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Conserved domains on  [gi|20532000|sp|Q9WV71|]
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RecName: Full=Ankyrin repeat and SOCS box protein 4; Short=ASB-4

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];
1-289 3.60e-27

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.66  E-value: 3.60e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000   1 MDGITAPISKAGAAKLVKKDFLEALKTNDFGKLKAILIERQIDVDTVFEVEDENMILASYKQGYWLPSYKLKSSWATGLH 80
Cdd:COG0666  13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  81 LSVLLGHVECLMVLLDHNATINCR-PNGKTPLHVACEIANLECVKILCDRGAKLNCYSLSGHTALHFCTTPSSILCAKQL 159
Cdd:COG0666  93 AAARNGDLEIVKLLLEAGADVNARdKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000 160 VLRGANVNMKtnNQDEETPLHTAAHFGLSELVAFYVENGAIVDSMNAHMETPLAIAtywalrfkeqeYSREHHLICRTLL 239
Cdd:COG0666 173 LEAGADVNAR--DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA-----------AENGNLEIVKLLL 239

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 20532000 240 DNNAEVNARDDDFKSPLHKAAWNCDHVLMHMMLEAGAEANLMDINGCAAI 289
Cdd:COG0666 240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
 379-426 5.82e-14

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: 65.92  E-value: 5.82e-14
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 20532000 379 NTPRTLMHLSRCAIRKALHNRCHKAIPMLSLPLPLKKYLLLEPEGIIY 426
Cdd:cd03723   1 GTPRSLQHLCRCAIRKLLGSRCHKLVPQLSLPTSLKNYLLLEPEGVLY 48
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-289 3.60e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.66  E-value: 3.60e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000   1 MDGITAPISKAGAAKLVKKDFLEALKTNDFGKLKAILIERQIDVDTVFEVEDENMILASYKQGYWLPSYKLKSSWATGLH 80
Cdd:COG0666  13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  81 LSVLLGHVECLMVLLDHNATINCR-PNGKTPLHVACEIANLECVKILCDRGAKLNCYSLSGHTALHFCTTPSSILCAKQL 159
Cdd:COG0666  93 AAARNGDLEIVKLLLEAGADVNARdKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000 160 VLRGANVNMKtnNQDEETPLHTAAHFGLSELVAFYVENGAIVDSMNAHMETPLAIAtywalrfkeqeYSREHHLICRTLL 239
Cdd:COG0666 173 LEAGADVNAR--DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA-----------AENGNLEIVKLLL 239

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 20532000 240 DNNAEVNARDDDFKSPLHKAAWNCDHVLMHMMLEAGAEANLMDINGCAAI 289
Cdd:COG0666 240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
 379-426 5.82e-14

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: 65.92  E-value: 5.82e-14
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 20532000 379 NTPRTLMHLSRCAIRKALHNRCHKAIPMLSLPLPLKKYLLLEPEGIIY 426
Cdd:cd03723   1 GTPRSLQHLCRCAIRKLLGSRCHKLVPQLSLPTSLKNYLLLEPEGVLY 48
Ank_2 pfam12796
Ankyrin repeats (3 copies);
79-169 4.66e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 4.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000    79 LHLSVLLGHVECLMVLLDHNATINCR-PNGKTPLHVACEIANLECVKILCDRGAKLNCysLSGHTALHFCTTPSSILCAK 157
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQdKNGRTALHLAAKNGHLEIVKLLLEHADVNLK--DNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 20532000   158 QLVLRGANVNMK 169
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 89-313 1.45e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.84  E-value: 1.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000   89 ECLMVLLDHNATINCR-PNGKTPLHVACEIANLECVKILCDRGAKLNCYSLSGHTALHFCTTPSSILCAKQLVLRGANVN 167
Cdd:PHA02874 105 DMIKTILDCGIDVNIKdAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  168 MKTNNQdeETPLHTAAHFGLSELVAFYVENGAIVDSMNAHMETPLAIATYwalrfkeqeysreHHLICRTLLDNNAEVNA 247
Cdd:PHA02874 185 VKDNNG--ESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII-------------HNRSAIELLINNASIND 249

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20532000  248 RDDDFKSPLHKA-AWNCDHVLMHMMLEAGAEANLMDINGCAAIQYVLKVTSVRPAAQPEICYQLLLN 313
Cdd:PHA02874 250 QDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDIIANAVLIK 316
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 380-407 8.38e-07

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: 45.23  E-value: 8.38e-07
                          10        20
                  ....*....|....*....|....*...
gi 20532000   380 TPRTLMHLSRCAIRKALHNRCHKAIPML 407
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKL 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 106-135 4.79e-05

