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Conserved domains on  [gi|755493980|ref|XP_011246255|]
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ankyrin repeat and SOCS box protein 18 isoform X2 [Mus musculus]

Protein Classification

ankyrin repeat domain-containing protein( domain architecture ID 11429852)

ankyrin repeat (ANK) domain-containing protein is involved in mediating protein-protein interactions

Gene Ontology:  GO:0005515
PubMed:  33435370|17176038

Graphical summary

 Zoom to residue level

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
93-225 9.08e-25

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.95  E-value: 9.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980  93 TPLCIAAAHGHESCVRHLLSRKADPNA-SPGGRGALHEACLGNHTACARLLLQHGADPDLLNSEGLAPLHLCRTPASLGC 171
Cdd:COG0666  122 TPLHLAAYNGNLEIVKLLLEAGADVNAqDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755493980 172 ARELLEHGATVQLEGGPGRdTPLHVAAQRGLDEHAQLYLGFGARVDARNGRGET 225
Cdd:COG0666  202 VKLLLEAGADVNAKDNDGK-TALDLAAENGNLEIVKLLLEAGADLNAKDKDGLT 254
PTZ00322 super family cl31426
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 254-337 1.33e-08

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


The actual alignment was detected with superfamily member PTZ00322:

Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980 254 GGAAADARDEDERSPLHKACGHARPGLCTLLLRHGADAGALDYGGASPLARALQTATcapptapQRTVQVLLNH------ 327
Cdd:PTZ00322 104 GGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF-------REVVQLLSRHsqchfe 176

                         90
                 ....*....|.
gi 755493980 328 -GSRSVwPDAF 337
Cdd:PTZ00322 177 lGANAK-PDSF 186
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
93-225 9.08e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.95  E-value: 9.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980  93 TPLCIAAAHGHESCVRHLLSRKADPNA-SPGGRGALHEACLGNHTACARLLLQHGADPDLLNSEGLAPLHLCRTPASLGC 171
Cdd:COG0666  122 TPLHLAAYNGNLEIVKLLLEAGADVNAqDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755493980 172 ARELLEHGATVQLEGGPGRdTPLHVAAQRGLDEHAQLYLGFGARVDARNGRGET 225
Cdd:COG0666  202 VKLLLEAGADVNAKDNDGK-TALDLAAENGNLEIVKLLLEAGADLNAKDKDGLT 254
Ank_2 pfam12796
Ankyrin repeats (3 copies);
95-180 1.74e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 1.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980   95 LCIAAAHGHESCVRHLLSRKADPNA-SPGGRGALHEACLGNHTACARLLLQHgADPDlLNSEGLAPLHLCRTPASLGCAR 173
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLqDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78


                  ....*..
gi 755493980  174 ELLEHGA 180
Cdd:pfam12796  79 LLLEKGA 85
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 91-162 7.15e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.30  E-value: 7.15e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755493980  91 LTTPLCIAAAHGHESCVRHLLSRKADPNASP-GGRGALHEACLGNHTACARLLLQHGADPDLLNSEGLAPLHL 162
Cdd:PTZ00322  82 LTVELCQLAASGDAVGARILLTGGADPNCRDyDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 254-337 1.33e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980 254 GGAAADARDEDERSPLHKACGHARPGLCTLLLRHGADAGALDYGGASPLARALQTATcapptapQRTVQVLLNH------ 327
Cdd:PTZ00322 104 GGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF-------REVVQLLSRHsqchfe 176

                         90
                 ....*....|.
gi 755493980 328 -GSRSVwPDAF 337
Cdd:PTZ00322 177 lGANAK-PDSF 186
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 12-201 4.97e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 54.25  E-value: 4.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980  12 LQILQKMSQEPQI----RAGTPELAFHAALLAGDLDHIRLLMDqcfwdanAVFEISNGEMewqvtslatfgLSGLwtleY 87
Cdd:cd22192   30 VQAIKKLLKCPSCdlfqRGALGETALHVAALYDNLEAAVVLME-------AAPELVNEPM-----------TSDL----Y 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980  88 QREltTPLCIAAAHGHESCVRHLLSRKAD---PNA-----SPGGRGALH--------EACLGNHtACARLLLQHGADPDL 151
Cdd:cd22192   88 QGE--TALHIAVVNQNLNLVRELIARGADvvsPRAtgtffRPGPKNLIYygehplsfAACVGNE-EIVRLLIEHGADIRA 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755493980 152 LNSEGLAPLHLCRTPASLGCARELLE-------HGATVQLEGGPGRD--TPLHVAAQRG 201
Cdd:cd22192  165 QDSLGNTVLHILVLQPNKTFACQMYDlilsydkEDDLQPLDLVPNNQglTPFKLAAKEG 223
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 93-119 4.75e-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: 4.75e-05
                           10        20
                   ....*....|....*....|....*..
gi 755493980    93 TPLCIAAAHGHESCVRHLLSRKADPNA 119
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 93-210 2.79e-03

