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Conserved domains on  [gi|2079055816|ref|XP_042788194|]
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ankyrin repeat and SOCS box protein 3 isoform X1 [Panthera leo]

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];
16-269 2.33e-49

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.68  E-value: 2.33e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  16 LAAREGNVKVLRKLLRKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIHADsseNYIKTKTFEGFCALHLAASQGHWKIV 95
Cdd:COG0666    27 AAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAG---ADINAKDDGGNTLLHAAARNGDLEIV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  96 HILLEAGADPNATTSEETTPLFLAVENGHIDVLRLLLRYGANVNGSHSMcGWNALHQATFQENGEIIKLLLKKGADKECQ 175
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNAR 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 176 DDFGITPLFVAAQYGKLESLSILISSGANVNCQALDEATPLFIAAQEGHTECVELLLSSGADPDLYCNEDDwqLPIHAAA 255
Cdd:COG0666   183 DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGL--TALLLAA 260
                         250
                  ....*....|....
gi 2079055816 256 QMGHTEILELLIPL 269
Cdd:COG0666   261 AAGAALIVKLLLLA 274
SOCS_ASB3 cd03722
SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a ...
459-509 6.38e-24

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: 94.47  E-value: 6.38e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2079055816 459 ACLPSLTHLCRLEIRSCLKPEHLRSDSFICQLPLPRSLHNYLLYAEVLRMN 509
Cdd:cd03722     1 ASVPSLTHLCRLEIRSSLKSERLRSDSFICQLPLPRSLQDYLLYSDVLRMY 51
PHA03100 super family cl39094
ankyrin repeat protein; Provisional
160-405 1.75e-11

ankyrin repeat protein; Provisional


The actual alignment was detected with superfamily member PHA03100:

Pssm-ID: 476869 [Multi-domain]  Cd Length: 422  Bit Score: 66.23  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 160 EIIKLLLKKGADKECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDEATPLFIAAQEGHT-----ECVELLLSS 234
Cdd:PHA03100   16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEY 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 235 GADPDLYCNEDDWQLPIHAAAQMGHTEILELLIPLTNRVCDTGPDKVSPVYSAVFGGHE--ECLEMLLQHGYSPDAqmcl 312
Cdd:PHA03100   96 GANVNAPDNNGITPLLYAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINA---- 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 313 ifgfsspmcmafqKESceffgiVNILLKYGAQLNE--------LHLAycLKYEKFLVFRYFLKKGCPLapwNHISEF--- 381
Cdd:PHA03100  172 -------------KNR------VNYLLSYGVPINIkdvygftpLHYA--VYNNNPEFVKYLLDLGANP---NLVNKYgdt 227
                         250       260
                  ....*....|....*....|....*
gi 2079055816 382 -ISHAIKaqTTYKEWLPSLLLAGFD 405
Cdd:PHA03100  228 pLHIAIL--NNNKEIFKLLLNNGPS 250
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
16-269 2.33e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.68  E-value: 2.33e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  16 LAAREGNVKVLRKLLRKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIHADsseNYIKTKTFEGFCALHLAASQGHWKIV 95
Cdd:COG0666    27 AAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAG---ADINAKDDGGNTLLHAAARNGDLEIV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  96 HILLEAGADPNATTSEETTPLFLAVENGHIDVLRLLLRYGANVNGSHSMcGWNALHQATFQENGEIIKLLLKKGADKECQ 175
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNAR 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 176 DDFGITPLFVAAQYGKLESLSILISSGANVNCQALDEATPLFIAAQEGHTECVELLLSSGADPDLYCNEDDwqLPIHAAA 255
Cdd:COG0666   183 DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGL--TALLLAA 260
                         250
                  ....*....|....
gi 2079055816 256 QMGHTEILELLIPL 269
Cdd:COG0666   261 AAGAALIVKLLLLA 274
SOCS_ASB3 cd03722
SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a ...
459-509 6.38e-24

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: 94.47  E-value: 6.38e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2079055816 459 ACLPSLTHLCRLEIRSCLKPEHLRSDSFICQLPLPRSLHNYLLYAEVLRMN 509
Cdd:cd03722     1 ASVPSLTHLCRLEIRSSLKSERLRSDSFICQLPLPRSLQDYLLYSDVLRMY 51
PHA03100 PHA03100
ankyrin repeat protein; Provisional
22-237 4.80e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 101.28  E-value: 4.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  22 NVKVLRKLLRKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIhaDSSENyIKTKTFEGFCALHLAASQGH-----WKIVH 96
Cdd:PHA03100   14 KVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILL--DNGAD-INSSTKNNSTPLHYLSNIKYnltdvKEIVK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  97 ILLEAGADPNATTSEETTPLFLAVEN--GHIDVLRLLLRYGANVNgSHSMCGWNALHQATFQ--ENGEIIKLLLKKGAD- 171
Cdd:PHA03100   91 LLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVN-IKNSDGENLLHLYLESnkIDLKILKLLIDKGVDi 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 172 -KECQ--------------DDFGITPLFVAAQYGKLESLSILISSGANVNCQALDEATPLFIAAQEGHTECVELLLSSGA 236
Cdd:PHA03100  170 nAKNRvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249

                  .
gi 2079055816 237 D 237
Cdd:PHA03100  250 S 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
83-176 1.99e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 1.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  83 LHLAASQGHWKIVHILLEAGADPNATTSEETTPLFLAVENGHIDVLRLLLRYganVNGSHSMCGWNALHQATFQENGEII 162
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 2079055816 163 KLLLKKGADKECQD 176
Cdd:pfam12796  78 KLLLEKGADINVKD 91
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
42-234 3.08e-16

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: 81.60  E-value: 3.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  42 RGW-MPIHEAAYHNSVECLRMLIHADSSENYikTKTFEGFCALHLAASQGHWKIVHILLEAgaDP----NATTSE---ET 113
Cdd:cd22192    15 RISeSPLLLAAKENDVQAIKKLLKCPSCDLF--QRGALGETALHVAALYDNLEAAVVLMEA--APelvnEPMTSDlyqGE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 114 TPLFLAVENGHIDVLRLLLRYGANVN-----------GSHSMC--GWNALHQATFQENGEIIKLLLKKGADKECQDDFGI 180
Cdd:cd22192    91 TALHIAVVNQNLNLVRELIARGADVVspratgtffrpGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2079055816 181 TPLFV-AAQYGKL---ESLSILISSGANVNCQALDEA------TPLFIAAQEGHTECVELLLSS 234
Cdd:cd22192   171 TVLHIlVLQPNKTfacQMYDLILSYDKEDDLQPLDLVpnnqglTPFKLAAKEGNIVMFQHLVQK 234
PHA03100 PHA03100
ankyrin repeat protein; Provisional
160-405 1.75e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.23  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 160 EIIKLLLKKGADKECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDEATPLFIAAQEGHT-----ECVELLLSS 234
Cdd:PHA03100   16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEY 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 235 GADPDLYCNEDDWQLPIHAAAQMGHTEILELLIPLTNRVCDTGPDKVSPVYSAVFGGHE--ECLEMLLQHGYSPDAqmcl 312
Cdd:PHA03100   96 GANVNAPDNNGITPLLYAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINA---- 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 313 ifgfsspmcmafqKESceffgiVNILLKYGAQLNE--------LHLAycLKYEKFLVFRYFLKKGCPLapwNHISEF--- 381
Cdd:PHA03100  172 -------------KNR------VNYLLSYGVPINIkdvygftpLHYA--VYNNNPEFVKYLLDLGANP---NLVNKYgdt 227
                         250       260
                  ....*....|....*....|....*
gi 2079055816 382 -ISHAIKaqTTYKEWLPSLLLAGFD 405
Cdd:PHA03100  228 pLHIAIL--NNNKEIFKLLLNNGPS 250
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
462-501 2.83e-10

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


Pssm-ID: 462192  Cd Length: 39  Bit Score: 55.25  E-value: 2.83e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2079055816 462 PSLTHLCRLEIRSCLKPehlRSDSFICQLPLPRSLHNYLL 501
Cdd:pfam07525   3 RSLQHLCRLAIRRALGK---RRLGAIDKLPLPPLLKDYLL 39
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
462-502 2.64e-09

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: 52.41  E-value: 2.64e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2079055816  462 PSLTHLCRLEIRSCLKpehlrsdsFICQLPLPRSLHNYLLY 502
Cdd:smart00969   1 RSLQHLCRLAIRRSLG--------GIDKLPLPPRLKDYLLY 33
Ank_2 pfam12796
Ankyrin repeats (3 copies);
251-346 7.18e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.42  E-value: 7.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 251 IHAAAQMGHTEILELLIPLTNRVCDTGPDKVSPVYSAVFGGHEECLEMLLQHgysPDAQMCLifGFSSPMCMAFQKESCE 330
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKD--NGRTALHYAARSGHLE 75
                          90
                  ....*....|....*.
gi 2079055816 331 ffgIVNILLKYGAQLN 346
Cdd:pfam12796  76 ---IVKLLLEKGADIN 88
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
114-139 5.60e-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: 42.96  E-value: 5.60e-06
                           10        20
                   ....*....|....*....|....*.
gi 2079055816  114 TPLFLAVENGHIDVLRLLLRYGANVN 139
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
16-151 2.99e-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: 47.00  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  16 LAAREGNVKVLRKLLR-KGRSVDVADNRgwmpIHEAA--YHNSVE-CLRMLIHADSSE------NYIKTKTF-EGFCALH 84
Cdd:TIGR00870  58 VAAIENENLELTELLLnLSCRGAVGDTL----LHAISleYVDAVEaILLHLLAAFRKSgplelaNDQYTSEFtPGITALH 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  85 LAASQGHWKIVHILLEAGADPNAT-------TSEETT-------PLFLAVENGHIDVLRLLLRYGANVNGSHSMcGWNAL 150
Cdd:TIGR00870 134 LAAHRQNYEIVKLLLERGASVPARacgdffvKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSL-GNTLL 212