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: 40.26  E-value: 4.79e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 20532000    106 NGKTPLHVACEIANLECVKILCDRGAKLNC 135
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 77-180 3.47e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 42.69  E-value: 3.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  77 TGLHLSVLLGHVECLMVLLDH-----NATINCRP-NGKTPLHVACEIANLECVKILCDRGAKLN-------CYSLSGHTA 143
Cdd:cd22192  53 TALHVAALYDNLEAAVVLMEAapelvNEPMTSDLyQGETALHIAVVNQNLNLVRELIARGADVVspratgtFFRPGPKNL 132

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 20532000 144 LHF---------CTTPSSILcaKQLVLRGANvnmkTNNQDE--ETPLH 180
Cdd:cd22192 133 IYYgehplsfaaCVGNEEIV--RLLIEHGAD----IRAQDSlgNTVLH 174
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 107-201 4.21e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.76  E-value: 4.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000   107 GKTPLHVACEIANLECVKILCDRGAKLN-------CYSLSGHTALHFcttpssilcakqlvlrganvnmktnnqdEETPL 179
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVParacgdfFVKSQGVDSFYH----------------------------GESPL 179

                          90       100
                  ....*....|....*....|..
gi 20532000   180 HTAAHFGLSELVAFYVENGAIV 201
Cdd:TIGR00870 180 NAAACLGSPSIVALLSEDPADI 201
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
1-289 3.60e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 109.66  E-value: 3.60e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000   1 MDGITAPISKAGAAKLVKKDFLEALKTNDFGKLKAILIERQIDVDTVFEVEDENMILASYKQGYWLPSYKLKSSWATGLH 80
Cdd:COG0666  13 AALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLH 92

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  81 LSVLLGHVECLMVLLDHNATINCR-PNGKTPLHVACEIANLECVKILCDRGAKLNCYSLSGHTALHFCTTPSSILCAKQL 159
Cdd:COG0666  93 AAARNGDLEIVKLLLEAGADVNARdKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLL 172

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000 160 VLRGANVNMKtnNQDEETPLHTAAHFGLSELVAFYVENGAIVDSMNAHMETPLAIAtywalrfkeqeYSREHHLICRTLL 239
Cdd:COG0666 173 LEAGADVNAR--DNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLA-----------AENGNLEIVKLLL 239

                       250       260       270       280       290
                ....*....|....*....|....*....|....*....|....*....|
gi 20532000 240 DNNAEVNARDDDFKSPLHKAAWNCDHVLMHMMLEAGAEANLMDINGCAAI 289
Cdd:COG0666 240 EAGADLNAKDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
32-294 8.58e-27

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.89  E-value: 8.58e-27
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  32 KLKAILIERQIDVDTVFEVEDENMILASYKQGYWLPSYKLKSSWATGLHLSVLLGHVECLMVLLDHNATINCR-PNGKTP 110
Cdd:COG0666  11 LLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKdDGGNTL 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000 111 LHVACEIANLECVKILCDRGAKLNCYSLSGHTALHFCTTPSSILCAKQLVLRGANVNMKTNNQdeETPLHTAAHFGLSEL 190
Cdd:COG0666  91 LHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDG--NTPLHLAAANGNLEI 168

                       170       180       190       200       210       220       230       240
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000 191 VAFYVENGAIVDSMNAHMETPLAIATYwalrfkeqeysREHHLICRTLLDNNAEVNARDDDFKSPLHKAAWNCDHVLMHM 270
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETPLHLAAE-----------NGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKL 237

                       250       260
                ....*....|....*....|....
gi 20532000 271 MLEAGAEANLMDINGCAAIQYVLK 294
Cdd:COG0666 238 LLEAGADLNAKDKDGLTALLLAAA 261
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
 379-426 5.82e-14

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: 65.92  E-value: 5.82e-14
                        10        20        30        40
                ....*....|....*....|....*....|....*....|....*...
gi 20532000 379 NTPRTLMHLSRCAIRKALHNRCHKAIPMLSLPLPLKKYLLLEPEGIIY 426
Cdd:cd03723   1 GTPRSLQHLCRCAIRKLLGSRCHKLVPQLSLPTSLKNYLLLEPEGVLY 48
Ank_2 pfam12796
Ankyrin repeats (3 copies);
79-169 4.66e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 4.66e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000    79 LHLSVLLGHVECLMVLLDHNATINCR-PNGKTPLHVACEIANLECVKILCDRGAKLNCysLSGHTALHFCTTPSSILCAK 157
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQdKNGRTALHLAAKNGHLEIVKLLLEHADVNLK--DNGRTALHYAARSGHLEIVK 78

