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Conserved domains on  [gi|118572910|sp|Q2IBG0|]
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RecName: Full=Ankyrin repeat, SAM and basic leucine zipper domain-containing protein 1; AltName: Full=Germ cell-specific ankyrin, SAM and basic leucine zipper domain-containing protein

Protein Classification

ANKYR and SAM_ASZ1 domain-containing protein( domain architecture ID 12789531)

ANKYR and SAM_ASZ1 domain-containing protein

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-250 4.56e-40

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.87  E-value: 4.56e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  53 ALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASIANVELVRVLLNRGA--NASfDKDKQTILITACsARGSEEqilk 130
Cdd:COG0666   94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAdvNAQ-DNDGNTPLHLAA-ANGNLE---- 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910 131 CVELLLSRNADPNIACRRLMTPIMYAARDGHPQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVVLKLLELGANKML 210
Cdd:COG0666  168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 118572910 211 QTKDGKIPSEIAKRNKHLEIFNFLSLTLNPLEGNLKQLTK 250
Cdd:COG0666  248 KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 272-333 4.93e-22

SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine Zipper) also known as GASZ (Germ cell-specific Ankyrin, SAM, leucine Zipper) subfamily is a potential protein-protein interaction domain. Proteins of this group are involved in the repression of transposable elements during spermatogenesis, oogenesis, and preimplantation embryogenesis. They support synthesis of PIWI-interacting RNA via association with some PIWI proteins, such as MILI and MIWI. This association is required for initiation and maintenance of retrotransposon repression during the meiosis. In mice lacking ASZ1, DNA damage and delayed germ cell maturation was observed due to retrotransposons releasing from their repressed state.


:

Pssm-ID: 188920  Cd Length: 64  Bit Score: 89.27  E-value: 4.93e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118572910 272 SYTAFGDLEIFLHGLGLEHMTDLLKEKDITLRHLLTMRKDEFTKNGITS-KDQEKILSALKEL 333
Cdd:cd09521    1 SYSKLDDLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQpGDQKKILDAIKEV 63
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-250 4.56e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.87  E-value: 4.56e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  53 ALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASIANVELVRVLLNRGA--NASfDKDKQTILITACsARGSEEqilk 130
Cdd:COG0666   94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAdvNAQ-DNDGNTPLHLAA-ANGNLE---- 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910 131 CVELLLSRNADPNIACRRLMTPIMYAARDGHPQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVVLKLLELGANKML 210
Cdd:COG0666  168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 118572910 211 QTKDGKIPSEIAKRNKHLEIFNFLSLTLNPLEGNLKQLTK 250
Cdd:COG0666  248 KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 272-333 4.93e-22

SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine Zipper) also known as GASZ (Germ cell-specific Ankyrin, SAM, leucine Zipper) subfamily is a potential protein-protein interaction domain. Proteins of this group are involved in the repression of transposable elements during spermatogenesis, oogenesis, and preimplantation embryogenesis. They support synthesis of PIWI-interacting RNA via association with some PIWI proteins, such as MILI and MIWI. This association is required for initiation and maintenance of retrotransposon repression during the meiosis. In mice lacking ASZ1, DNA damage and delayed germ cell maturation was observed due to retrotransposons releasing from their repressed state.


Pssm-ID: 188920  Cd Length: 64  Bit Score: 89.27  E-value: 4.93e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118572910 272 SYTAFGDLEIFLHGLGLEHMTDLLKEKDITLRHLLTMRKDEFTKNGITS-KDQEKILSALKEL 333
Cdd:cd09521    1 SYSKLDDLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQpGDQKKILDAIKEV 63
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 59-234 1.15e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.88  E-value: 1.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  59 ISLVQELLDSGISVDSSFRYGWTPLMYAASI-----ANVELVRVLLNRGA--NASFDKDKQTILITACSARGSeeqiLKC 131
Cdd:PHA03100  48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGAnvNAPDNNGITPLLYAISKKSNS----YSI 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910 132 VELLLSRNADPNIACRRLMTPIMYAARDGHP--QVVALLVAHGAEVNAQ----------------DENGYTALTWAARQG 193
Cdd:PHA03100 124 VEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKnrvnyllsygvpinikDVYGFTPLHYAVYNN 203

