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Conserved domains on  [gi|118572911|sp|Q07DX6|]
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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

ankyrin repeat domain-containing protein( domain architecture ID 12789531)

ankyrin repeat domain-containing protein; ANK proteins mediate specific protein-protein interactions without necessarily recognizing specific primary sequences which allows for one ankyrin repeat domain to recognize and bind to a variety of intracellular substrates and may be involved in a wide array of functions

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 1.99e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.24  E-value: 1.99e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  53 AMTIGDVSLVQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDRGA--NASfEKDKQSILITACsAHGSEELilk 130
Cdd:COG0666   94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAdvNAQ-DNDGNTPLHLAA-ANGNLEI--- 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911 131 cVELLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKML 210
Cdd:COG0666  169 -VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 118572911 211 QTKDGKMPSEIAKRNKHHEIFNLLSFTLNPLEGKLQQLTK 250
Cdd:COG0666  248 KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 272-334 1.84e-23

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: 93.12  E-value: 1.84e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118572911 272 SYTAFGDLEVFLHGLGLEHMTDLLKERDITLRHLLTMREDEFTKNGITS-KDQQKILAALKELQ 334
Cdd:cd09521    1 SYSKLDDLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQpGDQKKILDAIKEVH 64
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-250 1.99e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.24  E-value: 1.99e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  53 AMTIGDVSLVQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDRGA--NASfEKDKQSILITACsAHGSEELilk 130
Cdd:COG0666   94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAdvNAQ-DNDGNTPLHLAA-ANGNLEI--- 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911 131 cVELLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKML 210
Cdd:COG0666  169 -VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 118572911 211 QTKDGKMPSEIAKRNKHHEIFNLLSFTLNPLEGKLQQLTK 250
Cdd:COG0666  248 KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 272-334 1.84e-23

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: 93.12  E-value: 1.84e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118572911 272 SYTAFGDLEVFLHGLGLEHMTDLLKERDITLRHLLTMREDEFTKNGITS-KDQQKILAALKELQ 334
Cdd:cd09521    1 SYSKLDDLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQpGDQKKILDAIKEVH 64
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 59-281 2.00e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 87.03  E-value: 2.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  59 VSLVQELLDSGISVDSTFQYGWTPLMYAASV-----ANAELVRVLLDRGANASFEKDKQS----ILITACSAHgseeliL 129
Cdd:PHA03100  48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGItpllYAISKKSNS------Y 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911 130 KCVELLLSRNADPNVACRRLMTPIMYAARDGH--TQVVALLVAHGAEVN----------------TQDENGYTALTWAAR 191
Cdd:PHA03100 122 SIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINaknrvnyllsygvpinIKDVYGFTPLHYAVY 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911 192 QGHKNIVLKLLELGANKMLQTKDGKMPSEIAKRNKHHEIFNLLS---------------FTLNPLEGKLQQLTKEDTICK 256
Cdd:PHA03100 202 NNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLnngpsiktiietllyFKDKDLNTITKIKMLKKSIMY 281

                        250       260
                 ....*....|....*....|....*.
gi 118572911 257 ILTTDSDREKDH-IFSSYTAFGDLEV 281
Cdd:PHA03100 282 MFLLDPGFYKNRkLIENSKSLKDVIN 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
129-211 5.64e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 5.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  129 LKCVELLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHgAEVNTQDeNGYTALTWAARQGHKNIVLKLLELGANK 208
Cdd:pfam12796  10 LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADI 87


                  ...
gi 118572911  209 MLQ 211
Cdd:pfam12796  88 NVK 90
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 57-169 3.65e-06

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: 49.24  E-value: 3.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  57 GDVSLVQELLDSGISV--------------DSTFQYGWTPLMYAASVANAELVRVLLDRGANA----SFEKDKQSILITA 118
Cdd:cd22192  100 QNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIraqdSLGNTVLHILVLQ 179

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 118572911 119 CSAHGSEELIlkcvELLLSRNADPNVAC------RRLMTPIMYAARDGHTQVVALLV 169
Cdd:cd22192  180 PNKTFACQMY----DLILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQHLV 232
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 282-333 5.76e-05