                          90
                  ....*....|..
gi 20532000   158 QLVLRGANVNMK 169
Cdd:pfam12796  79 LLLEKGADINVK 90
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 89-313 1.45e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 68.84  E-value: 1.45e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000   89 ECLMVLLDHNATINCR-PNGKTPLHVACEIANLECVKILCDRGAKLNCYSLSGHTALHFCTTPSSILCAKQLVLRGANVN 167
Cdd:PHA02874 105 DMIKTILDCGIDVNIKdAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYAN 184

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  168 MKTNNQdeETPLHTAAHFGLSELVAFYVENGAIVDSMNAHMETPLAIATYwalrfkeqeysreHHLICRTLLDNNAEVNA 247
Cdd:PHA02874 185 VKDNNG--ESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII-------------HNRSAIELLINNASIND 249

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 20532000  248 RDDDFKSPLHKA-AWNCDHVLMHMMLEAGAEANLMDINGCAAIQYVLKVTSVRPAAQPEICYQLLLN 313
Cdd:PHA02874 250 QDIDGSTPLHHAiNPPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIKDIIANAVLIK 316
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 93-316 5.93e-12

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 67.40  E-value: 5.93e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000   93 VLLDHNATINCRP-NGKTPLHVACEIANLECVKILCDRGAKLNCYSLSGHTALHFCTTPSSILCAKQLVLRGANVNMK-- 169
Cdd:PHA02876 163 MLLEGGADVNAKDiYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNIDTIKAIIDNRSNINKNdl 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  170 -----TNNQDEE--------------------TPLHTAAHF-GLSELVAFYVENGAIVDSMNAHMETPLAIatywalrFK 223
Cdd:PHA02876 243 sllkaIRNEDLEtslllydagfsvnsiddcknTPLHHASQApSLSRLVPKLLERGADVNAKNIKGETPLYL-------MA 315

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  224 EQEYSREHhliCRTLLDNNAEVNARDDDFKSPLHKAAW---NCDHVLmhMMLEAGAEANLMDINGCAAIQYVLKVTSVrp 300
Cdd:PHA02876 316 KNGYDTEN---IRTLIMLGADVNAADRLYITPLHQASTldrNKDIVI--TLLELGANVNARDYCDKTPIHYAAVRNNV-- 388

                        250
                 ....*....|....*.
gi 20532000  301 aaqpeICYQLLLNHGA 316
Cdd:PHA02876 389 -----VIINTLLDYGA 399
PHA03095 PHA03095
ankyrin-like protein; Provisional
 80-321 6.03e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 66.97  E-value: 6.03e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000   80 HLSVLLGHVECLMVLLDHNATINCRPN-GKTPLHVACEI--ANLECVKILCDRGAKLNCYSLSGHTALH-FCTTP-SSIL 154
Cdd:PHA03095 124 YLSGFNINPKVIRLLLRKGADVNALDLyGMTPLAVLLKSrnANVELLRLLIDAGADVYAVDDRFRSLLHhHLQSFkPRAR 203

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  155 CAKQLVLRGANVNmkTNNQDEETPLHTAAHFGLSE--LVAFYVENGAIVDSMNAHMETPLaiatYWALRFKEQEYsrehh 232
Cdd:PHA03095 204 IVRELIRAGCDPA--ATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPL----HYAAVFNNPRA----- 272

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  233 liCRTLLDNNAEVNARDDDFKSPLHKAAWNCDHVLMHMMLEAGAEANLMDingcAAIQYVLKVTSVRPAAQPEICYQLLL 312
Cdd:PHA03095 273 --CRRLIALGADINAVSSDGNTPLSLMVRNNNGRAVRAALAKNPSAETVA----ATLNTASVAGGDIPSDATRLCVAKVV 346


                 ....*....
gi 20532000  313 NHGAARIYP 321
Cdd:PHA03095 347 LRGAFSLLP 355
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 77-259 1.09e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 66.14  E-value: 1.09e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000   77 TGLHLSVLLGHVECLMVLLDHNATINCRP-NGKTPLHVACEIANLECVKILCDRGAKLNCYSLSGHTALHFCTTPSSILC 155
Cdd:PHA02874 126 TFLHYAIKKGDLESIKMLFEYGADVNIEDdNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGDYAC 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  156 AKQLVLRGANVNMKTNNQdeETPLHTAAHFGLSeLVAFYVENGAIVDSmNAHMETPLAIATYWALRFKeqeysrehhlIC 235
Cdd:PHA02874 206 IKLLIDHGNHIMNKCKNG--FTPLHNAIIHNRS-AIELLINNASINDQ-DIDGSTPLHHAINPPCDID----------II 271