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 118572910 194 HKNVVLKLLELGANKMLQTKDGKIPSEIAKRNKHLEIFNFL 234
Cdd:PHA03100 204 NPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
129-211 1.11e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 1.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  129 LKCVELLLSRNADPNIACRRLMTPIMYAARDGHPQVVALLVAHgAEVNAQDeNGYTALTWAARQGHKNVVLKLLELGANK 208
Cdd:pfam12796  10 LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADI 87


                  ...
gi 118572910  209 MLQ 211
Cdd:pfam12796  88 NVK 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 74-234 1.30e-05

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: 47.70  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  74 SSFRYGWTPLMYAASIANVELVRVLLNRGAnasfdkDKQTILITACSARGSEEQILKCVELLLSrnadpniacrrlmtpi 153
Cdd:cd22192   84 SDLYQGETALHIAVVNQNLNLVRELIARGA------DVVSPRATGTFFRPGPKNLIYYGEHPLS---------------- 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910 154 mYAARDGHPQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVVLKLLELGAN----------KMLQTKDGKIPSEIAK 223
Cdd:cd22192  142 -FAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYDLILSydkeddlqplDLVPNNQGLTPFKLAA 220

                        170
                 ....*....|.
gi 118572910 224 RNKHLEIFNFL 234
Cdd:cd22192  221 KEGNIVMFQHL 231
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 282-333 1.67e-04

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 39.56  E-value: 1.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 118572910  282 FLHGLGLEHMTDLLKEKDITLRHLLTMRKDEFTKNGITSK-DQEKILSALKEL 333
Cdd:pfam00536  11 WLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLgHRKKILYAIQRL 63
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 78-104 1.99e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 1.99e-04
                           10        20
                   ....*....|....*....|....*..
gi 118572910    78 YGWTPLMYAASIANVELVRVLLNRGAN 104
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-250 4.56e-40

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 145.87  E-value: 4.56e-40
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  53 ALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASIANVELVRVLLNRGA--NASfDKDKQTILITACsARGSEEqilk 130
Cdd:COG0666   94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAdvNAQ-DNDGNTPLHLAA-ANGNLE---- 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910 131 CVELLLSRNADPNIACRRLMTPIMYAARDGHPQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVVLKLLELGANKML 210
Cdd:COG0666  168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 118572910 211 QTKDGKIPSEIAKRNKHLEIFNFLSLTLNPLEGNLKQLTK 250
Cdd:COG0666  248 KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
50-234 1.65e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 144.33  E-value: 1.65e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  50 FKKALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASIANVELVRVLLNRGAN-ASFDKDKQTILITACsARGSEEqi 128
Cdd:COG0666   58 LLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADvNARDKDGETPLHLAA-YNGNLE-- 134

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910 129 lkCVELLLSRNADPNIACRRLMTPIMYAARDGHPQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVVLKLLELGANK 208
Cdd:COG0666  135 --IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADV 212

                        170       180
                 ....*....|....*....|....*.
gi 118572910 209 MLQTKDGKIPSEIAKRNKHLEIFNFL 234
Cdd:COG0666  213 NAKDNDGKTALDLAAENGNLEIVKLL 238
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 272-333 4.93e-22

SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine Zipper) also known as GASZ (Germ cell-specific Ankyrin, SAM, leucine Zipper) subfamily is a potential protein-protein interaction domain. Proteins of this group are involved in the repression of transposable elements during spermatogenesis, oogenesis, and preimplantation embryogenesis. They support synthesis of PIWI-interacting RNA via association with some PIWI proteins, such as MILI and MIWI. This association is required for initiation and maintenance of retrotransposon repression during the meiosis. In mice lacking ASZ1, DNA damage and delayed germ cell maturation was observed due to retrotransposons releasing from their repressed state.


Pssm-ID: 188920  Cd Length: 64  Bit Score: 89.27  E-value: 4.93e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 118572910 272 SYTAFGDLEIFLHGLGLEHMTDLLKEKDITLRHLLTMRKDEFTKNGITS-KDQEKILSALKEL 333
Cdd:cd09521    1 SYSKLDDLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQpGDQKKILDAIKEV 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
59-234 7.62e-21

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 92.71  E-value: 7.62e-21
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  59 ISLVQELLDSGISVDSSFRYGWTPLMYAASIANVELVRVLLNRGANASFDKDKQTILITACSARGSEEQILkcveLLLSR 138
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVAL----LLLAA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910 139 NADPNIACRRLMTPIMYAARDGHPQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVVLKLLELGANKMLQTKDGKIP 218
Cdd:COG0666   77 GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP 156

