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Conserved domains on  [gi|1469164932|ref|XP_026089120|]
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ankyrin repeat and SOCS box protein 2-like isoform X1 [Carassius auratus]

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];
172-420 1.49e-41

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.80  E-value: 1.49e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 172 LKILLKAKPETINKQTNKSQTPLMLAVCRKHFSCVEHLLEQGADPNLANNQWETPLYKACEKANEAIVELLLRFGASPTK 251
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 252 ACAQGGTPLHEAVRNKKLKITKMLIKAGAKLCAKNIYGIDSLFMAAQCNSVEVLNYLIYKGGNVNTQANDDASALFEACK 331
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 332 NGHAKAVEILLSQSADVNITNKTGLLPIHVAAKNGHDSIVAMLIPRTSMVKVR-SSGISSLHFAAENNKDSVLEILIDAG 410
Cdd:COG0666   196 NGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKdKDGLTALLLAAAAGAALIVKLLLLAL 275

                         250
                  ....*....|
gi 1469164932 411 YDVNAKMSDD 420
Cdd:COG0666   276 LLLAAALLDL 285
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
 616-655 2.17e-15

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: 70.22  E-value: 2.17e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1469164932 616 PCTLMHLCRLKIRQRLGIQRLCHISALPLPERLIMFLNYE 655
Cdd:cd03716     3 PRSLQHLCRLAIRRCLGRRRLELIKKLPLPPRLKDYLLYE 42
Ank_2 pfam12796
Ankyrin repeats (3 copies);
391-488 1.99e-12

Ankyrin repeats (3 copies);


:

Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 1.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 391 LHFAAENNKDSVLEILIDAGYDVNAKMSDDWskmyedhrsTALYSAVANSNIEAATMLLE-AGADPNLDIFNPLLVAVRI 469
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGR---------TALHLAAKNGHLEIVKLLLEhADVNLKDNGRTALHYAARS 71

                          90
                  ....*....|....*....
gi 1469164932 470 GSMEMVALLLKHGANVNAM 488
Cdd:pfam12796  72 GHLEIVKLLLEKGADINVK 90
PHA03100 super family cl39094
ankyrin repeat protein; Provisional
 82-248 4.99e-10

ankyrin repeat protein; Provisional


The actual alignment was detected with superfamily member PHA03100:

Pssm-ID: 476869 [Multi-domain]  Cd Length: 422  Bit Score: 61.99  E-value: 4.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932  82 NKSANIYRN----FHNRIFSKGQDKVIAWTRHNGNLQVTVEYMNDLDPILSAIWK--GDVKALQKIIHsKSKNLYEPNKD 155
Cdd:PHA03100   62 NSSTKNNSTplhyLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLD-NGANVNIKNSD 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 156 GWLPLHESAYYGSV--KCLKILLK------AKPET---------INKQTNKSQTPLMLAVCRKHFSCVEHLLEQGADPNL 218
Cdd:PHA03100  141 GENLLHLYLESNKIdlKILKLLIDkgvdinAKNRVnyllsygvpINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNL 220

                         170       180       190
                  ....*....|....*....|....*....|
gi 1469164932 219 ANNQWETPLYKACEKANEAIVELLLRFGAS 248
Cdd:PHA03100  221 VNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
172-420 1.49e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.80  E-value: 1.49e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 172 LKILLKAKPETINKQTNKSQTPLMLAVCRKHFSCVEHLLEQGADPNLANNQWETPLYKACEKANEAIVELLLRFGASPTK 251
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 252 ACAQGGTPLHEAVRNKKLKITKMLIKAGAKLCAKNIYGIDSLFMAAQCNSVEVLNYLIYKGGNVNTQANDDASALFEACK 331
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 332 NGHAKAVEILLSQSADVNITNKTGLLPIHVAAKNGHDSIVAMLIPRTSMVKVR-SSGISSLHFAAENNKDSVLEILIDAG 410
Cdd:COG0666   196 NGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKdKDGLTALLLAAAAGAALIVKLLLLAL 275

                         250
                  ....*....|
gi 1469164932 411 YDVNAKMSDD 420
Cdd:COG0666   276 LLLAAALLDL 285
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 135-426 1.68e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.43  E-value: 1.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 135 VKALQKIIHSKSKNLYEpNKDGWLPLHESAYYGSVKCLKILLKaKPETINKQTNKSQTPLMLAVCRKH-----FSCVEHL 209
Cdd:PHA03100   15 VKNIKYIIMEDDLNDYS-YKKPVLPLYLAKEARNIDVVKILLD-NGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 210 LEQGADPNLANNQWETPL-YKACEKANEA-IVELLLRFGASPTKACAQGGTPLHEAVRNK--KLKITKMLIKAGAKLCAK 285
Cdd:PHA03100   93 LEYGANVNAPDNNGITPLlYAISKKSNSYsIVEYLLDNGANVNIKNSDGENLLHLYLESNkiDLKILKLLIDKGVDINAK 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 286 NiygidslfmaaqcnsveVLNYLIYKGGNVNTQANDDASALFEACKNGHAKAVEILLSQSADVNITNKTGLLPIHVAAKN 365
Cdd:PHA03100  173 N-----------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILN 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469164932 366 GHDSIVAMLIPRTSMVKVRSSGISSLHFAAENNKDS--------VLEILIDAGYDVNAKMSDDWSKMYE 426
Cdd:PHA03100  236 NNKEIFKLLLNNGPSIKTIIETLLYFKDKDLNTITKikmlkksiMYMFLLDPGFYKNRKLIENSKSLKD 304
Ank_2 pfam12796
Ankyrin repeats (3 copies);
326-416 2.33e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 2.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 326 LFEACKNGHAKAVEILLSQSADVNITNKTGLLPIHVAAKNGHDSIVAMLIPRtSMVKVRSSGISSLHFAAENNKDSVLEI 405
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|.
gi 1469164932 406 LIDAGYDVNAK 416
Cdd:pfam12796  80 LLEKGADINVK 90
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
 616-655 2.17e-15

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: 70.22  E-value: 2.17e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1469164932 616 PCTLMHLCRLKIRQRLGIQRLCHISALPLPERLIMFLNYE 655
Cdd:cd03716     3 PRSLQHLCRLAIRRCLGRRRLELIKKLPLPPRLKDYLLYE 42
Ank_2 pfam12796
Ankyrin repeats (3 copies);
391-488 1.99e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 1.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 391 LHFAAENNKDSVLEILIDAGYDVNAKMSDDWskmyedhrsTALYSAVANSNIEAATMLLE-AGADPNLDIFNPLLVAVRI 469
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGR---------TALHLAAKNGHLEIVKLLLEhADVNLKDNGRTALHYAARS 71

                          90
                  ....*....|....*....
gi 1469164932 470 GSMEMVALLLKHGANVNAM 488
Cdd:pfam12796  72 GHLEIVKLLLEKGADINVK 90
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 616-652 3.20e-12

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: 61.03  E-value: 3.20e-12
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1469164932 616 PCTLMHLCRLKIRQRLGIQRLCHISALPLPERLIMFL 652
Cdd:pfam07525   2 PRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYL 38
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 125-261 5.61e-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: 5.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 125 PILSAIWKGDVKALQKIIHSKSKNLYEPNKDGWLPLHESAYYGSVKCLKILLKAKPETINK----QTNKSQTPLMLAVCR 200
Cdd:cd22192    20 PLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGETALHIAVVN 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469164932 201 KHFSCVEHLLEQGAD------------PNLANNQW--ETPL-YKACEkANEAIVELLLRFGASPTKACAQGGTPLH 261
Cdd:cd22192   100 QNLNLVRELIARGADvvspratgtffrPGPKNLIYygEHPLsFAACV-GNEEIVRLLIEHGADIRAQDSLGNTVLH 174
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 388-519 5.47e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.07  E-value: 5.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 388 ISSLHFAAENNKDSVLEILIDAGYDVNAKMSDDWSKMYedhrSTALYSAVANSNIEAATMLLEAGADPNLDIFN---PLL 464
Cdd:PHA03100   36 VLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLH----YLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNgitPLL 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1469164932 465 VAV--RIGSMEMVALLLKHGANVNAMLPTHPTSFPAALVFCLRFMLMMKCLLDNGCD 519
Cdd:PHA03100  112 YAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILKLLIDKGVD 168
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 82-248 4.99e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.99  E-value: 4.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932  82 NKSANIYRN----FHNRIFSKGQDKVIAWTRHNGNLQVTVEYMNDLDPILSAIWK--GDVKALQKIIHsKSKNLYEPNKD 155
Cdd:PHA03100   62 NSSTKNNSTplhyLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLD-NGANVNIKNSD 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 156 GWLPLHESAYYGSV--KCLKILLK------AKPET---------INKQTNKSQTPLMLAVCRKHFSCVEHLLEQGADPNL 218
Cdd:PHA03100  141 GENLLHLYLESNKIdlKILKLLIDkgvdinAKNRVnyllsygvpINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNL 220

                         170       180       190
                  ....*....|....*....|....*....|
gi 1469164932 219 ANNQWETPLYKACEKANEAIVELLLRFGAS 248
Cdd:PHA03100  221 VNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
 617-655 1.26e-07

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: 47.79  E-value: 1.26e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1469164932  617 CTLMHLCRLKIRQRLGiqrlcHISALPLPERLIMFLNYE 655
Cdd:smart00969   1 RSLQHLCRLAIRRSLG-----GIDKLPLPPRLKDYLLYY 34
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 385-491 3.15e-05