                        170       180
                 ....*....|....*....|....
gi 20532000  236 RTLLDNNAEVNARDDDFKSPLHKA 259
Cdd:PHA02874 272 DILLYHKADISIKDNKGENPIDTA 295
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 109-285 2.23e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 65.07  E-value: 2.23e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  109 TPLHVACEIANLECVKILCDRGAKLNCYSLSGHTALHFCTTPSSIL-----CAKQLVLRGANVNMKTNNQDeeTPLHTAA 183
Cdd:PHA03100  37 LPLYLAKEARNIDVVKILLDNGADINSSTKNNSTPLHYLSNIKYNLtdvkeIVKLLLEYGANVNAPDNNGI--TPLLYAI 114

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  184 --HFGLSELVAFYVENGAIVDSMNAHMETPLAIATywalrfkeqEYSREHHLICRTLLDNNAEVNA-------------- 247
Cdd:PHA03100 115 skKSNSYSIVEYLLDNGANVNIKNSDGENLLHLYL---------ESNKIDLKILKLLIDKGVDINAknrvnyllsygvpi 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 20532000  248 --RDDDFKSPLHKAAWNCDHVLMHMMLEAGAEANLMDING 285
Cdd:PHA03100 186 niKDVYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYG 225
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 77-316 4.38e-11

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 64.70  E-value: 4.38e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000   77 TGLHLSVLLGHVECLMVLLDHNATINcrpngKTPLHVACEIAN--LECVKILCDRGAKLNCYSLSGHTALHFCT-TPSSI 153
Cdd:PHA02876 213 SVLECAVDSKNIDTIKAIIDNRSNIN-----KNDLSLLKAIRNedLETSLLLYDAGFSVNSIDDCKNTPLHHASqAPSLS 287

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  154 LCAKQLVLRGANVNMKtnNQDEETPLHTAAHFGL-SELVAFYVENGAIVDSMNAHMETPLAIATYWAlRFKEqeysrehh 232
Cdd:PHA02876 288 RLVPKLLERGADVNAK--NIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTLD-RNKD-------- 356

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  233 lICRTLLDNNAEVNARDDDFKSPLHKAAWNCDHVLMHMMLEAGAEANLMDINGCAAIQYVLKVTSvrpaaqPEICYQLLL 312
Cdd:PHA02876 357 -IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGTN------PYMSVKTLI 429


                 ....
gi 20532000  313 NHGA 316
Cdd:PHA02876 430 DRGA 433
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 61-282 6.55e-11

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 63.92  E-value: 6.55e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000   61 KQGYWLPSYKLKSSwaTGLHLSVLLGHV-----ECLMVLLDHNATIN-CRPNGKTPLHVA--CEIANLECVKILCDRGAK 132
Cdd:PHA03100  56 DNGADINSSTKNNS--TPLHYLSNIKYNltdvkEIVKLLLEYGANVNaPDNNGITPLLYAisKKSNSYSIVEYLLDNGAN 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  133 LNCYSLSGHTALHF----CTTPSSILcaKQLVLRGANVNMKTNnqdeetplhtaahfglselVAFYVENGAIVDSMNAHM 208
Cdd:PHA03100 134 VNIKNSDGENLLHLylesNKIDLKIL--KLLIDKGVDINAKNR-------------------VNYLLSYGVPINIKDVYG 192

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 20532000  209 ETPLAIATYwalrfkeqeysREHHLICRTLLDNNAEVNARDDDFKSPLHKAAWNCDHVLMHMMLEAGAEANLMD 282
Cdd:PHA03100 193 FTPLHYAVY-----------NNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
Ank_2 pfam12796
Ankyrin repeats (3 copies);
77-134 1.03e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.82  E-value: 1.03e-10
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 20532000    77 TGLHLSVLLGHVECLMVLLDHnATINCRPNGKTPLHVACEIANLECVKILCDRGAKLN 134
Cdd:pfam12796  32 TALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADIN 88
Ank_2 pfam12796
Ankyrin repeats (3 copies);
111-205 1.04e-10

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 57.82  E-value: 1.04e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000   111 LHVACEIANLECVKILCDRGAKLNCYSLSGHTALHFCTTPSSILCAKQLvLRGANVNMKTNNQdeeTPLHTAAHFGLSEL 190
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLL-LEHADVNLKDNGR---TALHYAARSGHLEI 76

