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Conserved domains on  [gi|2217297704|ref|XP_047287429|]
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ankyrin repeat and SOCS box protein 2 isoform X4 [Homo sapiens]

Protein Classification

Graphical summary

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List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-313 1.92e-47

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.05  E-value: 1.92e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704  71 ADPLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGqvgclkvlqracerkNAEAVKILVQHNADTNHRCNR 150
Cdd:COG0666    55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNG---------------DLEIVKLLLEAGADVNARDKD 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 151 GWTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHE 230
Cdd:COG0666   120 GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 231 EVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSR-TRIRRSGVSPLHLAAERNHDEVLEALLSARFDVN 309
Cdd:COG0666   200 EIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADlNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279

                  ....
gi 2217297704 310 TPLA 313
Cdd:COG0666   280 AALL 283
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
504-548 7.43e-24

SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ASB2 targets specific proteins to destruction by the proteasome in leukemia cells that have been induced to differentiate. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


:

Pssm-ID: 239691  Cd Length: 45  Bit Score: 94.16  E-value: 7.43e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2217297704 504 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ 548
Cdd:cd03721     1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ 45
Ank_2 pfam12796
Ankyrin repeats (3 copies);
286-382 4.66e-12

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 4.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 286 LHLAAERNHDEVLEALLSARFDVNtplaperarLYEDRRSSALYFAVVNNNVYATELLLQHgADPNRDVI--SPLLVAIR 363
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNgrTALHYAAR 70
                          90
                  ....*....|....*....
gi 2217297704 364 HGCLRTMQLLLDHGANIDA 382
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-313 1.92e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.05  E-value: 1.92e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704  71 ADPLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGqvgclkvlqracerkNAEAVKILVQHNADTNHRCNR 150
Cdd:COG0666    55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNG---------------DLEIVKLLLEAGADVNARDKD 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 151 GWTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHE 230
Cdd:COG0666   120 GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 231 EVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSR-TRIRRSGVSPLHLAAERNHDEVLEALLSARFDVN 309
Cdd:COG0666   200 EIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADlNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279

                  ....
gi 2217297704 310 TPLA 313
Cdd:COG0666   280 AALL 283
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
504-548 7.43e-24

SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ASB2 targets specific proteins to destruction by the proteasome in leukemia cells that have been induced to differentiate. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239691  Cd Length: 45  Bit Score: 94.16  E-value: 7.43e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2217297704 504 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ 548
Cdd:cd03721     1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ 45
PHA03095 PHA03095
ankyrin-like protein; Provisional
126-393 2.10e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 100.10  E-value: 2.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 126 CERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRN---DLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQ-LEALR 201
Cdd:PHA03095   22 ASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIK 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 202 FLAKYGADINTQ--ASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHI--ASKKGNYRIVQMLLPVTSRTR 277
Cdd:PHA03095  102 LLIKAGADVNAKdkVGRTPLHVYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVllKSRNANVELLRLLIDAGADVY 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 278 IRRS-GVSPLHLAAE--RNHDEVLEALLSARFDV-------NTPLaPERARLYEDRRS--------------------SA 327
Cdd:PHA03095  182 AVDDrFRSLLHHHLQsfKPRARIVRELIRAGCDPaatdmlgNTPL-HSMATGSSCKRSlvlplliagisinarnrygqTP 260
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217297704 328 LYFAVVNNNVYATELLLQHGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAFPA 393
Cdd:PHA03095  261 LHYAAVFNNPRACRRLIALGADINavsSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTASVA 329
Ank_2 pfam12796
Ankyrin repeats (3 copies);
122-213 3.38e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 3.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 122 LQRACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSgGAKVESKNaYGITPLFVAAQSGQLEALR 201
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|..
gi 2217297704 202 FLAKYGADINTQ 213
Cdd:pfam12796  79 LLLEKGADINVK 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
69-270 4.03e-12

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: 68.89  E-value: 4.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704  69 RPAD-PLIKAIKDGDEEALKTMIK-EGKNLAEPNKEGWLPLHEAAYYGQVGCLKVLqracerknAEAVKILVqhNADTNH 146
Cdd:cd22192    15 RISEsPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVL--------MEAAPELV--NEPMTS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 147 RCNRGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAKYGADINT 212
Cdd:cd22192    85 DLYQGETALHIAVVNQNLNLVRELIARGADVVSPRAtgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRA 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217297704 213 QASDNASALY----EACKNEHEEVVEFLLSQGADANK------TNKDGLLPLHIASKKGNYRIVQMLL 270
Cdd:cd22192   165 QDSLGNTVLHilvlQPNKTFACQMYDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLV 232
Ank_2 pfam12796
Ankyrin repeats (3 copies);
286-382 4.66e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 4.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 286 LHLAAERNHDEVLEALLSARFDVNtplaperarLYEDRRSSALYFAVVNNNVYATELLLQHgADPNRDVI--SPLLVAIR 363
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNgrTALHYAAR 70
                          90
                  ....*....|....*....
gi 2217297704 364 HGCLRTMQLLLDHGANIDA 382
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
505-543 1.55e-11

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


Pssm-ID: 462192  Cd Length: 39  Bit Score: 59.10  E-value: 1.55e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2217297704 505 PPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLK 543
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
507-545 1.71e-08

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


Pssm-ID: 198037  Cd Length: 34  Bit Score: 50.10  E-value: 1.71e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217297704  507 RPLAHLCRLRVRKAIGKyriklLDTLPLPGRLIRYLKYE 545
Cdd:smart00969   1 RSLQHLCRLAIRRSLGG-----IDKLPLPPRLKDYLLYY 34
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
72-270 1.18e-07

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: 54.70  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704  72 DPLIKAIKDGDEEALKTMIKEGKNLAEpnkEGWLPLHEAAYYGQVGC----LKVLQRACERKNAEAVkilvqhNADTNHR 147
Cdd:TIGR00870  54 SALFVAAIENENLELTELLLNLSCRGA---VGDTLLHAISLEYVDAVeailLHLLAAFRKSGPLELA------NDQYTSE 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 148 CNRGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAKYGADINTQ 213
Cdd:TIGR00870 125 FTPGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTA 204
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217297704 214 AS-----DNASALYEACKNEHEEVV----EFLLSQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 270
Cdd:TIGR00870 205 DSlgntlLHLLVMENEFKAEYEELScqmyNFALSLLDKLRDSkelevilNHQGLTPLKLAAKEGRIVLFRLKL 277
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
252-399 1.35e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 54.25  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 252 LPLHIASKKGNYRIVQMLLpVTSRTRIRRSGV---SPLHLAAERNHDEVLEALL-SARFDVNTPLAPErarLYEDRrsSA 327
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLL-KCPSCDLFQRGAlgeTALHVAALYDNLEAAVVLMeAAPELVNEPMTSD---LYQGE--TA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 328 LYFAVVNNNVYATELLLQHGAD------------PNRDVI-----SPLLVAIRHGCLRTMQLLLDHGANIDA-------- 382
Cdd:cd22192    93 LHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIRAqdslgntv 172
                         170
                  ....*....|....*....
gi 2217297704 383 --YIATHPTAFPATIMFAM 399
Cdd:cd22192   173 lhILVLQPNKTFACQMYDL 191
PHA02884 PHA02884
ankyrin repeat protein; Provisional
266-416 1.16e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 50.37  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 266 VQMLLPVTSRTRIRRSGVspLHLAAERNHDEVLEALLSARFDVNTPLAperarLYEDRRSSALYFAVVNNNVYATELLLQ 345
Cdd:PHA02884   19 IIFYIAIKKKNKICIANI--LYSSIKFHYTDIIDAILKLGADPEAPFP-----LSENSKTNPLIYAIDCDNDDAAKLLIR 91
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217297704 346 HGADPNR----DVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAFPATIMFamkCLSLLKFLMdlgCDGE 416
Cdd:PHA02884   92 YGADVNRyaeeAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALMI---CNNFLAFMI---CDNE 160
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
183-211 2.24e-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: 2.24e-04
                           10        20
                   ....*....|....*....|....*....
gi 2217297704  183 YGITPLFVAAQSGQLEALRFLAKYGADIN 211
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
71-313 1.92e-47