                  .
gi 2079055816 151 H 151
Cdd:TIGR00870 213 H 213
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
16-269 2.33e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.68  E-value: 2.33e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  16 LAAREGNVKVLRKLLRKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIHADsseNYIKTKTFEGFCALHLAASQGHWKIV 95
Cdd:COG0666    27 AAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAG---ADINAKDDGGNTLLHAAARNGDLEIV 103
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  96 HILLEAGADPNATTSEETTPLFLAVENGHIDVLRLLLRYGANVNGSHSMcGWNALHQATFQENGEIIKLLLKKGADKECQ 175
Cdd:COG0666   104 KLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDND-GNTPLHLAAANGNLEIVKLLLEAGADVNAR 182
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 176 DDFGITPLFVAAQYGKLESLSILISSGANVNCQALDEATPLFIAAQEGHTECVELLLSSGADPDLYCNEDDwqLPIHAAA 255
Cdd:COG0666   183 DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGL--TALLLAA 260
                         250
                  ....*....|....
gi 2079055816 256 QMGHTEILELLIPL 269
Cdd:COG0666   261 AAGAALIVKLLLLA 274
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
26-303 2.41e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.68  E-value: 2.41e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  26 LRKLLRKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIHADSSENYIKTKTFEGFCALHLAASQGHWKIVHILLEAGADP 105
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 106 NATTSEETTPLFLAVENGHIDVLRLLLRYGANVNgSHSMCGWNALHQATFQENGEIIKLLLKKGADKECQDDFGITPLFV 185
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVN-ARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 186 AAQYGKLESLSILISSGANVNCQALDEATPLFIAAQEGHTECVELLLSSGADPDLYCNEDDWqlPIHAAAQMGHTEILEL 265
Cdd:COG0666   160 AAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKT--ALDLAAENGNLEIVKL 237
                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 2079055816 266 LIPLTNRVCDTGPDKVSPVYSAVFGGHEECLEMLLQHG 303
Cdd:COG0666   238 LLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLAL 275
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
16-249 3.26e-49

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 171.29  E-value: 3.26e-49
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  16 LAAREGNVKVLRKLLRKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIHADSSenyIKTKTFEGFCALHLAASQGHWKIV 95
Cdd:COG0666    60 AAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGAD---VNARDKDGETPLHLAAYNGNLEIV 136
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  96 HILLEAGADPNATTSEETTPLFLAVENGHIDVLRLLLRYGANVNGSHSMcGWNALHQATFQENGEIIKLLLKKGADKECQ 175
Cdd:COG0666   137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDND-GETPLHLAAENGHLEIVKLLLEAGADVNAK 215
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2079055816 176 DDFGITPLFVAAQYGKLESLSILISSGANVNCQALDEATPLFIAAQEGHTECVELLLSSGADPDLYCNEDDWQL 249
Cdd:COG0666   216 DNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
94-346 5.93e-31

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 121.60  E-value: 5.93e-31
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  94 IVHILLEAGADPNATTSEETTPLFLAVENGHIDVLRLLLRYGANVNGSHSMCGWNALHQATFQENGEIIKLLLKKGADKE 173
Cdd:COG0666     2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADIN 81
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 174 CQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDEATPLFIAAQEGHTECVELLLSSGADPDLycNEDDWQLPIHA 253
Cdd:COG0666    82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNA--QDNDGNTPLHL 159
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 254 AAQMGHTEILELLIpltNRVCD---TGPDKVSPVYSAVFGGHEECLEMLLQHGYSPDAQMCLifgFSSPMCMAFQKESce 330
Cdd:COG0666   160 AAANGNLEIVKLLL---EAGADvnaRDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDND---GKTALDLAAENGN-- 231
                         250
                  ....*....|....*.
gi 2079055816 331 fFGIVNILLKYGAQLN 346
Cdd:COG0666   232 -LEIVKLLLEAGADLN 246
SOCS_ASB3 cd03722
SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a ...
459-509 6.38e-24

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: 94.47  E-value: 6.38e-24
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2079055816 459 ACLPSLTHLCRLEIRSCLKPEHLRSDSFICQLPLPRSLHNYLLYAEVLRMN 509
Cdd:cd03722     1 ASVPSLTHLCRLEIRSSLKSERLRSDSFICQLPLPRSLQDYLLYSDVLRMY 51
PHA03100 PHA03100
ankyrin repeat protein; Provisional
22-237 4.80e-23

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 101.28  E-value: 4.80e-23
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  22 NVKVLRKLLRKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIhaDSSENyIKTKTFEGFCALHLAASQGH-----WKIVH 96
Cdd:PHA03100   14 KVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILL--DNGAD-INSSTKNNSTPLHYLSNIKYnltdvKEIVK 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  97 ILLEAGADPNATTSEETTPLFLAVEN--GHIDVLRLLLRYGANVNgSHSMCGWNALHQATFQ--ENGEIIKLLLKKGAD- 171
Cdd:PHA03100   91 LLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLDNGANVN-IKNSDGENLLHLYLESnkIDLKILKLLIDKGVDi 169
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 172 -KECQ--------------DDFGITPLFVAAQYGKLESLSILISSGANVNCQALDEATPLFIAAQEGHTECVELLLSSGA 236
Cdd:PHA03100  170 nAKNRvnyllsygvpinikDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGP 249

                  .
gi 2079055816 237 D 237
Cdd:PHA03100  250 S 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
83-176 1.99e-22

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 91.33  E-value: 1.99e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  83 LHLAASQGHWKIVHILLEAGADPNATTSEETTPLFLAVENGHIDVLRLLLRYganVNGSHSMCGWNALHQATFQENGEII 162
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 2079055816 163 KLLLKKGADKECQD 176
Cdd:pfam12796  78 KLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
150-240 3.23e-21

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 88.25  E-value: 3.23e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 150 LHQATFQENGEIIKLLLKKGADKECQDDFGITPLFVAAQYGKLESLSILISSgANVNCQaLDEATPLFIAAQEGHTECVE 229
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|.
gi 2079055816 230 LLLSSGADPDL 240
Cdd:pfam12796  79 LLLEKGADINV 89
PHA03095 PHA03095
ankyrin-like protein; Provisional
23-241 1.66e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 94.32  E-value: 1.66e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  23 VKVLRKLLRKGRSVDVADNRGWMPIHEAAYHNSVE-CLRMLIHADSSENYiktKTFEGFCALH--LAASQGHWKIVHILL 99
Cdd:PHA03095   63 KDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNA---KDKVGRTPLHvyLSGFNINPKVIRLLL 139
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 100 EAGADPNATTSEETTPLFLAVENGHIDV--LRLLLRYGANVNGShSMCGWNALHQ--ATFQENGEIIKLLLKKGADKECQ 175
Cdd:PHA03095  140 RKGADVNALDLYGMTPLAVLLKSRNANVelLRLLIDAGADVYAV-DDRFRSLLHHhlQSFKPRARIVRELIRAGCDPAAT 218
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2079055816 176 DDFGITPLFVAAQYGKLESLSI--LISSGANVNCQALDEATPLFIAAQEGHTECVELLLSSGADPDLY 241
Cdd:PHA03095  219 DMLGNTPLHSMATGSSCKRSLVlpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAV 286
PHA03095 PHA03095
ankyrin-like protein; Provisional
49-370 3.75e-20

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 93.17  E-value: 3.75e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  49 EAAYHNSVECLRMLIHADSSENYikTKTFeGFCALHLAASQGHWK---IVHILLEAGADPNATTSEETTPLFLAVENGH- 124
Cdd:PHA03095   20 LNASNVTVEEVRRLLAAGADVNF--RGEY-GKTPLHLYLHYSSEKvkdIVRLLLEAGADVNAPERCGFTPLHLYLYNATt 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 125 IDVLRLLLRYGANVNGSHSmCGWNALHQ--ATFQENGEIIKLLLKKGADKECQDDFGITPLFVaaqygkleslsILISSG 202
Cdd:PHA03095   97 LDVIKLLIKAGADVNAKDK-VGRTPLHVylSGFNINPKVIRLLLRKGADVNALDLYGMTPLAV-----------LLKSRN 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 203 ANVncqaldeatplfiaaqeghtECVELLLSSGADPdlYCNEDDWQLPIHAAAQMGHTeilellipltnrvcdtgpdkvs 282
Cdd:PHA03095  165 ANV--------------------ELLRLLIDAGADV--YAVDDRFRSLLHHHLQSFKP---------------------- 200
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 283 pvysavfggHEECLEMLLQHGYSPDAQMCLifgFSSPMCMAFQKESCEFFGIVNILLKyGAQLNE--------LHLAYCl 354
Cdd:PHA03095  201 ---------RARIVRELIRAGCDPAATDML---GNTPLHSMATGSSCKRSLVLPLLIA-GISINArnrygqtpLHYAAV- 266
                         330
                  ....*....|....*.
gi 2079055816 355 kYEKFLVFRYFLKKGC 370
Cdd:PHA03095  267 -FNNPRACRRLIALGA 281
PHA02875 PHA02875
ankyrin repeat protein; Provisional
21-240 2.31e-19