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: 41.10  E-value: 5.76e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 118572911  282 FLHGLGLEHMTDLLKERDITLRHLLTMREDEFTKNGITSK-DQQKILAALKEL 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 1.42e-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: 38.72  E-value: 1.42e-04
                           10        20
                   ....*....|....*....|....*..
gi 118572911    78 YGWTPLMYAASVANAELVRVLLDRGAN 104
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-250 1.99e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.24  E-value: 1.99e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  53 AMTIGDVSLVQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDRGA--NASfEKDKQSILITACsAHGSEELilk 130
Cdd:COG0666   94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAdvNAQ-DNDGNTPLHLAA-ANGNLEI--- 168

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911 131 cVELLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKML 210
Cdd:COG0666  169 -VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 118572911 211 QTKDGKMPSEIAKRNKHHEIFNLLSFTLNPLEGKLQQLTK 250
Cdd:COG0666  248 KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-234 2.74e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 141.24  E-value: 2.74e-38
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  53 AMTIGDVSLVQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDRGANASFEKDKQSILITACSAHGSEELilkcV 132
Cdd:COG0666   61 AALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEI----V 136

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911 133 ELLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKMLQT 212
Cdd:COG0666  137 KLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKD 216

                        170       180
                 ....*....|....*....|..
gi 118572911 213 KDGKMPSEIAKRNKHHEIFNLL 234
Cdd:COG0666  217 NDGKTALDLAAENGNLEIVKLL 238
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 272-334 1.84e-23

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: 93.12  E-value: 1.84e-23
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118572911 272 SYTAFGDLEVFLHGLGLEHMTDLLKERDITLRHLLTMREDEFTKNGITS-KDQQKILAALKELQ 334
Cdd:cd09521    1 SYSKLDDLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQpGDQKKILDAIKEVH 64
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
59-234 4.04e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 90.40  E-value: 4.04e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  59 VSLVQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDRGANASFEKDKQSILITACSAHGSEELILkcveLLLSR 138
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVAL----LLLAA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911 139 NADPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKMLQTKDGKMP 218
Cdd:COG0666   77 GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP 156

                        170
                 ....*....|....*.
gi 118572911 219 SEIAKRNKHHEIFNLL 234
Cdd:COG0666  157 LHLAAANGNLEIVKLL 172
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 59-281 2.00e-18

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 87.03  E-value: 2.00e-18
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  59 VSLVQELLDSGISVDSTFQYGWTPLMYAASV-----ANAELVRVLLDRGANASFEKDKQS----ILITACSAHgseeliL 129
Cdd:PHA03100  48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGItpllYAISKKSNS------Y 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911 130 KCVELLLSRNADPNVACRRLMTPIMYAARDGH--TQVVALLVAHGAEVN----------------TQDENGYTALTWAAR 191
Cdd:PHA03100 122 SIVEYLLDNGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINaknrvnyllsygvpinIKDVYGFTPLHYAVY 201

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911 192 QGHKNIVLKLLELGANKMLQTKDGKMPSEIAKRNKHHEIFNLLS---------------FTLNPLEGKLQQLTKEDTICK 256
Cdd:PHA03100 202 NNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLnngpsiktiietllyFKDKDLNTITKIKMLKKSIMY 281

                        250       260
                 ....*....|....*....|....*.
gi 118572911 257 ILTTDSDREKDH-IFSSYTAFGDLEV 281
Cdd:PHA03100 282 MFLLDPGFYKNRkLIENSKSLKDVIN 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
129-211 5.64e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 78.62  E-value: 5.64e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  129 LKCVELLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHgAEVNTQDeNGYTALTWAARQGHKNIVLKLLELGANK 208
Cdd:pfam12796  10 LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADI 87


                  ...
gi 118572911  209 MLQ 211
Cdd:pfam12796  88 NVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
83-179 9.71e-15

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 69.37  E-value: 9.71e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911   83 LMYAASVANAELVRVLLDRGANASF-EKDKQSILITACSaHGSEElilkCVELLLSrNADPNVACRRlMTPIMYAARDGH 161
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLqDKNGRTALHLAAK-NGHLE----IVKLLLE-HADVNLKDNG-RTALHYAARSGH 73

                          90
                  ....*....|....*...
gi 118572911  162 TQVVALLVAHGAEVNTQD 179
Cdd:pfam12796  74 LEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 58-232 9.73e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 73.14  E-value: 9.73e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  58 DVSLVQELLDSGISVDSTFQYGWTPL-MYAASV-ANAELVRVLLDRGANAsFEKD--KQSIL-ITACSAHGSEelilKCV 132
Cdd:PHA03095 131 NPKVIRLLLRKGADVNALDLYGMTPLaVLLKSRnANVELLRLLIDAGADV-YAVDdrFRSLLhHHLQSFKPRA----RIV 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911 133 ELLLSRNADPNVACRRLMTPIMYAARDGHTQ--VVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKML 210
Cdd:PHA03095 206 RELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285