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 167.05  E-value: 1.92e-47
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704  71 ADPLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGqvgclkvlqracerkNAEAVKILVQHNADTNHRCNR 150
Cdd:COG0666    55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNG---------------DLEIVKLLLEAGADVNARDKD 119
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 151 GWTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHE 230
Cdd:COG0666   120 GETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHL 199
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 231 EVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSR-TRIRRSGVSPLHLAAERNHDEVLEALLSARFDVN 309
Cdd:COG0666   200 EIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADlNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLA 279

                  ....
gi 2217297704 310 TPLA 313
Cdd:COG0666   280 AALL 283
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
122-391 6.93e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 149.33  E-value: 6.93e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 122 LQRACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALR 201
Cdd:COG0666    25 LLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVK 104
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 202 FLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL----PVTSRTr 277
Cdd:COG0666   105 LLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLeagaDVNARD- 183
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 278 irRSGVSPLHLAAERNHDEVLEALLSARFDVNTPlaperarlyEDRRSSALYFAVVNNNVYATELLLQHGADPN---RDV 354
Cdd:COG0666   184 --NDGETPLHLAAENGHLEIVKLLLEAGADVNAK---------DNDGKTALDLAAENGNLEIVKLLLEAGADLNakdKDG 252
                         250       260       270
                  ....*....|....*....|....*....|....*..
gi 2217297704 355 ISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAF 391
Cdd:COG0666   253 LTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
131-390 6.51e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 138.55  E-value: 6.51e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 131 AEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADI 210
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 211 NTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL----PVTSRTrirRSGVSPL 286
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLeagaDVNAQD---NDGNTPL 157
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 287 HLAAERNHDEVLEALLSARFDVNTPlaperarlyEDRRSSALYFAVVNNNVYATELLLQHGADPN---RDVISPLLVAIR 363
Cdd:COG0666   158 HLAAANGNLEIVKLLLEAGADVNAR---------DNDGETPLHLAAENGHLEIVKLLLEAGADVNakdNDGKTALDLAAE 228
                         250       260
                  ....*....|....*....|....*..
gi 2217297704 364 HGCLRTMQLLLDHGANIDAYIATHPTA 390
Cdd:COG0666   229 NGNLEIVKLLLEAGADLNAKDKDGLTA 255
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
504-548 7.43e-24

SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ASB2 targets specific proteins to destruction by the proteasome in leukemia cells that have been induced to differentiate. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239691  Cd Length: 45  Bit Score: 94.16  E-value: 7.43e-24
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2217297704 504 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYENTQ 548
Cdd:cd03721     1 EPPRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQETQ 45
PHA03095 PHA03095
ankyrin-like protein; Provisional
126-393 2.10e-22

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 100.10  E-value: 2.10e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 126 CERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRN---DLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQ-LEALR 201
Cdd:PHA03095   22 ASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSsekVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIK 101
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 202 FLAKYGADINTQ--ASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHI--ASKKGNYRIVQMLLPVTSRTR 277
Cdd:PHA03095  102 LLIKAGADVNAKdkVGRTPLHVYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAVllKSRNANVELLRLLIDAGADVY 181
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 278 IRRS-GVSPLHLAAE--RNHDEVLEALLSARFDV-------NTPLaPERARLYEDRRS--------------------SA 327
Cdd:PHA03095  182 AVDDrFRSLLHHHLQsfKPRARIVRELIRAGCDPaatdmlgNTPL-HSMATGSSCKRSlvlplliagisinarnrygqTP 260
                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217297704 328 LYFAVVNNNVYATELLLQHGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAFPA 393
Cdd:PHA03095  261 LHYAAVFNNPRACRRLIALGADINavsSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVAATLNTASVA 329
PHA02876 PHA02876
ankyrin repeat protein; Provisional
74-382 4.05e-22

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 100.52  E-value: 4.05e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704  74 LIKAIKDGDEEALKTMI-KEGKNLAEPNKEGWLPLHEAAYYGQVGC------------------LKVLQRACERKNAEAV 134
Cdd:PHA02876  148 LIKERIQQDELLIAEMLlEGGADVNAKDIYCITPIHYAAERGNAKMvnlllsygadvniialddLSVLECAVDSKNIDTI 227
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 135 KILVqhnaDTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEAL-RFLAKYGADINTQ 213
Cdd:PHA02876  228 KAII----DNRSNINKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAK 303
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 214 ASDNASALYEACKNEHE-EVVEFLLSQGADANKTNKDGLLPLHIASKKGNYR-IVQMLLPVTSRTRIRR-SGVSPLHLAA 290
Cdd:PHA02876  304 NIKGETPLYLMAKNGYDtENIRTLIMLGADVNAADRLYITPLHQASTLDRNKdIVITLLELGANVNARDyCDKTPIHYAA 383
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 291 ERNHDEVLEALLSARFDVNTplaperarlYEDRRSSALYFAVVNNNVY-ATELLLQHGAD---PNRDVISPLLVAIRHGC 366
Cdd:PHA02876  384 VRNNVVIINTLLDYGADIEA---------LSQKIGTALHFALCGTNPYmSVKTLIDRGANvnsKNKDLSTPLHYACKKNC 454
                         330
                  ....*....|....*..
gi 2217297704 367 -LRTMQLLLDHGANIDA 382
Cdd:PHA02876  455 kLDVIEMLLDNGADVNA 471
PHA03100 PHA03100
ankyrin repeat protein; Provisional
122-345 8.86e-22

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.81  E-value: 8.86e-22
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 122 LQRACERKNAEAVKILVQHNADTNHRCNRGWTALH-----ESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQ--S 194
Cdd:PHA03100   39 LYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHylsniKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkkS 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 195 GQLEALRFLAKYGADINTQASDNASALYEACKNEHE--EVVEFLLSQGADANKTNK-DGLL---------------PLHI 256
Cdd:PHA03100  119 NSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKNRvNYLLsygvpinikdvygftPLHY 198
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 257 ASKKGNYRIVQMLLPVTSRTRIR-RSGVSPLHLAAERNHDEVLEALLSARFDVNTplaperarlyedRRSSALYFAVVN- 334
Cdd:PHA03100  199 AVYNNNPEFVKYLLDLGANPNLVnKYGDTPLHIAILNNNKEIFKLLLNNGPSIKT------------IIETLLYFKDKDl 266
                         250
                  ....*....|.
gi 2217297704 335 NNVYATELLLQ 345
Cdd:PHA03100  267 NTITKIKMLKK 277
PHA03100 PHA03100
ankyrin repeat protein; Provisional
73-270 7.60e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 95.12  E-value: 7.60e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704  73 PLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHeaayygqvgcLKVLQRACERKNAEAVKILVQHNADTNHRCNRGW 152
Cdd:PHA03100   38 PLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLH----------YLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGI 107
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 153 TALHESVSR--NDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQ--LEALRFLAKYGADIN--------------TQA 214
Cdd:PHA03100  108 TPLLYAISKksNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINaknrvnyllsygvpINI 187
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217297704 215 SDN--ASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 270
Cdd:PHA03100  188 KDVygFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLL 245
Ank_2 pfam12796
Ankyrin repeats (3 copies);
122-213 3.38e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 85.17  E-value: 3.38e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 122 LQRACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSgGAKVESKNaYGITPLFVAAQSGQLEALR 201
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKD-NGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|..
gi 2217297704 202 FLAKYGADINTQ 213
Cdd:pfam12796  79 LLLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
221-310 1.04e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.01  E-value: 1.04e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 221 LYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPvTSRTRIRRSGVSPLHLAAERNHDEVLEA 300
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKL 79
                          90
                  ....*....|
gi 2217297704 301 LLSARFDVNT 310
Cdd:pfam12796  80 LLEKGADINV 89
PHA02878 PHA02878
ankyrin repeat protein; Provisional
70-376 1.83e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 91.48  E-value: 1.83e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704  70 PADPLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHeaayygqvgclkvlqRACERKNAEAVKILVQhnadTNHRCN 149
Cdd:PHA02878   37 PFIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLH---------------IICKEPNKLGMKEMIR----SINKCS 97
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 150 RGWT--ALHESVSRNDLEVMQILVSGgakvESKNAYGITPLFVAAQSG----QLEALRFLAKYGADINTQASDN-ASALY 222
Cdd:PHA02878   98 VFYTlvAIKDAFNNRNVEIFKIILTN----RYKNIQTIDLVYIDKKSKddiiEAEITKLLLSYGADINMKDRHKgNTALH 173
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 223 EACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIRRS-GVSPLHLAAERNHD-EVLEA 300
Cdd:PHA02878  174 YATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKcGNTPLHISVGYCKDyDILKL 253
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 301 LLSARFDVNtplaperARLYeDRRSSALYFAVVNNNVyaTELLLQHGADPNR---DVISPLLVAIR-HGCLRTMQLLLDH 376
Cdd:PHA02878  254 LLEHGVDVN-------AKSY-ILGLTALHSSIKSERK--LKLLLEYGADINSlnsYKLTPLSSAVKqYLCINIGRILISN 323
Ank_2 pfam12796
Ankyrin repeats (3 copies);
155-247 8.80e-19