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 90.44  E-value: 2.31e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  21 GNVKVLRKLLRKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIHADSSENYiKTKTFEGfcALHLAASQGHWKIVHILLE 100
Cdd:PHA02875   13 GELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDV-KYPDIES--ELHDAVEEGDVKAVEELLD 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 101 AGADPNATTSEE-TTPLFLAVENGHIDVLRLLLRYGANVNGShSMCGWNALHQATFQENGEIIKLLLKKGADKECQDDFG 179
Cdd:PHA02875   90 LGKFADDVFYKDgMTPLHLATILKKLDIMKLLIARGADPDIP-NTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2079055816 180 ITPLFVAAQYGKLESLSILISSGANVNCQALD-EATPLFIAAQEGHTECVELLLSSGADPDL 240
Cdd:PHA02875  169 CTPLIIAMAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLFIKRGADCNI 230
PHA03100 PHA03100
ankyrin repeat protein; Provisional
22-206 2.20e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 87.41  E-value: 2.20e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  22 NVKVLRKLLRKGRSVD--VADNRGWMPIHEAAYHNS---VECLRMLIhadSSENYIKTKTFEGFCALHLAASQ--GHWKI 94
Cdd:PHA03100   47 NIDVVKILLDNGADINssTKNNSTPLHYLSNIKYNLtdvKEIVKLLL---EYGANVNAPDNNGITPLLYAISKksNSYSI 123
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  95 VHILLEAGADPNATTSEETTPLFLAVENGHID--VLRLLLRYGANVN-----------GSH----SMCGWNALHQATFQE 157
Cdd:PHA03100  124 VEYLLDNGANVNIKNSDGENLLHLYLESNKIDlkILKLLIDKGVDINaknrvnyllsyGVPinikDVYGFTPLHYAVYNN 203
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*....
gi 2079055816 158 NGEIIKLLLKKGADKECQDDFGITPLFVAAQYGKLESLSILISSGANVN 206
Cdd:PHA03100  204 NPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIK 252
Ank_2 pfam12796
Ankyrin repeats (3 copies);
116-208 1.77e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 1.77e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 116 LFLAVENGHIDVLRLLLRYGANVNgSHSMCGWNALHQATFQENGEIIKLLLKKgADKECQDDfGITPLFVAAQYGKLESL 195
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN-LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIV 77
                          90
                  ....*....|...
gi 2079055816 196 SILISSGANVNCQ 208
Cdd:pfam12796  78 KLLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
16-108 2.09e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.08  E-value: 2.09e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  16 LAAREGNVKVLRKLLRKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIhadssENYIKTKTFEGFCALHLAASQGHWKIV 95
Cdd:pfam12796   3 LAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-----EHADVNLKDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|...
gi 2079055816  96 HILLEAGADPNAT 108
Cdd:pfam12796  78 KLLLEKGADINVK 90
PHA02876 PHA02876
ankyrin repeat protein; Provisional
83-398 3.53e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 84.73  E-value: 3.53e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  83 LHLAASQGHWKIVHILLEAGADPNATTSEETTPLFLAVENGHIDVLRLLLRYGANVNGSHSmcgwnALHQATFQENGEII 162
Cdd:PHA02876  182 IHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNDL-----SLLKAIRNEDLETS 256
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 163 KLLLKKGADKECQDDFGITPLFVAAQYGKLESL-SILISSGANVNCQALDEATPLFIAAQEGH-TECVELLLSSGADPD- 239
Cdd:PHA02876  257 LLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYdTENIRTLIMLGADVNa 336
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 240 ---LY--------------------------CNEDDW--QLPIHAAAQMGHTEILELLI-------PLTNRV-------- 273
Cdd:PHA02876  337 adrLYitplhqastldrnkdivitllelganVNARDYcdKTPIHYAAVRNNVVIINTLLdygadieALSQKIgtalhfal 416
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 274 CDTGP-------------------DKVSPV-YSAVFGGHEECLEMLLQHGYSPDAqmcLIFGFSSPMCMAFqkescEFFG 333
Cdd:PHA02876  417 CGTNPymsvktlidrganvnsknkDLSTPLhYACKKNCKLDVIEMLLDNGADVNA---INIQNQYPLLIAL-----EYHG 488
                         330       340       350       360       370       380
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2079055816 334 IVNILLKYGAQLNELHLAYCLKYEKFLVFRYFLKKGCplapwnhISEFISHAIKAQTTYKEWLPS 398
Cdd:PHA02876  489 IVNILLHYGAELRDSRVLHKSLNDNMFSFRYIIAHIC-------IQDFIRHDIRNEVNPLKRVPT 546
PHA02874 PHA02874
ankyrin repeat protein; Provisional
17-256 5.29e-17

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 83.47  E-value: 5.29e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  17 AAREGNVKVLRKLLRKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIhadssENYIKTKTFEGFCAlhlaasqgHWKIVH 96
Cdd:PHA02874   42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI-----DNGVDTSILPIPCI--------EKDMIK 108
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  97 ILLEAGADPNATTSEETTPLFLAVENGHIDVLRLLLRYGANVNgSHSMCGWNALHQATFQENGEIIKLLLKKGADKECQD 176
Cdd:PHA02874  109 TILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVN-IEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 177 DFGITPLFVAAQYGKLESLSILISSGANVNCQALDEATPLFIAAQEGHTeCVELLLSSGA--DPDLycnedDWQLPIHAA 254
Cdd:PHA02874  188 NNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNRS-AIELLINNASinDQDI-----DGSTPLHHA 261

                  ..
gi 2079055816 255 AQ 256
Cdd:PHA02874  262 IN 263
Ank_2 pfam12796
Ankyrin repeats (3 copies);
183-267 1.04e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 75.15  E-value: 1.04e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 183 LFVAAQYGKLESLSILISSGANVNCQALDEATPLFIAAQEGHTECVELLLSSgADPDLYCNEddwQLPIHAAAQMGHTEI 262
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNG---RTALHYAARSGHLEI 76

                  ....*
gi 2079055816 263 LELLI 267
Cdd:pfam12796  77 VKLLL 81
Ank_2 pfam12796
Ankyrin repeats (3 copies);
216-309 1.37e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.77  E-value: 1.37e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 216 LFIAAQEGHTECVELLLSSGADPDlyCNEDDWQLPIHAAAQMGHTEILELLIPLTNrvCDTGPDKVSPVYSAVFGGHEEC 295
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN--LQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNGRTALHYAARSGHLEI 76
                          90
                  ....*....|....
gi 2079055816 296 LEMLLQHGYSPDAQ 309
Cdd:pfam12796  77 VKLLLEKGADINVK 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
42-234 3.08e-16

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: 81.60  E-value: 3.08e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  42 RGW-MPIHEAAYHNSVECLRMLIHADSSENYikTKTFEGFCALHLAASQGHWKIVHILLEAgaDP----NATTSE---ET 113
Cdd:cd22192    15 RISeSPLLLAAKENDVQAIKKLLKCPSCDLF--QRGALGETALHVAALYDNLEAAVVLMEA--APelvnEPMTSDlyqGE 90
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 114 TPLFLAVENGHIDVLRLLLRYGANVN-----------GSHSMC--GWNALHQATFQENGEIIKLLLKKGADKECQDDFGI 180
Cdd:cd22192    91 TALHIAVVNQNLNLVRELIARGADVVspratgtffrpGPKNLIyyGEHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGN 170
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2079055816 181 TPLFV-AAQYGKL---ESLSILISSGANVNCQALDEA------TPLFIAAQEGHTECVELLLSS 234
Cdd:cd22192   171 TVLHIlVLQPNKTfacQMYDLILSYDKEDDLQPLDLVpnnqglTPFKLAAKEGNIVMFQHLVQK 234
PHA02875 PHA02875
ankyrin repeat protein; Provisional
49-267 3.43e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.81  E-value: 3.43e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  49 EAAYHNSVECLRMLIHADSSENYiktKTFEGFCALHLAASQGHWKIVHILLEAGADPNATTSEETTPLFLAVENGHIDVL 128
Cdd:PHA02875    8 DAILFGELDIARRLLDIGINPNF---EIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 129 RLLLRYGANVNGSHSMCGWNALHQATFQENGEIIKLLLKKGADKECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQ 208
Cdd:PHA02875   85 EELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIE 164
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 2079055816 209 ALDEATPLFIAAQEGHTECVELLLSSGADPDLYCNEDDWQLpIHAAAQMGHTEILELLI 267
Cdd:PHA02875  165 DCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGCVAA-LCYAIENNKIDIVRLFI 222
PHA03100 PHA03100
ankyrin repeat protein; Provisional
93-305 1.26e-15

