NCBI Home Page NCBI Site Search page NCBI Guide that lists and describes the NCBI resources
Conserved domains on  [gi|966936467|ref|XP_014990787|]
View 

ankyrin repeat and SOCS box protein 10 isoform X1 [Macaca mulatta]

Protein Classification

Graphical summary

 Zoom to residue level

show extra options »

Show site features     Horizontal zoom: ×

List of domain hits

Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
114-358 2.23e-35

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.16  E-value: 2.23e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 114 EELTTPLHVAASRGHTEVLRLLLRRRARPD-SAPGGRTALHEACAAGHTACVHVLLVAGADPNIADQDGKRPLHLCRGPG 192
Cdd:COG0666   52 ALGALLLLAAALAGDLLVALLLLAAGADINaKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 193 TLECAELLLRFGARVDGRSEEEEeTPLHVAARLGHVELADLLLRRGACPDARDAEGWTPLlaacdircqstadaeattar 272
Cdd:COG0666  132 NLEIVKLLLEAGADVNAQDNDGN-TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL-------------------- 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 273 clqlcslllsagadadaadrdkhrplHLACRRGHAAVVELLLSCGVSANAMDYGGHTPLHcalqgpaAALAQSPEHVVRA 352
Cdd:COG0666  191 --------------------------HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALD-------LAAENGNLEIVKL 237

                 ....*.
gi 966936467 353 LLNHGA 358
Cdd:COG0666  238 LLEAGA 243
SOCS super family cl02533
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
421-467 8.68e-06

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.


The actual alignment was detected with superfamily member cd03723:

Pssm-ID: 470605  Cd Length: 48  Bit Score: 42.81  E-value: 8.68e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 966936467 421 QPRSLQHLSRCALRSHLEGSLPHALLRLPLPPRLLRYLQLDFEGVLY 467
Cdd:cd03723    2 TPRSLQHLCRCAIRKLLGSRCHKLVPQLSLPTSLKNYLLLEPEGVLY 48
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
114-358 2.23e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.16  E-value: 2.23e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 114 EELTTPLHVAASRGHTEVLRLLLRRRARPD-SAPGGRTALHEACAAGHTACVHVLLVAGADPNIADQDGKRPLHLCRGPG 192
Cdd:COG0666   52 ALGALLLLAAALAGDLLVALLLLAAGADINaKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 193 TLECAELLLRFGARVDGRSEEEEeTPLHVAARLGHVELADLLLRRGACPDARDAEGWTPLlaacdircqstadaeattar 272
Cdd:COG0666  132 NLEIVKLLLEAGADVNAQDNDGN-TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL-------------------- 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 273 clqlcslllsagadadaadrdkhrplHLACRRGHAAVVELLLSCGVSANAMDYGGHTPLHcalqgpaAALAQSPEHVVRA 352
Cdd:COG0666  191 --------------------------HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALD-------LAAENGNLEIVKL 237

                 ....*.
gi 966936467 353 LLNHGA 358
Cdd:COG0666  238 LLEAGA 243
Ank_2 pfam12796
Ankyrin repeats (3 copies);
152-245 3.46e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.78  E-value: 3.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467  152 LHEACAAGHTACVHVLLVAGADPNIADQDGKRPLHLCRGPGTLECAELLLRFgarVDGRSEEEEETPLHVAARLGHVELA 231
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 966936467  232 DLLLRRGACPDARD 245
Cdd:pfam12796  78 KLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
148-334 2.99e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.51  E-value: 2.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 148 GRTALHeacAAGHTAC------VHVLLVAGADPNIADQDGKRPLHLC-RGPGTLECAELLLRFGARVDGRSeEEEETPLH 220
Cdd:PHA03095  47 GKTPLH---LYLHYSSekvkdiVRLLLEAGADVNAPERCGFTPLHLYlYNATTLDVIKLLIKAGADVNAKD-KVGRTPLH 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 221 VAARlG---HVELADLLLRRGACPDARDAEGWTPL-----------------------LAACDIRCQSTADAEATTARCL 274
Cdd:PHA03095 123 VYLS-GfniNPKVIRLLLRKGADVNALDLYGMTPLavllksrnanvellrllidagadVYAVDDRFRSLLHHHLQSFKPR 201
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966936467 275 QLCSLLLSAGADADAADRDKHR-PLHLA-----CRRGhaaVVELLLSCGVSANAMDYGGHTPLHCA 334
Cdd:PHA03095 202 ARIVRELIRAGCDPAATDMLGNtPLHSMatgssCKRS---LVLPLLIAGISINARNRYGQTPLHYA 264
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
421-467 8.68e-06