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: 47.18  E-value: 3.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 385 SSGISSLHFAAENNKDSVLE---ILIDAGYD-------VNAKMSDDWskmYEDHrsTALYSAVANSNIEAATMLLEAGAD 454
Cdd:cd21882    24 ATGKTCLHKAALNLNDGVNEaimLLLEAAPDsgnpkelVNAPCTDEF---YQGQ--TALHIAIENRNLNLVRLLVENGAD 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1469164932 455 PNL----DIFN------------PLLVAVRIGSMEMVALLLKHGANVNAMLPT 491
Cdd:cd21882    99 VSAratgRFFRkspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQPAALEAQ 151
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 299-487 2.12e-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: 44.69  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 299 CNSVEVLNY-LIYKGG----NVNTQAND--DASALFEACK-NGHAKAVEILLSQSADVnitnKTGLLPIHVAAKNGHDSI 370
Cdd:TIGR00870  22 LPAAERGDLaSVYRDLeepkKLNINCPDrlGRSALFVAAIeNENLELTELLLNLSCRG----AVGDTLLHAISLEYVDAV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 371 VAMLIPR---------TSMVKVRSS-----GISSLHFAAENNKDSVLEILIDAGYDVNAKMSDDWSkMYEDHRSTALYSA 436
Cdd:TIGR00870  98 EAILLHLlaafrksgpLELANDQYTseftpGITALHLAAHRQNYEIVKLLLERGASVPARACGDFF-VKSQGVDSFYHGE 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1469164932 437 vansnieaatmlleagadpnldifNPLLVAVRIGSMEMVALLLKHGANVNA 487
Cdd:TIGR00870 177 ------------------------SPLNAAACLGSPSIVALLSEDPADILT 203
Ank_4 pfam13637
Ankyrin repeats (many copies);
123-176 2.81e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 2.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1469164932 123 LDPILSAIWKGDVKALqKIIHSKSKNLYEPNKDGWLPLHESAYYGSVKCLKILL 176
Cdd:pfam13637   2 LTALHAAAASGHLELL-RLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 192-218 1.71e-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: 36.41  E-value: 1.71e-03
                           10        20
                   ....*....|....*....|....*..
gi 1469164932  192 TPLMLAVCRKHFSCVEHLLEQGADPNL 218
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 460-487 8.52e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 8.52e-03
                           10        20
                   ....*....|....*....|....*...
gi 1469164932  460 FNPLLVAVRIGSMEMVALLLKHGANVNA 487
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
172-420 1.49e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.80  E-value: 1.49e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 172 LKILLKAKPETINKQTNKSQTPLMLAVCRKHFSCVEHLLEQGADPNLANNQWETPLYKACEKANEAIVELLLRFGASPTK 251
Cdd:COG0666    36 LLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNA 115

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 252 ACAQGGTPLHEAVRNKKLKITKMLIKAGAKLCAKNIYGIDSLFMAAQCNSVEVLNYLIYKGGNVNTQANDDASALFEACK 331
Cdd:COG0666   116 RDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAE 195

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 332 NGHAKAVEILLSQSADVNITNKTGLLPIHVAAKNGHDSIVAMLIPRTSMVKVR-SSGISSLHFAAENNKDSVLEILIDAG 410
Cdd:COG0666   196 NGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKdKDGLTALLLAAAAGAALIVKLLLLAL 275

                         250
                  ....*....|
gi 1469164932 411 YDVNAKMSDD 420
Cdd:COG0666   276 LLLAAALLDL 285
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
82-359 1.57e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.80  E-value: 1.57e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932  82 NKSANIYRNFHNRIFSKGQDKVIAWTRHNGNLQVTVEYMNDLDPILSAIWKGDVKALQKIIHSKSKNLYEPNKDGWLPLH 161
Cdd:COG0666    13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 162 ESAYYGSVKCLKILLKAKPEtINKQTNKSQTPLMLAVCRKHFSCVEHLLEQGADPNLANNQWETPLYKACEKANEAIVEL 241
Cdd:COG0666    93 AAARNGDLEIVKLLLEAGAD-VNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKL 171

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 242 LLRFGASPTKACAQGGTPLHEAVRNKKLKITKMLIKAGAKLCAKNIYGIDSLFMAAQCNSVEVLNYLIYKGGNVNTQAND 321
Cdd:COG0666   172 LLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKD 251

                         250       260       270
                  ....*....|....*....|....*....|....*...
gi 1469164932 322 DASALFEACKNGHAKAVEILLSQSADVNITNKTGLLPI 359
Cdd:COG0666   252 GLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
121-375 1.77e-41

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 152.42  E-value: 1.77e-41
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 121 NDLDPILSAIWKGDVKALQKIIHSKSKNLYEPNKDGWLPLHESAYYGSVKCLKILLKAKPEtINKQTNKSQTPLMLAVCR 200
Cdd:COG0666    19 LLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGAD-INAKDDGGNTLLHAAARN 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 201 KHFSCVEHLLEQGADPNLANNQWETPLYKACEKANEAIVELLLRFGASPTKACAQGGTPLHEAVRNKKLKITKMLIKAGA 280
Cdd:COG0666    98 GDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGA 177

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 281 KLCAKNIYGIDSLFMAAQCNSVEVLNYLIYKGGNVNTQANDDASALFEACKNGHAKAVEILLSQSADVNITNKTGLLPIH 360
Cdd:COG0666   178 DVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALL 257

                         250
                  ....*....|....*
gi 1469164932 361 VAAKNGHDSIVAMLI 375
Cdd:COG0666   258 LAAAAGAALIVKLLL 272
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
172-461 3.98e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.17  E-value: 3.98e-38
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 172 LKILLKAKPETINKQTNKSQTPLMLAVCRKHFSCVEHLLEQGADPNLANNQWETPLYKACEKANEAIVELLLRFGASPTK 251
Cdd:COG0666     3 LLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINA 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 252 ACAQGGTPLHEAVRNKKLKITKMLIKAGAKLCAKNIYGIDSLFMAAQCNSVEVLNYLIYKGGNVNTQANDDASALFEACK 331
Cdd:COG0666    83 KDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAA 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 332 NGHAKAVEILLSQSADVNITNKTGLLPIHVAAKNGHDSIVAMLIPRTSMVKVR-SSGISSLHFAAENNKDSVLEILIDAG 410
Cdd:COG0666   163 NGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKdNDGKTALDLAAENGNLEIVKLLLEAG 242

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1469164932 411 YDVNAKMSDDWskmyedhrsTALYSAVANSNIEAATMLLEAGADPNLDIFN 461
Cdd:COG0666   243 ADLNAKDKDGL---------TALLLAAAAGAALIVKLLLLALLLLAAALLD 284
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
206-500 9.13e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 9.13e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 206 VEHLLEQGADPNLANNQWETPLYKACEKANEAIVELLLRFGASPTKACAQGGTPLHEAVRNKKLKITKMLIKAGAKLCAK 285
Cdd:COG0666     4 LLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAK 83

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 286 NIYGIDSLFMAAQCNSVEVLNYLIYKGGNVNTQANDDASALFEACKNGHAKAVEILLSQSADVNITNKTGLLPIHVAAKN 365
Cdd:COG0666    84 DDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAAN 163

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 366 GHDSIVamliprtsmvkvrssgisslhfaaennkdsvlEILIDAGYDVNAKMSDDWskmyedhrsTALYSAVANSNIEAA 445
Cdd:COG0666   164 GNLEIV--------------------------------KLLLEAGADVNARDNDGE---------TPLHLAAENGHLEIV 202

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1469164932 446 TMLLEAGADPNL---DIFNPLLVAVRIGSMEMVALLLKHGANVNAMLPTHPTSFPAAL 500
Cdd:COG0666   203 KLLLEAGADVNAkdnDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
269-487 8.00e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 119.67  E-value: 8.00e-30
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 269 LKITKMLIKAGAKLCAKNIYGIDSLFMAAQCNSVEVLNYLIYKGGNVNTQANDDASALFEACKNGHAKAVEILLSQSADV 348
Cdd:COG0666     1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADI 80

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 349 NITNKTGLLPIHVAAKNGHDSIVAMLIPRTSMVKVR-SSGISSLHFAAENNKDSVLEILIDAGYDVNAKMSDDWskmyed 427
Cdd:COG0666    81 NAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARdKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGN------ 154

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469164932 428 hrsTALYSAVANSNIEAATMLLEAGADPNL---DIFNPLLVAVRIGSMEMVALLLKHGANVNA 487
Cdd:COG0666   155 ---TPLHLAAANGNLEIVKLLLEAGADVNArdnDGETPLHLAAENGHLEIVKLLLEAGADVNA 214
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 135-426 1.68e-21

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 97.43  E-value: 1.68e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 135 VKALQKIIHSKSKNLYEpNKDGWLPLHESAYYGSVKCLKILLKaKPETINKQTNKSQTPLMLAVCRKH-----FSCVEHL 209
Cdd:PHA03100   15 VKNIKYIIMEDDLNDYS-YKKPVLPLYLAKEARNIDVVKILLD-NGADINSSTKNNSTPLHYLSNIKYnltdvKEIVKLL 92

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 210 LEQGADPNLANNQWETPL-YKACEKANEA-IVELLLRFGASPTKACAQGGTPLHEAVRNK--KLKITKMLIKAGAKLCAK 285
Cdd:PHA03100   93 LEYGANVNAPDNNGITPLlYAISKKSNSYsIVEYLLDNGANVNIKNSDGENLLHLYLESNkiDLKILKLLIDKGVDINAK 172

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 286 NiygidslfmaaqcnsveVLNYLIYKGGNVNTQANDDASALFEACKNGHAKAVEILLSQSADVNITNKTGLLPIHVAAKN 365
Cdd:PHA03100  173 N-----------------RVNYLLSYGVPINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILN 235

                         250       260       270       280       290       300
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469164932 366 GHDSIVAMLIPRTSMVKVRSSGISSLHFAAENNKDS--------VLEILIDAGYDVNAKMSDDWSKMYE 426
Cdd:PHA03100  236 NNKEIFKLLLNNGPSIKTIIETLLYFKDKDLNTITKikmlkksiMYMFLLDPGFYKNRKLIENSKSLKD 304
PHA03095 PHA03095
ankyrin-like protein; Provisional
 206-483 2.02e-21

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 97.79  E-value: 2.02e-21
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 206 VEHLLEQGADPNLANNQWETPL-YKACEKANEAIVELLLRFGASPTKACAQGGTPLHEAVRNK--KLKITKMLIKAGAKL 282
Cdd:PHA03095   66 VRLLLEAGADVNAPERCGFTPLhLYLYNATTLDVIKLLIKAGADVNAKDKVGRTPLHVYLSGFniNPKVIRLLLRKGADV 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 283 CAKNIYGIDSL--FMAAQCNSVEVLNYLIYKGGNVNTQANDDASALFEACKNGHAKA--VEILLSQSADVNITNKTGLLP 358
Cdd:PHA03095  146 NALDLYGMTPLavLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRAriVRELIRAGCDPAATDMLGNTP 225

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 359 IHVAAKNG--HDSIVAMLIPRTSMVKVR-SSGISSLHFAAENNKDSVLEILIDAGYDVNAKMSDDwskmyedhrSTALYS 435
Cdd:PHA03095  226 LHSMATGSscKRSLVLPLLIAGISINARnRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDG---------NTPLSL 296

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1469164932 436 AVANSNIEAATMLLEAGADPN-----LDIFNPLLVAVRI-GSMEMVALLLKHGA 483
Cdd:PHA03095  297 MVRNNNGRAVRAALAKNPSAEtvaatLNTASVAGGDIPSdATRLCVAKVVLRGA 350
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 265-491 8.69e-20

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 92.42  E-value: 8.69e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 265 RNKKLKITKMLIKAGAKLCAKNIYGIDSLFMAAQCNSVEVLNYLIYKGGNVNTQANDDASALFEACKNGHA-----KAVE 339
Cdd:PHA03100   11 RIIKVKNIKYIIMEDDLNDYSYKKPVLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNltdvkEIVK 90