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: 39.68  E-value: 2.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980   93 TPLCIAAAHGHESCVRHLLSRKADPNA---------SPGGRGALHE-------ACLGNhTACARLLLQHGADPDLLNSEG 156
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPAracgdffvkSQGVDSFYHGesplnaaACLGS-PSIVALLSEDPADILTADSLG 208

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755493980  157 LAPLHLC---------RTPASLGCARELLEHGA----TVQLEGGPGRD--TPLHVAAQRGLDEHAQLYL 210
Cdd:TIGR00870 209 NTLLHLLvmenefkaeYEELSCQMYNFALSLLDklrdSKELEVILNHQglTPLKLAAKEGRIVLFRLKL 277
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
93-225 9.08e-25

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 101.95  E-value: 9.08e-25
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980  93 TPLCIAAAHGHESCVRHLLSRKADPNA-SPGGRGALHEACLGNHTACARLLLQHGADPDLLNSEGLAPLHLCRTPASLGC 171
Cdd:COG0666  122 TPLHLAAYNGNLEIVKLLLEAGADVNAqDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEI 201

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 755493980 172 ARELLEHGATVQLEGGPGRdTPLHVAAQRGLDEHAQLYLGFGARVDARNGRGET 225
Cdd:COG0666  202 VKLLLEAGADVNAKDNDGK-TALDLAAENGNLEIVKLLLEAGADLNAKDKDGLT 254
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
91-307 3.07e-22

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 95.02  E-value: 3.07e-22
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980  91 LTTPLCIAAAHGHESCVRHLLSRKADPNA-SPGGRGALHEACLGNHTACARLLLQHGADPDLLNSEGLAPLHLCRTPASL 169
Cdd:COG0666   54 GALLLLAAALAGDLLVALLLLAAGADINAkDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNL 133

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980 170 GCARELLEHGATVQLEGGPGRdTPLHVAAQRGLDEHAQLYLGFGARVDARNGRGETalsaacgaaarspdeharclrlca 249
Cdd:COG0666  134 EIVKLLLEAGADVNAQDNDGN-TPLHLAAANGNLEIVKLLLEAGADVNARDNDGET------------------------ 188

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 755493980 250 lllrggaaadardedersPLHKACGHARPGLCTLLLRHGADAGALDYGGASPLARALQ 307
Cdd:COG0666  189 ------------------PLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAE 228
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
92-225 4.39e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 86.16  E-value: 4.39e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980  92 TTPLCIAAAHGHESCVRHLLSRKADPNA-SPGGRGALHEACLGNHTACARLLLQHGADPDLLNSEGLAPLHLCRTPASLG 170
Cdd:COG0666  154 NTPLHLAAANGNLEIVKLLLEAGADVNArDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLE 233

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755493980 171 CARELLEHGATVQLEGGPGrDTPLHVAAQRGLDEHAQLYLGFGARVDARNGRGET 225
Cdd:COG0666  234 IVKLLLEAGADLNAKDKDG-LTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
Ank_2 pfam12796
Ankyrin repeats (3 copies);
95-180 1.74e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.52  E-value: 1.74e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980   95 LCIAAAHGHESCVRHLLSRKADPNA-SPGGRGALHEACLGNHTACARLLLQHgADPDlLNSEGLAPLHLCRTPASLGCAR 173
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLqDKNGRTALHLAAKNGHLEIVKLLLEH-ADVN-LKDNGRTALHYAARSGHLEIVK 78


                  ....*..
gi 755493980  174 ELLEHGA 180
Cdd:pfam12796  79 LLLEKGA 85
Ank_2 pfam12796
Ankyrin repeats (3 copies);
127-220 2.35e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.14  E-value: 2.35e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980  127 LHEACLGNHTACARLLLQHGADPDLLNSEGLAPLHLCrtpASLG---CARELLEHgatVQLEGGPGRDTPLHVAAQRGLD 203
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLA---AKNGhleIVKLLLEH---ADVNLKDNGRTALHYAARSGHL 74