                        170       180
                 ....*....|....*....|..
gi 118572911 211 QTKDGKMPSEIAKRNKHHEIFN 232
Cdd:PHA03095 286 VSSDGNTPLSLMVRNNNGRAVR 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
57-144 4.62e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 64.75  E-value: 4.62e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911   57 GDVSLVQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDRgANASFEKDKQSILITACSaHGSEElilkCVELLL 136
Cdd:pfam12796   8 GNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAAR-SGHLE----IVKLLL 81


                  ....*...
gi 118572911  137 SRNADPNV 144
Cdd:pfam12796  82 EKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
153-234 2.47e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 2.47e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  153 IMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKMlqTKDGKMPSEIAKRNKHHEIFN 232
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78


                  ..
gi 118572911  233 LL 234
Cdd:pfam12796  79 LL 80
Ank_4 pfam13637
Ankyrin repeats (many copies);
150-202 8.09e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.98  E-value: 8.09e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 118572911  150 MTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLL 202
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 53-218 2.09e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.67  E-value: 2.09e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  53 AMTIGDVSLVQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDRGANASfekdkqsILITACSAHGSEELILKCv 132
Cdd:PHA02874  42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTS-------ILPIPCIEKDMIKTILDC- 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911 133 elllsrNADPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKMLQT 212
Cdd:PHA02874 114 ------GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187


                 ....*.
gi 118572911 213 KDGKMP 218
Cdd:PHA02874 188 NNGESP 193
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 53-207 2.48e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 62.32  E-value: 2.48e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  53 AMTIGDVSLVQELLDSGISVDSTF-QYGWTPLMYAASVANAELVRVLLDRGANASFEK-DKQSILITACSAHGseeliLK 130
Cdd:PHA02875  75 AVEEGDVKAVEELLDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNtDKFSPLHLAVMMGD-----IK 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118572911 131 CVELLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENG-YTALTWAARQGHKNIVLKLLELGAN 207
Cdd:PHA02875 150 GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGAD 227
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 65-207 2.65e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 59.69  E-value: 2.65e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  65 LLDSGISVDSTFQYGWTPLMYAASVAN-AELVRVLLDRGA--NASFEKDKQSILITACSAHGSEElilkcVELLLSRNAD 141
Cdd:PHA02876 259 LYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGAdvNAKNIKGETPLYLMAKNGYDTEN-----IRTLIMLGAD 333

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118572911 142 PNVACRRLMTPIMYAAR-DGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGAN 207
Cdd:PHA02876 334 VNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 53-207 3.07e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 58.85  E-value: 3.07e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  53 AMTIGDVSLVQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDRGANASFEK-DKQSILITAC---SAHGSEEL- 127
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAIPDVKYpDIESELHDAVeegDVKAVEELl 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911 128 ----------------------ILKCVE---LLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENG 182
Cdd:PHA02875  89 dlgkfaddvfykdgmtplhlatILKKLDimkLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCG 168

                        170       180
                 ....*....|....*....|....*
gi 118572911 183 YTALTWAARQGHKNIVLKLLELGAN 207
Cdd:PHA02875 169 CTPLIIAMAKGDIAICKMLLDSGAN 193
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 141-235 4.33e-09

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 58.76  E-value: 4.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911 141 DPNVAcRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKMLQTKDGKMPSE 220
Cdd:PTZ00322  75 DPVVA-HMLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153

                         90
                 ....*....|....*
gi 118572911 221 IAKRNKHHEIFNLLS 235
Cdd:PTZ00322 154 LAEENGFREVVQLLS 168
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 53-255 7.75e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 57.96  E-value: 7.75e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  53 AMTIGDVSLVQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDRGANASFeKDKQ--SILITACSA-HGSEELIL 129
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI-RDANgnTALWNAISAkHHKIFRIL 610

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911 130 kcveLLLSRNADPNVACRRLMTpimyAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKM 209
Cdd:PLN03192 611 ----YHFASISDPHAAGDLLCT----AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVD 682