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


Pssm-ID: 239693  Cd Length: 48  Bit Score: 42.81  E-value: 8.68e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 966936467 421 QPRSLQHLSRCALRSHLEGSLPHALLRLPLPPRLLRYLQLDFEGVLY 467
Cdd:cd03723    2 TPRSLQHLCRCAIRKLLGSRCHKLVPQLSLPTSLKNYLLLEPEGVLY 48
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
148-176 7.04e-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: 39.88  E-value: 7.04e-05
                           10        20
                   ....*....|....*....|....*....
gi 966936467   148 GRTALHEACAAGHTACVHVLLVAGADPNI 176
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
118-252 1.73e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.85  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 118 TPLHVAASRGHTEVLRLLLrrrarpDSAPG------------GRTALHEACAAGHTACVHVLLVAGADPNIADQDGkrpL 185
Cdd:cd22192   53 TALHVAALYDNLEAAVVLM------EAAPElvnepmtsdlyqGETALHIAVVNQNLNLVRELIARGADVVSPRATG---T 123
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966936467 186 HLCRGPGTLecaellLRFGarvdgrseeeeETPLHVAARLGHVELADLLLRRGACPDARDAEGWTPL 252
Cdd:cd22192  124 FFRPGPKNL------IYYG-----------EHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
421-444 1.59e-03

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: 35.99  E-value: 1.59e-03
                          10        20
                  ....*....|....*....|....
gi 966936467  421 QPRSLQHLSRCALRSHLEGSLPHA 444
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGA 24
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
114-358 2.23e-35

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 133.16  E-value: 2.23e-35
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 114 EELTTPLHVAASRGHTEVLRLLLRRRARPD-SAPGGRTALHEACAAGHTACVHVLLVAGADPNIADQDGKRPLHLCRGPG 192
Cdd:COG0666   52 ALGALLLLAAALAGDLLVALLLLAAGADINaKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNG 131
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 193 TLECAELLLRFGARVDGRSEEEEeTPLHVAARLGHVELADLLLRRGACPDARDAEGWTPLlaacdircqstadaeattar 272
Cdd:COG0666  132 NLEIVKLLLEAGADVNAQDNDGN-TPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPL-------------------- 190
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 273 clqlcslllsagadadaadrdkhrplHLACRRGHAAVVELLLSCGVSANAMDYGGHTPLHcalqgpaAALAQSPEHVVRA 352
Cdd:COG0666  191 --------------------------HLAAENGHLEIVKLLLEAGADVNAKDNDGKTALD-------LAAENGNLEIVKL 237

                 ....*.
gi 966936467 353 LLNHGA 358
Cdd:COG0666  238 LLEAGA 243
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
97-358 3.34e-30

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 118.90  E-value: 3.34e-30
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467  97 DFRFNIRALRLWSLTYEEELTTPLHVAASRGHTEVLRLLLRRRARPDSAP-GGRTALHEACAAGHTACVHVLLVAGADPN 175
Cdd:COG0666    2 LLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADaLGALLLLAAALAGDLLVALLLLAAGADIN 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 176 IADQDGKRPLHLCRGPGTLECAELLLRFGARVDGRSEEEEeTPLHVAARLGHVELADLLLRRGACPDARDAEGWTPLlaa 255
Cdd:COG0666   82 AKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGE-TPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTPL--- 157
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 256 cdircqstadaeattarclqlcslllsagadadaadrdkhrplHLACRRGHAAVVELLLSCGVSANAMDYGGHTPLHcal 335
Cdd:COG0666  158 -------------------------------------------HLAAANGNLEIVKLLLEAGADVNARDNDGETPLH--- 191
                        250       260
                 ....*....|....*....|...
gi 966936467 336 qgpAAALAQSPEhVVRALLNHGA 358
Cdd:COG0666  192 ---LAAENGHLE-IVKLLLEAGA 210
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
118-256 1.83e-26

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 108.50  E-value: 1.83e-26
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 118 TPLHVAASRGHTEVLRLLLRRRARPDSA-PGGRTALHEACAAGHTACVHVLLVAGADPNIADQDGKRPLHLCRGPGTLEC 196
Cdd:COG0666  122 TPLHLAAYNGNLEIVKLLLEAGADVNAQdNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 197 AELLLRFGARVDGRSeEEEETPLHVAARLGHVELADLLLRRGACPDARDAEGWTPLLAAC 256
Cdd:COG0666  202 VKLLLEAGADVNAKD-NDGKTALDLAAENGNLEIVKLLLEAGADLNAKDKDGLTALLLAA 260
Ank_2 pfam12796
Ankyrin repeats (3 copies);
152-245 3.46e-20