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 78.94  E-value: 1.26e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  93 KIVHILLEAGADPNATTSEETTPLFLAVENGHIDVLRLLLRYGANVNgSHSMCGWNALH-----QATFQENGEIIKLLLK 167
Cdd:PHA03100   16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADIN-SSTKNNSTPLHylsniKYNLTDVKEIVKLLLE 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 168 KGADKECQDDFGITPLFVAAQyGKLESLSI---LISSGANVNCQALDEATPLFIAAQEGH--TECVELLLSSGAD----- 237
Cdd:PHA03100   95 YGANVNAPDNNGITPLLYAIS-KKSNSYSIveyLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDinakn 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 238 --------------PDLYCNEddwqlPIHAAAQMGHTEILELLIPLTNRVCDTGPDKVSPVYSAVFGGHEECLEMLLQHG 303
Cdd:PHA03100  174 rvnyllsygvpiniKDVYGFT-----PLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNG 248

                  ..
gi 2079055816 304 YS 305
Cdd:PHA03100  249 PS 250
PHA02874 PHA02874
ankyrin repeat protein; Provisional
59-288 8.21e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 76.54  E-value: 8.21e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  59 LRMLIHA---DSSENYIKTKTF-------EGFCALHLAASQGHWKIVHILLEAGADPNATTSEETTPLFLAVENGHIDVL 128
Cdd:PHA02874    5 LRMCIYSgdiEAIEKIIKNKGNcinisvdETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDII 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 129 RLLLRYGANVN------------GSHSMCGWNA----------LHQATFQENGEIIKLLLKKGADKECQDDFGITPLFVA 186
Cdd:PHA02874   85 KLLIDNGVDTSilpipciekdmiKTILDCGIDVnikdaelktfLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIA 164
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 187 AQYGKLESLSILISSGANVNCQALDEATPLFIAAQEGHTECVELLLSSGADPDLYCNEDdwQLPIHAAAqMGHTEILELL 266
Cdd:PHA02874  165 IKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNG--FTPLHNAI-IHNRSAIELL 241
                         250       260
                  ....*....|....*....|...
gi 2079055816 267 IplTNR-VCDTGPDKVSPVYSAV 288
Cdd:PHA02874  242 I--NNAsINDQDIDGSTPLHHAI 262
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
86-266 1.82e-14

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 76.45  E-value: 1.82e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  86 AASQGHWKIVHILLEAGADPNATTSEETTPLFLAVENGHIDVLRLLLRYGANV-----NGSHSMcgWNAL---HQATFQe 157
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVhirdaNGNTAL--WNAIsakHHKIFR- 608
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 158 ngeiIKLLLKKGADKECQDDFgitpLFVAAQYGKLESLSILISSGANVNCQALDEATPLFIAAQEGHTECVELLLSSGAD 237
Cdd:PLN03192  609 ----ILYHFASISDPHAAGDL----LCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
                         170       180
                  ....*....|....*....|....*....
gi 2079055816 238 PDLYCNEDDwqlpihaaaqMGHTEILELL 266
Cdd:PLN03192  681 VDKANTDDD----------FSPTELRELL 699
PHA02878 PHA02878
ankyrin repeat protein; Provisional
24-209 3.38e-14

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 74.92  E-value: 3.38e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  24 KVLRKLLRKGRSVDVAD-NRGWMPIHEAAYHNSVECLRMLIHADSSENyIKTKTFEGfcALHLAASQGHWKIVHILLEAG 102
Cdd:PHA02878  148 EITKLLLSYGADINMKDrHKGNTALHYATENKDQRLTELLLSYGANVN-IPDKTNNS--PLHHAVKHYNKPIVHILLENG 224
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 103 ADPNATTSEETTPLFLAVEN-GHIDVLRLLLRYGANVNGSHSMCGWNALHQATFQEngEIIKLLLKKGADKECQDDFGIT 181
Cdd:PHA02878  225 ASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSYILGLTALHSSIKSE--RKLKLLLEYGADINSLNSYKLT 302
                         170       180
                  ....*....|....*....|....*....
gi 2079055816 182 PLFVAA-QYGKLESLSILISsgaNVNCQA 209
Cdd:PHA02878  303 PLSSAVkQYLCINIGRILIS---NICLLK 328
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
462-502 2.81e-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: 2.81e-13
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2079055816 462 PSLTHLCRLEIRSCLKPEHLrsdSFICQLPLPRSLHNYLLY 502
Cdd:cd03716     4 RSLQHLCRLAIRRCLGRRRL---ELIKKLPLPPRLKDYLLY 41
PHA02878 PHA02878
ankyrin repeat protein; Provisional
1-237 4.21e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 71.45  E-value: 4.21e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816   1 MDFTEAYSDTCSTVGL-----AAREGNVKVLRKLLRKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIhadssENYIKTK 75
Cdd:PHA02878   23 IDHTENYSTSASLIPFiplhqAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMI-----RSINKCS 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  76 TFEGFCALHLAASQGHWKIVHILLEAGADPNATTSEETTPLFLAVENGHIDVLRLLLRYGANVNGSHSMCGWNALHQATF 155
Cdd:PHA02878   98 VFYTLVAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHKGNTALHYATE 177
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 156 QENGEIIKLLLKKGADKECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDEATPLFIAAQE-GHTECVELLLSS 234
Cdd:PHA02878  178 NKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEH 257

                  ...
gi 2079055816 235 GAD 237
Cdd:PHA02878  258 GVD 260
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
462-502 1.04e-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: 1.04e-12
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2079055816 462 PSLTHLCRLEIRSCLKPehlRSDSFICQLPLPRSLHNYLLY 502
Cdd:cd03587     3 RSLQHLCRLAIRRCLGK---RRLDLIDKLPLPPRLKDYLLY 40
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
17-183 6.57e-12

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 68.36  E-value: 6.57e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  17 AAREGNVKVLRKLLRKGRSVDVADNRGWMPIHEAAYHNSVECLRMLI-HADSsenyIKTKTFEGFCALHLAASQGHWKIV 95
Cdd:PLN03192  532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLkHACN----VHIRDANGNTALWNAISAKHHKIF 607
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  96 HILLEAGADPNATTSEETtpLFLAVENGHIDVLRLLLRYGANVNgSHSMCGWNALHQATFQENGEIIKLLLKKGADKEC- 174
Cdd:PLN03192  608 RILYHFASISDPHAAGDL--LCTAAKRNDLTAMKELLKQGLNVD-SEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKa 684
                         170
                  ....*....|.
gi 2079055816 175 --QDDFGITPL 183
Cdd:PLN03192  685 ntDDDFSPTEL 695
PHA03095 PHA03095
ankyrin-like protein; Provisional
22-243 8.40e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 67.36  E-value: 8.40e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  22 NVKVLRKLLRKGRSVDVADNRGWMPIHeaAY---HN-SVECLRMLIHADSsenYIKTKTFEGFCALH--LAASQGHWKIV 95
Cdd:PHA03095  131 NPKVIRLLLRKGADVNALDLYGMTPLA--VLlksRNaNVELLRLLIDAGA---DVYAVDDRFRSLLHhhLQSFKPRARIV 205
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  96 HILLEAGADPNATTSEETTPLflavenghidvlrlllryganvngsHSMcgwnalhqATFQENGEIIKL-LLKKGADKEC 174
Cdd:PHA03095  206 RELIRAGCDPAATDMLGNTPL-------------------------HSM--------ATGSSCKRSLVLpLLIAGISINA 252
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2079055816 175 QDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDEATPLFIAAQEGHTECVELLLSSGADPDLYCN 243
Cdd:PHA03095  253 RNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAA 321
PHA03100 PHA03100
ankyrin repeat protein; Provisional
160-405 1.75e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 66.23  E-value: 1.75e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 160 EIIKLLLKKGADKECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDEATPLFIAAQEGHT-----ECVELLLSS 234
Cdd:PHA03100   16 KNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVKLLLEY 95
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 235 GADPDLYCNEDDWQLPIHAAAQMGHTEILELLIPLTNRVCDTGPDKVSPVYSAVFGGHE--ECLEMLLQHGYSPDAqmcl 312
Cdd:PHA03100   96 GANVNAPDNNGITPLLYAISKKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINA---- 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 313 ifgfsspmcmafqKESceffgiVNILLKYGAQLNE--------LHLAycLKYEKFLVFRYFLKKGCPLapwNHISEF--- 381
Cdd:PHA03100  172 -------------KNR------VNYLLSYGVPINIkdvygftpLHYA--VYNNNPEFVKYLLDLGANP---NLVNKYgdt 227
                         250       260
                  ....*....|....*....|....*
gi 2079055816 382 -ISHAIKaqTTYKEWLPSLLLAGFD 405
Cdd:PHA03100  228 pLHIAIL--NNNKEIFKLLLNNGPS 250
PHA02875 PHA02875
ankyrin repeat protein; Provisional
149-369 3.95e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 65.01  E-value: 3.95e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 149 ALHQATFQENGEIIKLLLKKGADKECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDEATPLFIAAQEGHTECV 228
Cdd:PHA02875    5 ALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAV 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 229 ELLLSSG--ADPDLYcneDDWQLPIHAAAQMGHTEILELLIPLTNRVCDTGPDKVSPVYSAVFGGHEECLEMLLQHGYSP 306
Cdd:PHA02875   85 EELLDLGkfADDVFY---KDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL 161
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 307 DAQMCliFGFsSPMCMAFQKESCEffgIVNILLKYGAQLNELH-------LAYCLKYEKFLVFRYFLKKG 369
Cdd:PHA02875  162 DIEDC--CGC-TPLIIAMAKGDIA---ICKMLLDSGANIDYFGkngcvaaLCYAIENNKIDIVRLFIKRG 225
PHA02874 PHA02874
ankyrin repeat protein; Provisional
17-189 9.32e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.83  E-value: 9.32e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  17 AAREGNVKVLRKLLRKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIHADSsenYIKTKTFEGFCALHLAASQGHWKIVH 96
Cdd:PHA02874  131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGA---YANVKDNNGESPLHNAAEYGDYACIK 207
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  97 ILLEAGADPNATTSEETTPLFLAVENGHiDVLRLLLRyGANVNgSHSMCGWNALHQA-TFQENGEIIKLLLKKGADKECQ 175
Cdd:PHA02874  208 LLIDHGNHIMNKCKNGFTPLHNAIIHNR-SAIELLIN-NASIN-DQDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIK 284
                         170
                  ....*....|....
gi 2079055816 176 DDFGITPLFVAAQY 189
Cdd:PHA02874  285 DNKGENPIDTAFKY 298
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
462-501 2.83e-10