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 81.32  E-value: 8.80e-19
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 155 LHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYgADINTQaSDNASALYEACKNEHEEVVE 234
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLK-DNGRTALHYAARSGHLEIVK 78
                          90
                  ....*....|...
gi 2217297704 235 FLLSQGADANKTN 247
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
73-312 1.51e-18

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 88.10  E-value: 1.51e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704  73 PLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAyygQVGCLKVlqracerknaeaVKILVQHNADTnhrcnrgw 152
Cdd:PHA02874   38 PLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAI---KIGAHDI------------IKLLIDNGVDT-------- 94
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 153 TALHESVSRNDLevMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEV 232
Cdd:PHA02874   95 SILPIPCIEKDM--IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDI 172
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 233 VEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIR-RSGVSPLHLAAERNHdEVLEALLSARF----D 307
Cdd:PHA02874  173 IKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKcKNGFTPLHNAIIHNR-SAIELLINNASindqD 251

                  ....*..
gi 2217297704 308 VN--TPL 312
Cdd:PHA02874  252 IDgsTPL 258
PHA03100 PHA03100
ankyrin repeat protein; Provisional
185-386 4.40e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 86.64  E-value: 4.40e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 185 ITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEH-----EEVVEFLLSQGADANKTNKDGLLPLHIAS- 258
Cdd:PHA03100   36 VLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLLLEYGANVNAPDNNGITPLLYAIs 115
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 259 -KKGNYRIVQMLLPVTSRTRIRRS-GVSPLHLAAERNHD--EVLEALLSARFDVNtplAPERARLY----------EDRR 324
Cdd:PHA03100  116 kKSNSYSIVEYLLDNGANVNIKNSdGENLLHLYLESNKIdlKILKLLIDKGVDIN---AKNRVNYLlsygvpinikDVYG 192
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217297704 325 SSALYFAVVNNNVYATELLLQHGADPN-RDVI--SPLLVAIRHGCLRTMQLLLDHGANIDAYIAT 386
Cdd:PHA03100  193 FTPLHYAVYNNNPEFVKYLLDLGANPNlVNKYgdTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257
Ank_2 pfam12796
Ankyrin repeats (3 copies);
188-270 7.36e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 7.36e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 188 LFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQgADANKTNkDGLLPLHIASKKGNYRIVQ 267
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVK 78

                  ...
gi 2217297704 268 MLL 270
Cdd:pfam12796  79 LLL 81
PHA02875 PHA02875
ankyrin repeat protein; Provisional
191-388 4.93e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 80.42  E-value: 4.93e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 191 AAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 270
Cdd:PHA02875    9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELL 88
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 271 PVTSRTR--IRRSGVSPLHLAAERNHDEVLEALLSARFDVNTPlaperarlyEDRRSSALYFAVVNNNVYATELLLQHGA 348
Cdd:PHA02875   89 DLGKFADdvFYKDGMTPLHLATILKKLDIMKLLIARGADPDIP---------NTDKFSPLHLAVMMGDIKGIELLIDHKA 159
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2217297704 349 DPNRD---VISPLLVAIRHGCLRTMQLLLDHGANIDaYIATHP 388
Cdd:PHA02875  160 CLDIEdccGCTPLIIAMAKGDIAICKMLLDSGANID-YFGKNG 201
PHA02875 PHA02875
ankyrin repeat protein; Provisional
122-309 1.69e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 78.49  E-value: 1.69e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 122 LQRACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVES---KNayGITPLFVAAQSGQLE 198
Cdd:PHA02875   39 IKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDvfyKD--GMTPLHLATILKKLD 116
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 199 ALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRI 278
Cdd:PHA02875  117 IMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDY 196
                         170       180       190
                  ....*....|....*....|....*....|...
gi 2217297704 279 --RRSGVSPLHLAAERNHDEVLEALLSARFDVN 309
Cdd:PHA02875  197 fgKNGCVAALCYAIENNKIDIVRLFIKRGADCN 229
PHA02876 PHA02876
ankyrin repeat protein; Provisional
155-414 8.85e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 77.41  E-value: 8.85e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 155 LHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNAS--------------- 219
Cdd:PHA02876  149 IKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSvlecavdsknidtik 228
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 220 --------------ALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNY-RIVQMLLPVTSRTRIRR-SGV 283
Cdd:PHA02876  229 aiidnrsninkndlSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNiKGE 308
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 284 SPLHLAAERNHD-EVLEALLSARFDVN-------TPL--------------------APERARLYEDRrsSALYFAVVNN 335
Cdd:PHA02876  309 TPLYLMAKNGYDtENIRTLIMLGADVNaadrlyiTPLhqastldrnkdivitllelgANVNARDYCDK--TPIHYAAVRN 386
                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 336 NVYATELLLQHGADPnrDVISPLLVAIRHGCL------RTMQLLLDHGANIDA---YIAThptafPATIMFAMKC-LSLL 405
Cdd:PHA02876  387 NVVIINTLLDYGADI--EALSQKIGTALHFALcgtnpyMSVKTLIDRGANVNSknkDLST-----PLHYACKKNCkLDVI 459

                  ....*....
gi 2217297704 406 KFLMDLGCD 414
Cdd:PHA02876  460 EMLLDNGAD 468
Ank_2 pfam12796
Ankyrin repeats (3 copies);
74-181 1.27e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.37  E-value: 1.27e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704  74 LIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGqvgclkvlqracerkNAEAVKILVQHnADTNHRCNrGWT 153
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNG---------------HLEIVKLLLEH-ADVNLKDN-GRT 63
                          90       100
                  ....*....|....*....|....*...
gi 2217297704 154 ALHESVSRNDLEVMQILVSGGAKVESKN 181
Cdd:pfam12796  64 ALHYAARSGHLEIVKLLLEKGADINVKD 91
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
504-545 3.62e-14

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: 66.37  E-value: 3.62e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2217297704 504 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 545
Cdd:cd03716     1 STPRSLQHLCRLAIRRCLGRRRLELIKKLPLPPRLKDYLLYE 42
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
506-545 6.35e-14