                        170
                 ....*....|....*.
gi 118572910 219 SEIAKRNKHLEIFNFL 234
Cdd:COG0666  157 LHLAAANGNLEIVKLL 172
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 59-234 1.15e-19

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 90.88  E-value: 1.15e-19
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  59 ISLVQELLDSGISVDSSFRYGWTPLMYAASI-----ANVELVRVLLNRGA--NASFDKDKQTILITACSARGSeeqiLKC 131
Cdd:PHA03100  48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGAnvNAPDNNGITPLLYAISKKSNS----YSI 123

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910 132 VELLLSRNADPNIACRRLMTPIMYAARDGHP--QVVALLVAHGAEVNAQ----------------DENGYTALTWAARQG 193
Cdd:PHA03100 124 VEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINAKnrvnyllsygvpinikDVYGFTPLHYAVYNN 203

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 118572910 194 HKNVVLKLLELGANKMLQTKDGKIPSEIAKRNKHLEIFNFL 234
Cdd:PHA03100 204 NPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
129-211 1.11e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 77.85  E-value: 1.11e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  129 LKCVELLLSRNADPNIACRRLMTPIMYAARDGHPQVVALLVAHgAEVNAQDeNGYTALTWAARQGHKNVVLKLLELGANK 208
Cdd:pfam12796  10 LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADI 87


                  ...
gi 118572910  209 MLQ 211
Cdd:pfam12796  88 NVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
83-179 1.65e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 74.38  E-value: 1.65e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910   83 LMYAASIANVELVRVLLNRGANASF-DKDKQTILITACSaRGSEEqilkCVELLLSrNADPNIACRRlMTPIMYAARDGH 161
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLqDKNGRTALHLAAK-NGHLE----IVKLLLE-HADVNLKDNG-RTALHYAARSGH 73

                          90
                  ....*....|....*...
gi 118572910  162 PQVVALLVAHGAEVNAQD 179
Cdd:pfam12796  74 LEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
57-144 1.02e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.68  E-value: 1.02e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910   57 GDISLVQELLDSGISVDSSFRYGWTPLMYAASIANVELVRVLLNRgANASFDKDKQTILITACSARgseeqILKCVELLL 136
Cdd:pfam12796   8 GNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSG-----HLEIVKLLL 81


                  ....*...
gi 118572910  137 SRNADPNI 144
Cdd:pfam12796  82 EKGADINV 89
PHA03095 PHA03095
ankyrin-like protein; Provisional
 65-240 1.28e-13

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 72.75  E-value: 1.28e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  65 LLDSGISVDSSFRYGWTPLmyAASI----ANVELVRVLLNRGANAsFDKD--KQTIL-ITACSARGSEeqilKCVELLLS 137
Cdd:PHA03095 138 LLRKGADVNALDLYGMTPL--AVLLksrnANVELLRLLIDAGADV-YAVDdrFRSLLhHHLQSFKPRA----RIVRELIR 210

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910 138 RNADPNIACRRLMTPIMYAARDGHPQ--VVALLVAHGAEVNAQDENGYTALTWAARQGHKNVVLKLLELGANKMLQTKDG 215
Cdd:PHA03095 211 AGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDG 290

                        170       180
                 ....*....|....*....|....*.
gi 118572910 216 KIPSEIAKRNKHLEIFN-FLSLTLNP 240
Cdd:PHA03095 291 NTPLSLMVRNNNGRAVRaALAKNPSA 316
Ank_2 pfam12796
Ankyrin repeats (3 copies);
153-234 5.37e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 5.37e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  153 IMYAARDGHPQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVVLKLLELGANKMlqTKDGKIPSEIAKRNKHLEIFN 232
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78


                  ..
gi 118572910  233 FL 234
Cdd:pfam12796  79 LL 80
Ank_4 pfam13637
Ankyrin repeats (many copies);
150-202 7.50e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 7.50e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 118572910  150 MTPIMYAARDGHPQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVVLKLL 202
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 53-207 3.99e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.55  E-value: 3.99e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  53 ALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASIANVELVRVLLNRGA----------------------------- 103
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipdvkypdieselhdaveegdvkaveell 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910 104 ------NASFDKDKQTILITAcsargSEEQILKCVELLLSRNADPNIACRRLMTPIMYAARDGHPQVVALLVAHGAEVNA 177
Cdd:PHA02875  89 dlgkfaDDVFYKDGMTPLHLA-----TILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163