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


Pssm-ID: 462192  Cd Length: 39  Bit Score: 55.25  E-value: 2.83e-10
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2079055816 462 PSLTHLCRLEIRSCLKPehlRSDSFICQLPLPRSLHNYLL 501
Cdd:pfam07525   3 RSLQHLCRLAIRRALGK---RRLGAIDKLPLPPLLKDYLL 39
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
48-134 1.11e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 61.07  E-value: 1.11e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  48 HEAAYHNSVEcLRMLIHADSSENyikTKTFEGFCALHLAASQGHWKIVHILLEAGADPNATTSEETTPLFLAVENGHIDV 127
Cdd:PTZ00322   88 QLAASGDAVG-ARILLTGGADPN---CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREV 163

                  ....*..
gi 2079055816 128 LRLLLRY 134
Cdd:PTZ00322  164 VQLLSRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
212-267 2.00e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 53.43  E-value: 2.00e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2079055816 212 EATPLFIAAQEGHTECVELLLSSGADPDlYCNEDDWQlPIHAAAQMGHTEILELLI 267
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADIN-AVDGNGET-ALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
7-139 2.22e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.62  E-value: 2.22e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816   7 YSDTCSTVGLAAREGNVKVLRKLLRKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIHADSSENyikTKTFEGFCALHLA 86
Cdd:PHA02875   99 YKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLD---IEDCCGCTPLIIA 175
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2079055816  87 ASQGHWKIVHILLEAGADPNATTSE-ETTPLFLAVENGHIDVLRLLLRYGANVN 139
Cdd:PHA02875  176 MAKGDIAICKMLLDSGANIDYFGKNgCVAALCYAIENNKIDIVRLFIKRGADCN 229
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
462-502 2.64e-09

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: 52.41  E-value: 2.64e-09
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|.
gi 2079055816  462 PSLTHLCRLEIRSCLKpehlrsdsFICQLPLPRSLHNYLLY 502
Cdd:smart00969   1 RSLQHLCRLAIRRSLG--------GIDKLPLPPRLKDYLLY 33
PHA02884 PHA02884
ankyrin repeat protein; Provisional
91-219 3.90e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 58.07  E-value: 3.90e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  91 HWKIVHILLEAGADPNA----TTSEETTPLFLAVENGHIDVLRLLLRYGANVNgshsmcgwnalhqaTFQENGEIiklll 166
Cdd:PHA02884   45 YTDIIDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVN--------------RYAEEAKI----- 105
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2079055816 167 kkgadkecqddfgiTPLFVAAQYGKLESLSILISSGANVNCQALDEATPLFIA 219
Cdd:PHA02884  106 --------------TPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELA 144
SOCS_ASB14 cd03730
SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a ...
463-504 4.97e-09

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: 52.54  E-value: 4.97e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2079055816 463 SLTHLCRLEIRSCLKPEHLRSDSFICQLPLPRSLHNYLLYAE 504
Cdd:cd03730     5 SLKHLCRLKIRACMGRLRLRCPVFMSFLPLPNRLKAYILYKE 46
PHA02878 PHA02878
ankyrin repeat protein; Provisional
59-348 6.12e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 58.35  E-value: 6.12e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  59 LRMLIHADSSENYIKTKTFEGFCALHLAASQGHWKIVHILLEAGADPNATTSEETTPLFLAVENGHIDVLRLLLRYGANV 138
Cdd:PHA02878   17 LKYIEYIDHTENYSTSASLIPFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKC 96
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 139 NGSHSMcgwNALHQATFQENGEIIKLLLKKGADKECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDE-ATPLF 217
Cdd:PHA02878   97 SVFYTL---VAIKDAFNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRHKgNTALH 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 218 IAAQEGHTECVELLLSSGADPDL--YCNEDdwqlPIHAAAQMGHTEILELLI---PLTN--RVCDTGPDKVSPVYSAVFg 290
Cdd:PHA02878  174 YATENKDQRLTELLLSYGANVNIpdKTNNS----PLHHAVKHYNKPIVHILLengASTDarDKCGNTPLHISVGYCKDY- 248
                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2079055816 291 gheECLEMLLQHGYSPDAQmCLIFGFsSPMCMAFQKESceffgIVNILLKYGAQLNEL 348
Cdd:PHA02878  249 ---DILKLLLEHGVDVNAK-SYILGL-TALHSSIKSER-----KLKLLLEYGADINSL 296
PHA02989 PHA02989
ankyrin repeat protein; Provisional
93-206 6.53e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 58.21  E-value: 6.53e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  93 KIVHILLEAGADPNATTSEETTPLFLAVENGHI---DVLRLLLRYGANVNGSHSMCGWNALHQ--ATFQENGEIIKLLLK 167
Cdd:PHA02989   89 KIVKLLLKFGADINLKTFNGVSPIVCFIYNSNInncDMLRFLLSKGINVNDVKNSRGYNLLHMylESFSVKKDVIKILLS 168
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 2079055816 168 KGADK-ECQDDFGITPLFV----AAQYGKLESLSILISSGANVN 206
Cdd:PHA02989  169 FGVNLfEKTSLYGLTPMNIylrnDIDVISIKVIKYLIKKGVNIE 212
Ank_4 pfam13637
Ankyrin repeats (many copies);
82-132 6.88e-09