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: 65.95  E-value: 6.35e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2217297704 506 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 545
Cdd:cd03587     2 PRSLQHLCRLAIRRCLGKRRLDLIDKLPLPPRLKDYLLYK 41
PHA02859 PHA02859
ankyrin repeat protein; Provisional
65-261 5.14e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 68.31  E-value: 5.14e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704  65 YPWTRPADPLIKAIKDGDEEALKTMIK---EGKNLAEPnkegwlPLHEaayygqvgCLKVlqracERKNAEAVKILVQHN 141
Cdd:PHA02859   16 YLFYRYCNPLFYYVEKDDIEGVKKWIKfvnDCNDLYET------PIFS--------CLEK-----DKVNVEILKFLIENG 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 142 ADTNHRC-NRGWTALHESVSRN---DLEVMQILVSGGAKVESKNAYGITPL--FVAAQSGQLEALRFLAKYGADINTQAS 215
Cdd:PHA02859   77 ADVNFKTrDNNLSALHHYLSFNknvEPEILKILIDSGSSITEEDEDGKNLLhmYMCNFNVRINVIKLLIDSGVSFLNKDF 156
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 2217297704 216 DNASALYEACK-NEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKG 261
Cdd:PHA02859  157 DNNNILYSYILfHSDKKIFDFLTSLGIDINETNKSGYNCYDLIKFRN 203
PHA02876 PHA02876
ankyrin repeat protein; Provisional
73-280 1.50e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 70.09  E-value: 1.50e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704  73 PLIKAIKDG-DEEALKTMIKEGKNLAEPNKEGWLPLHEAAyygqvgclkVLQRacerkNAEAVKILVQHNADTNHRCNRG 151
Cdd:PHA02876  310 PLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQAS---------TLDR-----NKDIVITLLELGANVNARDYCD 375
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 152 WTALHESVSRNDLEVMQILVSGGAKVES-KNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHE 230
Cdd:PHA02876  376 KTPIHYAAVRNNVVIINTLLDYGADIEAlSQKIGTALHFALCGTNPYMSVKTLIDRGANVNSKNKDLSTPLHYACKKNCK 455
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2217297704 231 -EVVEFLLSQGADANKTNKDGLLPLHIASkkGNYRIVQMLLPVTSRTRIRR 280
Cdd:PHA02876  456 lDVIEMLLDNGADVNAINIQNQYPLLIAL--EYHGIVNILLHYGAELRDSR 504
PHA02874 PHA02874
ankyrin repeat protein; Provisional
194-388 2.49e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.84  E-value: 2.49e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 194 SGQLEALRFLAKYGAD-INTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPv 272
Cdd:PHA02874   11 SGDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLID- 89
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 273 tsrtrirrSGVSPLHLAAERNHDEVLEALLSARFDVNTplaperarlyEDRRSSA-LYFAVVNNNVYATELLLQHGADPN 351
Cdd:PHA02874   90 --------NGVDTSILPIPCIEKDMIKTILDCGIDVNI----------KDAELKTfLHYAIKKGDLESIKMLFEYGADVN 151
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|..
gi 2217297704 352 RDVIS---PLLVAIRHGCLRTMQLLLDHGA--NIDAYIATHP 388
Cdd:PHA02874  152 IEDDNgcyPIHIAIKHNFFDIIKLLLEKGAyaNVKDNNGESP 193
PHA03095 PHA03095
ankyrin-like protein; Provisional
83-310 3.02e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.90  E-value: 3.02e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704  83 EEALKTMIKEGKNLAEPNKEGWLPLHEaayygqvgCLKVLqraceRKNAEAVKILVQHNADTNHRCNRGWTALHESVSRN 162
Cdd:PHA03095   97 LDVIKLLIKAGADVNAKDKVGRTPLHV--------YLSGF-----NINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSR 163
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 163 --DLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEA--LRFLAKYGADIN-TQASDN----ASALYEACKNeheEVV 233
Cdd:PHA03095  164 naNVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRAriVRELIRAGCDPAaTDMLGNtplhSMATGSSCKR---SLV 240
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 234 EFLLSQGADANKTNKDGLLPLHIASKKGN----YRIVQMLLPVTSRTrirRSGVSPLHLAAERNHDEVLEALLSARFDVN 309
Cdd:PHA03095  241 LPLLIAGISINARNRYGQTPLHYAAVFNNpracRRLIALGADINAVS---SDGNTPLSLMVRNNNGRAVRAALAKNPSAE 317

                  .
gi 2217297704 310 T 310
Cdd:PHA03095  318 T 318
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
69-270 4.03e-12

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: 68.89  E-value: 4.03e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704  69 RPAD-PLIKAIKDGDEEALKTMIK-EGKNLAEPNKEGWLPLHEAAYYGQVGCLKVLqracerknAEAVKILVqhNADTNH 146
Cdd:cd22192    15 RISEsPLLLAAKENDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVL--------MEAAPELV--NEPMTS 84
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 147 RCNRGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAKYGADINT 212
Cdd:cd22192    85 DLYQGETALHIAVVNQNLNLVRELIARGADVVSPRAtgtffrpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIRA 164
                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 2217297704 213 QASDNASALY----EACKNEHEEVVEFLLSQGADANK------TNKDGLLPLHIASKKGNYRIVQMLL 270
Cdd:cd22192   165 QDSLGNTVLHilvlQPNKTFACQMYDLILSYDKEDDLqpldlvPNNQGLTPFKLAAKEGNIVMFQHLV 232
PHA02874 PHA02874
ankyrin repeat protein; Provisional
129-380 4.31e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.07  E-value: 4.31e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 129 KNAEAVKILVQHNAD-TNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYG 207
Cdd:PHA02874   12 GDIEAIEKIIKNKGNcINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNG 91
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 208 AD-----------------------INTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYR 264
Cdd:PHA02874   92 VDtsilpipciekdmiktildcgidVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFD 171
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 265 IVQMLLPVTSRTRIRR-SGVSPLHLAAERNHDEVLEALLSARFDVNTPLaperarlyeDRRSSALYFAVVNNNVyATELL 343
Cdd:PHA02874  172 IIKLLLEKGAYANVKDnNGESPLHNAAEYGDYACIKLLIDHGNHIMNKC---------KNGFTPLHNAIIHNRS-AIELL 241
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|
gi 2217297704 344 LQHGADPNRDV--ISPLLVAIRHGC-LRTMQLLLDHGANI 380
Cdd:PHA02874  242 INNASINDQDIdgSTPLHHAINPPCdIDIIDILLYHKADI 281
Ank_2 pfam12796
Ankyrin repeats (3 copies);
286-382 4.66e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.06  E-value: 4.66e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 286 LHLAAERNHDEVLEALLSARFDVNtplaperarLYEDRRSSALYFAVVNNNVYATELLLQHgADPNRDVI--SPLLVAIR 363
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADAN---------LQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNgrTALHYAAR 70
                          90
                  ....*....|....*....
gi 2217297704 364 HGCLRTMQLLLDHGANIDA 382
Cdd:pfam12796  71 SGHLEIVKLLLEKGADINV 89
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
505-543 1.55e-11

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


Pssm-ID: 462192  Cd Length: 39  Bit Score: 59.10  E-value: 1.55e-11
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2217297704 505 PPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLK 543
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYLL 39
Ank_4 pfam13637
Ankyrin repeats (many copies);
219-270 2.30e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 58.83  E-value: 2.30e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217297704 219 SALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 270
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
74-249 1.87e-10

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 63.73  E-value: 1.87e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704  74 LIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGClkvlqracerknaeaVKILVQHNADTNHRCNRGWT 153
Cdd:PLN03192  529 LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDC---------------VLVLLKHACNVHIRDANGNT 593
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 154 ALHESVSRNDLEVMQILVSGgAKVESKNAYGiTPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVV 233
Cdd:PLN03192  594 ALWNAISAKHHKIFRILYHF-ASISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMV 671
                         170
                  ....*....|....*.
gi 2217297704 234 EFLLSQGADANKTNKD 249
Cdd:PLN03192  672 RLLIMNGADVDKANTD 687
PHA02878 PHA02878
ankyrin repeat protein; Provisional
213-382 3.23e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 62.59  E-value: 3.23e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 213 QASDNASA-----LYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIRRSGVSpLH 287
Cdd:PHA02878   28 NYSTSASLipfipLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLVA-IK 106
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 288 LAAERNHDEVLEALLSARFDVN--------------TPLAPERARLY-----------EDRRSSALYFAVVNNNVYATEL 342
Cdd:PHA02878  107 DAFNNRNVEIFKIILTNRYKNIqtidlvyidkkskdDIIEAEITKLLlsygadinmkdRHKGNTALHYATENKDQRLTEL 186
                         170       180       190       200
                  ....*....|....*....|....*....|....*....|...
gi 2217297704 343 LLQHGADPN---RDVISPLLVAIRHGCLRTMQLLLDHGANIDA 382
Cdd:PHA02878  187 LLSYGANVNipdKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229
Ank_4 pfam13637
Ankyrin repeats (many copies);
186-237 4.72e-10