                        170       180       190
                 ....*....|....*....|....*....|
gi 118572910 178 QDENGYTALTWAARQGHKNVVLKLLELGAN 207
Cdd:PHA02875 164 EDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 44-218 1.14e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 60.36  E-value: 1.14e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  44 EEKSETFKKALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASIANVELVRVLLNRGANASfdkdkqtILITACSARG 123
Cdd:PHA02874  33 DETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTS-------ILPIPCIEKD 105

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910 124 SEEQILKCvelllsrNADPNIACRRLMTPIMYAARDGHPQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVVLKLLE 203
Cdd:PHA02874 106 MIKTILDC-------GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLE 178

                        170
                 ....*....|....*
gi 118572910 204 LGANKMLQTKDGKIP 218
Cdd:PHA02874 179 KGAYANVKDNNGESP 193
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 41-154 4.47e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.46  E-value: 4.47e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  41 LPGEEKSETFKKALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASIANVELVRVLLNRGANASFdKDKQTILITACS 120
Cdd:PHA02875 130 IPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDY-FGKNGCVAALCY 208

                         90       100       110
                 ....*....|....*....|....*....|....
gi 118572910 121 ArgSEEQILKCVELLLSRNADPNIacrrlMTPIM 154
Cdd:PHA02875 209 A--IENNKIDIVRLFIKRGADCNI-----MFMIE 235
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 52-207 7.31e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 58.15  E-value: 7.31e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  52 KALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASIANV-ELVRVLLNRGA--NASFDKDKQTILITACSARGSEEqi 128
Cdd:PHA02876 246 KAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGAdvNAKNIKGETPLYLMAKNGYDTEN-- 323

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910 129 lkcVELLLSRNADPNIACRRLMTPIMYAAR-DGHPQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVVLKLLELGAN 207
Cdd:PHA02876 324 ---IRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
Ank_5 pfam13857
Ankyrin repeats (many copies);
134-186 8.42e-09

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 51.58  E-value: 8.42e-09
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 118572910  134 LLLSRNADPNIACRRLMTPIMYAARDGHPQVVALLVAHGAEVNAQDENGYTAL 186
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA03095 PHA03095
ankyrin-like protein; Provisional
 73-207 3.32e-08

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 55.80  E-value: 3.32e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  73 DSSFRYgwtplMYAASIANVELVRVLLNRGANASFDKDKQTILITACsARGSEEQILKCVELLLSRNADPNIACRRLMTP 152
Cdd:PHA03095  13 AALYDY-----LLNASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLY-LHYSSEKVKDIVRLLLEAGADVNAPERCGFTP 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 118572910 153 IMYAARDGH-PQVVALLVAHGAEVNAQDENGYTAL-TWAARQG-HKNVVLKLLELGAN 207
Cdd:PHA03095  87 LHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLhVYLSGFNiNPKVIRLLLRKGAD 144
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 55-207 3.34e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 56.03  E-value: 3.34e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  55 TTGDISLVQELLDSGISVDSSFRYGWTPLMYAASIANVELVRVLLNRGANASF-DKDKQTILITACSARgsEEQILKcVE 133
Cdd:PLN03192 534 STGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIrDANGNTALWNAISAK--HHKIFR-IL 610

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118572910 134 LLLSRNADPNIACRRLMTpimyAARDGHPQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVVLKLLELGAN 207
Cdd:PLN03192 611 YHFASISDPHAAGDLLCT----AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 47-234 3.84e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.35  E-value: 3.84e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  47 SETFKKALTTGDISLVQELLDS-----GISVDSSFrygwTPLMYAASIANVELVRVLLNRGANASFDKDK-QTILITACS 120
Cdd:PHA02874   2 SQDLRMCIYSGDIEAIEKIIKNkgnciNISVDETT----TPLIDAIRSGDAKIVELFIKHGADINHINTKiPHPLLTAIK 77

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910 121 ARGSeeqilKCVELLLSRNADPNIacrrLMTPimyaarDGHPQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVVLK 200
Cdd:PHA02874  78 IGAH-----DIIKLLIDNGVDTSI----LPIP------CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKM 142