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 51.89  E-value: 6.88e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2079055816  82 ALHLAASQGHWKIVHILLEAGADPNATTSEETTPLFLAVENGHIDVLRLLL 132
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
197-307 1.79e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 57.22  E-value: 1.79e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 197 ILISSGANVNCQALDEATPLFIAAQEGHTECVELLLSSGADPDLYcnEDDWQLPIHAAAQMGHTEILELLipLTNRVCDT 276
Cdd:PTZ00322  100 ILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLL--DKDGKTPLELAEENGFREVVQLL--SRHSQCHF 175
                          90       100       110
                  ....*....|....*....|....*....|.
gi 2079055816 277 GPDKVSPVYSavFGGHEECLEMLLQHGYSPD 307
Cdd:PTZ00322  176 ELGANAKPDS--FTGKPPSLEDSPISSHHPD 204
Ank_4 pfam13637
Ankyrin repeats (many copies);
181-232 2.08e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 50.35  E-value: 2.08e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2079055816 181 TPLFVAAQYGKLESLSILISSGANVNCQALDEATPLFIAAQEGHTECVELLL 232
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
84-178 3.20e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 3.20e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  84 HLAASqGHWKIVHILLEAGADPNATTSEETTPLFLAVENGHIDVLRLLLRYGANVNGSHSMcGWNALHQATFQENGEIIK 163
Cdd:PTZ00322   88 QLAAS-GDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKD-GKTPLELAEENGFREVVQ 165
                          90
                  ....*....|....*
gi 2079055816 164 LLLkkgadKECQDDF 178
Cdd:PTZ00322  166 LLS-----RHSQCHF 175
PHA02878 PHA02878
ankyrin repeat protein; Provisional
17-120 4.05e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 55.66  E-value: 4.05e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  17 AAREGNVKVLRKLLRKGRSVDVADNRGWMPIHEA-AYHNSVECLRMLIHADSSENyIKTkTFEGFCALHLAASQGhwKIV 95
Cdd:PHA02878  208 AVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVN-AKS-YILGLTALHSSIKSE--RKL 283
                          90       100
                  ....*....|....*....|....*
gi 2079055816  96 HILLEAGADPNATTSEETTPLFLAV 120
Cdd:PHA02878  284 KLLLEYGADINSLNSYKLTPLSSAV 308
Ank_4 pfam13637
Ankyrin repeats (many copies);
112-166 5.12e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 49.20  E-value: 5.12e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2079055816 112 ETTPLFLAVENGHIDVLRLLLRYGANVNGSHSmCGWNALHQATFQENGEIIKLLL 166
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDG-NGETALHFAASNGNVEVLKLLL 54
PHA02884 PHA02884
ankyrin repeat protein; Provisional
122-244 6.61e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 54.22  E-value: 6.61e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 122 NGHIDVLRLLLR-----YGANVNGSHSMCGWNALHQATFQENGEIIKLLLKKGADKECQDDFG----ITPLFVAAQYGKL 192
Cdd:PHA02884    4 INLIDIITLLCRifyiiFYIAIKKKNKICIANILYSSIKFHYTDIIDAILKLGADPEAPFPLSenskTNPLIYAIDCDND 83
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2079055816 193 ESLSILISSGANVNCQAlDEA--TPLFIAAQEGHTECVELLLSSGADPDLYCNE 244
Cdd:PHA02884   84 DAAKLLIRYGADVNRYA-EEAkiTPLYISVLHGCLKCLEILLSYGADINIQTND 136
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
462-502 2.23e-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: 2.23e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2079055816 462 PSLTHLCRLEIRSCLKPEHlrsdsfICQLPLPRSLHNYLLY 502
Cdd:cd03717     4 RSLQHLCRFVIRQCTRRDL------IDQLPLPRRLKDYLKE 38
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
162-233 3.61e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.98  E-value: 3.61e-07
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2079055816 162 IKLLLKKGADKECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDEATPLFIAAQEGHTECVELLLS 233
Cdd:PTZ00322   98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
SOCS_SSB1_4 cd03718
SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box ...
461-502 3.72e-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: 46.53  E-value: 3.72e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2079055816 461 LPsLTHLCRLEIRSCLKPEHLRSdsfICQLPLPRSLHNYLLY 502
Cdd:cd03718     4 LP-LMDLCRRRVRVALGRDRLEE---IEQLPLPPSLKNYLLY 41
PHA02876 PHA02876
ankyrin repeat protein; Provisional
156-249 4.26e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 52.76  E-value: 4.26e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 156 QENGEIIKLLLKKGADKECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDEATPLFIAAQEGHTECVELLLSSG 235
Cdd:PHA02876  155 QDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNR 234
                          90
                  ....*....|....
gi 2079055816 236 ADpdlyCNEDDWQL 249
Cdd:PHA02876  235 SN----INKNDLSL 244
Ank_4 pfam13637
Ankyrin repeats (many copies);
17-63 5.60e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 46.50  E-value: 5.60e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*..
gi 2079055816  17 AAREGNVKVLRKLLRKGRSVDVADNRGWMPIHEAAYHNSVECLRMLI 63
Cdd:pfam13637   8 AAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_2 pfam12796
Ankyrin repeats (3 copies);
251-346 7.18e-07

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 47.42  E-value: 7.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 251 IHAAAQMGHTEILELLIPLTNRVCDTGPDKVSPVYSAVFGGHEECLEMLLQHgysPDAQMCLifGFSSPMCMAFQKESCE 330
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKD--NGRTALHYAARSGHLE 75
                          90
                  ....*....|....*.
gi 2079055816 331 ffgIVNILLKYGAQLN 346
Cdd:pfam12796  76 ---IVKLLLEKGADIN 88
PHA02946 PHA02946
ankyin-like protein; Provisional
78-234 9.50e-07

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 51.21  E-value: 9.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  78 EGFCALHLAASQGHWKIVHILLEAGADPNATTSEETTPLFL--AVENGHIDVLRLLLRYGANVNGSHSMCGWNALHQATf 155
Cdd:PHA02946   71 DGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYlsGTDDEVIERINLLVQYGAKINNSVDEEGCGPLLACT- 149
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 156 QENGEIIKLLLKKGADKECQDDFGITPL--FVAAQYGKLESLSILISSGANVNCQALDEATPLFIAAQE--GHTECVELL 231
Cdd:PHA02946  150 DPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKtvKNVDIINLL 229

                  ...
gi 2079055816 232 LSS 234
Cdd:PHA02946  230 LPS 232
PHA02798 PHA02798
ankyrin-like protein; Provisional
93-206 1.00e-06

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 51.37  E-value: 1.00e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  93 KIVHILLEAGADPNATTSEETTPLFLAVEN-----GHIDVLRLLLRYGANVN-----GSHSMCGwnALHQATFQeNGEII 162
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINkknsdGETPLYC--LLSNGYIN-NLEIL 128
                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*..
gi 2079055816 163 KLLLKKGADKECQDDFGITPLFVAAQYG---KLESLSILISSGANVN 206
Cdd:PHA02798  129 LFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKGVDIN 175
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
58-200 1.92e-06

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


Pssm-ID: 411978 [Multi-domain]  Cd Length: 680  Bit Score: 50.53  E-value: 1.92e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  58 CLRMLIHADSSEnyiktKTFEGFCALHLAASQGHWKIVHILLEAGADPNA---------TTSEE-----TTPLFLAVENG 123
Cdd:cd22194   125 ILDRFINAEYTE-----EAYEGQTALNIAIERRQGDIVKLLIAKGADVNAhakgvffnpKYKHEgfyfgETPLALAACTN 199
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 124 HIDVLRLLLRYGANVNGSHSMCGWNALHQ-ATFQENGE-----IIKL---LLKKGADKECQ---DDFGITPLFVAAQYGK 191
Cdd:cd22194   200 QPEIVQLLMEKESTDITSQDSRGNTVLHAlVTVAEDSKtqndfVKRMydmILLKSENKNLEtirNNEGLTPLQLAAKMGK 279

                  ....*....
gi 2079055816 192 LESLSILIS 200
Cdd:cd22194   280 AEILKYILS 288
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
114-139 5.60e-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: 42.96  E-value: 5.60e-06
                           10        20
                   ....*....|....*....|....*.
gi 2079055816  114 TPLFLAVENGHIDVLRLLLRYGANVN 139
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02874 PHA02874
ankyrin repeat protein; Provisional
180-379 1.07e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.04  E-value: 1.07e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 180 ITPLFVAAQYGKLESLSILISSGANVNCQALDEATPLFIAAQEGHTECVELLLSSGADPDLycneddwqLPIHAAAQMGH 259
Cdd:PHA02874   36 TTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTSI--------LPIPCIEKDMI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 260 TEILELLIPLTNRvcdtGPDKVSPVYSAVFGGHEECLEMLLQhgYSPDAQMCLIFGfSSPMCMAFQKEsceFFGIVNILL 339
Cdd:PHA02874  108 KTILDCGIDVNIK----DAELKTFLHYAIKKGDLESIKMLFE--YGADVNIEDDNG-CYPIHIAIKHN---FFDIIKLLL 177
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*.
gi 2079055816 340 KYGAQLN------ELHLAYCLKYEKFLVFRYFLKKGcplapwNHIS 379
Cdd:PHA02874  178 EKGAYANvkdnngESPLHNAAEYGDYACIKLLIDHG------NHIM 217
PHA02798 PHA02798
ankyrin-like protein; Provisional
104-244 1.13e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.91  E-value: 1.13e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 104 DPNATTSEETT-PLFLAVENGHIDVLRLLLRYGANVNG-----SHSMCGWNAlHQATFQENGEIIKLLLKKGADKECQDD 177
Cdd:PHA02798   29 NPNEIVNEYSIfQKYLQRDSPSTDIVKLFINLGANVNGldneySTPLCTILS-NIKDYKHMLDIVKILIENGADINKKNS 107
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2079055816 178 FGITPLFVAAQYG---KLESLSILISSGANVNCQALDEATPLFIAAQEGHT---ECVELLLSSGADPDLYCNE 244
Cdd:PHA02798  108 DGETPLYCLLSNGyinNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNNK 180
PHA02874 PHA02874
ankyrin repeat protein; Provisional
11-139 1.31e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 47.65  E-value: 1.31e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  11 CSTVGLAAREGNVKVLRKLLRKGRSVDVADNRGWMPIHEAAYHNSVECLRMLIhadSSENYIKTKTFEGFCALHLAASqg 90
Cdd:PHA02874  158 CYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLI---DHGNHIMNKCKNGFTPLHNAII-- 232
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 2079055816  91 HWKIVHILLEAGADPNATTSEETTPLFLAVENG-HIDVLRLLLRYGANVN 139
Cdd:PHA02874  233 HNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADIS 282
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
463-504 1.34e-05