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 55.36  E-value: 4.72e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 2217297704 186 TPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLL 237
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03095 PHA03095
ankyrin-like protein; Provisional
70-239 1.33e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 57.34  E-value: 1.33e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704  70 PADPLIKAiKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYgqvgclkvlqracERKNAEAVKILVQHNADTNHRCN 149
Cdd:PHA03095  155 PLAVLLKS-RNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQS-------------FKPRARIVRELIRAGCDPAATDM 220
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 150 RGWTALHE--SVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKN 227
Cdd:PHA03095  221 LGNTPLHSmaTGSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRN 300
                         170
                  ....*....|..
gi 2217297704 228 EHEEVVEFLLSQ 239
Cdd:PHA03095  301 NNGRAVRAALAK 312
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
507-545 1.71e-08

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


Pssm-ID: 198037  Cd Length: 34  Bit Score: 50.10  E-value: 1.71e-08
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 2217297704  507 RPLAHLCRLRVRKAIGKyriklLDTLPLPGRLIRYLKYE 545
Cdd:smart00969   1 RSLQHLCRLAIRRSLGG-----IDKLPLPPRLKDYLLYY 34
PHA02798 PHA02798
ankyrin-like protein; Provisional
134-363 1.85e-08

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 56.77  E-value: 1.85e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 134 VKILVQHNADTNHRCNRGWTALHESVSR---NDLEVMQILVSGGAKVESKNAYGITPLFVAAQSG---QLEALRFLAKYG 207
Cdd:PHA02798   92 VKILIENGADINKKNSDGETPLYCLLSNgyiNNLEILLFMIENGADTTLLDKDGFTMLQVYLQSNhhiDIEIIKLLLEKG 171
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 208 ADINTQASDNA-SALYEACKNEHE----EVVEFLLSQGADANKTNK-------DGLLPLHIASKKGNYRIVQMLLPVTSR 275
Cdd:PHA02798  172 VDINTHNNKEKyDTLHCYFKYNIDridaDILKLFVDNGFIINKENKshkkkfmEYLNSLLYDNKRFKKNILDFIFSYIDI 251
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 276 TRIRRSGVSPLHLAAERNHDEVLEALLSARFDVN--TPLAperarlyedrrSSALYFAVVNNNVYATELLLQHgaDPNRD 353
Cdd:PHA02798  252 NQVDELGFNPLYYSVSHNNRKIFEYLLQLGGDINiiTELG-----------NTCLFTAFENESKFIFNSILNK--KPNKN 318
                         250
                  ....*....|
gi 2217297704 354 VISPLLVAIR 363
Cdd:PHA02798  319 TISYTYYKLR 328
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
192-270 2.29e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.83  E-value: 2.29e-08
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 2217297704 192 AQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 270
Cdd:PTZ00322   90 AASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLS 168
SOCS_SSB1_4 cd03718
SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box ...
506-545 2.83e-08

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: 49.99  E-value: 2.83e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2217297704 506 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 545
Cdd:cd03718     3 PLPLMDLCRRRVRVALGRDRLEEIEQLPLPPSLKNYLLYQ 42
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
46-270 4.83e-08

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: 55.92  E-value: 4.83e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704  46 PTTAEATASACTNRQPAHFYPWT-RPADPLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLP---LHE--AAYYGQVGCL 119
Cdd:cd22194    20 PQSPQDDTPSNPNSPSAELAKEEqRDKKKRLKKVSEAAVEELGELLKELKDLSRRRRKTDVPdflMHKltASDTGKTCLM 99
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 120 KVLQRACERKNaEAVKILVQH-----------NADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESKNA------ 182
Cdd:cd22194   100 KALLNINENTK-EIVRILLAFaeengildrfiNAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVNAHAKgvffnp 178
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 183 --------YGITPLFVAAQSGQLEALRFLAKYGADI--------NT------QASDNASA-------LYE----ACKNEH 229
Cdd:cd22194   179 kykhegfyFGETPLALAACTNQPEIVQLLMEKESTDitsqdsrgNTvlhalvTVAEDSKTqndfvkrMYDmillKSENKN 258
                         250       260       270       280
                  ....*....|....*....|....*....|....*....|.
gi 2217297704 230 EEVVefllsqgadankTNKDGLLPLHIASKKGNYRIVQMLL 270
Cdd:cd22194   259 LETI------------RNNEGLTPLQLAAKMGKAEILKYIL 287
SOCS_ASB1 cd03720
SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a ...
506-545 8.05e-08

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


Pssm-ID: 239690  Cd Length: 42  Bit Score: 48.57  E-value: 8.05e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2217297704 506 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 545
Cdd:cd03720     3 PRSLLSLCRIAVRRALGKQRLSLICSLPLPDPIKKFLLHE 42
SOCS_ASB14 cd03730
SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a ...
504-545 9.79e-08

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


Pssm-ID: 239700  Cd Length: 57  Bit Score: 48.69  E-value: 9.79e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2217297704 504 EPPRPLAHLCRLRVRKAIGKYRIK---LLDTLPLPGRLIRYLKYE 545
Cdd:cd03730     1 TNPRSLKHLCRLKIRACMGRLRLRcpvFMSFLPLPNRLKAYILYK 45
PHA02946 PHA02946
ankyin-like protein; Provisional
77-288 9.91e-08

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 54.29  E-value: 9.91e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704  77 AIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAyygqvgclkvlqracERKNAEAVKILVQHNADTNHRCNRGWTALH 156
Cdd:PHA02946   46 GIKGLDERFVEELLHRGYSPNETDDDGNYPLHIAS---------------KINNNRIVAMLLTHGADPNACDKQHKTPLY 110
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 157 ESVSRND--LEVMQILVSGGAKVE-SKNAYGITPLFVAAQSGQLEALRFLA-KYGADINTQASDNASALYEACKNEHEEV 232
Cdd:PHA02946  111 YLSGTDDevIERINLLVQYGAKINnSVDEEGCGPLLACTDPSERVFKKIMSiGFEARIVDKFGKNHIHRHLMSDNPKAST 190
                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 2217297704 233 VEFLLSQGADANKTNKDGLLPLHIASKK--GNYRIVQMLLPVTSRTRIRRSGVSPLHL 288
Cdd:PHA02946  191 ISWMMKLGISPSKPDHDGNTPLHIVCSKtvKNVDIINLLLPSTDVNKQNKFGDSPLTL 248
Ank_4 pfam13637
Ankyrin repeats (many copies);
72-122 1.11e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.42  E-value: 1.11e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 2217297704  72 DPLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVGCLKVL 122
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
72-270 1.18e-07

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: 54.70  E-value: 1.18e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704  72 DPLIKAIKDGDEEALKTMIKEGKNLAEpnkEGWLPLHEAAYYGQVGC----LKVLQRACERKNAEAVkilvqhNADTNHR 147
Cdd:TIGR00870  54 SALFVAAIENENLELTELLLNLSCRGA---VGDTLLHAISLEYVDAVeailLHLLAAFRKSGPLELA------NDQYTSE 124
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 148 CNRGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAKYGADINTQ 213
Cdd:TIGR00870 125 FTPGITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTA 204
                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217297704 214 AS-----DNASALYEACKNEHEEVV----EFLLSQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 270
Cdd:TIGR00870 205 DSlgntlLHLLVMENEFKAEYEELScqmyNFALSLLDKLRDSkelevilNHQGLTPLKLAAKEGRIVLFRLKL 277
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
252-399 1.35e-07

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 54.25  E-value: 1.35e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 252 LPLHIASKKGNYRIVQMLLpVTSRTRIRRSGV---SPLHLAAERNHDEVLEALL-SARFDVNTPLAPErarLYEDRrsSA 327
Cdd:cd22192    19 SPLLLAAKENDVQAIKKLL-KCPSCDLFQRGAlgeTALHVAALYDNLEAAVVLMeAAPELVNEPMTSD---LYQGE--TA 92
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 328 LYFAVVNNNVYATELLLQHGAD------------PNRDVI-----SPLLVAIRHGCLRTMQLLLDHGANIDA-------- 382
Cdd:cd22192    93 LHIAVVNQNLNLVRELIARGADvvspratgtffrPGPKNLiyygeHPLSFAACVGNEEIVRLLIEHGADIRAqdslgntv 172
                         170
                  ....*....|....*....
gi 2217297704 383 --YIATHPTAFPATIMFAM 399
Cdd:cd22192   173 lhILVLQPNKTFACQMYDL 191
SOCS_SSB4 cd03743
SOCS (suppressors of cytokine signaling) box of SSB4 (SPRY domain-containing SOCS box ...
506-545 1.89e-07