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 84.78  E-value: 3.46e-20
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467  152 LHEACAAGHTACVHVLLVAGADPNIADQDGKRPLHLCRGPGTLECAELLLRFgarVDGRSEEEEETPLHVAARLGHVELA 231
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH---ADVNLKDNGRTALHYAARSGHLEIV 77
                          90
                  ....*....|....
gi 966936467  232 DLLLRRGACPDARD 245
Cdd:pfam12796  78 KLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
117-252 2.27e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.09  E-value: 2.27e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 117 TTPLHVAASRGHTEVLRLLLRRRARPDSA-PGGRTALHEACAAGHTACVHVLLVAGADPNIADQDGKRPLHLCRGPGTLE 195
Cdd:COG0666  154 NTPLHLAAANGNLEIVKLLLEAGADVNARdNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 966936467 196 CAELLLRFGARVDGRsEEEEETPLHVAARLGHVELADLLLRRGACPDARDAEGWTPL 252
Cdd:COG0666  234 IVKLLLEAGADLNAK-DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLTLL 289
PHA03095 PHA03095
ankyrin-like protein; Provisional
148-334 2.99e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 68.51  E-value: 2.99e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 148 GRTALHeacAAGHTAC------VHVLLVAGADPNIADQDGKRPLHLC-RGPGTLECAELLLRFGARVDGRSeEEEETPLH 220
Cdd:PHA03095  47 GKTPLH---LYLHYSSekvkdiVRLLLEAGADVNAPERCGFTPLHLYlYNATTLDVIKLLIKAGADVNAKD-KVGRTPLH 122
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 221 VAARlG---HVELADLLLRRGACPDARDAEGWTPL-----------------------LAACDIRCQSTADAEATTARCL 274
Cdd:PHA03095 123 VYLS-GfniNPKVIRLLLRKGADVNALDLYGMTPLavllksrnanvellrllidagadVYAVDDRFRSLLHHHLQSFKPR 201
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 966936467 275 QLCSLLLSAGADADAADRDKHR-PLHLA-----CRRGhaaVVELLLSCGVSANAMDYGGHTPLHCA 334
Cdd:PHA03095 202 ARIVRELIRAGCDPAATDMLGNtPLHSMatgssCKRS---LVLPLLIAGISINARNRYGQTPLHYA 264
Ank_2 pfam12796
Ankyrin repeats (3 copies);
219-358 1.40e-11

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 60.51  E-value: 1.40e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467  219 LHVAARLGHVELADLLLRRGACPDARDAEGWTpllaacdircqstadaeattarclqlcslllsagadadaadrdkhrPL 298
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRT----------------------------------------------AL 34
                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467  299 HLACRRGHAAVVELLLSCgVSANAMDYgGHTPLHCalqgpaAALAQSPEhVVRALLNHGA 358
Cdd:pfam12796  35 HLAAKNGHLEIVKLLLEH-ADVNLKDN-GRTALHY------AARSGHLE-IVKLLLEKGA 85
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
152-248 9.31e-11

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 64.15  E-value: 9.31e-11
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 152 LHEACAAGHTACVHVLLVAGADPNIADQDGKRPLHLCRGPGTLECAELLLRFGARVDgRSEEEEETPLHVAARLGHVELA 231
Cdd:PTZ00322  86 LCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPT-LLDKDGKTPLELAEENGFREVV 164
                         90
                 ....*....|....*..
gi 966936467 232 DLLLRRGACPDARDAEG 248
Cdd:PTZ00322 165 QLLSRHSQCHFELGANA 181
PHA03095 PHA03095
ankyrin-like protein; Provisional
167-358 1.42e-10

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 63.12  E-value: 1.42e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 167 LLVAGADPNIADQDGKRPLHLCRGPGTLECAE---LLLRFGARVDGRsEEEEETPLHVAARLGHVE-LADLLLRRGACPD 242
Cdd:PHA03095  33 LLAAGADVNFRGEYGKTPLHLYLHYSSEKVKDivrLLLEAGADVNAP-ERCGFTPLHLYLYNATTLdVIKLLIKAGADVN 111
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 243 ARDAEGWTPLlaacdircqstadaeattarclqlcslllsagadadaadrdkHrpLHLACRRGHAAVVELLLSCGVSANA 322
Cdd:PHA03095 112 AKDKVGRTPL------------------------------------------H--VYLSGFNINPKVIRLLLRKGADVNA 147
                        170       180       190
                 ....*....|....*....|....*....|....*.
gi 966936467 323 MDYGGHTPLHCALQGPAAALAqspehVVRALLNHGA 358
Cdd:PHA03095 148 LDLYGMTPLAVLLKSRNANVE-----LLRLLIDAGA 178
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
148-223 1.12e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.68  E-value: 1.12e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 148 GRTALHEACAAGHTACVHVLLVAGADPNIADQDGKRPLHLCRGPGTLECAELLLR-------FGAR-----VDGRSEEEE 215
Cdd:PTZ00322 115 GRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRhsqchfeLGANakpdsFTGKPPSLE 194