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


Pssm-ID: 239701  Cd Length: 56  Bit Score: 42.51  E-value: 1.34e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2079055816 463 SLTHLCRLEIRSCLKPEHLRSDSFICQLPLPRSLHNYLLYAE 504
Cdd:cd03731     5 PLKHLCRLKIRKLMGLQKLQQPSSMKKLPLPPALKRYILYKE 46
Ank_4 pfam13637
Ankyrin repeats (many copies);
250-300 2.12e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.88  E-value: 2.12e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2079055816 250 PIHAAAQMGHTEILELLIPLTNRVCDTGPDKVSPVYSAVFGGHEECLEMLL 300
Cdd:pfam13637   4 ALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
78-109 2.44e-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: 41.12  E-value: 2.44e-05
                          10        20        30
                  ....*....|....*....|....*....|...
gi 2079055816  78 EGFCALHLAASQ-GHWKIVHILLEAGADPNATT 109
Cdd:pfam00023   1 DGNTPLHLAAGRrGNLEIVKLLLSKGADVNARD 33
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
16-151 2.99e-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: 47.00  E-value: 2.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  16 LAAREGNVKVLRKLLR-KGRSVDVADNRgwmpIHEAA--YHNSVE-CLRMLIHADSSE------NYIKTKTF-EGFCALH 84
Cdd:TIGR00870  58 VAAIENENLELTELLLnLSCRGAVGDTL----LHAISleYVDAVEaILLHLLAAFRKSgplelaNDQYTSEFtPGITALH 133
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  85 LAASQGHWKIVHILLEAGADPNAT-------TSEETT-------PLFLAVENGHIDVLRLLLRYGANVNGSHSMcGWNAL 150
Cdd:TIGR00870 134 LAAHRQNYEIVKLLLERGASVPARacgdffvKSQGVDsfyhgesPLNAAACLGSPSIVALLSEDPADILTADSL-GNTLL 212

                  .
gi 2079055816 151 H 151
Cdd:TIGR00870 213 H 213
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
220-302 3.63e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.43  E-value: 3.63e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 220 AQEGHTECVELLLSSGADPDlyCNEDDWQLPIHAAAQMGHTEILELLIPLTNRVCDTGPDKVSPVYSAVFGGHEECLEML 299
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPN--CRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167

                  ...
gi 2079055816 300 LQH 302
Cdd:PTZ00322  168 SRH 170
Ank_4 pfam13637
Ankyrin repeats (many copies);
146-199 3.78e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.11  E-value: 3.78e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2079055816 146 GWNALHQATFQENGEIIKLLLKKGADKECQDDFGITPLFVAAQYGKLESLSILI 199
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02989 PHA02989
ankyrin repeat protein; Provisional
24-232 6.44e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 45.50  E-value: 6.44e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  24 KVLRKLLRKGRSVDVADNRGWMPIHEAAYH---NSVECLRMLIhadSSENYIKT-KTFEGFCALH--LAASQGHWKIVHI 97
Cdd:PHA02989   89 KIVKLLLKFGADINLKTFNGVSPIVCFIYNsniNNCDMLRFLL---SKGINVNDvKNSRGYNLLHmyLESFSVKKDVIKI 165
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  98 LLEAGADPNATTS-EETTPLFLAVENG----HIDVLRLLLRYGANVNGShsmcgwNALHQA---TFQENGEI-----IKL 164
Cdd:PHA02989  166 LLSFGVNLFEKTSlYGLTPMNIYLRNDidviSIKVIKYLIKKGVNIETN------NNGSESvleSFLDNNKIlskkeFKV 239
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 165 L--LKKGADKECQDDFGITPLFVAAQYGKLESLSILISSGANVNCQALDEATPLFIAAQEGHTECVELLL 232
Cdd:PHA02989  240 LnfILKYIKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNRIL 309
SOCS_SOCS7 cd03741
SOCS (suppressors of cytokine signaling) box of SOCS7-like proteins. Together with CIS1, the ...
463-502 7.12e-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: 40.47  E-value: 7.12e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2079055816 463 SLTHLCRLEIRSCLKPEHlrsdsfICQLPLPRSLHNYLLY 502
Cdd:cd03741     5 SLQHLCRFVIRKLVRRDH------IPALPLPRRLIDYLRE 38
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
114-267 7.99e-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: 45.46  E-value: 7.99e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 114 TPLF-LAVENGHIDVLRLLLRYGANVNgshsmCGWNALHQATFQENG---EIIKLLLKKGADK--------ECQDDF--G 179
Cdd:TIGR00870  54 SALFvAAIENENLELTELLLNLSCRGA-----VGDTLLHAISLEYVDaveAILLHLLAAFRKSgplelandQYTSEFtpG 128
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 180 ITPLFVAAQYGKLESLSILISSGANVNCQAldeatplfiaaqeghtECVELLLSSGADpDLYCNEddwqLPIHAAAQMGH 259
Cdd:TIGR00870 129 ITALHLAAHRQNYEIVKLLLERGASVPARA----------------CGDFFVKSQGVD-SFYHGE----SPLNAAACLGS 187

                  ....*...
gi 2079055816 260 TEILELLI 267
Cdd:TIGR00870 188 PSIVALLS 195
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
59-199 2.01e-04

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


Pssm-ID: 411980 [Multi-domain]  Cd Length: 649  Bit Score: 44.03  E-value: 2.01e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  59 LRMLIHADSSENYIKTKTfegfcALHLAASQGHWKIVHILLEAGADPNATTSEE--------------TTPLFLAVENGH 124
Cdd:cd22196    79 LKEFVNAAYTDSYYKGQT-----ALHIAIERRNMHLVELLVQNGADVHARASGEffkkkkggpgfyfgELPLSLAACTNQ 153
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 125 IDVLRLLLR---YGANVNGSHSMcGWNALHQA-----TFQENGEIIKL----LLKKGAD-------KECQDDFGITPLFV 185
Cdd:cd22196   154 LDIVKFLLEnphSPADISARDSM-GNTVLHALvevadNTPENTKFVTKmyneILILGAKirpllklEEITNKKGLTPLKL 232
                         170
                  ....*....|....
gi 2079055816 186 AAQYGKLESLSILI 199
Cdd:cd22196   233 AAKTGKIGIFAYIL 246
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
181-312 2.06e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.85  E-value: 2.06e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 181 TPLFVAAQYGKLESLSILISSGANVNCQ--ALDEaTPLFIAAQEGHTECVELLLSsgADPDLYCNEDDWQL-----PIHA 253
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLLKCPSCDLFQrgALGE-TALHVAALYDNLEAAVVLME--AAPELVNEPMTSDLyqgetALHI 95
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2079055816 254 AAQMGHTEILELLIP-----LTNRVCDT----GPDKV-----SPVYSAVFGGHEECLEMLLQHGYSPDAQMCL 312
Cdd:cd22192    96 AVVNQNLNLVRELIArgadvVSPRATGTffrpGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIRAQDSL 168
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
114-139 2.16e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 38.39  E-value: 2.16e-04
                          10        20
                  ....*....|....*....|....*.
gi 2079055816 114 TPLFLAVENGHIDVLRLLLRYGANVN 139
Cdd:pfam13606   4 TPLHLAARNGRLEIVKLLLENGADIN 29
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
463-501 2.21e-04

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


Pssm-ID: 239693  Cd Length: 48  Bit Score: 38.96  E-value: 2.21e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2079055816 463 SLTHLCRLEIRSCLkpeHLRSDSFICQLPLPRSLHNYLL 501
Cdd:cd03723     5 SLQHLCRCAIRKLL---GSRCHKLVPQLSLPTSLKNYLL 40
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
214-240 2.45e-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: 38.34  E-value: 2.45e-04
                           10        20
                   ....*....|....*....|....*..
gi 2079055816  214 TPLFIAAQEGHTECVELLLSSGADPDL 240
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
211-240 2.52e-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: 38.42  E-value: 2.52e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 2079055816 211 DEATPLFIAA-QEGHTECVELLLSSGADPDL 240
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNA 31
SOCS smart00253
suppressors of cytokine signalling; suppressors of cytokine signalling
461-502 2.54e-04

suppressors of cytokine signalling; suppressors of cytokine signalling


Pssm-ID: 128549  Cd Length: 43  Bit Score: 38.82  E-value: 2.54e-04
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|..
gi 2079055816  461 LPSLTHLCRLEIRSCLKPEHlrsdsfICQLPLPRSLHNYLLY 502
Cdd:smart00253   7 VPSLQHLCRFTIRRCTRTDQ------IKTLPLPPKLKDYLSY 42
Ank_5 pfam13857
Ankyrin repeats (many copies);
98-153 2.67e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.87  E-value: 2.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 2079055816  98 LLEAG-ADPNATTSEETTPLFLAVENGHIDVLRLLLRYGANVNgSHSMCGWNALHQA 153
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLN-LKDEEGLTALDLA 56
SOCS_ASB6 cd03725
SOCS (suppressors of cytokine signaling) box of ASB6-like proteins. ASB family members have a ...
462-501 2.92e-04

SOCS (suppressors of cytokine signaling) box of ASB6-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ASB6 interacts with the adaptor protein APS and recruits elongin B/C to the insulin receptor signaling complex. 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: 239695  Cd Length: 44  Bit Score: 38.58  E-value: 2.92e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2079055816 462 PSLTHLCRLEIRSCLKPEHLrsDSFICQLPLPRSLHNYLL 501
Cdd:cd03725     4 PPLKHLCRVFIRLCLRPWPV--DVKVKALPLPDRLKWYLL 41
Ank_5 pfam13857
Ankyrin repeats (many copies);
74-119 3.96e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.48  E-value: 3.96e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 2079055816  74 TKTFEGFCALHLAASQGHWKIVHILLEAGADPNATTSEETTPLFLA 119
Cdd:pfam13857  11 RLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
114-139 4.64e-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: 37.65  E-value: 4.64e-04
                          10        20
                  ....*....|....*....|....*..
gi 2079055816 114 TPLFLAV-ENGHIDVLRLLLRYGANVN 139
Cdd:pfam00023   4 TPLHLAAgRRGNLEIVKLLLSKGADVN 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
82-107 6.10e-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: 6.10e-04
                           10        20
                   ....*....|....*....|....*.
gi 2079055816   82 ALHLAASQGHWKIVHILLEAGADPNA 107
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
SOCS_SSB1 cd03744
SOCS (suppressors of cytokine signaling) box of SSB1 (SPRY domain-containing SOCS box proteins) ...
463-502 9.06e-04