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 340 ILLSQSADVNITNKTGLLPIHVAA--KNGHDSIVAMLIPRTSMVK-VRSSGISSLHFAAENNKD--SVLEILIDAGYDVN 414
Cdd:PHA03100   91 LLLEYGANVNAPDNNGITPLLYAIskKSNSYSIVEYLLDNGANVNiKNSDGENLLHLYLESNKIdlKILKLLIDKGVDIN 170

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 415 AKMSDDW--SKMYE----DHR-STALYSAVANSNIEAATMLLEAGADPNL-DIFN--PLLVAVRIGSMEMVALLLKHGAN 484
Cdd:PHA03100  171 AKNRVNYllSYGVPinikDVYgFTPLHYAVYNNNPEFVKYLLDLGANPNLvNKYGdtPLHIAILNNNKEIFKLLLNNGPS 250


                  ....*..
gi 1469164932 485 VNAMLPT 491
Cdd:PHA03100  251 IKTIIET 257
Ank_2 pfam12796
Ankyrin repeats (3 copies);
326-416 2.33e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.46  E-value: 2.33e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 326 LFEACKNGHAKAVEILLSQSADVNITNKTGLLPIHVAAKNGHDSIVAMLIPRtSMVKVRSSGISSLHFAAENNKDSVLEI 405
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKL 79

                          90
                  ....*....|.
gi 1469164932 406 LIDAGYDVNAK 416
Cdd:pfam12796  80 LLEKGADINVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
194-286 3.37e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.08  E-value: 3.37e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 194 LMLAVCRKHFSCVEHLLEQGADPNLANNQWETPLYKACEKANEAIVELLLRFGASptKACAQGGTPLHEAVRNKKLKITK 273
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADV--NLKDNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1469164932 274 MLIKAGAKLCAKN 286
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 159-485 1.12e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 83.96  E-value: 1.12e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 159 PLHESAYYGSVKCLKILLKAKPEtINKQTNKSQTPLMLAVCRKHFSCVEHLLEqgadpNLAN-NQWETPLYKACEKANEA 237
Cdd:PHA02876  181 PIHYAAERGNAKMVNLLLSYGAD-VNIIALDDLSVLECAVDSKNIDTIKAIID-----NRSNiNKNDLSLLKAIRNEDLE 254

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 238 IVELLLRFGASPTKACAQGGTPLHEAVRNKKL-KITKMLIKAGAKLCAKNIYGIDSLF-MAAQCNSVEVLNYLIYKGGNV 315
Cdd:PHA02876  255 TSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYlMAKNGYDTENIRTLIMLGADV 334

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 316 NTQANDDASALFEACKNGHAKAVEI-LLSQSADVNITNKTGLLPIHVAAKNGHDSIVAMLIPRTSMVKVRSSGI-SSLHF 393
Cdd:PHA02876  335 NAADRLYITPLHQASTLDRNKDIVItLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIgTALHF 414

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 394 A-AENNKDSVLEILIDAGYDVNAKMSDdwskmyedhRSTAL-YSAVANSNIEAATMLLEAGADPN-LDIFN--PLLVAvr 468
Cdd:PHA02876  415 AlCGTNPYMSVKTLIDRGANVNSKNKD---------LSTPLhYACKKNCKLDVIEMLLDNGADVNaINIQNqyPLLIA-- 483

                         330
                  ....*....|....*..
gi 1469164932 469 IGSMEMVALLLKHGANV 485
Cdd:PHA02876  484 LEYHGIVNILLHYGAEL 500
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 130-461 1.33e-16

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 82.70  E-value: 1.33e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 130 IWKGDVKALQKIIHSKSKNLYEPNKDGWLPLHESAYYGSVKCLKILLKAKPEtINKQTNKSQTPLMLAVCRKHFSCVEHL 209
Cdd:PHA02874    9 IYSGDIEAIEKIIKNKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGAD-INHINTKIPHPLLTAIKIGAHDIIKLL 87

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 210 LEQGADPNLannqwetpLYKACekANEAIVELLLRFGASPTKACAQGGTPLHEAVRNKKLKITKMLIKAGAKLCAKNIYG 289
Cdd:PHA02874   88 IDNGVDTSI--------LPIPC--IEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNG 157

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 290 IDSLFMAAQCNSVEVLNYLIYKGGNVNTQANDDASALFEACKNGHAKAVEILLSQSADVNITNKTGLLPIHVAAKNGHdS 369
Cdd:PHA02874  158 CYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAIIHNR-S 236

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 370 IVAMLIPRTSMVKVRSSGISSLHFAAENNKD-SVLEILIDAGYDVNAKMSD-----DWSKMYEDhRSTALYSAVANsnie 443
Cdd:PHA02874  237 AIELLINNASINDQDIDGSTPLHHAINPPCDiDIIDILLYHKADISIKDNKgenpiDTAFKYIN-KDPVIKDIIAN---- 311

                         330
                  ....*....|....*...
gi 1469164932 444 aATMLLEAGADPNLDIFN 461
Cdd:PHA02874  312 -AVLIKEADKLKDSDFLE 328
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 176-468 6.76e-16

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 80.69  E-value: 6.76e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 176 LKAKPETINKQTNKSQT-------PLMLAVCRKHFSCVEHLLEQGADPNLANNQWETPLYKACEKANE-AIVELLlrfgA 247
Cdd:PHA02878   16 ILKYIEYIDHTENYSTSaslipfiPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKlGMKEMI----R 91

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 248 SPTKaCAQGGT--PLHEAVRNKKLKITKMLIKAGaklcAKNIYGIDSLFMAAQCNS----VEVLNYLIYKGGNVNTQ-AN 320
Cdd:PHA02878   92 SINK-CSVFYTlvAIKDAFNNRNVEIFKIILTNR----YKNIQTIDLVYIDKKSKDdiieAEITKLLLSYGADINMKdRH 166

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 321 DDASALFEACKNGHAKAVEILLSQSADVNITNKTGLLPIHVAAKNGHDSIVAMLIPRTSMVKVRSS-GISSLHFAAENNK 399
Cdd:PHA02878  167 KGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKcGNTPLHISVGYCK 246

                         250       260       270       280       290       300       310
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1469164932 400 D-SVLEILIDAGYDVNAKMSddwskmyeDHRSTALYSAVANSniEAATMLLEAGADPNL---DIFNPLLVAVR 468
Cdd:PHA02878  247 DyDILKLLLEHGVDVNAKSY--------ILGLTALHSSIKSE--RKLKLLLEYGADINSlnsYKLTPLSSAVK 309
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 95-407 1.57e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 79.24  E-value: 1.57e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932  95 IFSKGQDKVIAWTRHNGN-LQVTVEymNDLDPILSAIWKGDVKALQKIIHSKSK----NLYEPNkdgwlPLHESAYYGSV 169
Cdd:PHA02874    9 IYSGDIEAIEKIIKNKGNcINISVD--ETTTPLIDAIRSGDAKIVELFIKHGADinhiNTKIPH-----PLLTAIKIGAH 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 170 KCLKILLkakpetinkqTNKSQTPLMLAVCRKHfSCVEHLLEQGADPNLANNQWETPLYKACEKANEAIVELLLRFGASP 249
Cdd:PHA02874   82 DIIKLLI----------DNGVDTSILPIPCIEK-DMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADV 150

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 250 TKACAQGGTPLHEAVRNKKLKITKMLIKAGAKLCAKNIYGIDSLFMAAQCNSVEVLNYLIYKGGNVNTQANDDASALFEA 329
Cdd:PHA02874  151 NIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNA 230

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 330 CKngHAKAVEILLSQSADVNITNKTGLLPIHVAAKNGHD-SIVAMLIPRTSMVKVR-SSGISSLHFAAEN-NKDSVLEIL 406
Cdd:PHA02874  231 II--HNRSAIELLINNASINDQDIDGSTPLHHAINPPCDiDIIDILLYHKADISIKdNKGENPIDTAFKYiNKDPVIKDI 308


                  .
gi 1469164932 407 I 407
Cdd:PHA02874  309 I 309
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 121-350 1.76e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 78.88  E-value: 1.76e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 121 NDLDPILSAIWKGDVKALQKIIHSKsknlYEPN---KDGWLPLHESAYYGSVKCLKILLK--AKPetiNKQTNKSQTPLM 195
Cdd:PHA02875    1 MDQVALCDAILFGELDIARRLLDIG----INPNfeiYDGISPIKLAMKFRDSEAIKLLMKhgAIP---DVKYPDIESELH 73

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 196 LAVCRKHFSCVEHLLEQGADPN-LANNQWETPLYKACEKANEAIVELLLRFGASPTKACAQGGTPLHEAVRNKKLKITKM 274
Cdd:PHA02875   74 DAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIEL 153

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1469164932 275 LIKAGAKLCAKNIYGIDSLFMAAQCNSVEVLNYLIYKGGNVN-TQANDDASALFEACKNGHAKAVEILLSQSADVNI 350
Cdd:PHA02875  154 LIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDyFGKNGCVAALCYAIENNKIDIVRLFIKRGADCNI 230
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
 616-655 2.17e-15

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: 70.22  E-value: 2.17e-15
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1469164932 616 PCTLMHLCRLKIRQRLGIQRLCHISALPLPERLIMFLNYE 655
Cdd:cd03716     3 PRSLQHLCRLAIRRCLGRRRLELIKKLPLPPRLKDYLLYE 42
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 191-414 3.10e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 78.11  E-value: 3.10e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 191 QTPLMLAVCRKHFSCVEHLLEQGADPNLANNQWETPLYKACEKANEAIVELLLRFGASPTKACAQGGTPLHEAVRNKKLK 270
Cdd:PHA02875    3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVK 82

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 271 ITKMLIKAGaKLCAKNIY--GIDSLFMAAQCNSVEVLNYLIYKGGNVNTQANDDASALFEACKNGHAKAVEILLSQSADV 348
Cdd:PHA02875   83 AVEELLDLG-KFADDVFYkdGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACL 161

                         170       180       190       200       210       220
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469164932 349 NITNKTGLLPIHVAAKNGHDSIVAMLIPRTSMVKV--RSSGISSLHFAAENNKDSVLEILIDAGYDVN 414
Cdd:PHA02875  162 DIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYfgKNGCVAALCYAIENNKIDIVRLFIKRGADCN 229
Ank_2 pfam12796
Ankyrin repeats (3 copies);
293-375 4.65e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 70.92  E-value: 4.65e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 293 LFMAAQCNSVEVLNYLIYKGGNVNTQANDDASALFEACKNGHAKAVEILLSQsADVNITNKtGLLPIHVAAKNGHDSIVA 372
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHYAARSGHLEIVK 78