                 ....*...
gi 966936467 216 ETPLHVAA 223
Cdd:PTZ00322 195 DSPISSHH 202
Ank_2 pfam12796
Ankyrin repeats (3 copies);
118-178 1.40e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.74  E-value: 1.40e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966936467  118 TPLHVAASRGHTEVLRLLLRRrARPDSAPGGRTALHEACAAGHTACVHVLLVAGADPNIAD 178
Cdd:pfam12796  32 TALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
298-361 1.67e-09

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 54.74  E-value: 1.67e-09
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966936467  298 LHLACRRGHAAVVELLLSCGVSANAMDYGGHTPLHcalqgpAAALAQSPEhVVRALLNHGAVRV 361
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALH------LAAKNGHLE-IVKLLLEHADVNL 57
PHA02874 PHA02874
ankyrin repeat protein; Provisional
164-358 1.74e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.43  E-value: 1.74e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 164 VHVLLVAGADPNIADQDGKRPLHLCRGPGTLECAELLLRFGARVDGRsEEEEETPLHVAARLGHVELADLLLRRGACPDA 243
Cdd:PHA02874 107 IKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIE-DDNGCYPIHIAIKHNFFDIIKLLLEKGAYANV 185
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 244 RDAEGWTPLLAACDIRCQSTADAEATTARCLQLCSLLLSAgadadaadrdkhrPLHLACRRGHaAVVELLLScGVSANAM 323
Cdd:PHA02874 186 KDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFT-------------PLHNAIIHNR-SAIELLIN-NASINDQ 250
                        170       180       190
                 ....*....|....*....|....*....|....*
gi 966936467 324 DYGGHTPLHCALQGPAAalaqspEHVVRALLNHGA 358
Cdd:PHA02874 251 DIDGSTPLHHAINPPCD------IDIIDILLYHKA 279
Ank_5 pfam13857
Ankyrin repeats (many copies);
200-252 2.98e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.96  E-value: 2.98e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 966936467  200 LLRFGARVDGRSEEEEETPLHVAARLGHVELADLLLRRGACPDARDAEGWTPL 252
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA03095 PHA03095
ankyrin-like protein; Provisional
148-264 4.01e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.33  E-value: 4.01e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 148 GRTALHEACAAGHT--ACVHVLLVAGADPNIADQDGKRPLHLCRGPGTleCAELLLRF----GARVDGRSEEEEeTPLHV 221
Cdd:PHA03095 187 FRSLLHHHLQSFKPraRIVRELIRAGCDPAATDMLGNTPLHSMATGSS--CKRSLVLPlliaGISINARNRYGQ-TPLHY 263
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....*.
gi 966936467 222 AARLGHVELADLLLRRGACPDARDAEGWTPLLAA---CDIRCQSTA 264
Cdd:PHA03095 264 AAVFNNPRACRRLIALGADINAVSSDGNTPLSLMvrnNNGRAVRAA 309
PHA02875 PHA02875
ankyrin repeat protein; Provisional
164-358 5.62e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 51.53  E-value: 5.62e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 164 VHVLLVAGADPNIADQDGKRPLHLCRGPGTLECAELLLRFGARVDGRSEEEEETPLHVAARLGHVELADLLLRRGACPDA 243
Cdd:PHA02875  51 IKLLMKHGAIPDVKYPDIESELHDAVEEGDVKAVEELLDLGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDI 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 244 RDAEGWTPLLAAC---DIR-CQSTADAEATTarclqlcslllsagadaDAADRDKHRPLHLACRRGHAAVVELLLSCGVS 319
Cdd:PHA02875 131 PNTDKFSPLHLAVmmgDIKgIELLIDHKACL-----------------DIEDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
                        170       180       190
                 ....*....|....*....|....*....|....*....
gi 966936467 320 ANAMDYGGHTPLHCalqgpaAALAQSPEHVVRALLNHGA 358
Cdd:PHA02875 194 IDYFGKNGCVAALC------YAIENNKIDIVRLFIKRGA 226
PHA02878 PHA02878
ankyrin repeat protein; Provisional
148-335 1.15e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 50.65  E-value: 1.15e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 148 GRTALHEACAAGHTACVHVLLVAGADPNIADQDGKRPLHLCRGPGTLECAELLLRFGARVDGRSEEEEeTPLHVA-ARLG 226
Cdd:PHA02878 168 GNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGN-TPLHISvGYCK 246
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 227 HVELADLLLRRGACPDARDAegwtpllaacdIRCQStadaeattarclqlcslllsagadadaadrdkhrPLHLACRrgH 306
Cdd:PHA02878 247 DYDILKLLLEHGVDVNAKSY-----------ILGLT----------------------------------ALHSSIK--S 279
                        170       180
                 ....*....|....*....|....*....
gi 966936467 307 AAVVELLLSCGVSANAMDYGGHTPLHCAL 335
Cdd:PHA02878 280 ERKLKLLLEYGADINSLNSYKLTPLSSAV 308
Ank_4 pfam13637
Ankyrin repeats (many copies);
217-256 2.10e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 44.57  E-value: 2.10e-06
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|
gi 966936467  217 TPLHVAARLGHVELADLLLRRGACPDARDAEGWTPLLAAC 256
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAA 42
Ank_4 pfam13637
Ankyrin repeats (many copies);
148-201 4.88e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.80  E-value: 4.88e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....
gi 966936467  148 GRTALHEACAAGHTACVHVLLVAGADPNIADQDGKRPLHLCRGPGTLECAELLL 201
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
SOCS_ASB4_ASB18 cd03723
SOCS (suppressors of cytokine signaling) box of ASB4 and ASB18 proteins. ASB family members ...
421-467 8.68e-06