                        170       180       190
                 ....*....|....*....|....*....|....
gi 118572910 201 LLELGANKMLQTKDGKIPSEIAKRNKHLEIFNFL 234
Cdd:PHA02874 143 LFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLL 176
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 141-235 5.97e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.29  E-value: 5.97e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910 141 DPNIAcRRLMTPIMYAARDGHPQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVVLKLLELGANKMLQTKDGKIPSE 220
Cdd:PTZ00322  75 DPVVA-HMLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153

                         90
                 ....*....|....*
gi 118572910 221 IAKRNKHLEIFNFLS 235
Cdd:PTZ00322 154 LAEENGFREVVQLLS 168
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 278-332 2.64e-07

SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of approximately 70 amino acids. This domain is found in the Fungi/Metazoa group and in a restricted number of bacteria. Proteins with SAM domains are represented by a wide variety of domain architectures and have different intracellular localization, including nucleus, cytoplasm and membranes. SAM domains have diverse functions. They can interact with proteins, RNAs and membrane lipids, contain site of phosphorylation and/or kinase docking site, and play a role in protein homo and hetero dimerization/oligomerization in processes ranging from signal transduction to regulation of transcription. Mutations in SAM domains have been linked to several diseases.


Pssm-ID: 188886 [Multi-domain]  Cd Length: 56  Bit Score: 47.23  E-value: 2.64e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 118572910 278 DLEIFLHGLGLEHMTDLLKEKDITLRHLLTMRKDEFTKNGITSK-DQEKILSALKE 332
Cdd:cd09487    1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPgHRKKILRAIQR 56
Ank_5 pfam13857
Ankyrin repeats (many copies);
168-222 4.32e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.57  E-value: 4.32e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 118572910  168 LVAHG-AEVNAQDENGYTALTWAARQGHKNVVLKLLELGANKMLQTKDGKIPSEIA 222
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
Ank_4 pfam13637
Ankyrin repeats (many copies);
47-99 9.12e-07

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 45.73  E-value: 9.12e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 118572910   47 SETFKKALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASIANVELVRVLL 99
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 45-234 1.17e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.22  E-value: 1.17e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  45 EKSETFKKALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASIANVELVRVLLNRGANASF--------------DKD 110
Cdd:PHA02876 144 EYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIialddlsvlecavdSKN 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910 111 KQTI----------------LITACSARGSEEQIL-----------------------------KCVELLLSRNADPNIA 145
Cdd:PHA02876 224 IDTIkaiidnrsninkndlsLLKAIRNEDLETSLLlydagfsvnsiddckntplhhasqapslsRLVPKLLERGADVNAK 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910 146 CRRLMTPIMYAARDGH-PQVVALLVAHGAEVNAQDENGYTALTWAAR-QGHKNVVLKLLELGANKMLQTKDGKIPSEIAK 223
Cdd:PHA02876 304 NIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAA 383

                        250
                 ....*....|.
gi 118572910 224 RNKHLEIFNFL 234
Cdd:PHA02876 384 VRNNVVIINTL 394
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 61-218 2.03e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 49.96  E-value: 2.03e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  61 LVQELLDSGISVDSSFRYGWTPLMYAASIANVELVRVLLNRGANASFDKDKQTILITACSARGSEEQIlkcvELLLSRNA 140
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDII----KLLLEKGA 181

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118572910 141 DPNIACRRLMTPIMYAARDGHPQVVALLVAHGAEVNAQDENGYTALTWAARqgHKNVVLKLLELGANKMLQTKDGKIP 218
Cdd:PHA02874 182 YANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTP 257
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 132-234 2.50e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.25  E-value: 2.50e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910 132 VELLLSRNADPNIACRRLMTPIMYAARDGHPQVVALLVAHGAEVNAQDENGYTALtW----------------------- 188
Cdd:PLN03192 541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL-Wnaisakhhkifrilyhfasisdp 619

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 118572910 189 ---------AARQGHKNVVLKLLELGANKMLQTKDGKIPSEIAKRNKHLEIFNFL 234
Cdd:PLN03192 620 haagdllctAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 61-199 4.22e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.29  E-value: 4.22e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  61 LVQELLDSGISVDSSFRYGWTPLMYAASIANVELVRVLLNRGAN-ASFDKDKQTILITACSARGSeeqiLKCVELLLSRN 139
Cdd:PHA02876 357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADiEALSQKIGTALHFALCGTNP----YMSVKTLIDRG 432