                  ...
gi 1469164932 373 MLI 375
Cdd:pfam12796  79 LLL 81
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 207-488 5.40e-15

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 78.57  E-value: 5.40e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 207 EHLLEQGADPNLANNQWETPLYKACEKANEAIVELLLRFGASPTKACAQGGTPLH------------------------- 261
Cdd:PHA02876  162 EMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLEcavdsknidtikaiidnrsninknd 241

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 262 ----EAVRNKKLKITKMLIKAGAKLCAKNIYGIDSLFMAAQCNSVEVL-NYLIYKGGNVNTQANDDASALFEACKNGH-A 335
Cdd:PHA02876  242 lsllKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLSRLvPKLLERGADVNAKNIKGETPLYLMAKNGYdT 321

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 336 KAVEILLSQSADVNITNKTGLLPIHVAAK-NGHDSIVAMLIPRTSMVKVRS-SGISSLHFAAENNKDSVLEILIDAGYDV 413
Cdd:PHA02876  322 ENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDyCDKTPIHYAAVRNNVVIINTLLDYGADI 401

                         250       260       270       280       290       300       310       320
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 414 NAkmsddwskmYEDHRSTALYSAVANSN-IEAATMLLEAGAD---PNLDIFNPLLVAVRIG-SMEMVALLLKHGANVNAM 488
Cdd:PHA02876  402 EA---------LSQKIGTALHFALCGTNpYMSVKTLIDRGANvnsKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAI 472
PHA03095 PHA03095
ankyrin-like protein; Provisional
 159-377 1.34e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 76.60  E-value: 1.34e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 159 PLHESAYYGSVKCLKI---LLKAKPEtINKQTNKSQTPLMLAVCrkhFSCVEH----LLEQGADPNLANNQWETPL--YK 229
Cdd:PHA03095   50 PLHLYLHYSSEKVKDIvrlLLEAGAD-VNAPERCGFTPLHLYLY---NATTLDviklLIKAGADVNAKDKVGRTPLhvYL 125

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 230 ACEKANEAIVELLLRFGASPTKACAQGGTPLHEAVRNKK--LKITKMLIKAGAKLCAKNIYG------------------ 289
Cdd:PHA03095  126 SGFNINPKVIRLLLRKGADVNALDLYGMTPLAVLLKSRNanVELLRLLIDAGADVYAVDDRFrsllhhhlqsfkprariv 205

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 290 --------------------IDSLFMAAQCNSVEVLNYLIyKGGNVNTQANDDASALFEACKNGHAKAVEILLSQSADVN 349
Cdd:PHA03095  206 reliragcdpaatdmlgntpLHSMATGSSCKRSLVLPLLI-AGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284

                         250       260
                  ....*....|....*....|....*...
gi 1469164932 350 ITNKTGLLPIHVAAKNGHDSIVAMLIPR 377
Cdd:PHA03095  285 AVSSDGNTPLSLMVRNNNGRAVRAALAK 312
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
 616-655 1.40e-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: 67.88  E-value: 1.40e-14
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1469164932 616 PCTLMHLCRLKIRQRLGIQRLCHISALPLPERLIMFLNYE 655
Cdd:cd03587     2 PRSLQHLCRLAIRRCLGKRRLDLIDKLPLPPRLKDYLLYK 41
Ank_2 pfam12796
Ankyrin repeats (3 copies);
160-250 2.58e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 68.60  E-value: 2.58e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 160 LHESAYYGSVKCLKILLKAKPEtINKQTNKSQTPLMLAVCRKHFSCVEHLLEQgADPNLANNQWeTPLYKACEKANEAIV 239
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGAD-ANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGR-TALHYAARSGHLEIV 77

                          90
                  ....*....|.
gi 1469164932 240 ELLLRFGASPT 250
Cdd:pfam12796  78 KLLLEKGADIN 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
260-352 8.48e-14

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 67.45  E-value: 8.48e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 260 LHEAVRNKKLKITKMLIKAGAKLCAKNIYGIDSLFMAAQCNSVEVLNYLIyKGGNVNTQaNDDASALFEACKNGHAKAVE 339
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLL-EHADVNLK-DNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|...
gi 1469164932 340 ILLSQSADVNITN 352
Cdd:pfam12796  79 LLLEKGADINVKD 91
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 170-316 1.26e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 73.76  E-value: 1.26e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 170 KCLKILLKAKPETINKQTNKSQTPLMLAVCRKHFSCVEHLLEQGADPNLANNQWETPLYKACEKANEAIVELLLRFGASP 249
Cdd:PHA02878  148 EITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST 227

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469164932 250 TKACAQGGTPLHEAV-RNKKLKITKMLIKAGAKLCAKN-IYGIDSLFMAAQcnSVEVLNYLIYKGGNVN 316
Cdd:PHA02878  228 DARDKCGNTPLHISVgYCKDYDILKLLLEHGVDVNAKSyILGLTALHSSIK--SERKLKLLLEYGADIN 294
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 289-488 3.51e-13

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 71.95  E-value: 3.51e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 289 GIDSLFMAAQCNSVEVLNYLIYKGGNVNTQANDDASALFEACKNGHAKAVEILLSQSADVN-ITNKTGLLPIHVAAKNGH 367
Cdd:PHA02875   35 GISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADdVFYKDGMTPLHLATILKK 114

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 368 DSIVAMLIPRTSMVKVRSSG-ISSLHFAAENNKDSVLEILIDAGYDVNakmsddwskmYED-HRSTALYSAVANSNIEAA 445
Cdd:PHA02875  115 LDIMKLLIARGADPDIPNTDkFSPLHLAVMMGDIKGIELLIDHKACLD----------IEDcCGCTPLIIAMAKGDIAIC 184

                         170       180       190       200
                  ....*....|....*....|....*....|....*....|....*..
gi 1469164932 446 TMLLEAGADPNLDIFNP----LLVAVRIGSMEMVALLLKHGANVNAM 488
Cdd:PHA02875  185 KMLLDSGANIDYFGKNGcvaaLCYAIENNKIDIVRLFIKRGADCNIM 231
Ank_2 pfam12796
Ankyrin repeats (3 copies);
129-220 1.92e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.60  E-value: 1.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 129 AIWKGDVKALQKIIHSKSkNLYEPNKDGWLPLHESAYYGSVKCLKILLKAKPetINKQTNKsQTPLMLAVCRKHFSCVEH 208
Cdd:pfam12796   4 AAKNGNLELVKLLLENGA-DANLQDKNGRTALHLAAKNGHLEIVKLLLEHAD--VNLKDNG-RTALHYAARSGHLEIVKL 79

                          90
                  ....*....|..
gi 1469164932 209 LLEQGADPNLAN 220
Cdd:pfam12796  80 LLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
391-488 1.99e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.21  E-value: 1.99e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 391 LHFAAENNKDSVLEILIDAGYDVNAKMSDDWskmyedhrsTALYSAVANSNIEAATMLLE-AGADPNLDIFNPLLVAVRI 469
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGR---------TALHLAAKNGHLEIVKLLLEhADVNLKDNGRTALHYAARS 71

                          90
                  ....*....|....*....
gi 1469164932 470 GSMEMVALLLKHGANVNAM 488
Cdd:pfam12796  72 GHLEIVKLLLEKGADINVK 90
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 616-652 3.20e-12

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: 61.03  E-value: 3.20e-12
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1469164932 616 PCTLMHLCRLKIRQRLGIQRLCHISALPLPERLIMFL 652
Cdd:pfam07525   2 PRSLQHLCRLAIRRALGKRRLGAIDKLPLPPLLKDYL 38
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 125-261 5.61e-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: 5.61e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 125 PILSAIWKGDVKALQKIIHSKSKNLYEPNKDGWLPLHESAYYGSVKCLKILLKAKPETINK----QTNKSQTPLMLAVCR 200
Cdd:cd22192    20 PLLLAAKENDVQAIKKLLKCPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPELVNEpmtsDLYQGETALHIAVVN 99

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1469164932 201 KHFSCVEHLLEQGAD------------PNLANNQW--ETPL-YKACEkANEAIVELLLRFGASPTKACAQGGTPLH 261
Cdd:cd22192   100 QNLNLVRELIARGADvvspratgtffrPGPKNLIYygEHPLsFAACV-GNEEIVRLLIEHGADIRAQDSLGNTVLH 174
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 206-352 2.58e-11

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 66.82  E-value: 2.58e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 206 VEHLLEQGADPNLANNQWETPLYKACEKANEAIVELLLRFGASPTKACAQGGTPLHEAVRNKKLKITKMLIKAGAklcAK 285
Cdd:PLN03192  541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILYHFAS---IS 617

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469164932 286 NIY-GIDSLFMAAQCNSVEVLNYLIYKGGNVNTQANDDASALFEACKNGHAKAVEILLSQSADVNITN 352
Cdd:PLN03192  618 DPHaAGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKAN 685
SOCS_ASB2 cd03721
SOCS (suppressors of cytokine signaling) box of ASB2-like proteins. ASB family members have a ...
 616-655 3.84e-11

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: 58.34  E-value: 3.84e-11
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1469164932 616 PCTLMHLCRLKIRQRLGIQRLCHISALPLPERLIMFLNYE 655
Cdd:cd03721     3 PRPLAHLCRLKVRTLIGINRIKLIDTLPLPPRLIRYLNHQ 42
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 388-519 5.47e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.07  E-value: 5.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 388 ISSLHFAAENNKDSVLEILIDAGYDVNAKMSDDWSKMYedhrSTALYSAVANSNIEAATMLLEAGADPNLDIFN---PLL 464
Cdd:PHA03100   36 VLPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLH----YLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNgitPLL 111

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*..
gi 1469164932 465 VAV--RIGSMEMVALLLKHGANVNAMLPTHPTSFPAALVFCLRFMLMMKCLLDNGCD 519
Cdd:PHA03100  112 YAIskKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKIDLKILKLLIDKGVD 168
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 260-522 1.51e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 64.31  E-value: 1.51e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 260 LHEAVRNKKLKITKMLIKAGAKLCAKNIYGIDSLFMAAQCNSVEVLNYLIYKGGNVNTQANDDASALFEACKNGHAKAVE 339
Cdd:PHA02876  149 IKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIK 228

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 340 ILLSQSADVN---------ITN---KTGLL-----------------PIHVAAKNGHDS-IVAMLIPRTSMVKVRS-SGI 388
Cdd:PHA02876  229 AIIDNRSNINkndlsllkaIRNedlETSLLlydagfsvnsiddckntPLHHASQAPSLSrLVPKLLERGADVNAKNiKGE 308