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


Pssm-ID: 239693  Cd Length: 48  Bit Score: 42.81  E-value: 8.68e-06
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 966936467 421 QPRSLQHLSRCALRSHLEGSLPHALLRLPLPPRLLRYLQLDFEGVLY 467
Cdd:cd03723    2 TPRSLQHLCRCAIRKLLGSRCHKLVPQLSLPTSLKNYLLLEPEGVLY 48
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
148-178 1.54e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.51  E-value: 1.54e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 966936467  148 GRTALHEACA-AGHTACVHVLLVAGADPNIAD 178
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
118-243 1.75e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 47.17  E-value: 1.75e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 118 TPLHVAASRGHTE---VLRLLLRRRARPDSapGGRTALHEACAAGHTACVHVL--LVAGADPNIADQdgkrplHLCRGP- 191
Cdd:PLN03192 560 TPLHIAASKGYEDcvlVLLKHACNVHIRDA--NGNTALWNAISAKHHKIFRILyhFASISDPHAAGD------LLCTAAk 631
                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|...
gi 966936467 192 -GTLECAELLLRFGARVDGRsEEEEETPLHVAARLGHVELADLLLRRGACPDA 243
Cdd:PLN03192 632 rNDLTAMKELLKQGLNVDSE-DHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
216-245 1.87e-05

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 41.51  E-value: 1.87e-05
                          10        20        30
                  ....*....|....*....|....*....|.
gi 966936467  216 ETPLHVAA-RLGHVELADLLLRRGACPDARD 245
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARD 33
PHA02878 PHA02878
ankyrin repeat protein; Provisional
195-358 2.47e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.41  E-value: 2.47e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 195 ECAELLLRFGARVDGRSEEEEETPLHVAARLGHVELADLLLRRGACPDARDaegwtpllaacdiRCQSTadaeattarcl 274
Cdd:PHA02878 148 EITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVNIPD-------------KTNNS----------- 203
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 275 qlcslllsagadadaadrdkhrPLHLACRRGHAAVVELLLSCGVSANAMDYGGHTPLHCALqgpAAALAQSpehVVRALL 354
Cdd:PHA02878 204 ----------------------PLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISV---GYCKDYD---ILKLLL 255

                 ....
gi 966936467 355 NHGA 358
Cdd:PHA02878 256 EHGV 259
Ank_4 pfam13637
Ankyrin repeats (many copies);
117-168 2.54e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 41.49  E-value: 2.54e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 966936467  117 TTPLHVAASRGHTEVLRLLLRRRARPDSAPG-GRTALHEACAAGHTACVHVLL 168
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGnGETALHFAASNGNVEVLKLLL 54
PHA03100 PHA03100
ankyrin repeat protein; Provisional
164-324 3.38e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 46.20  E-value: 3.38e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 164 VHVLLVAGADPNIADQDGKRPLHLC--RGPGTLECAELLLRFGARVDGRSEEEEeTPLHVAARLGHVEL----------- 230
Cdd:PHA03100  89 VKLLLEYGANVNAPDNNGITPLLYAisKKSNSYSIVEYLLDNGANVNIKNSDGE-NLLHLYLESNKIDLkilkllidkgv 167
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 231 -------ADLLLRRGACPDARDAEGWTPLLAACD----------IRCQstADAEATTARClqlcslllsagadadaadrd 293
Cdd:PHA03100 168 dinaknrVNYLLSYGVPINIKDVYGFTPLHYAVYnnnpefvkylLDLG--ANPNLVNKYG-------------------- 225
                        170       180       190
                 ....*....|....*....|....*....|.
gi 966936467 294 kHRPLHLACRRGHAAVVELLLSCGVSANAMD 324
Cdd:PHA03100 226 -DTPLHIAILNNNKEIFKLLLNNGPSIKTII 255
PHA02946 PHA02946
ankyin-like protein; Provisional
164-332 4.10e-05