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: 47.64  E-value: 1.89e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2217297704 506 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 545
Cdd:cd03743     3 PLPLMDLCRRSARQALGRHRLHHIQSLPLPQTLKNYLQYQ 42
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
506-544 2.28e-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: 2.28e-07
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2217297704 506 PRPLAHLCRLRVRKAIGKYRIkllDTLPLPGRLIRYLKY 544
Cdd:cd03717     3 VRSLQHLCRFVIRQCTRRDLI---DQLPLPRRLKDYLKE 38
PHA02875 PHA02875
ankyrin repeat protein; Provisional
73-211 2.51e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.07  E-value: 2.51e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704  73 PLIKAIKDGDEEALKTMIKEGKNLAEPNKEGWLPLHEAAYYGQVgclkvlqracerknaEAVKILVQHNADTNHRCNRGW 152
Cdd:PHA02875  105 PLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI---------------KGIELLIDHKACLDIEDCCGC 169
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217297704 153 TALHESVSRNDLEVMQILVSGGAKVE--SKNAyGITPLFVAAQSGQLEALRFLAKYGADIN 211
Cdd:PHA02875  170 TPLIIAMAKGDIAICKMLLDSGANIDyfGKNG-CVAALCYAIENNKIDIVRLFIKRGADCN 229
Ank_4 pfam13637
Ankyrin repeats (many copies);
118-171 2.64e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 2.64e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217297704 118 CLKVLQRACERKNAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILV 171
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
107-270 3.00e-07

Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily (TRPV), named after the vanilloid receptor 1 (TRPV1), consists of six members: four thermo-sensing channels (TRPV1, TRPV2, TRPV3, and TRPV4) and two Ca2+ selective channels (TRPV5 and TRPV6). The calcium-selective channels TRPV5 and TRPV6 can be heterotetramers and are important for general Ca2+ homeostasis. All four channels within the TRPV1-4 group show temperature-invoked currents when expressed in heterologous cell systems, ranging from activation at ~25C for TRPV4 to ~52C for TRPV2. The structure of TRPV shows the typical topology features of all Transient Receptor Potential (TRP) ion channel family members, such as six transmembrane regions, a short hydrophobic stretch between transmembrane segments 5 and 6 and large intracellular N- and C-terminal domains. The TRP family consists of membrane proteins that function as ion channels that communicate between the cell and its environment, by a vast array of physical or chemical stimuli, including radiation (in the form of temperature, infrared ,or light) and pressure (osmotic or mechanical). TRP channels are formed by a tetrameric complex of channel subunits. Based on sequence identity, the mammalian TRP channel family is classified into six subfamilies, with significant sequence similarity within the transmembrane domains, but very low similarity in their N- and C-terminal cytoplasmic regions. The six subfamilies are named based on their first member: TRPC (canonical), TRPV (vanilloid), TRPM (melastatin), TRPA (ankyrin), TRPML (mucolipin), and TRPP (polycystic).


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 53.35  E-value: 3.00e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 107 LHEAAYY---GQVGCLKVLQRACerKNAEAVKILVqhNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESKNA- 182
Cdd:cd21882    30 LHKAALNlndGVNEAIMLLLEAA--PDSGNPKELV--NAPCTDEFYQGQTALHIAIENRNLNLVRLLVENGADVSARATg 105
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 183 ------------YGITPLFVAAQSGQLEALRFLAKYGADI-NTQASDNAS-----ALYEACKNEHE------EVVEFLLS 238
Cdd:cd21882   106 rffrkspgnlfyFGELPLSLAACTNQEEIVRLLLENGAQPaALEAQDSLGntvlhALVLQADNTPEnsafvcQMYNLLLS 185
                         170       180       190
                  ....*....|....*....|....*....|....*....
gi 2217297704 239 QGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 270
Cdd:cd21882   186 YGAHLDPTqqleeipNHQGLTPLKLAAVEGKIVMFQHIL 224
SOCS_SOCS7 cd03741
SOCS (suppressors of cytokine signaling) box of SOCS7-like proteins. Together with CIS1, the ...
507-546 4.91e-07

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: 46.63  E-value: 4.91e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2217297704 507 RPLAHLCRLRVRKAIgkyRIKLLDTLPLPGRLIRYLKYEN 546
Cdd:cd03741     4 QSLQHLCRFVIRKLV---RRDHIPALPLPRRLIDYLREKH 40
PHA02884 PHA02884
ankyrin repeat protein; Provisional
266-416 1.16e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 50.37  E-value: 1.16e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 266 VQMLLPVTSRTRIRRSGVspLHLAAERNHDEVLEALLSARFDVNTPLAperarLYEDRRSSALYFAVVNNNVYATELLLQ 345
Cdd:PHA02884   19 IIFYIAIKKKNKICIANI--LYSSIKFHYTDIIDAILKLGADPEAPFP-----LSENSKTNPLIYAIDCDNDDAAKLLIR 91
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217297704 346 HGADPNR----DVISPLLVAIRHGCLRTMQLLLDHGANIDAYIATHPTAFPATIMFamkCLSLLKFLMdlgCDGE 416
Cdd:PHA02884   92 YGADVNRyaeeAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALMI---CNNFLAFMI---CDNE 160
SOCS smart00253
suppressors of cytokine signalling; suppressors of cytokine signalling
500-544 1.54e-06

suppressors of cytokine signalling; suppressors of cytokine signalling


Pssm-ID: 128549  Cd Length: 43  Bit Score: 44.98  E-value: 1.54e-06
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 2217297704  500 KEKAEPPRPLAHLCRLRVRKAIGKYRIKlldTLPLPGRLIRYLKY 544
Cdd:smart00253   1 LPRPSNVPSLQHLCRFTIRRCTRTDQIK---TLPLPPKLKDYLSY 42
PHA03095 PHA03095
ankyrin-like protein; Provisional
217-437 2.30e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.02  E-value: 2.30e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 217 NASALY---EACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNY---RIVQMLLP----VTSRTrirRSGVSPL 286
Cdd:PHA03095   11 MEAALYdylLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSEkvkDIVRLLLEagadVNAPE---RCGFTPL 87
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 287 HLAAERNHDE-VLEALLSARFDVN-------TPLaperarlyedrrssALYFAVVNNNVYATELLLQHGADPN-RDV--I 355
Cdd:PHA03095   88 HLYLYNATTLdVIKLLIKAGADVNakdkvgrTPL--------------HVYLSGFNINPKVIRLLLRKGADVNaLDLygM 153
                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 356 SPLLVAIR-HGC-LRTMQLLLDHGANIDAYIATHPTAFPATIMFAMKCLSLLKFLMDLGCDgePCFSCLYGNGP-HPPAP 432
Cdd:PHA03095  154 TPLAVLLKsRNAnVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRARIVRELIRAGCD--PAATDMLGNTPlHSMAT 231

                  ....*
gi 2217297704 433 QPSSR 437
Cdd:PHA03095  232 GSSCK 236
SOCS_SSB2 cd03719
SOCS (suppressors of cytokine signaling) box of SSB2 (SPRY domain-containing SOCS box proteins) ...
504-545 4.92e-06

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


Pssm-ID: 239689  Cd Length: 42  Bit Score: 43.47  E-value: 4.92e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 2217297704 504 EPPRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 545
Cdd:cd03719     1 AEPHSLLHLSRLCVRHALGDTRLGQVSALPLPPAMKRYLLYQ 42
SOCS_SSB1 cd03744
SOCS (suppressors of cytokine signaling) box of SSB1 (SPRY domain-containing SOCS box proteins) ...
506-545 5.47e-06

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


Pssm-ID: 239713  Cd Length: 42  Bit Score: 43.43  E-value: 5.47e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2217297704 506 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 545
Cdd:cd03744     3 PLPLMDLCRRSVRLALGRERLSEIHTLPLPASLKNYLLYQ 42
Ank_4 pfam13637
Ankyrin repeats (many copies);
151-203 6.99e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 6.99e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217297704 151 GWTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFL 203
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLL 53
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
504-545 7.37e-06