                          90
                  ....*....|....*
gi 20532000   191 VAFYVENGAIVDSMN 205
Cdd:pfam12796  77 VKLLLEKGADINVKD 91
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 24-283 2.66e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 62.39  E-value: 2.66e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000   24 ALKTNDFGKLKAILIER----QIDVDTVFEVEDENM--ILASYKQGYWLPSYKLKSSwaTGLHLSVLLGHVECLM-VLLD 96
Cdd:PHA02876 218 AVDSKNIDTIKAIIDNRsninKNDLSLLKAIRNEDLetSLLLYDAGFSVNSIDDCKN--TPLHHASQAPSLSRLVpKLLE 295

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000   97 HNATINCRP-NGKTPLHVACEIA-NLECVKILCDRGAKLNCYSLSGHTALHFCTT----PSSILCAKQLvlrGANVNMKt 170
Cdd:PHA02876 296 RGADVNAKNiKGETPLYLMAKNGyDTENIRTLIMLGADVNAADRLYITPLHQASTldrnKDIVITLLEL---GANVNAR- 371

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  171 nNQDEETPLHTAAHFGLSELVAFYVENGAIVDSMNAHMETPLAIATYwalrfkeqeySREHHLICRTLLDNNAEVNARDD 250
Cdd:PHA02876 372 -DYCDKTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALC----------GTNPYMSVKTLIDRGANVNSKNK 440

                        250       260       270
                 ....*....|....*....|....*....|....
gi 20532000  251 DFKSPLHKAAW-NCDHVLMHMMLEAGAEANLMDI 283
Cdd:PHA02876 441 DLSTPLHYACKkNCKLDVIEMLLDNGADVNAINI 474
PHA03095 PHA03095
ankyrin-like protein; Provisional
 94-285 2.14e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 59.27  E-value: 2.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000   94 LLDHNATINCR-PNGKTPLHVACEIANLECVKI---LCDRGAKLNCYSLSGHTALHFCTTPSSIL-CAKQLVLRGANVNM 168
Cdd:PHA03095  33 LLAAGADVNFRgEYGKTPLHLYLHYSSEKVKDIvrlLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNA 112

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  169 KTNNQDeeTPLHT-----AAHFGLselVAFYVENGAIVDSMNAHMETPLAIAT--------------------------- 216
Cdd:PHA03095 113 KDKVGR--TPLHVylsgfNINPKV---IRLLLRKGADVNALDLYGMTPLAVLLksrnanvellrllidagadvyavddrf 187

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  217 -----YWALRFKEQE-----------------------------YSREHHLICRTLLDNNAEVNARDDDFKSPLHKAAWN 262
Cdd:PHA03095 188 rsllhHHLQSFKPRArivreliragcdpaatdmlgntplhsmatGSSCKRSLVLPLLIAGISINARNRYGQTPLHYAAVF 267

                        250       260
                 ....*....|....*....|...
gi 20532000  263 CDHVLMHMMLEAGAEANLMDING 285
Cdd:PHA03095 268 NNPRACRRLIALGADINAVSSDG 290
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 116-282 9.21e-09

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 57.20  E-value: 9.21e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  116 EIANLECVKILCDRGAKLNCYSL-SGHTALHFCTTPSSILCAKQLVLRGANVNM--KTNNqdeeTPLHTAAHFGLSELVA 192
Cdd:PHA02878 143 DIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIpdKTNN----SPLHHAVKHYNKPIVH 218

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  193 FYVENGAIVDSMNAHMETPLAIATYWALRFKeqeysrehhlICRTLLDNNAEVNARDDDFK-SPLHKAAWNCDhvLMHMM 271
Cdd:PHA02878 219 ILLENGASTDARDKCGNTPLHISVGYCKDYD----------ILKLLLEHGVDVNAKSYILGlTALHSSIKSER--KLKLL 286

                        170
                 ....*....|.
gi 20532000  272 LEAGAEANLMD 282
Cdd:PHA02878 287 LEYGADINSLN 297
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 54-289 6.31e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.15  E-value: 6.31e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000   54 NMILASYK-QGYWLPSYKLKSSWATgLHLSVLLGHVECLMVLLDHNATINCR-PNGKTPLHVACEIANLECVKILCDRGA 131
Cdd:PHA02875  14 ELDIARRLlDIGINPNFEIYDGISP-IKLAMKFRDSEAIKLLMKHGAIPDVKyPDIESELHDAVEEGDVKAVEELLDLGK 92

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  132 KLN-CYSLSGHTALHFCTTPSSILCAKQLVLRGANVNMktNNQDEETPLHTAAHFGLSELVAFYVENGAIVDSMNAHMET 210
Cdd:PHA02875  93 FADdVFYKDGMTPLHLATILKKLDIMKLLIARGADPDI--PNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCT 170