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 389 SSLHFAAENNKDSV-LEILIDAGYDVNAKmsddwSKMYedhrSTALYSA-VANSNIEAATMLLEAGADPNLDIF---NPL 463
Cdd:PHA02876  309 TPLYLMAKNGYDTEnIRTLIMLGADVNAA-----DRLY----ITPLHQAsTLDRNKDIVITLLELGANVNARDYcdkTPI 379

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1469164932 464 LVAVRIGSMEMVALLLKHGANVNAMLPTHPTSFPAALVFCLRFMlMMKCLLDNGCDAQS 522
Cdd:PHA02876  380 HYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTNPYM-SVKTLIDRGANVNS 437
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 201-492 1.74e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.44  E-value: 1.74e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 201 KHFSCVEHLLE-QGADPNLANNQWETPLYKACEKANEAIVELLLRFGASPTKACAQGGTPLHEAVRNKKLKITKMLIkag 279
Cdd:PHA02874   12 GDIEAIEKIIKnKGNCINISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLI--- 88

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 280 aklcaknIYGIDSLFMAAQCNSVEVLNYLIYKGGNVNTQANDDASALFEACKNGHAKAVEILLSQSADVNITNKTGLLPI 359
Cdd:PHA02874   89 -------DNGVDTSILPIPCIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPI 161

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 360 HVAAKNghdsivamliprtsmvkvrssgisslhfaaenNKDSVLEILIDAGydvnakmsddwskmyedhrstaLYSAVAN 439
Cdd:PHA02874  162 HIAIKH--------------------------------NFFDIIKLLLEKG----------------------AYANVKD 187

                         250       260       270       280       290
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1469164932 440 SNIEAatmlleagadpnldifnPLLVAVRIGSMEMVALLLKHGANV-----NAMLPTH 492
Cdd:PHA02874  188 NNGES-----------------PLHNAAEYGDYACIKLLIDHGNHImnkckNGFTPLH 228
PHA03095 PHA03095
ankyrin-like protein; Provisional
 156-344 3.86e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 62.73  E-value: 3.86e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 156 GWLPLHESAYYGSV-KCLKILLKAKPEtINKQTNKSQTPL--MLAVCRKHFSCVEHLLEQGADPNLANNQWETPLY---- 228
Cdd:PHA03095   83 GFTPLHLYLYNATTlDVIKLLIKAGAD-VNAKDKVGRTPLhvYLSGFNINPKVIRLLLRKGADVNALDLYGMTPLAvllk 161

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 229 --------------KACE-------------------KANEAIVELLLRFGASPTKACAQGGTPLHEAVRNKKLKITKM- 274
Cdd:PHA03095  162 srnanvellrllidAGADvyavddrfrsllhhhlqsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCKRSLVl 241

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469164932 275 -LIKAGAKLCAKNIYGIDSLFMAAQCNSVEVLNYLIYKGGNVNTQANDDASALFEACKNGHAKAVEILLSQ 344
Cdd:PHA03095  242 pLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAK 312
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 82-248 4.99e-10

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 61.99  E-value: 4.99e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932  82 NKSANIYRN----FHNRIFSKGQDKVIAWTRHNGNLQVTVEYMNDLDPILSAIWK--GDVKALQKIIHsKSKNLYEPNKD 155
Cdd:PHA03100   62 NSSTKNNSTplhyLSNIKYNLTDVKEIVKLLLEYGANVNAPDNNGITPLLYAISKksNSYSIVEYLLD-NGANVNIKNSD 140

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 156 GWLPLHESAYYGSV--KCLKILLK------AKPET---------INKQTNKSQTPLMLAVCRKHFSCVEHLLEQGADPNL 218
Cdd:PHA03100  141 GENLLHLYLESNKIdlKILKLLIDkgvdinAKNRVnyllsygvpINIKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNL 220

                         170       180       190
                  ....*....|....*....|....*....|
gi 1469164932 219 ANNQWETPLYKACEKANEAIVELLLRFGAS 248
Cdd:PHA03100  221 VNKYGDTPLHIAILNNNKEIFKLLLNNGPS 250
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 322-486 1.97e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.00  E-value: 1.97e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 322 DASALFEACKNGHAKAVEILLSQSADVNITNKTGLLPIHVAAKNGHDSIVAMLIPRTSMVKVRSSGISS-LHFAAENNKD 400
Cdd:PHA02875    2 DQVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYPDIESeLHDAVEEGDV 81

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 401 SVLEILIDAGydvnaKMSDDwsKMYEDHrSTALYSAVANSNIEAATMLLEAGAD---PNLDIFNPLLVAVRIGSMEMVAL 477
Cdd:PHA02875   82 KAVEELLDLG-----KFADD--VFYKDG-MTPLHLATILKKLDIMKLLIARGADpdiPNTDKFSPLHLAVMMGDIKGIEL 153


                  ....*....
gi 1469164932 478 LLKHGANVN 486
Cdd:PHA02875  154 LIDHKACLD 162
SOCS_ASB1 cd03720
SOCS (suppressors of cytokine signaling) box of ASB1-like proteins. ASB family members have a ...
 616-655 3.29e-09

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: 52.81  E-value: 3.29e-09
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1469164932 616 PCTLMHLCRLKIRQRLGIQRLCHISALPLPERLIMFLNYE 655
Cdd:cd03720     3 PRSLLSLCRIAVRRALGKQRLSLICSLPLPDPIKKFLLHE 42
SOCS_SSB4 cd03743
SOCS (suppressors of cytokine signaling) box of SSB4 (SPRY domain-containing SOCS box ...
 616-655 1.05e-08

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: 51.50  E-value: 1.05e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1469164932 616 PCTLMHLCRLKIRQRLGIQRLCHISALPLPERLIMFLNYE 655
Cdd:cd03743     3 PLPLMDLCRRSARQALGRHRLHHIQSLPLPQTLKNYLQYQ 42
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 226-487 1.25e-08

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.97  E-value: 1.25e-08
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 226 PLYKACEKANEAIVELLLRFGASPTKACAQGGTPLHEAVRNKKLKITKMLIKAGAKLCAKNIY-GIDSLFmaaQCNSVEV 304
Cdd:PHA02878   40 PLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLvAIKDAF---NNRNVEI 116

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 305 LNYLIykggnVNTQANDDASALFEACKNGH-----AKAVEILLSQSADVNItnktgllpihvaaknghdsivamliprts 379
Cdd:PHA02878  117 FKIIL-----TNRYKNIQTIDLVYIDKKSKddiieAEITKLLLSYGADINM----------------------------- 162

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 380 mvKVRSSGISSLHFAAENNKDSVLEILIDAGYDVNAKMSDDWSKMYEdhrstalysAVANSNIEAATMLLEAGAdpNLDI 459
Cdd:PHA02878  163 --KDRHKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHH---------AVKHYNKPIVHILLENGA--STDA 229

                         250       260       270
                  ....*....|....*....|....*....|....
gi 1469164932 460 FN-----PLLVAV-RIGSMEMVALLLKHGANVNA 487
Cdd:PHA02878  230 RDkcgntPLHISVgYCKDYDILKLLLEHGVDVNA 263
SOCS_ASB15 cd03731
SOCS (suppressors of cytokine signaling) box of ASB15-like proteins. ASB family members have a ...
 616-655 9.35e-08

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: 49.06  E-value: 9.35e-08
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 1469164932 616 PCTLMHLCRLKIRQRLGIQRLCHISA---LPLP---ERLIMFLNYE 655
Cdd:cd03731     3 PRPLKHLCRLKIRKLMGLQKLQQPSSmkkLPLPpalKRYILYKEYD 48
SOCS_box smart00969
The SOCS box acts as a bridge between specific substrate- binding domains and more generic ...
 617-655 1.26e-07

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: 47.79  E-value: 1.26e-07
                           10        20        30
                   ....*....|....*....|....*....|....*....
gi 1469164932  617 CTLMHLCRLKIRQRLGiqrlcHISALPLPERLIMFLNYE 655
Cdd:smart00969   1 RSLQHLCRLAIRRSLG-----GIDKLPLPPRLKDYLLYY 34
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 293-519 2.02e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 54.12  E-value: 2.02e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 293 LFMAAQCNSVEVLNYLIYKGGNVNTQANDDASALFEACKNGHAKAVEILLSQSADVNITNKtgLLPIHVAAKNGHDSIVA 372
Cdd:PHA02878   41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYT--LVAIKDAFNNRNVEIFK 118

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 373 MLIpRTSMVKVRSSGISSLhfaAENNKDSVLE-----ILIDAGYDVNAKMsddwskmyEDHRSTALYSAVANSNIEAATM 447
Cdd:PHA02878  119 IIL-TNRYKNIQTIDLVYI---DKKSKDDIIEaeitkLLLSYGADINMKD--------RHKGNTALHYATENKDQRLTEL 186

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1469164932 448 LLEAGADPN-LDIFN--PLLVAVRIGSMEMVALLLKHGANVNAMLPTHPTSFPAALVFCLRFMLmMKCLLDNGCD 519
Cdd:PHA02878  187 LLSYGANVNiPDKTNnsPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDI-LKLLLEHGVD 260
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 209-277 2.22e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 54.13  E-value: 2.22e-07
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1469164932 209 LLEQGADPNLANNQWETPLYKACEKANEAIVELLLRFGASPTKACAQGGTPLHEAVRNKKLKITKMLIK 277
Cdd:PTZ00322  101 LLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSR 169
Ank_4 pfam13637
Ankyrin repeats (many copies);
324-375 3.26e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 47.27  E-value: 3.26e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1469164932 324 SALFEACKNGHAKAVEILLSQSADVNITNKTGLLPIHVAAKNGHDSIVAMLI 375
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 351-487 6.50e-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: 52.71  E-value: 6.50e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 351 TNKTGLLPIHVAAK-NGHDSIVAMLI-PRTSMVKVRSSGISSLHFAAENNKDSVLEILIDAGYD-VNAKMSddwSKMYED 427
Cdd:cd22192    13 QKRISESPLLLAAKeNDVQAIKKLLKcPSCDLFQRGALGETALHVAALYDNLEAAVVLMEAAPElVNEPMT---SDLYQG 89

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1469164932 428 HrsTALYSAVANSNIEAATMLLEAGADP---------------NLDIF--NPLLVAVRIGSMEMVALLLKHGANVNA 487
Cdd:cd22192    90 E--TALHIAVVNQNLNLVRELIARGADVvspratgtffrpgpkNLIYYgeHPLSFAACVGNEEIVRLLIEHGADIRA 164
SOCS_SSB1_4 cd03718
SOCS (suppressors of cytokine signaling) box of SSB1 and SSB4 (SPRY domain-containing SOCS box ...
 616-655 6.81e-07