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


Pssm-ID: 239701  Cd Length: 56  Bit Score: 43.28  E-value: 7.37e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*
gi 2217297704 504 EPPRPLAHLCRLRVRKAIGKYRIKLLDT---LPLPGRLIRYLKYE 545
Cdd:cd03731     1 ENPRPLKHLCRLKIRKLMGLQKLQQPSSmkkLPLPPALKRYILYK 45
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
155-349 7.75e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 48.71  E-value: 7.75e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 155 LHESVSRNDLEVMQILVSGGAkvESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVE 234
Cdd:PLN03192  498 LQHHKELHDLNVGDLLGDNGG--EHDDPNMASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVL 575
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 235 FLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIRRSGvSPLHLAAERNHDEVLEALLSARFDVNTplap 314
Cdd:PLN03192  576 VLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFASISDPHAAG-DLLCTAAKRNDLTAMKELLKQGLNVDS---- 650
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2217297704 315 erarlyEDRR-SSALYFAVVNNNVYATELLLQHGAD 349
Cdd:PLN03192  651 ------EDHQgATALQVAMAEDHVDMVRLLIMNGAD 680
PHA02946 PHA02946
ankyin-like protein; Provisional
213-270 1.55e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 47.36  E-value: 1.55e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 213 QASDNASALYEAC--KNEHEEVVEFLLSQGADANKTNKDGLLPLHIASKKGNYRIVQMLL 270
Cdd:PHA02946   33 EPSGNYHILHAYCgiKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLL 92
PHA02859 PHA02859
ankyrin repeat protein; Provisional
177-309 1.83e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165195 [Multi-domain]  Cd Length: 209  Bit Score: 45.97  E-value: 1.83e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 177 VESKNAYGITPLF--VAAQSGQLEALRFLAKYGADINTQASD-NASALYEAC---KNEHEEVVEFLLSQGADANKTNKDG 250
Cdd:PHA02859   44 VNDCNDLYETPIFscLEKDKVNVEILKFLIENGADVNFKTRDnNLSALHHYLsfnKNVEPEILKILIDSGSSITEEDEDG 123
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 251 LLPLHIASKKGNYRIVQMLLpvtsrtrIRRSGVSPLHLAAERNH-----------DEVLEALLSARFDVN 309
Cdd:PHA02859  124 KNLLHMYMCNFNVRINVIKL-------LIDSGVSFLNKDFDNNNilysyilfhsdKKIFDFLTSLGIDIN 186
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
168-238 2.28e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 47.20  E-value: 2.28e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 2217297704 168 QILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEFLLS 238
Cdd:PTZ00322   99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_2 pfam12796
Ankyrin repeats (3 copies);
73-147 2.73e-05

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 42.80  E-value: 2.73e-05
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 2217297704  73 PLIKAIKDGDEEALKTMIKegKNLAEPNKEGWLPLHEAAYYGQVgclkvlqracerknaEAVKILVQHNADTNHR 147
Cdd:pfam12796  33 ALHLAAKNGHLEIVKLLLE--HADVNLKDNGRTALHYAARSGHL---------------EIVKLLLEKGADINVK 90
SOCS_ASB13 cd03729
SOCS (suppressors of cytokine signaling) box of ASB13-like proteins. ASB family members have a ...
506-544 2.73e-05

SOCS (suppressors of cytokine signaling) box of ASB13-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239699  Cd Length: 42  Bit Score: 41.31  E-value: 2.73e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2217297704 506 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKY 544
Cdd:cd03729     3 PLSLQQLCRINLRKALGTRALEKIAKLNIPNRIIDYLSY 41
SOCS_ASB5 cd03724
SOCS (suppressors of cytokine signaling) box of ASB5-like proteins. ASB family members have a ...
506-544 3.00e-05

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


Pssm-ID: 239694  Cd Length: 42  Bit Score: 41.40  E-value: 3.00e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 2217297704 506 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKY 544
Cdd:cd03724     3 PSSLCQLCRLCIRNYIGRSRLHLIPQLQLPTLLKNFLQY 41
SOCS_ASB7 cd03726
SOCS (suppressors of cytokine signaling) box of ASB7-like proteins. ASB family members have a ...
506-545 3.88e-05

SOCS (suppressors of cytokine signaling) box of ASB7-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239696  Cd Length: 45  Bit Score: 40.99  E-value: 3.88e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 2217297704 506 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYE 545
Cdd:cd03726     3 PRTLQDLCRIKIRHCIGLQNLKLLDELPIAKVMKDYLKHK 42
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
150-270 1.23e-04

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 44.79  E-value: 1.23e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 150 RGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFL---AKYGADINT 212
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKgrffqpkyqgegfyFGELPLSLAACTNQPDIVQYLlenEHQPADIEA 154
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217297704 213 QASDNAS---ALYEACKNEHEE------VVEFLLSQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 270
Cdd:cd22193   155 QDSRGNTvlhALVTVADNTKENtkfvtrMYDMILIRGAKLCPTveleeirNNDGLTPLQLAAKMGKIEILKYIL 228
Ank_5 pfam13857
Ankyrin repeats (many copies);
203-257 1.32e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 40.02  E-value: 1.32e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 2217297704 203 LAKYGADINTQASDNASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIA 257
Cdd:pfam13857   2 LEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02989 PHA02989
ankyrin repeat protein; Provisional
156-237 1.33e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 44.73  E-value: 1.33e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 156 HESVSRNDLEVMQILVSGgAKVESKNAYGITPLFVAAQSGQLEALRFLAKYGADINTQASDNASALYEACKNEHEEVVEF 235
Cdd:PHA02989  229 NKILSKKEFKVLNFILKY-IKINKKDKKGFNPLLISAKVDNYEAFNYLLKLGDDIYNVSKDGDTVLTYAIKHGNIDMLNR 307

                  ..
gi 2217297704 236 LL 237
Cdd:PHA02989  308 IL 309
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
183-212 1.86e-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: 38.78  E-value: 1.86e-04
                          10        20        30
                  ....*....|....*....|....*....|
gi 2217297704 183 YGITPLFVAAQSGQLEALRFLAKYGADINT 212
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
183-211 2.24e-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: 2.24e-04
                           10        20
                   ....*....|....*....|....*....
gi 2217297704  183 YGITPLFVAAQSGQLEALRFLAKYGADIN 211
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADIN 29
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
506-546 2.64e-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: 2.64e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2217297704 506 PRPLAHLCRLRVRKAIGKYRIKLLDTLPLPGRLIRYLKYEN 546
Cdd:cd03723     3 PRSLQHLCRCAIRKLLGSRCHKLVPQLSLPTSLKNYLLLEP 43
TRPV1 cd22196
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 1; Vanilloid receptor 1 ...
150-270 2.96e-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: 43.64  E-value: 2.96e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 150 RGWTALHESVSRNDLEVMQILVSGGAKVESKNA--------------YGITPLFVAAQSGQLEALRFLAK---YGADINT 212
Cdd:cd22196    93 KGQTALHIAIERRNMHLVELLVQNGADVHARASgeffkkkkggpgfyFGELPLSLAACTNQLDIVKFLLEnphSPADISA 172
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217297704 213 QASDNAS---ALYEACKNEHE------EVVEFLLSQGADANK-------TNKDGLLPLHIASKKGNYRIVQMLL 270
Cdd:cd22196   173 RDSMGNTvlhALVEVADNTPEntkfvtKMYNEILILGAKIRPllkleeiTNKKGLTPLKLAAKTGKIGIFAYIL 246
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
282-309 4.37e-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: 37.57  E-value: 4.37e-04
                           10        20
                   ....*....|....*....|....*...
gi 2217297704  282 GVSPLHLAAERNHDEVLEALLSARFDVN 309
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADIN 29
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
177-351 7.73e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.38  E-value: 7.73e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 177 VESKNAYGITPLFVAAQSGQLEALRFLAKYgadINTQASDNASALYEACKNEHEeVVEFLLSQGADANKtnKDGLLPLHI 256
Cdd:TIGR00870  45 INCPDRLGRSALFVAAIENENLELTELLLN---LSCRGAVGDTLLHAISLEYVD-AVEAILLHLLAAFR--KSGPLELAN 118
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 257 ASKKGNYrivqmllpvtsrTRirrsGVSPLHLAAERNHDEVLEALLSARFDVNTP-------LAPERARLYEDRRSSALY 329
Cdd:TIGR00870 119 DQYTSEF------------TP----GITALHLAAHRQNYEIVKLLLERGASVPARacgdffvKSQGVDSFYHGESPLNAA 182
                         170       180
                  ....*....|....*....|..
gi 2217297704 330 FAVVNNNVYAteLLLQHGADPN 351
Cdd:TIGR00870 183 ACLGSPSIVA--LLSEDPADIL 202
PHA03100 PHA03100
ankyrin repeat protein; Provisional
323-414 1.41e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 41.19  E-value: 1.41e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 323 RRSSALYFAVVNNNVYATELLLQHGADPNRDV-----ISPLLVAIRHGC---LRTMQLLLDHGANIDAYIATHPTAFPAT 394
Cdd:PHA03100   34 KPVLPLYLAKEARNIDVVKILLDNGADINSSTknnstPLHYLSNIKYNLtdvKEIVKLLLEYGANVNAPDNNGITPLLYA 113
                          90       100
                  ....*....|....*....|
gi 2217297704 395 IMFAMKCLSLLKFLMDLGCD 414
Cdd:PHA03100  114 ISKKSNSYSIVEYLLDNGAN 133
Ank_4 pfam13637
Ankyrin repeats (many copies);
324-374 1.50e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 1.50e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 2217297704 324 RSSALYFAVVNNNVYATELLLQHGADPNR---DVISPLLVAIRHGCLRTMQLLL 374
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAvdgNGETALHFAASNGNVEVLKLLL 54
TRPV2 cd22197
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 2; TRPV2 is closely ...
150-270 1.64e-03