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20532000  211 PLAIATywalrfkeqeySREHHLICRTLLDnnaevnardddfksplhkaawncdhvlmhmmleAGAEANLMDINGCAAI 289
Cdd:PHA02875 171 PLIIAM-----------AKGDIAICKMLLD---------------------------------SGANIDYFGKNGCVAA 205
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
 380-407 8.38e-07

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: 45.23  E-value: 8.38e-07
                          10        20
                  ....*....|....*....|....*...
gi 20532000   380 TPRTLMHLSRCAIRKALHNRCHKAIPML 407
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGAIDKL 28
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
 379-407 1.00e-06

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: 45.18  E-value: 1.00e-06
                        10        20
                ....*....|....*....|....*....
gi 20532000 379 NTPRTLMHLSRCAIRKALHNRCHKAIPML 407
Cdd:cd03716   1 STPRSLQHLCRLAIRRCLGRRRLELIKKL 29
Ank_2 pfam12796
Ankyrin repeats (3 copies);
179-282 1.97e-06

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 45.88  E-value: 1.97e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000   179 LHTAAHFGLSELVAFYVENGAIVDSMNAHMETPLAIATywalrfkeqeySREHHLICRTLLDnNAEVNARDDDfKSPLHK 258
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAA-----------KNGHLEIVKLLLE-HADVNLKDNG-RTALHY 67

                          90       100
                  ....*....|....*....|....
gi 20532000   259 AAWNCDHVLMHMMLEAGAEANLMD 282
Cdd:pfam12796  68 AARSGHLEIVKLLLEKGADINVKD 91
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 177-294 3.56e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.81  E-value: 3.56e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  177 TPLHTAAHFGLSELVAFYVENGAIVDSMNAHMETPLAIatywALRFKEQEYSR-----------------EHHLIcRTLL 239
Cdd:PHA02874  37 TPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLT----AIKIGAHDIIKllidngvdtsilpipciEKDMI-KTIL 111

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 20532000  240 DNNAEVNARDDDFKSPLHKAAWNCDHVLMHMMLEAGAEANLMDINGCAAIQYVLK 294
Cdd:PHA02874 112 DCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIK 166
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 79-281 3.58e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 48.83  E-value: 3.58e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000   79 LHLSVLLGHVECLMVLLDHNATIN--CRPNGKTPLHVACEIANLECVKILCDRGAklncyslsghtalhfcttpssilca 156
Cdd:PHA02875  72 LHDAVEEGDVKAVEELLDLGKFADdvFYKDGMTPLHLATILKKLDIMKLLIARGA------------------------- 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  157 kqlvlrganvNMKTNNQDEETPLHTAAHFGLSELVAFYVENGAIVDSMNAHMETPLAIATywalrfkeqeySREHHLICR 236
Cdd:PHA02875 127 ----------DPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAM-----------AKGDIAICK 185

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*..
gi 20532000  237 TLLDNNAEVN--ARDDDFkSPLHKAAWNCDHVLMHMMLEAGAEANLM 281
Cdd:PHA02875 186 MLLDSGANIDyfGKNGCV-AALCYAIENNKIDIVRLFIKRGADCNIM 231
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 101-283 8.65e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.95  E-value: 8.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  101 INCRPngKTPLHVACEIANLECVKILCDRGAKLNCYSLSGHTALHF-CTTPSSIlcAKQLVLRGANvnmKTNNQDEETPL 179
Cdd:PHA02878  33 ASLIP--FIPLHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIiCKEPNKL--GMKEMIRSIN---KCSVFYTLVAI 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  180 HTAahfglselvaFYVENGAIVDSMNAHMETPLAIATYWALRFKEQEYSREHHLIcRTLLDNNAEVNARDDDF-KSPLHK 258
Cdd:PHA02878 106 KDA----------FNNRNVEIFKIILTNRYKNIQTIDLVYIDKKSKDDIIEAEIT-KLLLSYGADINMKDRHKgNTALHY 174

                        170       180
                 ....*....|....*....|....*
gi 20532000  259 AAWNCDHVLMHMMLEAGAEANLMDI 283
Cdd:PHA02878 175 ATENKDQRLTELLLSYGANVNIPDK 199
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 94-215 1.03e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.57  E-value: 1.03e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000   94 LLDHNATINCRPNG-KTPLHVACEIANLECVKILCDRGAKLNCYSLSGHTALHFCTTP-SSILCAKQLVLRGANVNMKTN 171
Cdd:PHA02878 187 LLSYGANVNIPDKTnNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYcKDYDILKLLLEHGVDVNAKSY 266