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


Pssm-ID: 239688  Cd Length: 42  Bit Score: 46.14  E-value: 6.81e-07
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1469164932 616 PCTLMHLCRLKIRQRLGIQRLCHISALPLPERLIMFLNYE 655
Cdd:cd03718     3 PLPLMDLCRRRVRVALGRDRLEEIEQLPLPPSLKNYLLYQ 42
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 164-322 8.46e-07

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 52.18  E-value: 8.46e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 164 AYYGSVKCLKILLKAKPETiNKQTNKSQTPLMLAVCRKHFSCVEHLLEQGADPNLANNQWETPLYKACEKANEAIVELLL 243
Cdd:PLN03192  533 ASTGNAALLEELLKAKLDP-DIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTALWNAISAKHHKIFRILY 611

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 244 RFG-ASPTKAcaqGGTPLHEAVRNKKLKITKMLIKAGAKLCAKNIYGIDSLFMAAQCNSVEVLNYLIYKGGNVNTQANDD 322
Cdd:PLN03192  612 HFAsISDPHA---AGDLLCTAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTDD 688
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 316-454 1.94e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 51.02  E-value: 1.94e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 316 NTQANDD---ASALFEACKNGHAKAVEILLSQSADVNITNKTGLLPIHVAAKNGHDSIVAMLIPRTSMVKVRS------- 385
Cdd:PLN03192  516 NGGEHDDpnmASNLLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDangntal 595

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 386 -SGISSLH------------------------FAAENNKDSVLEILIDAGYDVNAkmsddwskmyEDHR-STALYSAVAN 439
Cdd:PLN03192  596 wNAISAKHhkifrilyhfasisdphaagdllcTAAKRNDLTAMKELLKQGLNVDS----------EDHQgATALQVAMAE 665

                         170
                  ....*....|....*
gi 1469164932 440 SNIEAATMLLEAGAD 454
Cdd:PLN03192  666 DHVDMVRLLIMNGAD 680
SOCS_SOCS7 cd03741
SOCS (suppressors of cytokine signaling) box of SOCS7-like proteins. Together with CIS1, the ...
 618-654 2.89e-06

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: 44.70  E-value: 2.89e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1469164932 618 TLMHLCRLKIRQRLgiqRLCHISALPLPERLIMFLNY 654
Cdd:cd03741     5 SLQHLCRFVIRKLV---RRDHIPALPLPRRLIDYLRE 38
SOCS_SOCS_like cd03717
SOCS (suppressors of cytokine signaling) box of SOCS-like proteins. The CIS/SOCS family of ...
 618-654 2.96e-06

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


Pssm-ID: 239687  Cd Length: 39  Bit Score: 44.12  E-value: 2.96e-06
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1469164932 618 TLMHLCRLKIRQRLGIQrlcHISALPLPERLIMFLNY 654
Cdd:cd03717     5 SLQHLCRFVIRQCTRRD---LIDQLPLPRRLKDYLKE 38
Ank_5 pfam13857
Ankyrin repeats (many copies);
175-227 3.24e-06

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 44.64  E-value: 3.24e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1469164932 175 LLKAKPETINKQTNKSQTPLMLAVCRKHFSCVEHLLEQGADPNLANNQWETPL 227
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_4 pfam13637
Ankyrin repeats (many copies);
225-276 3.37e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 3.37e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1469164932 225 TPLYKACEKANEAIVELLLRFGASPTKACAQGGTPLHEAVRNKKLKITKMLI 276
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_4 pfam13637
Ankyrin repeats (many copies);
192-243 5.14e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.19  E-value: 5.14e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1469164932 192 TPLMLAVCRKHFSCVEHLLEQGADPNLANNQWETPLYKACEKANEAIVELLL 243
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SOCS_SSB2 cd03719
SOCS (suppressors of cytokine signaling) box of SSB2 (SPRY domain-containing SOCS box proteins) ...
 616-655 5.95e-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: 5.95e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1469164932 616 PCTLMHLCRLKIRQRLGIQRLCHISALPLPERLIMFLNYE 655
Cdd:cd03719     3 PHSLLHLSRLCVRHALGDTRLGQVSALPLPPAMKRYLLYQ 42
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 160-311 1.29e-05

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: 48.34  E-value: 1.29e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 160 LHESAYY---GSVKCLKILLKAKPETINKQT----------NKSQTPLMLAVCRKHFSCVEHLLEQGADPNLANNQ---- 222
Cdd:cd21882    30 LHKAALNlndGVNEAIMLLLEAAPDSGNPKElvnapctdefYQGQTALHIAIENRNLNLVRLLVENGADVSARATGrffr 109

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 223 ---------WETPL-YKACEKaNEAIVELLLRFGASPTKACAQ---GGTPLH-------EAVRNKKLKIT--KMLIKAGA 280
Cdd:cd21882   110 kspgnlfyfGELPLsLAACTN-QEEIVRLLLENGAQPAALEAQdslGNTVLHalvlqadNTPENSAFVCQmyNLLLSYGA 188

                         170       180       190
                  ....*....|....*....|....*....|....*...
gi 1469164932 281 KLC-------AKNIYGIDSLFMAAQCNSVEVLNYLIYK 311
Cdd:cd21882   189 HLDptqqleeIPNHQGLTPLKLAAVEGKIVMFQHILQR 226
SOCS_ASB14 cd03730
SOCS (suppressors of cytokine signaling) box of ASB14-like proteins. ASB family members have a ...
 616-655 1.50e-05

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: 42.91  E-value: 1.50e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 1469164932 616 PCTLMHLCRLKIRQRLGIQRL-CHI--SALPLPERLIMFLNYE 655
Cdd:cd03730     3 PRSLKHLCRLKIRACMGRLRLrCPVfmSFLPLPNRLKAYILYK 45
SOCS_SSB1 cd03744
SOCS (suppressors of cytokine signaling) box of SSB1 (SPRY domain-containing SOCS box proteins) ...
 616-655 2.11e-05

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: 41.89  E-value: 2.11e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1469164932 616 PCTLMHLCRLKIRQRLGIQRLCHISALPLPERLIMFLNYE 655
Cdd:cd03744     3 PLPLMDLCRRSVRLALGRERLSEIHTLPLPASLKNYLLYQ 42
PHA02798 PHA02798
ankyrin-like protein; Provisional
 238-457 2.25e-05

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 47.52  E-value: 2.25e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 238 IVELLLRFGASPTKACAQGGTPLHEAVRN-----KKLKITKMLIKAGAKLCAKNIYGIDSLFMA---AQCNSVEVLNYLI 309
Cdd:PHA02798   53 IVKLFINLGANVNGLDNEYSTPLCTILSNikdykHMLDIVKILIENGADINKKNSDGETPLYCLlsnGYINNLEILLFMI 132

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 310 YKGGNVNTQANDDASALFEACKNGHA---KAVEILLSQSADVN-ITNKTGLLPIHVAAKNGHD----SIVAMLIPRTSMV 381
Cdd:PHA02798  133 ENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINtHNNKEKYDTLHCYFKYNIDridaDILKLFVDNGFII 212

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 382 KVRSsgisslhfaaENNKDSVLEILIDAGYDVNAKMSD--DWSKMYEDHRS------TALYSAVANSNIEAATMLLEAGA 453
Cdd:PHA02798  213 NKEN----------KSHKKKFMEYLNSLLYDNKRFKKNilDFIFSYIDINQvdelgfNPLYYSVSHNNRKIFEYLLQLGG 282


                  ....
gi 1469164932 454 DPNL 457
Cdd:PHA02798  283 DINI 286
Ank_4 pfam13637
Ankyrin repeats (many copies);
389-449 2.27e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 42.26  E-value: 2.27e-05
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1469164932 389 SSLHFAAENNKDSVLEILIDAGYDVNAKMSDDWskmyedhrsTALYSAVANSNIEAATMLL 449
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGE---------TALHFAASNGNVEVLKLLL 54
TRPV3 cd22194
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), type 3; TRPV3 is a ...
 224-377 2.55e-05

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: 47.45  E-value: 2.55e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 224 ETPLYKACEKANE---AIVELLLRFG-----------ASPTKACAQGGTPLHEAVRNKKLKITKMLIKAGAKL--CAKNI 287
Cdd:cd22194    95 KTCLMKALLNINEntkEIVRILLAFAeengildrfinAEYTEEAYEGQTALNIAIERRQGDIVKLLIAKGADVnaHAKGV 174

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 288 ------------YGIDSLFMAAQCNSVEVLNYLIYKGGNV----NTQANDDASALFEACKNGHA------KAVEILLSQS 345
Cdd:cd22194   175 ffnpkykhegfyFGETPLALAACTNQPEIVQLLMEKESTDitsqDSRGNTVLHALVTVAEDSKTqndfvkRMYDMILLKS 254

                         170       180       190
                  ....*....|....*....|....*....|....*
gi 1469164932 346 ADVN---ITNKTGLLPIHVAAKNGHDSIVAMLIPR 377
Cdd:cd22194   255 ENKNletIRNNEGLTPLQLAAKMGKAEILKYILSR 289
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 385-491 3.15e-05

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: 47.18  E-value: 3.15e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 385 SSGISSLHFAAENNKDSVLE---ILIDAGYD-------VNAKMSDDWskmYEDHrsTALYSAVANSNIEAATMLLEAGAD 454
Cdd:cd21882    24 ATGKTCLHKAALNLNDGVNEaimLLLEAAPDsgnpkelVNAPCTDEF---YQGQ--TALHIAIENRNLNLVRLLVENGAD 98

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|...
gi 1469164932 455 PNL----DIFN------------PLLVAVRIGSMEMVALLLKHGANVNAMLPT 491
Cdd:cd21882    99 VSAratgRFFRkspgnlfyfgelPLSLAACTNQEEIVRLLLENGAQPAALEAQ 151
SOCS_ASB7 cd03726
SOCS (suppressors of cytokine signaling) box of ASB7-like proteins. ASB family members have a ...
 616-655 3.26e-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: 41.37  E-value: 3.26e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1469164932 616 PCTLMHLCRLKIRQRLGIQRLCHISALPLPERLIMFLNYE 655
Cdd:cd03726     3 PRTLQDLCRIKIRHCIGLQNLKLLDELPIAKVMKDYLKHK 42
PHA03095 PHA03095
ankyrin-like protein; Provisional
 153-287 4.01e-05

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 46.56  E-value: 4.01e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 153 NKDGWLPLHESAYYGSVKCLKIL-LKAKPETINKQTNKSQTPLMLAVCRKHFSCVEHLLEQGADPNLANNQWETPLYKAC 231
Cdd:PHA03095  219 DMLGNTPLHSMATGSSCKRSLVLpLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMV 298