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 45.82  E-value: 4.10e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 164 VHVLLVAGADPNIADQDGKRPLHLCRGPGTLECAELLLRFGARVDGrSEEEEETPLHVAARLGH--VELADLLLRRGA-C 240
Cdd:PHA02946  55 VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNA-CDKQHKTPLYYLSGTDDevIERINLLVQYGAkI 133
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 241 PDARDAEGWTPLLAACDircqstadaeatTARCLQLCSLLLSAGADADAADRDKHRPLHLACRRGHAAVVELLLSCGVSA 320
Cdd:PHA02946 134 NNSVDEEGCGPLLACTD------------PSERVFKKIMSIGFEARIVDKFGKNHIHRHLMSDNPKASTISWMMKLGISP 201
                        170
                 ....*....|..
gi 966936467 321 NAMDYGGHTPLH 332
Cdd:PHA02946 202 SKPDHDGNTPLH 213
PHA03100 PHA03100
ankyrin repeat protein; Provisional
198-358 5.56e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 45.43  E-value: 5.56e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 198 ELLLRFGARVDGrSEEEEETPLHVAARLGHV-----ELADLLLRRGACPDARDAEGWTPLL-AACDIRCQST-------- 263
Cdd:PHA03100  52 KILLDNGADINS-STKNNSTPLHYLSNIKYNltdvkEIVKLLLEYGANVNAPDNNGITPLLyAISKKSNSYSiveylldn 130
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 264 -ADAEATTARClqlcslllsagadadaadrdkHRPLHLACRRGHA--AVVELLLSCGVSANAMD-------YG------- 326
Cdd:PHA03100 131 gANVNIKNSDG---------------------ENLLHLYLESNKIdlKILKLLIDKGVDINAKNrvnyllsYGvpinikd 189
                        170       180       190
                 ....*....|....*....|....*....|....
gi 966936467 327 --GHTPLHcalqgpAAALAQSPEhVVRALLNHGA 358
Cdd:PHA03100 190 vyGFTPLH------YAVYNNNPE-FVKYLLDLGA 216
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
148-176 7.04e-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: 39.88  E-value: 7.04e-05
                           10        20
                   ....*....|....*....|....*....
gi 966936467   148 GRTALHEACAAGHTACVHVLLVAGADPNI 176
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02875 PHA02875
ankyrin repeat protein; Provisional
149-358 7.27e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 44.98  E-value: 7.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 149 RTALHEACAAGHTACVHVLLVAGADPNIADQDGKRPLHLCRGPGTLECAELLLRFGARVDgRSEEEEETPLHVAARLGHV 228
Cdd:PHA02875   3 QVALCDAILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPD-VKYPDIESELHDAVEEGDV 81
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 229 ELADLLLRRGA-CPDARDAEGWTPLLAacdircqstadaeATTARCLQLCSLLLSAGADADAADRDKHRPLHLACRRGHA 307
Cdd:PHA02875  82 KAVEELLDLGKfADDVFYKDGMTPLHL-------------ATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDI 148
                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 966936467 308 AVVELLLSCGVSANAMDYGGHTPLhcalqgpAAALAQSPEHVVRALLNHGA 358
Cdd:PHA02875 149 KGIELLIDHKACLDIEDCCGCTPL-------IIAMAKGDIAICKMLLDSGA 192
PHA02946 PHA02946
ankyin-like protein; Provisional
148-219 1.18e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 44.27  E-value: 1.18e-04
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 966936467 148 GRTALHEACAAGHTACVHVLLVAGADPNIADQDGKRPLHLCRGPG--TLECAELLLRFGARVDGRSEEEEETPL 219
Cdd:PHA02946  72 GNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYYLSGTDdeVIERINLLVQYGAKINNSVDEEGCGPL 145
PHA02876 PHA02876
ankyrin repeat protein; Provisional
148-358 1.43e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 44.28  E-value: 1.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 148 GRTALHEACAAGH-TACVHVLLVAGADPNIADQDGKRPLH----LCRGPGTLECaelLLRFGARVDGRsEEEEETPLHVA 222
Cdd:PHA02876 307 GETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHqastLDRNKDIVIT---LLELGANVNAR-DYCDKTPIHYA 382
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 223 ARLGHVELADLLLRRGACPDARDAEGWTPL-LAACD----IRCQSTADAEATTARCLQLCSLllsagadadaadrdkhrP 297
Cdd:PHA02876 383 AVRNNVVIINTLLDYGADIEALSQKIGTALhFALCGtnpyMSVKTLIDRGANVNSKNKDLST-----------------P 445
                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 966936467 298 LHLACRRG-HAAVVELLLSCGVSANAMDYGGHTPLHCALQgpaaalaqsPEHVVRALLNHGA 358
Cdd:PHA02876 446 LHYACKKNcKLDVIEMLLDNGADVNAINIQNQYPLLIALE---------YHGIVNILLHYGA 498
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
118-252 1.73e-04