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118572910 140 ADPNIACRRLMTPIMYAARDG-HPQVVALLVAHGAEVNAQD-ENGYTALTWAARQGHKNVVL 199
Cdd:PHA02876 433 ANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINiQNQYPLLIALEYHGIVNILL 494
PHA03095 PHA03095
ankyrin-like protein; Provisional
 58-204 4.27e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 48.87  E-value: 4.27e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  58 DISLVQELLDSGISVDSSFRYGWTPL---MYAASIANVELVRVLLNRGAnasfDKDKQTIL----ITACSARGSEEQILK 130
Cdd:PHA03095  26 TVEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGA----DVNAPERCgftpLHLYLYNATTLDVIK 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 118572910 131 cveLLLSRNADPNIACRRLMTPI-MYAARDG-HPQVVALLVAHGAEVNAQDENGYTALtwAARQGHKNVVLKLLEL 204
Cdd:PHA03095 102 ---LLIKAGADVNAKDKVGRTPLhVYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSRNANVELLRL 172
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 46-222 7.74e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.04  E-value: 7.74e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  46 KSETF-KKALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASIANVELVRVLLNRGANASF-DKDKQTILITAcsarg 123
Cdd:PHA02874 123 ELKTFlHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVkDNNGESPLHNA----- 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910 124 SEEQILKCVELLLSRNADPNIACRRLMTPIMYAARdgHPQVVALLVAHGAEVNAQDENGYTALTWAARQG-HKNVVLKLL 202
Cdd:PHA02874 198 AEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILL 275

                        170       180
                 ....*....|....*....|
gi 118572910 203 ELGANKMLQTKDGKIPSEIA 222
Cdd:PHA02874 276 YHKADISIKDNKGENPIDTA 295
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 91-222 1.08e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 47.95  E-value: 1.08e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  91 NVELVR-VLLNRganasFDKDKQTILITACSARGSEEQILKCVELLLSRNADPNIACR-RLMTPIMYAARDGHPQVVALL 168
Cdd:PHA02878 113 NVEIFKiILTNR-----YKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELL 187

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....
gi 118572910 169 VAHGAEVNAQDENGYTALTWAARQGHKNVVLKLLELGANKMLQTKDGKIPSEIA 222
Cdd:PHA02878 188 LSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 74-234 1.30e-05

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: 47.70  E-value: 1.30e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  74 SSFRYGWTPLMYAASIANVELVRVLLNRGAnasfdkDKQTILITACSARGSEEQILKCVELLLSrnadpniacrrlmtpi 153
Cdd:cd22192   84 SDLYQGETALHIAVVNQNLNLVRELIARGA------DVVSPRATGTFFRPGPKNLIYYGEHPLS---------------- 141

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910 154 mYAARDGHPQVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVVLKLLELGAN----------KMLQTKDGKIPSEIAK 223
Cdd:cd22192  142 -FAACVGNEEIVRLLIEHGADIRAQDSLGNTVLHILVLQPNKTFACQMYDLILSydkeddlqplDLVPNNQGLTPFKLAA 220

                        170
                 ....*....|.
gi 118572910 224 RNKHLEIFNFL 234
Cdd:cd22192  221 KEGNIVMFQHL 231
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 102-207 6.26e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.44  E-value: 6.26e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910 102 GANASFDKDKQTILITACSARGSEEQILKCVELLLSRNADPNIACRRLMTPIMYAARDGHPQVVALLVAHGAEVNAQDEN 181
Cdd:PHA02876 131 GNDIHYDKINESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD 210

                         90       100
                 ....*....|....*....|....*.
gi 118572910 182 GYTALTWAARQGHKNVVLKLLELGAN 207
Cdd:PHA02876 211 DLSVLECAVDSKNIDTIKAIIDNRSN 236
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 150-180 6.31e-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: 39.97  E-value: 6.31e-05
                          10        20        30
                  ....*....|....*....|....*....|..
gi 118572910  150 MTPIMYAA-RDGHPQVVALLVAHGAEVNAQDE 180
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 53-169 1.23e-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: 44.62  E-value: 1.23e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  53 ALTTGDISLVQELLDSGISVDSS------FR--------YGWTPLMYAASIANVELVRVLLNRGANA----SFDKDKQTI 114
Cdd:cd22192   96 AVVNQNLNLVRELIARGADVVSPratgtfFRpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIraqdSLGNTVLHI 175