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 118572911 210 LQTKDGKMPSE-----IAKRNKHHEIFNLLSFTLNPLEGKLQQLTKEDTIC 255
Cdd:PLN03192 683 KANTDDDFSPTelrelLQKRELGHSITIVDSVPADEPDLGRDGGSRPGRLQ 733
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 61-218 2.25e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 56.13  E-value: 2.25e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  61 LVQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDRGANASFEKDKQSILITACSAHGSEELIlkcvELLLSRNA 140
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDII----KLLLEKGA 181

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118572911 141 DPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARqgHKNIVLKLLELGANKMLQTKDGKMP 218
Cdd:PHA02874 182 YANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTP 257
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 57-234 3.69e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 55.35  E-value: 3.69e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  57 GDVSLVQELLDS-----GISVDSTFqygwTPLMYAASVANAELVRVLLDRGANASFEKDK-QSILITACSAHGSeelilK 130
Cdd:PHA02874  12 GDIEAIEKIIKNkgnciNISVDETT----TPLIDAIRSGDAKIVELFIKHGADINHINTKiPHPLLTAIKIGAH-----D 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911 131 CVELLLSRNADPNVacrrLMTPimyaarDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKML 210
Cdd:PHA02874  83 IIKLLIDNGVDTSI----LPIP------CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNI 152

                        170       180
                 ....*....|....*....|....
gi 118572911 211 QTKDGKMPSEIAKRNKHHEIFNLL 234
Cdd:PHA02874 153 EDDNGCYPIHIAIKHNFFDIIKLL 176
Ank_5 pfam13857
Ankyrin repeats (many copies);
134-186 4.10e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 49.65  E-value: 4.10e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 118572911  134 LLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTAL 186
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
Ank_5 pfam13857
Ankyrin repeats (many copies);
168-222 9.25e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.50  E-value: 9.25e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 118572911  168 LVAHG-AEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKMLQTKDGKMPSEIA 222
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 53-154 1.19e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 53.84  E-value: 1.19e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  53 AMTIGDVSLVQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDRGANASFeKDKQSILITACSAHGSEELILkcV 132
Cdd:PHA02875 142 AVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDY-FGKNGCVAALCYAIENNKIDI--V 218

                         90       100
                 ....*....|....*....|..
gi 118572911 133 ELLLSRNADPNVacrrlMTPIM 154
Cdd:PHA02875 219 RLFIKRGADCNI-----MFMIE 235
PHA03095 PHA03095
ankyrin-like protein; Provisional
 87-207 1.98e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.10  E-value: 1.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  87 ASVANAELVRVLLDRGANASFEKDKQSILITACsAHGSEELILKCVELLLSRNADPNVACRRLMTPIMYAARDGHT-QVV 165
Cdd:PHA03095  22 ASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLY-LHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVI 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 118572911 166 ALLVAHGAEVNTQDENGYTAL-TWAARQG-HKNIVLKLLELGAN 207
Cdd:PHA03095 101 KLLIKAGADVNAKDKVGRTPLhVYLSGFNiNPKVIRLLLRKGAD 144
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 278-332 2.60e-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: 2.60e-07
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 118572911 278 DLEVFLHGLGLEHMTDLLKERDITLRHLLTMREDEFTKNGITSK-DQQKILAALKE 332
Cdd:cd09487    1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPgHRKKILRAIQR 56
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 58-234 8.22e-07

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 51.42  E-value: 8.22e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  58 DVSLVQELLDSGISVDSTFQYGWTPLMYAASVAN----AELVR----------------------------VLLDRgana 105
Cdd:PHA02878  49 NLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNklgmKEMIRsinkcsvfytlvaikdafnnrnveifkiILTNR---- 124

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911 106 sFEKDKQSILITACSAHGSEELILKCVELLLSRNADPNVACR-RLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYT 184
Cdd:PHA02878 125 -YKNIQTIDLVYIDKKSKDDIIEAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNS 203

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|.
gi 118572911 185 ALTWAARQGHKNIVLKLLELGANKMLQTKDGKMPSEIA-KRNKHHEIFNLL 234
Cdd:PHA02878 204 PLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLL 254
PHA03095 PHA03095
ankyrin-like protein; Provisional
 58-204 1.79e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 50.02  E-value: 1.79e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  58 DVSLVQELLDSGISVDSTFQYGWTPL---MYAASVANAELVRVLLDRGANASfekdkqsiLITACSA--------HGSEE 126
Cdd:PHA03095  26 TVEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVN--------APERCGFtplhlylyNATTL 97