                          90
                  ....*....|....*..
gi 755493980  204 EHAQLYLGFGARVDARN 220
Cdd:pfam12796  75 EIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
93-153 4.04e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 61.67  E-value: 4.04e-12
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755493980   93 TPLCIAAAHGHESCVRHLLSrKADPNASPGGRGALHEACLGNHTACARLLLQHGADPDLLN 153
Cdd:pfam12796  32 TALHLAAKNGHLEIVKLLLE-HADVNLKDNGRTALHYAARSGHLEIVKLLLEKGADINVKD 91
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
109-328 1.51e-10

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 61.12  E-value: 1.51e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980 109 HLLSRKADPNASPGGRGALHEACLGNHTACARLLLQHGADPDLLNSEGLAPLHLCRTPASLGCARELLEHGATVQLEGGP 188
Cdd:COG0666    7 LLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVALLLLAAGADINAKDDG 86

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980 189 GrDTPLHVAAQRGLDEHAQLYLGFGARVDARNGRGETalSAACGAAARSPD------EHarclrlcalllrgGAAADARD 262
Cdd:COG0666   87 G-NTLLHAAARNGDLEIVKLLLEAGADVNARDKDGET--PLHLAAYNGNLEivklllEA-------------GADVNAQD 150

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 755493980 263 EDERSPLHKACGHARPGLCTLLLRHGADAGALDYGGASPLARALQTATcapptapQRTVQVLLNHG 328
Cdd:COG0666  151 NDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGH-------LEIVKLLLEAG 209
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 91-162 7.15e-10

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 60.30  E-value: 7.15e-10
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755493980  91 LTTPLCIAAAHGHESCVRHLLSRKADPNASP-GGRGALHEACLGNHTACARLLLQHGADPDLLNSEGLAPLHL 162
Cdd:PTZ00322  82 LTVELCQLAASGDAVGARILLTGGADPNCRDyDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLEL 154
PHA03095 PHA03095
ankyrin-like protein; Provisional
 107-306 2.37e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 58.50  E-value: 2.37e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980 107 VRHLLSRKADPNASPG-GRGALHeACLGN---HTACARLLLQHGADPDLLNSEGLAPLH--LCRTPASLGCARELLEHGA 180
Cdd:PHA03095 100 IKLLIKAGADVNAKDKvGRTPLH-VYLSGfniNPKVIRLLLRKGADVNALDLYGMTPLAvlLKSRNANVELLRLLIDAGA 178

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980 181 ---TVQLEggpgRDTPLHVAAQ---------RGLdehaqlyLGFGARVDARNGRGETALsaacgaaarspdeHARCLRLC 248
Cdd:PHA03095 179 dvyAVDDR----FRSLLHHHLQsfkprarivREL-------IRAGCDPAATDMLGNTPL-------------HSMATGSS 234

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 755493980 249 ALLL------RGGAAADARDEDERSPLHKACGHARPGLCTLLLRHGADAGALDYGGASPLARAL 306
Cdd:PHA03095 235 CKRSlvlpllIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNTPLSLMV 298
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 254-337 1.33e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 56.45  E-value: 1.33e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980 254 GGAAADARDEDERSPLHKACGHARPGLCTLLLRHGADAGALDYGGASPLARALQTATcapptapQRTVQVLLNH------ 327
Cdd:PTZ00322 104 GGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLELAEENGF-------REVVQLLSRHsqchfe 176

                         90
                 ....*....|.
gi 755493980 328 -GSRSVwPDAF 337
Cdd:PTZ00322 177 lGANAK-PDSF 186
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 12-201 4.97e-08

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


Pssm-ID: 411976 [Multi-domain]  Cd Length: 609  Bit Score: 54.25  E-value: 4.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980  12 LQILQKMSQEPQI----RAGTPELAFHAALLAGDLDHIRLLMDqcfwdanAVFEISNGEMewqvtslatfgLSGLwtleY 87
Cdd:cd22192   30 VQAIKKLLKCPSCdlfqRGALGETALHVAALYDNLEAAVVLME-------AAPELVNEPM-----------TSDL----Y 87

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980  88 QREltTPLCIAAAHGHESCVRHLLSRKAD---PNA-----SPGGRGALH--------EACLGNHtACARLLLQHGADPDL 151
Cdd:cd22192   88 QGE--TALHIAVVNQNLNLVRELIARGADvvsPRAtgtffRPGPKNLIYygehplsfAACVGNE-EIVRLLIEHGADIRA 164