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118572910 115 LITACSARGSEEQIlkcvELLLSRNADPNIAC------RRLMTPIMYAARDGHPQVVALLV 169
Cdd:cd22192  176 LVLQPNKTFACQMY----DLILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQHLV 232
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 61-218 1.24e-04

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 44.18  E-value: 1.24e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  61 LVQELLDSGISVDSSFRYGWTPLMYAASIANVELVRVLLNRGANASFD-KDKQTILITACSARGSeeqilkCVELLLSrN 139
Cdd:PHA02874 172 IIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKcKNGFTPLHNAIIHNRS------AIELLIN-N 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910 140 ADPNIACRRLMTPIMYAARdgHP---QVVALLVAHGAEVNAQDENGYTALTWAARQGHKNVVLKllELGANKMLQTKDGK 216
Cdd:PHA02874 245 ASINDQDIDGSTPLHHAIN--PPcdiDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIK--DIIANAVLIKEADK 320


                 ..
gi 118572910 217 IP 218
Cdd:PHA02874 321 LK 322
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 78-104 1.26e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 1.26e-04
                          10        20
                  ....*....|....*....|....*..
gi 118572910   78 YGWTPLMYAASIANVELVRVLLNRGAN 104
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
PHA03095 PHA03095
ankyrin-like protein; Provisional
 60-106 1.30e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 44.25  E-value: 1.30e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 118572910  60 SLVQELLDSGISVDSSFRYGWTPLMYAASIANVELVRVLLNRGANAS 106
Cdd:PHA03095 238 SLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN 284
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 282-333 1.67e-04

SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily conserved protein binding domain that is involved in the regulation of numerous developmental processes in diverse eukaryotes. The SAM domain can potentially function as a protein interaction module through its ability to homo- and heterooligomerise with other SAM domains.


Pssm-ID: 425739  Cd Length: 64  Bit Score: 39.56  E-value: 1.67e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 118572910  282 FLHGLGLEHMTDLLKEKDITLRHLLTMRKDEFTKNGITSK-DQEKILSALKEL 333
Cdd:pfam00536  11 WLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLgHRKKILYAIQRL 63
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 78-104 1.99e-04

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 38.34  E-value: 1.99e-04
                           10        20
                   ....*....|....*....|....*..
gi 118572910    78 YGWTPLMYAASIANVELVRVLLNRGAN 104
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 95-182 4.82e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 4.82e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  95 VRVLLNRGANA-SFDKDKQTILITACsARGSeeqiLKCVELLLSRNADPNIACRRLMTPIMYAARDGHPQVVALLVAHGA 173
Cdd:PTZ00322  98 ARILLTGGADPnCRDYDGRTPLHIAC-ANGH----VQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172


                 ....*....
gi 118572910 174 EVNAQDENG 182
Cdd:PTZ00322 173 CHFELGANA 181
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 53-192 5.45e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.17  E-value: 5.45e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  53 ALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASIANVELVRVLLNRGANASFDKDKQTILITACSARGSEEQILKcv 132
Cdd:PHA02878 175 ATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILK-- 252

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118572910 133 eLLLSRNADPNIACRRL-MTPIMYAARDghPQVVALLVAHGAEVNAQDENGYTALTWAARQ 192
Cdd:PHA02878 253 -LLLEHGVDVNAKSYILgLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 78-104 6.42e-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: 37.27  E-value: 6.42e-04
                          10        20
                  ....*....|....*....|....*...
gi 118572910   78 YGWTPLMYAASIA-NVELVRVLLNRGAN 104
Cdd:pfam00023   1 DGNTPLHLAAGRRgNLEIVKLLLSKGAD 28
PHA02946 PHA02946
ankyin-like protein; Provisional
 58-262 9.54e-04

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 41.58  E-value: 9.54e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  58 DISLVQELLDSGISVDSSFRYGWTPLMYAASIANVELVRVLLNRGANA-SFDKDKQTILITacsARGSEEQILKCVELLL 136
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPnACDKQHKTPLYY---LSGTDDEVIERINLLV 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910 137 SRNADPNIACRRLMTPIMYAARDGHPQVVALLVAHGAEVNAQDENGYTAL--TWAARQGHKNVVLKLLELGANKMLQTKD 214
Cdd:PHA02946 128 QYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHD 207