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 43.85  E-value: 1.73e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 118 TPLHVAASRGHTEVLRLLLrrrarpDSAPG------------GRTALHEACAAGHTACVHVLLVAGADPNIADQDGkrpL 185
Cdd:cd22192   53 TALHVAALYDNLEAAVVLM------EAAPElvnepmtsdlyqGETALHIAVVNQNLNLVRELIARGADVVSPRATG---T 123
                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 966936467 186 HLCRGPGTLecaellLRFGarvdgrseeeeETPLHVAARLGHVELADLLLRRGACPDARDAEGWTPL 252
Cdd:cd22192  124 FFRPGPKNL------IYYG-----------EHPLSFAACVGNEEIVRLLIEHGADIRAQDSLGNTVL 173
PHA02875 PHA02875
ankyrin repeat protein; Provisional
118-239 2.43e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.44  E-value: 2.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 118 TPLHVAASRGHTEVLRLLLRRRARPDSAPGGRTA-LHEACAAGHTACVHVLLVAGADPNIADQDGKRPLHLCRGPGTLEC 196
Cdd:PHA02875 104 TPLHLATILKKLDIMKLLIARGADPDIPNTDKFSpLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183
                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 966936467 197 AELLLRFGARVDGRSEEEEETPLHVAARLGHVELADLLLRRGA 239
Cdd:PHA02875 184 CKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGA 226
Ank_4 pfam13637
Ankyrin repeats (many copies);
296-337 2.54e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.79  E-value: 2.54e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 966936467  296 RPLHLACRRGHAAVVELLLSCGVSANAMDYGGHTPLHCALQG 337
Cdd:pfam13637   3 TALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASN 44
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
297-334 6.29e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 6.29e-04
                         10        20        30
                 ....*....|....*....|....*....|....*...
gi 966936467 297 PLHLACRRGHAAVVELLLSCGVSANAMDYGGHTPLHCA 334
Cdd:PTZ00322 118 PLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELA 155
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
297-322 7.00e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.80  E-value: 7.00e-04
                           10        20
                   ....*....|....*....|....*.
gi 966936467   297 PLHLACRRGHAAVVELLLSCGVSANA 322
Cdd:smart00248   5 PLHLAAENGNLEVVKLLLDKGADINA 30
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
297-324 7.44e-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: 7.44e-04
                          10        20
                  ....*....|....*....|....*....
gi 966936467  297 PLHLAC-RRGHAAVVELLLSCGVSANAMD 324
Cdd:pfam00023   5 PLHLAAgRRGNLEIVKLLLSKGADVNARD 33
Ank_5 pfam13857
Ankyrin repeats (many copies);
297-334 8.34e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 8.34e-04
                          10        20        30
                  ....*....|....*....|....*....|....*...
gi 966936467  297 PLHLACRRGHAAVVELLLSCGVSANAMDYGGHTPLHCA 334
Cdd:pfam13857  19 PLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
155-358 9.26e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 41.78  E-value: 9.26e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 155 ACAAGHTACVHVLLVAGADPNIADQDGKRPLHLCRGPGTLECAELLLRFGARVDGRsEEEEETPLHVAARLGHVELADLL 234
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIR-DANGNTALWNAISAKHHKIFRIL 610
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 235 LRRGACPDARdaegwtpllAACDIRCqstadaeattarclqlcslllsagadadaadrdkhrplhLACRRGHAAVVELLL 314
Cdd:PLN03192 611 YHFASISDPH---------AAGDLLC---------------------------------------TAAKRNDLTAMKELL 642
                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....
gi 966936467 315 SCGVSANAMDYGGHTplhcALQgpaAALAQSPEHVVRALLNHGA 358
Cdd:PLN03192 643 KQGLNVDSEDHQGAT----ALQ---VAMAEDHVDMVRLLIMNGA 679
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
217-243 1.16e-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: 1.16e-03
                           10        20
                   ....*....|....*....|....*..
gi 966936467   217 TPLHVAARLGHVELADLLLRRGACPDA 243
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02876 PHA02876
ankyrin repeat protein; Provisional
149-358 1.40e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 41.20  E-value: 1.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 149 RTALHEACAAGHTACVHVLLVAGADPNIADQDG---------------------------KRPLHLCRGPGT--LECAEL 199
Cdd:PHA02876 179 ITPIHYAAERGNAKMVNLLLSYGADVNIIALDDlsvlecavdsknidtikaiidnrsninKNDLSLLKAIRNedLETSLL 258
                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 200 LLRFGARVDGrSEEEEETPLHVAARLGHV-ELADLLLRRGACPDARDAEGWTPLLAAC-------DIRCQSTADAEATTA 271
Cdd:PHA02876 259 LYDAGFSVNS-IDDCKNTPLHHASQAPSLsRLVPKLLERGADVNAKNIKGETPLYLMAkngydteNIRTLIMLGADVNAA 337
                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 272 RCLQLCslllsagadadaadrdkhrPLHLACRRG-HAAVVELLLSCGVSANAMDYGGHTPLHcalqgpaAALAQSPEHVV 350
Cdd:PHA02876 338 DRLYIT-------------------PLHQASTLDrNKDIVITLLELGANVNARDYCDKTPIH-------YAAVRNNVVII 391