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 20532000  172 NQDeETPLHTAAHFglSELVAFYVENGAIVDSMNAHMETPLAIA 215
Cdd:PHA02878 267 ILG-LTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSA 307
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
 380-407 1.32e-05

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: 42.07  E-value: 1.32e-05
                        10        20
                ....*....|....*....|....*...
gi 20532000 380 TPRTLMHLSRCAIRKALHNRCHKAIPML 407
Cdd:cd03587   1 NPRSLQHLCRLAIRRCLGKRRLDLIDKL 28
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 77-207 1.60e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000   77 TGLHLSVLLGHVECLMVLLDHNATINCRP-NGKTPLHVACEIANLECVKILcdrgakLNCYSLSG-HTA---LHFCTTPS 151
Cdd:PLN03192 560 TPLHIAASKGYEDCVLVLLKHACNVHIRDaNGNTALWNAISAKHHKIFRIL------YHFASISDpHAAgdlLCTAAKRN 633

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 20532000  152 SILCAKQLVLRGANVNmkTNNQDEETPLHTAAHFGLSELVAFYVENGAIVDSMNAH 207
Cdd:PLN03192 634 DLTAMKELLKQGLNVD--SEDHQGATALQVAMAEDHVDMVRLLIMNGADVDKANTD 687
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 106-135 4.79e-05

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: 40.26  E-value: 4.79e-05
                           10        20        30
                   ....*....|....*....|....*....|
gi 20532000    106 NGKTPLHVACEIANLECVKILCDRGAKLNC 135
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 94-181 5.94e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.04  E-value: 5.94e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000   94 LLDHNATINCRPN-GKTPLHVACEIANLECVKILCDRGAKLNCYSLSGHTALHFCTTPSSILCAKQLVLRGANVNMKTNN 172
Cdd:PHA03100 178 LLSYGVPINIKDVyGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLNNGPSIKTIIET 257

                         90
                 ....*....|.
gi 20532000  173 --QDEETPLHT 181
Cdd:PHA03100 258 llYFKDKDLNT 268
Ank_4 pfam13637
Ankyrin repeats (many copies);
79-126 1.33e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.57  E-value: 1.33e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*....
gi 20532000    79 LHLSVLLGHVECLMVLLDHNATINCRP-NGKTPLHVACEIANLECVKIL 126
Cdd:pfam13637   5 LHAAAASGHLELLRLLLEKGADINAVDgNGETALHFAASNGNVEVLKLL 53
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 77-180 3.47e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 42.69  E-value: 3.47e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  77 TGLHLSVLLGHVECLMVLLDH-----NATINCRP-NGKTPLHVACEIANLECVKILCDRGAKLN-------CYSLSGHTA 143
Cdd:cd22192  53 TALHVAALYDNLEAAVVLMEAapelvNEPMTSDLyQGETALHIAVVNQNLNLVRELIARGADVVspratgtFFRPGPKNL 132

                        90       100       110       120
                ....*....|....*....|....*....|....*....|....*...
gi 20532000 144 LHF---------CTTPSSILcaKQLVLRGANvnmkTNNQDE--ETPLH 180
Cdd:cd22192 133 IYYgehplsfaaCVGNEEIV--RLLIEHGAD----IRAQDSlgNTVLH 174
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 107-201 4.21e-04

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


Pssm-ID: 273311 [Multi-domain]  Cd Length: 743  Bit Score: 42.76  E-value: 4.21e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000   107 GKTPLHVACEIANLECVKILCDRGAKLN-------CYSLSGHTALHFcttpssilcakqlvlrganvnmktnnqdEETPL 179
Cdd:TIGR00870 128 GITALHLAAHRQNYEIVKLLLERGASVParacgdfFVKSQGVDSFYH----------------------------GESPL 179

                          90       100
                  ....*....|....*....|..
gi 20532000   180 HTAAHFGLSELVAFYVENGAIV 201
Cdd:TIGR00870 180 NAAACLGSPSIVALLSEDPADI 201
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 69-159 5.18e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.17  E-value: 5.18e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  69 YKLKSSWATGLHLSVL---LGHVECLMVLLDH-----------NATINCRP-NGKTPLHVACEIANLECVKILCDRGAKL 133
Cdd:cd21882  20 YQRGATGKTCLHKAALnlnDGVNEAIMLLLEAapdsgnpkelvNAPCTDEFyQGQTALHIAIENRNLNLVRLLVENGADV 99