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755493980 152 LNSEGLAPLHLCRTPASLGCARELLE-------HGATVQLEGGPGRD--TPLHVAAQRG 201
Cdd:cd22192  165 QDSLGNTVLHILVLQPNKTFACQMYDlilsydkEDDLQPLDLVPNNQglTPFKLAAKEG 223
Ank_4 pfam13637
Ankyrin repeats (many copies);
92-143 5.68e-08

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 48.81  E-value: 5.68e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 755493980   92 TTPLCIAAAHGHESCVRHLLSRKADPNASPG-GRGALHEACLGNHTACARLLL 143
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGnGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 36-221 7.16e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.84  E-value: 7.16e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980  36 ALLAGDLDHIRLLMDQCFwdaNAVFEISNG------EMEWQVTSLATFGLSGLWTLEYQR-ELTTPLCIAAAHGHESCVR 108
Cdd:PHA02875   9 AILFGELDIARRLLDIGI---NPNFEIYDGispiklAMKFRDSEAIKLLMKHGAIPDVKYpDIESELHDAVEEGDVKAVE 85

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980 109 HLL--SRKADPNASPGGRGALHEACLGNHTACARLLLQHGADPDLLNSEGLAPLHLCRTPASLGCARELLEHGATVQLEG 186
Cdd:PHA02875  86 ELLdlGKFADDVFYKDGMTPLHLATILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIED 165

                        170       180       190
                 ....*....|....*....|....*....|....*..
gi 755493980 187 GPGRdTPLHVAAQRGLDEHAQLYLGFGARVD--ARNG 221
Cdd:PHA02875 166 CCGC-TPLIIAMAKGDIAICKMLLDSGANIDyfGKNG 201
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 139-211 2.14e-07

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 52.59  E-value: 2.14e-07
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 755493980 139 ARLLLQHGADPDLLNSEGLAPLHLCRTPASLGCARELLEHGATVQLEGGPGRdTPLHVAAQRGLDEHAQLYLG 211
Cdd:PTZ00322  98 ARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGK-TPLELAEENGFREVVQLLSR 169
PHA03095 PHA03095
ankyrin-like protein; Provisional
 107-312 1.19e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.02  E-value: 1.19e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980 107 VRHLLSRKADPN-ASPGGRGALHeACLgnHTACA------RLLLQHGADPDLLNSEGLAPLHLCRTPAS-LGCARELLEH 178
Cdd:PHA03095  30 VRRLLAAGADVNfRGEYGKTPLH-LYL--HYSSEkvkdivRLLLEAGADVNAPERCGFTPLHLYLYNATtLDVIKLLIKA 106

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980 179 GATVQLEGGPGRdTPLHVAAqRGLDEHA---QLYLGFGARVDARNGRGETALSAACGAAARSPDeharclrLCALLLRGG 255
Cdd:PHA03095 107 GADVNAKDKVGR-TPLHVYL-SGFNINPkviRLLLRKGADVNALDLYGMTPLAVLLKSRNANVE-------LLRLLIDAG 177

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|....*....
gi 755493980 256 AAADARDEDERSPLHKACG--HARPGLCTLLLRHGADAGALDYGGASPLARALQTATCA 312
Cdd:PHA03095 178 ADVYAVDDRFRSLLHHHLQsfKPRARIVRELIRAGCDPAATDMLGNTPLHSMATGSSCK 236
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 107-329 1.60e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 1.60e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980 107 VRHLLSRKADPNA-SPGGRGALH-EACLGNHTACARLLLQHGADPDLLNSEGLAPLHLCRT-PASLGCARELLEHGATVQ 183
Cdd:PHA02876 290 VPKLLERGADVNAkNIKGETPLYlMAKNGYDTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVN 369

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980 184 leggpGRD----TPLHVAAQRGLDEHAQLYLGFGARVDARNGRGETALSAACGAAarSPdeharcLRLCALLLRGGAAAD 259
Cdd:PHA02876 370 -----ARDycdkTPIHYAAVRNNVVIINTLLDYGADIEALSQKIGTALHFALCGT--NP------YMSVKTLIDRGANVN 436

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755493980 260 ARDEDERSPLHKAC-GHARPGLCTLLLRHGADAGALDYGGASPLARALQTatcapptapQRTVQVLLNHGS 329
Cdd:PHA02876 437 SKNKDLSTPLHYACkKNCKLDVIEMLLDNGADVNAINIQNQYPLLIALEY---------HGIVNILLHYGA 498
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 93-220 1.80e-05