                 ....*...
gi 966936467 351 RALLNHGA 358
Cdd:PHA02876 392 NTLLDYGA 399
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
297-322 1.55e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.08  E-value: 1.55e-03
                          10        20
                  ....*....|....*....|....*.
gi 966936467  297 PLHLACRRGHAAVVELLLSCGVSANA 322
Cdd:pfam13606   5 PLHLAARNGRLEIVKLLLENGADINA 30
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
216-239 1.59e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 36.08  E-value: 1.59e-03
                          10        20
                  ....*....|....*....|....
gi 966936467  216 ETPLHVAARLGHVELADLLLRRGA 239
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGA 26
SOCS_box pfam07525
SOCS box; The SOCS box acts as a bridge between specific substrate- binding domains and more ...
421-444 1.59e-03

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: 35.99  E-value: 1.59e-03
                          10        20
                  ....*....|....*....|....
gi 966936467  421 QPRSLQHLSRCALRSHLEGSLPHA 444
Cdd:pfam07525   1 TPRSLQHLCRLAIRRALGKRRLGA 24
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
148-176 2.19e-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: 2.19e-03
                          10        20
                  ....*....|....*....|....*....
gi 966936467  148 GRTALHEACAAGHTACVHVLLVAGADPNI 176
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
111-260 2.22e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 40.33  E-value: 2.22e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 111 TYEEELTTPLHVAASRGHTEVLRLLLRRRARPD-SAPGGRTALHEACAAGHTACVHVLLVAGADPNIADQDGKRPLHLCR 189
Cdd:PHA02874 119 IKDAELKTFLHYAIKKGDLESIKMLFEYGADVNiEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAA 198
                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 966936467 190 GPGTLECAELLLRFGARVDGRSeEEEETPLHVAarLGHVELADLLLRRGACPDARDAEGWTPLLAACDIRC 260
Cdd:PHA02874 199 EYGDYACIKLLIDHGNHIMNKC-KNGFTPLHNA--IIHNRSAIELLINNASINDQDIDGSTPLHHAINPPC 266
SOCS cd03587
SOCS (suppressors of cytokine signaling) box. The SOCS box is found in the C-terminal region ...
421-444 3.36e-03

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: 35.14  E-value: 3.36e-03
                         10        20
                 ....*....|....*....|....
gi 966936467 421 QPRSLQHLSRCALRSHLEGSLPHA 444
Cdd:cd03587    1 NPRSLQHLCRLAIRRCLGKRRLDL 24
Ank_5 pfam13857
Ankyrin repeats (many copies);
147-188 5.11e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.01  E-value: 5.11e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 966936467  147 GGRTALHEACAAGHTACVHVLLVAGADPNIADQDGKRPLHLC 188
Cdd:pfam13857  15 EGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02736 PHA02736
Viral ankyrin protein; Provisional
178-257 5.81e-03

Viral ankyrin protein; Provisional


Pssm-ID: 165103 [Multi-domain]  Cd Length: 154  Bit Score: 37.55  E-value: 5.81e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 966936467 178 DQDGKRPLHLCRGPGTLECAE---LLLRFGARVDGRSEEEEETPLHVAARLGHVELADLLLRR-GACPDARDAEGWTPLL 253
Cdd:PHA02736  52 NRHGKQCVHIVSNPDKADPQEklkLLMEWGADINGKERVFGNTPLHIAVYTQNYELATWLCNQpGVNMEILNYAFKTPYY 131

                 ....
gi 966936467 254 AACD 257
Cdd:PHA02736 132 VACE 135
SOCS_ASB_like cd03716
SOCS (suppressors of cytokine signaling) box of ASB (ankyrin repeat and SOCS box) and SSB ...
420-444 6.04e-03

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: 34.39  E-value: 6.04e-03
                         10        20
                 ....*....|....*....|....*
gi 966936467 420 RQPRSLQHLSRCALRSHLEGSLPHA 444
Cdd:cd03716    1 STPRSLQHLCRLAIRRCLGRRRLEL 25
 
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.
Help | Disclaimer | Write to the Help Desk
NCBI | NLM | NIH