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


Pssm-ID: 411981 [Multi-domain]  Cd Length: 640  Bit Score: 41.38  E-value: 1.64e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 150 RGWTALHESVSRNDLEVMQILVSGGAKVESKNA-------------YGITPLFVAAQSGQLEALRFLAKYGADI-NTQAS 215
Cdd:cd22197    93 RGHSALHIAIEKRSLQCVKLLVENGADVHARACgrffqkkqgtcfyFGELPLSLAACTKQWDVVNYLLENPHQPaSLQAQ 172
                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217297704 216 DNAS-----ALYEACKN--EHEEVV----EFLLSQGADANKT-------NKDGLLPLHIASKKGNYRIVQMLL 270
Cdd:cd22197   173 DSLGntvlhALVMIADNspENSALVikmyDGLLQAGARLCPTvqleeisNHEGLTPLKLAAKEGKIEIFRHIL 245
Ank_5 pfam13857
Ankyrin repeats (many copies);
137-188 1.74e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 1.74e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 2217297704 137 LVQH-NADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPL 188
Cdd:pfam13857   1 LLEHgPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
236-289 2.14e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.56  E-value: 2.14e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 2217297704 236 LLSQG-ADANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTRIR-RSGVSPLHLA 289
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKdEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
282-344 2.34e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.10  E-value: 2.34e-03
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 2217297704 282 GVSPLHLAAERNHDEVLEALLSARFDVNtplaperARLYEDRrsSALYFAVVNNNVYATELLL 344
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADIN-------AVDGNGE--TALHFAASNGNVEVLKLLL 54
PHA02741 PHA02741
hypothetical protein; Provisional
84-277 2.56e-03

hypothetical protein; Provisional


Pssm-ID: 165108 [Multi-domain]  Cd Length: 169  Bit Score: 38.87  E-value: 2.56e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704  84 EALKTMIKEGKNLAEPNKEGWLPLHEAAyygQVGCLKVLQRACERKNAEAVKILVQHNADTNHRCNRGWTALHEsvSRND 163
Cdd:PHA02741    2 ESPHFMTCLEEMIAEKNSEGENFFHEAA---RCGCFDIIARFTPFIRGDCHAAALNATDDAGQMCIHIAAEKHE--AQLA 76
                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 164 LEVMQILVSggakvesknaygitplfvaaqsgqlealrflakYGADINTQASDNA-SALYEACKNEHEEVVEFLLSQ-GA 241
Cdd:PHA02741   77 AEIIDHLIE---------------------------------LGADINAQEMLEGdTALHLAAHRRDHDLAEWLCCQpGI 123
                         170       180       190
                  ....*....|....*....|....*....|....*.
gi 2217297704 242 DANKTNKDGLLPLHIASKKGNYRIVQMLLPVTSRTR 277
Cdd:PHA02741  124 DLHFCNADNKSPFELAIDNEDVAMMQILREIVATSR 159
PHA02736 PHA02736
Viral ankyrin protein; Provisional
198-269 3.39e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 38.32  E-value: 3.39e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 2217297704 198 EALRFLAKYGADINTQASDNA-SALYEACKNEHEEVVEFLLSQ-GADANKTNKDGLLPLHIASKKGNYRIVQML 269
Cdd:PHA02736   72 EKLKLLMEWGADINGKERVFGnTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYYVACERHDAKMMNIL 145
SOCS_WSB_SWIP cd03733
SOCS (suppressors of cytokine signaling) box of WSB/SWiP-like proteins. This subfamily ...
509-544 3.78e-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: 35.48  E-value: 3.78e-03
                          10        20        30
                  ....*....|....*....|....*....|....*.
gi 2217297704 509 LAHLCRLRVRKAIGKYRIKlldTLPLPGRLIRYLKY 544
Cdd:cd03733     6 LQHLCRMALRRVMTTQQVL---ALPIPKKMKEFLTY 38
SOCS_ASB3 cd03722
SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a ...
509-546 5.30e-03

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


Pssm-ID: 239692  Cd Length: 51  Bit Score: 35.15  E-value: 5.30e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 2217297704 509 LAHLCRLRVRKAIGKYRIK---LLDTLPLPGRLIRYLKYEN 546
Cdd:cd03722     6 LTHLCRLEIRSSLKSERLRsdsFICQLPLPRSLQDYLLYSD 46
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
282-309 5.77e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.57  E-value: 5.77e-03
                          10        20
                  ....*....|....*....|....*....
gi 2217297704 282 GVSPLHLAAER-NHDEVLEALLSARFDVN 309
Cdd:pfam00023   2 GNTPLHLAAGRrGNLEIVKLLLSKGADVN 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
216-248 7.38e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.19  E-value: 7.38e-03
                          10        20        30
                  ....*....|....*....|....*....|....
gi 2217297704 216 DNASALYEAC-KNEHEEVVEFLLSQGADANKTNK 248
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
130-206 7.61e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.11  E-value: 7.61e-03
                          10        20        30        40        50        60        70
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 2217297704 130 NAEAVKILVQHNADTNHRCNRGWTALHESVSRNDLEVMQILVSGGAKVESKNAYGITPLFVAAQSGQLEALRFLAKY 206
Cdd:PTZ00322   94 DAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRH 170
SOCS_CIS1 cd03734
SOCS (suppressors of cytokine signaling) box of CIS (cytokine-inducible SH2 protein) 1-like ...
507-543 7.71e-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: 34.55  E-value: 7.71e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 2217297704 507 RPLAHLCRLRVRKAIGKyriklLDTLPLPGRLIRYLK 543
Cdd:cd03734     4 RSLQHLCRLVINRLVTD-----VDCLPLPRRMADYLR 35
PHA02884 PHA02884
ankyrin repeat protein; Provisional
179-259 7.86e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 38.43  E-value: 7.86e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 2217297704 179 SKNAYgITPLFVAAQSGQLEALRFLAKYGADINTQASD-NASALYEACKNEHEEVVEFLLSQGADANKTNKDGLLPLHIA 257
Cdd:PHA02884   66 SENSK-TNPLIYAIDCDNDDAAKLLIRYGADVNRYAEEaKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELA 144

                  ..
gi 2217297704 258 SK 259
Cdd:PHA02884  145 LM 146
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
216-245 8.35e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 8.35e-03
                           10        20        30
                   ....*....|....*....|....*....|
gi 2217297704  216 DNASALYEACKNEHEEVVEFLLSQGADANK 245
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
 
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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