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469164932 232 EKANEAIVELLLRfGASPTKACAQ--------GGTPLHEAvrnKKLKITKMLIKAGAKLCAKNI 287
Cdd:PHA03095  299 RNNNGRAVRAALA-KNPSAETVAAtlntasvaGGDIPSDA---TRLCVAKVVLRGAFSLLPEPI 358
PHA02946 PHA02946
ankyin-like protein; Provisional
 184-412 5.39e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 46.20  E-value: 5.39e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 184 NKQTNKSQTPLMLAVCRKHFSCVEHLLEQGADPNLANNQWETPLYKACEKANEAI--VELLLRFGASPTKACAQGGTPLH 261
Cdd:PHA02946   66 NETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDEVIerINLLVQYGAKINNSVDEEGCGPL 145

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 262 EAVRNKKLKITKMLIKAGAKLCAKNIYGIDSL--FMAAQCNSVEVLNYLIYKGGNVNTQANDDASALFEACKNGhAKAVE 339
Cdd:PHA02946  146 LACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHDGNTPLHIVCSKT-VKNVD 224

                         170       180       190       200       210       220       230
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 1469164932 340 I--LLSQSADVNITNKTGLLPIHVAAKNGHDS-IVAMLIPRTSMVKVRSSGISSLHfaaenNKDSVLEILIDAG--YD 412
Cdd:PHA02946  225 IinLLLPSTDVNKQNKFGDSPLTLLIKTLSPAhLINKLLSTSNVITDQTVNICIFY-----DRDDVLEIINDKGkqYD 297
SOCS_ASB_9_11 cd03728
SOCS (suppressors of cytokine signaling) box of ASB9 and 11 proteins. ASB family members have ...
 616-654 5.54e-05

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


Pssm-ID: 239698  Cd Length: 42  Bit Score: 40.93  E-value: 5.54e-05
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1469164932 616 PCTLMHLCRLKIRQRLGIQRLCHISALPLPERLIMFLNY 654
Cdd:cd03728     3 PPSLMQLCRLCIRKCFGRKQHHKIHKLHLPEPLKHFLLY 41
SOCS smart00253
suppressors of cytokine signalling; suppressors of cytokine signalling
 610-654 5.63e-05

suppressors of cytokine signalling; suppressors of cytokine signalling


Pssm-ID: 128549  Cd Length: 43  Bit Score: 40.74  E-value: 5.63e-05
                           10        20        30        40
                   ....*....|....*....|....*....|....*....|....*
gi 1469164932  610 KERSVLPCTLMHLCRLKIRQRLGIQrlcHISALPLPERLIMFLNY 654
Cdd:smart00253   1 LPRPSNVPSLQHLCRFTIRRCTRTD---QIKTLPLPPKLKDYLSY 42
SOCS_ASB3 cd03722
SOCS (suppressors of cytokine signaling) box of ASB3-like proteins. ASB family members have a ...
 619-655 5.86e-05

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: 40.93  E-value: 5.86e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 1469164932 619 LMHLCRLKIRQRLGIQRL---CHISALPLPERLIMFLNYE 655
Cdd:cd03722     6 LTHLCRLEIRSSLKSERLrsdSFICQLPLPRSLQDYLLYS 45
Ank_4 pfam13637
Ankyrin repeats (many copies);
256-309 6.75e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 40.72  E-value: 6.75e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1469164932 256 GGTPLHEAVRNKKLKITKMLIKAGAKLCAKNIYGIDSLFMAAQCNSVEVLNYLI 309
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 295-374 6.76e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 46.04  E-value: 6.76e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 295 MAAQCNSVEVlNYLIYKGGNVNTQANDDASALFEACKNGHAKAVEILLSQSADVNITNKTGLLPIHVAAKNGHDSIVAML 374
Cdd:PTZ00322   89 LAASGDAVGA-RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLL 167
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 191-221 7.12e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 40.35  E-value: 7.12e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 1469164932 191 QTPLMLAVCR-KHFSCVEHLLEQGADPNLANN 221
Cdd:pfam00023   3 NTPLHLAAGRrGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 392-481 8.17e-05

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 45.66  E-value: 8.17e-05
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 392 HFAAENnkDSV-LEILIDAGYDVNAKmsdDWskmyedHRSTALYSAVANSNIEAATMLLEAGADPNL---DIFNPLLVAV 467
Cdd:PTZ00322   88 QLAASG--DAVgARILLTGGADPNCR---DY------DGRTPLHIACANGHVQVVRVLLEFGADPTLldkDGKTPLELAE 156

                          90
                  ....*....|....
gi 1469164932 468 RIGSMEMVALLLKH 481
Cdd:PTZ00322  157 ENGFREVVQLLSRH 170
PHA02946 PHA02946
ankyin-like protein; Provisional
 228-360 1.02e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.43  E-value: 1.02e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 228 YKACEKANEAIVELLLRFGASPTKACAQGGTPLHEAVRNKKLKITKMLIKAGAKLCAKNIYGIDSLFMAAQCNS--VEVL 305
Cdd:PHA02946   44 YCGIKGLDERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDDevIERI 123

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1469164932 306 NYLIYKGGNVNTQANDDASALFEACKNGHAKAVEILLSQSADVNITNKTGLLPIH 360
Cdd:PHA02946  124 NLLVQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIH 178
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
 616-657 1.26e-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: 40.12  E-value: 1.26e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....
gi 1469164932 616 PCTLMHLCRLKIRQRLGiqRLCH--ISALPLPERLIMFLNYERE 657
Cdd:cd03723     3 PRSLQHLCRCAIRKLLG--SRCHklVPQLSLPTSLKNYLLLEPE 44
Ank_4 pfam13637
Ankyrin repeats (many copies);
293-342 1.41e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 1.41e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 1469164932 293 LFMAAQCNSVEVLNYLIYKGGNVNTQANDDASALFEACKNGHAKAVEILL 342
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 397-523 1.54e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 44.66  E-value: 1.54e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 397 NNKDSVLEILIDAGYDVNAKMSDDWSKMyedhRSTALYSAVANSNIEAATMLLEAGADPN---LDIFNPLLVAVRIGS-- 471
Cdd:PHA03100    7 LTKSRIIKVKNIKYIIMEDDLNDYSYKK----PVLPLYLAKEARNIDVVKILLDNGADINsstKNNSTPLHYLSNIKYnl 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 1469164932 472 ---MEMVALLLKHGANVNAMLPTHPTSFPAALVFCLRFMLMMKCLLDNGCDAQSC 523
Cdd:PHA03100   83 tdvKEIVKLLLEYGANVNAPDNNGITPLLYAISKKSNSYSIVEYLLDNGANVNIK 137
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 173-256 1.65e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 44.89  E-value: 1.65e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 173 KILLKAKPETiNKQTNKSQTPLMLAVCRKHFSCVEHLLEQGADPNLANNQWETPLYKACEKANEAIVELLLRFGASPTKA 252
Cdd:PTZ00322   99 RILLTGGADP-NCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQCHFEL 177


                  ....
gi 1469164932 253 CAQG 256
Cdd:PTZ00322  178 GANA 181
Ank_4 pfam13637
Ankyrin repeats (many copies);
429-479 1.65e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 1.65e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1469164932 429 RSTALYSAVANSNIEAATMLLEAGADPNL---DIFNPLLVAVRIGSMEMVALLL 479
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAvdgNGETALHFAASNGNVEVLKLLL 54
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 299-487 2.12e-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: 44.69  E-value: 2.12e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 299 CNSVEVLNY-LIYKGG----NVNTQAND--DASALFEACK-NGHAKAVEILLSQSADVnitnKTGLLPIHVAAKNGHDSI 370
Cdd:TIGR00870  22 LPAAERGDLaSVYRDLeepkKLNINCPDrlGRSALFVAAIeNENLELTELLLNLSCRG----AVGDTLLHAISLEYVDAV 97

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 371 VAMLIPR---------TSMVKVRSS-----GISSLHFAAENNKDSVLEILIDAGYDVNAKMSDDWSkMYEDHRSTALYSA 436
Cdd:TIGR00870  98 EAILLHLlaafrksgpLELANDQYTseftpGITALHLAAHRQNYEIVKLLLERGASVPARACGDFF-VKSQGVDSFYHGE 176

                         170       180       190       200       210
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1469164932 437 vansnieaatmlleagadpnldifNPLLVAVRIGSMEMVALLLKHGANVNA 487
Cdd:TIGR00870 177 ------------------------SPLNAAACLGSPSIVALLSEDPADILT 203
PHA02798 PHA02798
ankyrin-like protein; Provisional
 266-486 2.18e-04

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 44.44  E-value: 2.18e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 266 NKKLKITKMLIKAGAklcakNIYGIDSLFMAAQC----------NSVEVLNYLIYKGGNVNTQANDDASALFEACKNGHA 335
Cdd:PHA02798   48 SPSTDIVKLFINLGA-----NVNGLDNEYSTPLCtilsnikdykHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYI 122

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 336 KAVEILL---SQSADVNITNKTGLLPIHVAAKNGHD---SIVAMLIPRTSMVKVRSS--GISSLHFAAENNKD----SVL 403
Cdd:PHA02798  123 NNLEILLfmiENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVDINTHNNkeKYDTLHCYFKYNIDridaDIL 202

                         170       180       190       200       210       220       230       240
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 404 EILIDAGYDVNAKMSDDWSKMYEDHRSTALYSAVANSNIEAATMLLEAGADPNLDIFNPLLVAVRIGSMEMVALLLKHGA 483
Cdd:PHA02798  203 KLFVDNGFIINKENKSHKKKFMEYLNSLLYDNKRFKKNILDFIFSYIDINQVDELGFNPLYYSVSHNNRKIFEYLLQLGG 282


                  ...
gi 1469164932 484 NVN 486
Cdd:PHA02798  283 DIN 285
TRPV1-4 cd22193
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 1-4; TRPV1-4 are ...
 189-309 2.40e-04

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


Pssm-ID: 411977 [Multi-domain]  Cd Length: 607  Bit Score: 44.40  E-value: 2.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 189 KSQTPLMLAVCRKHFSCVEHLLEQGADPNLANNQ--------------WETPLYKACEKANEAIVELLLRFGASPTKACA 254
Cdd:cd22193    75 EGQTALHIAIERRQGDIVALLVENGADVHAHAKGrffqpkyqgegfyfGELPLSLAACTNQPDIVQYLLENEHQPADIEA 154

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1469164932 255 Q---GGTPLHEAV-------RNKKL--KITKMLIKAGAKLCA-------KNIYGIDSLFMAAQCNSVEVLNYLI 309
Cdd:cd22193   155 QdsrGNTVLHALVtvadntkENTKFvtRMYDMILIRGAKLCPtveleeiRNNDGLTPLQLAAKMGKIEILKYIL 228
Ank_4 pfam13637
Ankyrin repeats (many copies);
123-176 2.81e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.18  E-value: 2.81e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1469164932 123 LDPILSAIWKGDVKALqKIIHSKSKNLYEPNKDGWLPLHESAYYGSVKCLKILL 176
Cdd:pfam13637   2 LTALHAAAASGHLELL-RLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SOCS_ASB13 cd03729
SOCS (suppressors of cytokine signaling) box of ASB13-like proteins. ASB family members have a ...
 616-654 3.30e-04