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911 127 LILKcveLLLSRNADPNVACRRLMTPI-MYAARDG-HTQVVALLVAHGAEVNTQDENGYTALtwAARQGHKNIVLKLLEL 204
Cdd:PHA03095  98 DVIK---LLIKAGADVNAKDKVGRTPLhVYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSRNANVELLRL 172
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 57-169 3.65e-06

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: 49.24  E-value: 3.65e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  57 GDVSLVQELLDSGISV--------------DSTFQYGWTPLMYAASVANAELVRVLLDRGANA----SFEKDKQSILITA 118
Cdd:cd22192  100 QNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIraqdSLGNTVLHILVLQ 179

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 118572911 119 CSAHGSEELIlkcvELLLSRNADPNVAC------RRLMTPIMYAARDGHTQVVALLV 169
Cdd:cd22192  180 PNKTFACQMY----DLILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQHLV 232
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 58-234 3.92e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.29  E-value: 3.92e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  58 DVSLVQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDRGAN-------------------------------AS 106
Cdd:PHA02876 157 ELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADvniialddlsvlecavdsknidtikaiidnrSN 236

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911 107 FEKDKQSILITACSAHGSEELIL----------------------------KCVELLLSRNADPNVACRRLMTPIMYAAR 158
Cdd:PHA02876 237 INKNDLSLLKAIRNEDLETSLLLydagfsvnsiddckntplhhasqapslsRLVPKLLERGADVNAKNIKGETPLYLMAK 316

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118572911 159 DGH-TQVVALLVAHGAEVNTQDENGYTALTWAAR-QGHKNIVLKLLELGANKMLQTKDGKMPSEIAKRNKHHEIFNLL 234
Cdd:PHA02876 317 NGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 61-218 2.21e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 46.88  E-value: 2.21e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  61 LVQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDRGANASFE-KDKQSILITACSAHGSeelilkCVELLLSrN 139
Cdd:PHA02874 172 IIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKcKNGFTPLHNAIIHNRS------AIELLIN-N 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911 140 ADPNVACRRLMTPIMYAAR-DGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKllELGANKMLQTKDGKMP 218
Cdd:PHA02874 245 ASINDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIK--DIIANAVLIKEADKLK 322
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 61-199 2.41e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.98  E-value: 2.41e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  61 LVQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDRGANasFEKDKQSI-LITACSAHGSEELIlkCVELLLSRN 139
Cdd:PHA02876 357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD--IEALSQKIgTALHFALCGTNPYM--SVKTLIDRG 432

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 118572911 140 ADPNVACRRLMTPIMYAARDG-HTQVVALLVAHGAEVNTQD-ENGYTALTWAARQGHKNIVL 199
Cdd:PHA02876 433 ANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINiQNQYPLLIALEYHGIVNILL 494
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 102-189 3.27e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 46.60  E-value: 3.27e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911 102 GANASFEKDKQSILITACSAHGSEELILKCVELLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDEN 181
Cdd:PHA02876 131 GNDIHYDKINESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD 210


                 ....*...
gi 118572911 182 GYTALTWA 189
Cdd:PHA02876 211 DLSVLECA 218
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 282-333 5.76e-05

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: 41.10  E-value: 5.76e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 118572911  282 FLHGLGLEHMTDLLKERDITLRHLLTMREDEFTKNGITSK-DQQKILAALKEL 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 1.42e-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: 38.72  E-value: 1.42e-04
                           10        20
                   ....*....|....*....|....*..
gi 118572911    78 YGWTPLMYAASVANAELVRVLLDRGAN 104
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 78-104 2.92e-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: 38.01  E-value: 2.92e-04
                          10        20
                  ....*....|....*....|....*..
gi 118572911   78 YGWTPLMYAASVANAELVRVLLDRGAN 104
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 150-180 3.55e-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: 38.04  E-value: 3.55e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 118572911  150 MTPIMYAA-RDGHTQVVALLVAHGAEVNTQDE 180
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
Ank_4 pfam13637
Ankyrin repeats (many copies);
57-99 5.09e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 5.09e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 118572911   57 GDVSLVQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLL 99
Cdd:pfam13637  12 GHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 139-234 7.09e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 7.09e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911 139 NADPNVACRrlmtpIMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKMLQTKDGKMP 218
Cdd:PLN03192 520 HDDPNMASN-----LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTA 594

                         90
                 ....*....|....*.
gi 118572911 219 SEIAKRNKHHEIFNLL 234
Cdd:PLN03192 595 LWNAISAKHHKIFRIL 610
SAM_ANKS3 cd09519
SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a ...
 273-319 7.65e-04