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910 215 GKIPSEI--AKRNKHLEIFNFL--SLTLN--------PLEGNLKQLTKEETICKLLTTDS 262
Cdd:PHA02946 208 GNTPLHIvcSKTVKNVDIINLLlpSTDVNkqnkfgdsPLTLLIKTLSPAHLINKLLSTSN 267
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 181-207 1.43e-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: 1.43e-03
                           10        20
                   ....*....|....*....|....*..
gi 118572910   181 NGYTALTWAARQGHKNVVLKLLELGAN 207
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 150-177 1.55e-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: 1.55e-03
                           10        20
                   ....*....|....*....|....*...
gi 118572910   150 MTPIMYAARDGHPQVVALLVAHGAEVNA 177
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADINA 30
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 58-207 1.59e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 41.02  E-value: 1.59e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  58 DISLVQELLDSGISVDSSFRY-GWTPLMYAASIANVELVRVLLNRGANA-SFDKDKQTILITACSARGSeeqilKCVELL 135
Cdd:PHA02878 146 EAEITKLLLSYGADINMKDRHkGNTALHYATENKDQRLTELLLSYGANVnIPDKTNNSPLHHAVKHYNK-----PIVHIL 220

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 118572910 136 LSRNADPNIACRRLMTPIMYA-ARDGHPQVVALLVAHGAEVNAQDE-NGYTALTWAARQGHKnvvLK-LLELGAN 207
Cdd:PHA02878 221 LENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERK---LKlLLEYGAD 292
Ank_4 pfam13637
Ankyrin repeats (many copies);
129-169 1.62e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 1.62e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 118572910  129 LKCVELLLSRNADPNIACRRLMTPIMYAARDGHPQVVALLV 169
Cdd:pfam13637  14 LELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 150-177 2.11e-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: 2.11e-03
                          10        20
                  ....*....|....*....|....*...
gi 118572910  150 MTPIMYAARDGHPQVVALLVAHGAEVNA 177
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02798 PHA02798
ankyrin-like protein; Provisional
 92-207 3.40e-03

ankyrin-like protein; Provisional


Pssm-ID: 222931 [Multi-domain]  Cd Length: 489  Bit Score: 39.82  E-value: 3.40e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572910  92 VELVRVLLNRGANAS-FDKDKQTILITACSARGSEEQILKCVELLLSRNADPNIACRRLMTPIMYAARDGH---PQVVAL 167
Cdd:PHA02798  51 TDIVKLFINLGANVNgLDNEYSTPLCTILSNIKDYKHMLDIVKILIENGADINKKNSDGETPLYCLLSNGYinnLEILLF 130

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|...
gi 118572910 168 LVAHGAEVNAQDENGYTALTWAARQGHK---NVVLKLLELGAN 207
Cdd:PHA02798 131 MIENGADTTLLDKDGFTMLQVYLQSNHHidiEIIKLLLEKGVD 173
SAM_ANKS3 cd09519
SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a ...
 273-319 4.52e-03

SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a potential protein-protein interaction domain. Proteins of this subfamily have N-terminal ankyrin repeats and a C-terminal SAM domain. SAM is a widespread domain in signaling proteins. In many cases it mediates homo-dimerization/oligomerization.


Pssm-ID: 188918  Cd Length: 64  Bit Score: 35.55  E-value: 4.52e-03
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 118572910 273 YTAFGDLEIFLHGLGLEHMTDLLKEKDITLRHLLTMRKDEFTKNGIT 319
Cdd:cd09519    1 YTGPKDLSELLEQIGCSKYLPIFEEQDIDLRIFLTLTESDLKEIGIT 47
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 81-158 8.55e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 38.04  E-value: 8.55e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118572910  81 TPLMYAASIANVELVRVLLNRGANASFDKDKQTILITACSARGSEeqiLKCVELLLSRNADPNIACRRLMTPIMYAAR 158
Cdd:PHA02884  72 NPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYISVLHGC---LKCLEILLSYGADINIQTNDMVTPIELALM 146
Ank_4 pfam13637
Ankyrin repeats (many copies);
79-136 9.82e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 34.56  E-value: 9.82e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 118572910   79 GWTPLMYAASIANVELVRVLLNRGANAS-FDKDKQTILITACSaRGSEEqilkCVELLL 136
Cdd:pfam13637   1 ELTALHAAAASGHLELLRLLLEKGADINaVDGNGETALHFAAS-NGNVE----VLKLLL 54
 
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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