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: 38.61  E-value: 3.30e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1469164932 616 PCTLMHLCRLKIRQRLGIQRLCHISALPLPERLIMFLNY 654
Cdd:cd03729     3 PLSLQQLCRINLRKALGTRALEKIAKLNIPNRIIDYLSY 41
PHA02791 PHA02791
ankyrin-like protein; Provisional
 191-358 3.63e-04

ankyrin-like protein; Provisional


Pssm-ID: 165154 [Multi-domain]  Cd Length: 284  Bit Score: 43.11  E-value: 3.63e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 191 QTPLMLAVCRKHFSCVEHLLEQGADPNLANNqwETPLYKACEKANEAIVELLLRFGASPTKACAQGGTPLHEAVRNKKLK 270
Cdd:PHA02791   31 HSALYYAIADNNVRLVCTLLNAGALKNLLEN--EFPLHQAATLEDTKIVKILLFSGMDDSQFDDKGNTALYYAVDSGNMQ 108

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 271 ITKMLIKAGAKLCAKNIYGID-SLFMAAQCNSVEVLNYLIYKggnvnTQANDDASALFE----ACKNGHAKAVEILLSQS 345
Cdd:PHA02791  109 TVKLFVKKNWRLMFYGKTGWKtSFYHAVMLNDVSIVSYFLSE-----IPSTFDLAILLScihiTIKNGHVDMMILLLDYM 183

                         170
                  ....*....|...
gi 1469164932 346 ADVNITNKTGLLP 358
Cdd:PHA02791  184 TSTNTNNSLLFIP 196
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 432-490 3.74e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.44  E-value: 3.74e-04
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1469164932 432 ALYSAVANSNIEAATMLLEAGADPNLDIFN---PLLVAVRIGSMEMVALLLKHGANVNAMLP 490
Cdd:PHA02875    5 ALCDAILFGELDIARRLLDIGINPNFEIYDgisPIKLAMKFRDSEAIKLLMKHGAIPDVKYP 66
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 122-270 4.40e-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: 43.53  E-value: 4.40e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 122 DLDPILSAIWKGDVKALQKIIHSKSKNLYEpnkdGWLPLHESA--YYGSVK-CLKILLKAKPETIN------KQTN---K 189
Cdd:TIGR00870  52 GRSALFVAAIENENLELTELLLNLSCRGAV----GDTLLHAISleYVDAVEaILLHLLAAFRKSGPlelandQYTSeftP 127

                          90       100       110       120       130       140       150       160
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 190 SQTPLMLAVCRKHFSCVEHLLEQGADPNLANN--------------QWETPLYKACEKANEAIVELLLRFGASPTKACAQ 255
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVPARACgdffvksqgvdsfyHGESPLNAAACLGSPSIVALLSEDPADILTADSL 207

                         170
                  ....*....|....*
gi 1469164932 256 GGTPLHEAVRNKKLK 270
Cdd:TIGR00870 208 GNTLLHLLVMENEFK 222
SOCS_ASB5 cd03724
SOCS (suppressors of cytokine signaling) box of ASB5-like proteins. ASB family members have a ...
 616-654 6.80e-04

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


Pssm-ID: 239694  Cd Length: 42  Bit Score: 37.55  E-value: 6.80e-04
                          10        20        30
                  ....*....|....*....|....*....|....*....
gi 1469164932 616 PCTLMHLCRLKIRQRLGIQRLCHISALPLPERLIMFLNY 654
Cdd:cd03724     3 PSSLCQLCRLCIRNYIGRSRLHLIPQLQLPTLLKNFLQY 41
Ank_5 pfam13857
Ankyrin repeats (many copies);
345-394 7.89e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 38.10  E-value: 7.89e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|.
gi 1469164932 345 SADVNITNKTGLLPIHVAAKNGHDSIVAMLIPRTSMVKVR-SSGISSLHFA 394
Cdd:pfam13857   6 PIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKdEEGLTALDLA 56
PHA02989 PHA02989
ankyrin repeat protein; Provisional
 384-486 1.40e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222954 [Multi-domain]  Cd Length: 494  Bit Score: 41.65  E-value: 1.40e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 384 RSSGISSLHFAAENNKDSVLEILIDAGYDVNakmsddwskmYEDHRSTALYSAVANSNIEAA------TMLLEAGADPNL 457
Cdd:PHA02989   34 RGNSILLLYLKRKDVKIKIVKLLIDNGADVN----------YKGYIETPLCAVLRNREITSNkikkivKLLLKFGADINL 103

                          90       100       110
                  ....*....|....*....|....*....|....*
gi 1469164932 458 DIFN------PLLVAVRIGSMEMVALLLKHGANVN 486
Cdd:PHA02989  104 KTFNgvspivCFIYNSNINNCDMLRFLLSKGINVN 138
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 192-218 1.71e-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: 36.41  E-value: 1.71e-03
                           10        20
                   ....*....|....*....|....*..
gi 1469164932  192 TPLMLAVCRKHFSCVEHLLEQGADPNL 218
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 138-265 2.55e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 40.63  E-value: 2.55e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 138 LQKIIHSKSKNLYEPNKDGWLPLHESAYYGSVKCLKILLKAKPETiNKQTNKSQTPLMLAVCR-KHFSCVEHLLEQGADP 216
Cdd:PHA02878  183 LTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGAST-DARDKCGNTPLHISVGYcKDYDILKLLLEHGVDV 261

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1469164932 217 NLANNQWE-TPLYKACEkaNEAIVELLLRFGASPTKACAQGGTPLHEAVR 265
Cdd:PHA02878  262 NAKSYILGlTALHSSIK--SERKLKLLLEYGADINSLNSYKLTPLSSAVK 309
Ank_5 pfam13857
Ankyrin repeats (many copies);
209-263 2.87e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 36.17  E-value: 2.87e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1469164932 209 LLEQG-ADPNLANNQWETPLYKACEKANEAIVELLLRFGASPTKACAQGGTPLHEA 263
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SOCS_WSB_SWIP cd03733
SOCS (suppressors of cytokine signaling) box of WSB/SWiP-like proteins. This subfamily ...
 618-654 2.88e-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: 35.86  E-value: 2.88e-03
                          10        20        30
                  ....*....|....*....|....*....|....*..
gi 1469164932 618 TLMHLCRLKIRQRLGIQRlchISALPLPERLIMFLNY 654
Cdd:cd03733     5 SLQHLCRMALRRVMTTQQ---VLALPIPKKMKEFLTY 38
SOCS_ASB6 cd03725
SOCS (suppressors of cytokine signaling) box of ASB6-like proteins. ASB family members have a ...
 616-656 4.23e-03

SOCS (suppressors of cytokine signaling) box of ASB6-like proteins. ASB family members have a C-terminal SOCS box and an N-terminal ankyrin-related sequence. ASB6 interacts with the adaptor protein APS and recruits elongin B/C to the insulin receptor signaling complex. The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239695  Cd Length: 44  Bit Score: 35.50  E-value: 4.23e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 1469164932 616 PCTLMHLCRLKIRQRLGIQRL-CHISALPLPERLIMFLNYER 656
Cdd:cd03725     3 PPPLKHLCRVFIRLCLRPWPVdVKVKALPLPDRLKWYLLPEH 44
PHA02730 PHA02730
ankyrin-like protein; Provisional
 405-510 8.09e-03

ankyrin-like protein; Provisional


Pssm-ID: 165098 [Multi-domain]  Cd Length: 672  Bit Score: 39.24  E-value: 8.09e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 405 ILIDAgYDVNAKMSDDWSkMYEDHRSTALYSAVANSNIEAATMLLEAGADPNLDIFNPLLVAVRIGS------MEMVALL 478
Cdd:PHA02730  440 ILIDV-FDILSKYMDDID-MIDNENKTLLYYAVDVNNIQFARRLLEYGASVNTTSRSIINTAIQKSSyrrenkTKLVDLL 517

                          90       100       110
                  ....*....|....*....|....*....|....*.
gi 1469164932 479 LKHGANVNAMLPTHPTS----FPAALVFCLRFMLMM 510
Cdd:PHA02730  518 LSYHPTLETMIDAFNRDirylYPEPLLACIRYALIL 553
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 460-487 8.52e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.10  E-value: 8.52e-03
                           10        20
                   ....*....|....*....|....*...
gi 1469164932  460 FNPLLVAVRIGSMEMVALLLKHGANVNA 487
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
Ank_5 pfam13857
Ankyrin repeats (many copies);
314-362 8.66e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 8.66e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 1469164932 314 NVNTQANDDASALFEACKNGHAKAVEILLSQSADVNITNKTGLLPIHVA 362
Cdd:pfam13857   8 DLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
SOCS_WSB1_SWIP1 cd03746
SOCS (suppressors of cytokine signaling) box of WSB1/SWiP1-like proteins. This subfamily ...
 618-655 8.74e-03

SOCS (suppressors of cytokine signaling) box of WSB1/SWiP1-like proteins. This subfamily contains WSB-1 (SOCS-box-containing WD-40 protein), part of an E3 ubiquitin ligase for the thyroid-hormone-activating type 2 iodothyronine deiodinase (D2) and SWiP-1 (SOCS box and WD-repeats in Protein), a WD40-containing protein that is expressed in embryonic structures of chickens and regulated by Sonic Hedgehog (Shh). The general function of the SOCS box is the recruitment of the ubiquitin-transferase system. The SOCS box interacts with Elongins B and C, Cullin-5 or Cullin-2, Rbx-1, and E2. Therefore, SOCS-box-containing proteins probably function as E3 ubiquitin ligases and mediate the degradation of proteins associated through their N-terminal regions.


Pssm-ID: 239715  Cd Length: 40  Bit Score: 34.40  E-value: 8.74e-03
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 1469164932 618 TLMHLCRLKIRQRLGIQRlchISALPLPERLIMFLNYE 655
Cdd:cd03746     5 SLQHLCRMAIRRVMPTQQ---VKELPIPSKLLEFLTYR 39
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 426-512 9.82e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 38.43  E-value: 9.82e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1469164932 426 EDHRSTALYSAVANSNIEAATMLLEAGADPNL----DIFNPLLVAVRIGSMEMVALLLKHGANVNAMLPTHPTSFPAALV 501
Cdd:PHA02884   67 ENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRyaeeAKITPLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146

                          90
                  ....*....|.
gi 1469164932 502 FCLRFMLMMKC 512
Cdd:PHA02884  147 ICNNFLAFMIC 157
 
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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