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: 37.27  E-value: 9.06e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2079055816 463 SLTHLCRLEIRSCLKPEHLrsdSFICQLPLPRSLHNYLLY 502
Cdd:cd03744     5 PLMDLCRRSVRLALGRERL---SEIHTLPLPASLKNYLLY 41
SOCS_WSB_SWIP cd03733
SOCS (suppressors of cytokine signaling) box of WSB/SWiP-like proteins. This subfamily ...
461-502 1.18e-03

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


Pssm-ID: 239702  Cd Length: 39  Bit Score: 36.63  E-value: 1.18e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2079055816 461 LPSLTHLCRLEIRsclkpeHLRSDSFICQLPLPRSLHNYLLY 502
Cdd:cd03733     3 VSSLQHLCRMALR------RVMTTQQVLALPIPKKMKEFLTY 38
SOCS_SSB4 cd03743
SOCS (suppressors of cytokine signaling) box of SSB4 (SPRY domain-containing SOCS box ...
461-502 1.19e-03

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


Pssm-ID: 239712  Cd Length: 42  Bit Score: 36.86  E-value: 1.19e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2079055816 461 LPsLTHLCRLEIRSCLKPEHLRSdsfICQLPLPRSLHNYLLY 502
Cdd:cd03743     4 LP-LMDLCRRSARQALGRHRLHH---IQSLPLPQTLKNYLQY 41
PHA02859 PHA02859
ankyrin repeat protein; Provisional
114-185 1.35e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 40.19  E-value: 1.35e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2079055816 114 TPLFLAVENGHI--DVLRLLLRYGANVNGSHSMCGWNALHQ-ATFQEN--GEIIKLLLKKGADKECQDDFGITPLFV 185
Cdd:PHA02859   53 TPIFSCLEKDKVnvEILKFLIENGADVNFKTRDNNLSALHHyLSFNKNvePEILKILIDSGSSITEEDEDGKNLLHM 129
SOCS_ASB_9_11 cd03728
SOCS (suppressors of cytokine signaling) box of ASB9 and 11 proteins. ASB family members have ...
462-502 1.55e-03

SOCS (suppressors of cytokine signaling) box of ASB9 and 11 proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239698  Cd Length: 42  Bit Score: 36.31  E-value: 1.55e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2079055816 462 PSLTHLCRLEIRSCLKPEHLRSdsfICQLPLPRSLHNYLLY 502
Cdd:cd03728     4 PSLMQLCRLCIRKCFGRKQHHK---IHKLHLPEPLKHFLLY 41
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
78-107 1.75e-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: 1.75e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 2079055816  78 EGFCALHLAASQGHWKIVHILLEAGADPNA 107
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
59-200 2.48e-03

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 40.55  E-value: 2.48e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  59 LRMLIHADSSENYiktktFEGFCALHLAASQGHWKIVHILLEAGADPNAT--------TSEET------TPLFLAVENGH 124
Cdd:cd22193    61 LKRFINAEYTDEY-----YEGQTALHIAIERRQGDIVALLVENGADVHAHakgrffqpKYQGEgfyfgeLPLSLAACTNQ 135
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 125 IDVLRLLLRYG---ANVNGSHSMcGWNALHQAT-----FQENGEIIK----LLLKKGAD-------KECQDDFGITPLFV 185
Cdd:cd22193   136 PDIVQYLLENEhqpADIEAQDSR-GNTVLHALVtvadnTKENTKFVTrmydMILIRGAKlcptvelEEIRNNDGLTPLQL 214
                         170
                  ....*....|....*
gi 2079055816 186 AAQYGKLESLSILIS 200
Cdd:cd22193   215 AAKMGKIEILKYILQ 229
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
179-207 3.31e-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: 3.31e-03
                           10        20
                   ....*....|....*....|....*....
gi 2079055816  179 GITPLFVAAQYGKLESLSILISSGANVNC 207
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02859 PHA02859
ankyrin repeat protein; Provisional
113-243 3.86e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 39.03  E-value: 3.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 113 TTPLFLAVENGHIDVLRLLLRYGANVNGSHSmcgwNALHQATFQE--NGEIIKLLLKKGADKECQ-DDFGITPLFVAAQY 189
Cdd:PHA02859   22 CNPLFYYVEKDDIEGVKKWIKFVNDCNDLYE----TPIFSCLEKDkvNVEILKFLIENGADVNFKtRDNNLSALHHYLSF 97
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 2079055816 190 GK---LESLSILISSGANVNCQALDEATPL--FIAAQEGHTECVELLLSSGADP---DLYCN 243
Cdd:PHA02859   98 NKnvePEILKILIDSGSSITEEDEDGKNLLhmYMCNFNVRINVIKLLIDSGVSFlnkDFDNN 159
SOCS_CIS1 cd03734
SOCS (suppressors of cytokine signaling) box of CIS (cytokine-inducible SH2 protein) 1-like ...
461-500 3.97e-03

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


Pssm-ID: 239703  Cd Length: 41  Bit Score: 35.32  E-value: 3.97e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2079055816 461 LPSLTHLCRLEIRSCLKPehlrsdsfICQLPLPRSLHNYL 500
Cdd:cd03734     3 ARSLQHLCRLVINRLVTD--------VDCLPLPRRMADYL 34
PHA02736 PHA02736
Viral ankyrin protein; Provisional
125-203 4.02e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.93  E-value: 4.02e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 125 IDVLRLLLRYGANVNGSHSMCGWNALHQATFQENGEIIKLLLKK-GADKECQDDFGITPLFVAAQYGKLESLSILISSGA 203
Cdd:PHA02736   71 QEKLKLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNILRAKGA 150
PHA02859 PHA02859
ankyrin repeat protein; Provisional
55-182 6.61e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 38.26  E-value: 6.61e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  55 SVECLRMLIHADSSENYiKTKTfEGFCALHLAASQG---HWKIVHILLEAGADPNATTSEETTPLFLAVENGH--IDVLR 129
Cdd:PHA02859   65 NVEILKFLIENGADVNF-KTRD-NNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLHMYMCNFNvrINVIK 142
                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2079055816 130 LLLRYGANVNGSHSMCGwNALHQ-ATFQENGEIIKLLLKKGADKECQDDFGITP 182
Cdd:PHA02859  143 LLIDSGVSFLNKDFDNN-NILYSyILFHSDKKIFDFLTSLGIDINETNKSGYNC 195
PHA02741 PHA02741
hypothetical protein; Provisional
48-133 7.07e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 37.71  E-value: 7.07e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816  48 HEAAYHNSVECLRML---IHADSSENYIKTKTFEGFCALHLAA----SQGHWKIVHILLEAGADPNATTS-EETTPLFLA 119
Cdd:PHA02741   26 HEAARCGCFDIIARFtpfIRGDCHAAALNATDDAGQMCIHIAAekheAQLAAEIIDHLIELGADINAQEMlEGDTALHLA 105
                          90
                  ....*....|....
gi 2079055816 120 VENGHIDVLRLLLR 133
Cdd:PHA02741  106 AHRRDHDLAEWLCC 119
PHA02876 PHA02876
ankyrin repeat protein; Provisional
188-240 7.88e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 38.89  E-value: 7.88e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2079055816 188 QYGKLESLSILISSGANVNCQALDEATPLFIAAQEGHTECVELLLSSGADPDL 240
Cdd:PHA02876  154 QQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNI 206
PHA02798 PHA02798
ankyrin-like protein; Provisional
160-267 9.23e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 38.66  E-value: 9.23e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2079055816 160 EIIKLLLKKGADKECQDDFGITPLF-----VAAQYGKLESLSILISSGANVNCQALDEATPLFIAAQEGHTECVELLL-- 232
Cdd:PHA02798   52 DIVKLFINLGANVNGLDNEYSTPLCtilsnIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYINNLEILLfm 131
                          90       100       110
                  ....*....|....*....|....*....|....*....
gi 2079055816 233 -SSGADPDLYCNEDDWQLPIHaaAQMGHT---EILELLI 267
Cdd:PHA02798  132 iENGADTTLLDKDGFTMLQVY--LQSNHHidiEIIKLLL 168
SOCS_WSB2_SWIP2 cd03745
SOCS (suppressors of cytokine signaling) box of WSB2/SWiP2-like proteins. This family consists ...
461-502 9.58e-03

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: 34.10  E-value: 9.58e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2079055816 461 LPSLTHLCRLEIRSCLKPEHlrsdsfICQLPLPRSLHNYLLY 502
Cdd:cd03745     3 LPSLRHLCRKALRHFLTTYQ------VLALPIPKKMKEFLTY 38
 
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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