                        90       100       110
                ....*....|....*....|....*....|...
gi 20532000 134 NC------YSLSGHTALHFCTTPSSI-LCAKQL 159
Cdd:cd21882 100 SAratgrfFRKSPGNLFYFGELPLSLaACTNQE 132
TRPV cd21882
Transient Receptor Potential channel, Vanilloid subfamily (TRPV); The vanilloid TRP subfamily ...
 81-206 5.70e-04

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


Pssm-ID: 411975 [Multi-domain]  Cd Length: 600  Bit Score: 42.17  E-value: 5.70e-04
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000  81 LSVLLGHVECLMVLLDHNAtiNCRPN-GKTPLHVAC---EIANLECVKILCDRG-----------AKLNCYSLSGHTALH 145
Cdd:cd21882   1 LEELLGLLECLRWYLTDSA--YQRGAtGKTCLHKAAlnlNDGVNEAIMLLLEAApdsgnpkelvnAPCTDEFYQGQTALH 78

                        90       100       110       120       130       140       150
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 20532000 146 FCTTPSSILCAKQLVLRGANVNMKTNNQD-----------EETPLHTAAHFGLSELVAFYVENGAIVDSMNA 206
Cdd:cd21882  79 IAIENRNLNLVRLLVENGADVSARATGRFfrkspgnlfyfGELPLSLAACTNQEEIVRLLLENGAQPAALEA 150
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 106-135 7.21e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 7.21e-04
                          10        20        30
                  ....*....|....*....|....*....|.
gi 20532000   106 NGKTPLHVACEIA-NLECVKILCDRGAKLNC 135
Cdd:pfam00023   1 DGNTPLHLAAGRRgNLEIVKLLLSKGADVNA 31
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 77-199 7.67e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 41.52  E-value: 7.67e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000   77 TGLHLSVLLGHVECLMVLLDHNATINCRPNGK-TPLHVACEIANLECVKILCDRGAKLNCYSLSGHTALHFCTTPSSILC 155
Cdd:PHA02875 104 TPLHLATILKKLDIMKLLIARGADPDIPNTDKfSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 20532000  156 AKQLVLRGANVNMKTNNQDeETPLHTAAHFGLSELVAFYVENGA 199
Cdd:PHA02875 184 CKMLLDSGANIDYFGKNGC-VAALCYAIENNKIDIVRLFIKRGA 226
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 106-135 2.02e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 35.70  E-value: 2.02e-03
                          10        20        30
                  ....*....|....*....|....*....|
gi 20532000   106 NGKTPLHVACEIANLECVKILCDRGAKLNC 135
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 109-257 3.25e-03

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: 39.61  E-value: 3.25e-03
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000 109 TPLHVACEIANLECVKIL--------CDRGAKlncyslsGHTALHFCTTPSSiLCAKQLVLRGA----NVNMKTNNQDEE 176
Cdd:cd22192  19 SPLLLAAKENDVQAIKKLlkcpscdlFQRGAL-------GETALHVAALYDN-LEAAVVLMEAApelvNEPMTSDLYQGE 90

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 20532000 177 TPLHTAAHFGLSELVAFYVENGAIVdsmnahmETPLAIATYWALRFKEQEYSREHHL----------ICRTLLDNNAEVN 246
Cdd:cd22192  91 TALHIAVVNQNLNLVRELIARGADV-------VSPRATGTFFRPGPKNLIYYGEHPLsfaacvgneeIVRLLIEHGADIR 163

                       170
                ....*....|.
gi 20532000 247 ARDDDFKSPLH 257
Cdd:cd22192 164 AQDSLGNTVLH 174
Ank_5 pfam13857
Ankyrin repeats (many copies);
170-215 4.09e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 4.09e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|....*.
gi 20532000   170 TNNQDEETPLHTAAHFGLSELVAFYVENGAIVDSMNAHMETPLAIA 215
Cdd:pfam13857  11 RLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
92-147 4.52e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 4.52e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 20532000    92 MVLLDHNATINCRPNGKTPLHVACEIANLECVKILCDRGAKLNCYSLSGHTALHFC 147
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 220-298 4.59e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 39.28  E-value: 4.59e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 20532000  220 LRFKEQEYSREHHLICRTLLDNNAEVNARDDDFKSPLHKAAWNCDHVLMHMMLEAGAEANLMDINGCAAIQYVLKVTSV 298
Cdd:PHA02876 146 MKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALDDLSVLECAVDSKNI 224
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 236-285 7.61e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 38.73  E-value: 7.61e-03
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|
gi 20532000  236 RTLLDNNAEVNARDDDFKSPLHKAAWNCDHVLMHMMLEAGAEANLMDING 285
Cdd:PTZ00322  99 RILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDG 148
 
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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