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 46.40  E-value: 1.80e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980  93 TPLCIAAAHGHESCVRHLLSRKADPN-ASPGGRGALHEACLGNHTACARLLLQ--HGADP----DLLNseglaplhLCRT 165
Cdd:PLN03192 560 TPLHIAASKGYEDCVLVLLKHACNVHiRDANGNTALWNAISAKHHKIFRILYHfaSISDPhaagDLLC--------TAAK 631

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 755493980 166 PASLGCARELLEHGATVQLEGGPGRdTPLHVAAQRGLDEHAQLYLGFGARVDARN 220
Cdd:PLN03192 632 RNDLTAMKELLKQGLNVDSEDHQGA-TALQVAMAEDHVDMVRLLIMNGADVDKAN 685
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 93-119 4.75e-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: 4.75e-05
                           10        20
                   ....*....|....*....|....*..
gi 755493980    93 TPLCIAAAHGHESCVRHLLSRKADPNA 119
Cdd:smart00248   4 TPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 107-311 4.76e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 44.87  E-value: 4.76e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980 107 VRHLLSRKADPNASP--GGRGALHEACLGNHTACARLLLQHGADPDLLNSEGLAPLHLCRTPASLGCARELLEHGATVQL 184
Cdd:PHA02878 150 TKLLLSYGADINMKDrhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDA 229

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980 185 EGGPGrDTPLHVAAQRGLD-EHAQLYLGFGARVDARNG-RGETalsaacgaaarspdeharclrlcalllrggaaadard 262
Cdd:PHA02878 230 RDKCG-NTPLHISVGYCKDyDILKLLLEHGVDVNAKSYiLGLT------------------------------------- 271

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*....
gi 755493980 263 edersPLHKACghARPGLCTLLLRHGADAGALDYGGASPLARALQTATC 311
Cdd:PHA02878 272 -----ALHSSI--KSERKLKLLLEYGADINSLNSYKLTPLSSAVKQYLC 313
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 159-329 5.81e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.05  E-value: 5.81e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980 159 PLHLC-RTPASLGCARELLEHGATVQLEGGPGrDTPLHVAAQRGLD-EHAQLYLGFGARVDARNgRGETALSAACGAAAR 236
Cdd:PHA02876 276 PLHHAsQAPSLSRLVPKLLERGADVNAKNIKG-ETPLYLMAKNGYDtENIRTLIMLGADVNAAD-RLYITPLHQASTLDR 353

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980 237 SPDeharclrLCALLLRGGAAADARDEDERSPLHKACGHARPGLCTLLLRHGADAGALdyggASPLARALQTATCAppTA 316
Cdd:PHA02876 354 NKD-------IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADIEAL----SQKIGTALHFALCG--TN 420

                        170
                 ....*....|...
gi 755493980 317 PQRTVQVLLNHGS 329
Cdd:PHA02876 421 PYMSVKTLIDRGA 433
Ank_4 pfam13637
Ankyrin repeats (many copies);
123-163 7.37e-05

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 39.95  E-value: 7.37e-05
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 755493980  123 GRGALHEACLGNHTACARLLLQHGADPDLLNSEGLAPLHLC 163
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFA 41
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 93-214 1.04e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 43.83  E-value: 1.04e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980  93 TPLCIAAAHGHESCVRHLLSRKADPNASPGGR-GALHEACLGNHTACARLLLQHGADPDLLNSEGLAPLHLCRTPASLGC 171
Cdd:PHA02875 104 TPLHLATILKKLDIMKLLIARGADPDIPNTDKfSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAI 183

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 755493980 172 ARELLEHGATVQLEGGPGRDTPLHVAAQRGLDEHAQLYLGFGA 214
Cdd:PHA02875 184 CKMLLDSGANIDYFGKNGCVAALCYAIENNKIDIVRLFIKRGA 226
Ank_5 pfam13857
Ankyrin repeats (many copies);
115-163 5.87e-04

