYHAVMLNDVSIVSYFL 148
PHA02876 PHA02876
ankyrin repeat protein; Provisional
55-179 7.66e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.28  E-value: 7.66e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  55 AAREGNVKVLRKLLKKGRSVDVADNRGWMPIHEAAY-HNSVECLQMLI----NADSSENYIKMktfegfcALHLAASQG- 128
Cdd:PHA02876 382 AAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCgTNPYMSVKTLIdrgaNVNSKNKDLST-------PLHYACKKNc 454
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|.
gi 255982572 129 HWKIVQILLEAGADPNATTLEETTPLFLAVENGQIdvLRLLLQHGANVNGS 179
Cdd:PHA02876 455 KLDVIEMLLDNGADVNAINIQNQYPLLIALEYHGI--VNILLHYGAELRDS 503
PHA02946 PHA02946
ankyin-like protein; Provisional
144-255 8.43e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.88  E-value: 8.43e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572 144 NATTLEETTPLFLAVENGQIDVLRLLLQH---GANVNGSHSMCGWNSLHQASFQEnaeiiklLLRKGANKECQDDFGITP 220
Cdd:PHA02946   3 NIMSAEYYLSLYAKYNSKNLDVFRNMLQAiepSGNYHILHAYCGIKGLDERFVEE-------LLHRGYSPNETDDDGNYP 75
                         90       100       110
                 ....*....|....*....|....*....|....*
gi 255982572 221 LFVAAQYGKLESLSILISSGANVNCQALDKATPLF 255
Cdd:PHA02946  76 LHIASKINNNRIVAMLLTHGADPNACDKQHKTPLY 110
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
30-219 8.80e-03

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: 38.91  E-value: 8.80e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572   30 RPPGRLVKQMDFTeaYADTCSTVGLAAREGNVKVLRKLLKKGRS--VDVADNRGWMPIHEAAYHNSVECLQMLINADSSE 107
Cdd:TIGR00870   1 RGPLDIVPAEESP--LSDEEKAFLPAAERGDLASVYRDLEEPKKlnINCPDRLGRSALFVAAIENENLELTELLLNLSCR 78
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 255982572  108 NYIkmktfeGFCALHlAASQGHWKIVQ--ILLEAGADPNATTLEET------------TPLFLAVENGQIDVLRLLLQHG 173
Cdd:TIGR00870  79 GAV------GDTLLH-AISLEYVDAVEaiLLHLLAAFRKSGPLELAndqytseftpgiTALHLAAHRQNYEIVKLLLERG 151
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 255982572  174 ANVN----------GSHSMCGWNSLHQASFQE---NAEIIKLLLRKGANKECQDDFGIT 219
Cdd:TIGR00870 152 ASVParacgdffvkSQGVDSFYHGESPLNAAAclgSPSIVALLSEDPADILTADSLGNT 210
 
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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