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 37.33  E-value: 5.87e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|
gi 755493980  115 ADPNASPGGRG-ALHEACLGNHTACARLLLQHGADPDLLNSEGLAPLHLC 163
Cdd:pfam13857   7 IDLNRLDGEGYtPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 123-153 1.06e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.11  E-value: 1.06e-03
                          10        20        30
                  ....*....|....*....|....*....|..
gi 755493980  123 GRGALHEACL-GNHTACARLLLQHGADPDLLN 153
Cdd:pfam00023   2 GNTPLHLAAGrRGNLEIVKLLLSKGADVNARD 33
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 123-151 1.09e-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: 36.03  E-value: 1.09e-03
                           10        20
                   ....*....|....*....|....*....
gi 755493980   123 GRGALHEACLGNHTACARLLLQHGADPDL 151
Cdd:smart00248   2 GRTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 127-307 1.61e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 39.95  E-value: 1.61e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980 127 LHEACLGNHTACARLLLQHGADPDLLNSEGLAPLHLCRTPASLGCARELLEHGATVQLEGGPGrDTPLHVAAQRGLDEHA 206
Cdd:PHA02874 128 LHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNG-ESPLHNAAEYGDYACI 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980 207 QLYLGFGARVDARNGRGETaLSAACGAAARSPDEharclrlcalLLRGGAAADARDEDERSPLHKACGH-ARPGLCTLLL 285
Cdd:PHA02874 207 KLLIDHGNHIMNKCKNGFT-PLHNAIIHNRSAIE----------LLINNASINDQDIDGSTPLHHAINPpCDIDIIDILL 275

                        170       180
                 ....*....|....*....|..
gi 755493980 286 RHGADAGALDYGGASPLARALQ 307
Cdd:PHA02874 276 YHKADISIKDNKGENPIDTAFK 297
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 93-119 2.74e-03

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 34.96  E-value: 2.74e-03
                          10        20
                  ....*....|....*....|....*...
gi 755493980   93 TPLCIAAAH-GHESCVRHLLSRKADPNA 119
Cdd:pfam00023   4 TPLHLAAGRrGNLEIVKLLLSKGADVNA 31
trp TIGR00870
transient-receptor-potential calcium channel protein; The Transient Receptor Potential Ca2+ ...
 93-210 2.79e-03

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: 39.68  E-value: 2.79e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980   93 TPLCIAAAHGHESCVRHLLSRKADPNA---------SPGGRGALHE-------ACLGNhTACARLLLQHGADPDLLNSEG 156
Cdd:TIGR00870 130 TALHLAAHRQNYEIVKLLLERGASVPAracgdffvkSQGVDSFYHGesplnaaACLGS-PSIVALLSEDPADILTADSLG 208

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 755493980  157 LAPLHLC---------RTPASLGCARELLEHGA----TVQLEGGPGRD--TPLHVAAQRGLDEHAQLYL 210
Cdd:TIGR00870 209 NTLLHLLvmenefkaeYEELSCQMYNFALSLLDklrdSKELEVILNHQglTPLKLAAKEGRIVLFRLKL 277
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 92-160 7.00e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 38.32  E-value: 7.00e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 755493980  92 TTPLCIAAAHGHE-SCVRHLLSRKADPNASPGGRG--ALHEACLGNHTAcaRLLLQHGADPDLLNSEGLAPL 160
Cdd:PHA02878 235 NTPLHISVGYCKDyDILKLLLEHGVDVNAKSYILGltALHSSIKSERKL--KLLLEYGADINSLNSYKLTPL 304
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 86-302 7.06e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 37.94  E-value: 7.06e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980  86 EYQRELTTPLCIAAAHGHESCVRHLLSRKADPNASPGGRgALHEACLGNHTACARLLLQHGADpdllNSEGLAPLHLCRT 165
Cdd:PHA02878  65 QPDHRDLTPLHIICKEPNKLGMKEMIRSINKCSVFYTLV-AIKDAFNNRNVEIFKIILTNRYK----NIQTIDLVYIDKK 139

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 755493980 166 PAS----LGCARELLEHGATVQLEGGPGRDTPLHVAAQRGLDEHAQLYLGFGARVDarngrgetalsaacgaaarSPDEh 241
Cdd:PHA02878 140 SKDdiieAEITKLLLSYGADINMKDRHKGNTALHYATENKDQRLTELLLSYGANVN-------------------IPDK- 199

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 755493980 242 arclrlcalllrggaaadardeDERSPLHKACGHARPGLCTLLLRHGADAGALDYGGASPL 302
Cdd:PHA02878 200 ----------------------TNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPL 238
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 123-150 7.49e-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: 33.77  E-value: 7.49e-03
                          10        20
                  ....*....|....*....|....*...
gi 755493980  123 GRGALHEACLGNHTACARLLLQHGADPD 150
Cdd:pfam13606   2 GNTPLHLAARNGRLEIVKLLLENGADIN 29
 
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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