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: 37.86  E-value: 7.65e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 118572911 273 YTAFGDLEVFLHGLGLEHMTDLLKERDITLRHLLTMREDEFTKNGIT 319
Cdd:cd09519    1 YTGPKDLSELLEQIGCSKYLPIFEEQDIDLRIFLTLTESDLKEIGIT 47
Ank_4 pfam13637
Ankyrin repeats (many copies);
115-169 1.26e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 1.26e-03
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*
gi 118572911  115 LITACSAHGSEElilkCVELLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLV 169
Cdd:pfam13637   4 ALHAAAASGHLE----LLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 181-207 1.28e-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: 1.28e-03
                           10        20
                   ....*....|....*....|....*..
gi 118572911   181 NGYTALTWAARQGHKNIVLKLLELGAN 207
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 78-104 1.41e-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: 1.41e-03
                          10        20
                  ....*....|....*....|....*...
gi 118572911   78 YGWTPLMYAA-SVANAELVRVLLDRGAN 104
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGAD 28
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 150-176 3.24e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 34.87  E-value: 3.24e-03
                           10        20
                   ....*....|....*....|....*..
gi 118572911   150 MTPIMYAARDGHTQVVALLVAHGAEVN 176
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADIN 29
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 81-158 4.03e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 39.20  E-value: 4.03e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118572911  81 TPLMYAASVANAELVRVLLDRGANASFEKDKQSILITACSA-HGSeeliLKCVELLLSRNADPNVACRRLMTPIMYAAR 158
Cdd:PHA02884  72 NPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYISVlHGC----LKCLEILLSYGADINIQTNDMVTPIELALM 146
PHA02946 PHA02946
ankyin-like protein; Provisional
 58-262 4.04e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 39.65  E-value: 4.04e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  58 DVSLVQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDRGA--NASFEKDKQSILITAcsahGSEELILKCVELL 135
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGAdpNACDKQHKTPLYYLS----GTDDEVIERINLL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911 136 LSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTAL--TWAARQGHKNIVLKLLELGANKMLQTK 213
Cdd:PHA02946 127 VQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDH 206

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118572911 214 DGKMPSEI--AKRNKHHEIFNLL----------SFTLNPLEGKLQQLTKEDTICKILTTDS 262
Cdd:PHA02946 207 DGNTPLHIvcSKTVKNVDIINLLlpstdvnkqnKFGDSPLTLLIKTLSPAHLINKLLSTSN 267
Ank_5 pfam13857
Ankyrin repeats (many copies);
65-105 4.71e-03

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 35.40  E-value: 4.71e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|..
gi 118572911   65 LLDSG-ISVDSTFQYGWTPLMYAASVANAELVRVLLDRGANA 105
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDL 42
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 95-182 6.41e-03

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 39.11  E-value: 6.41e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  95 VRVLLDRGANA-SFEKDKQSILITACsAHGSeeliLKCVELLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHGA 173
Cdd:PTZ00322  98 ARILLTGGADPnCRDYDGRTPLHIAC-ANGH----VQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172


                 ....*....
gi 118572911 174 EVNTQDENG 182
Cdd:PTZ00322 173 CHFELGANA 181
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 150-177 6.91e-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: 34.16  E-value: 6.91e-03
                          10        20
                  ....*....|....*....|....*...
gi 118572911  150 MTPIMYAARDGHTQVVALLVAHGAEVNT 177
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 110-224 8.26e-03

ankyrin repeat protein; Provisional


Pssm-ID: 165212 [Multi-domain]  Cd Length: 300  Bit Score: 38.04  E-value: 8.26e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911 110 DKQSILITACSAHGSEelilkCVELLLSRNADPNV----ACRRLMTPIMYAARDGHTQVVALLVAHGAEVNT-QDENGYT 184
Cdd:PHA02884  32 CIANILYSSIKFHYTD-----IIDAILKLGADPEApfplSENSKTNPLIYAIDCDNDDAAKLLIRYGADVNRyAEEAKIT 106

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|
gi 118572911 185 ALTWAARQGHKNIVLKLLELGANKMLQTKDGKMPSEIAKR 224
Cdd:PHA02884 107 PLYISVLHGCLKCLEILLSYGADINIQTNDMVTPIELALM 146
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 58-234 9.08e-03

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 38.32  E-value: 9.08e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911  58 DVSLVQELLDSGISVD-STFQYGWTPLMYAASVANAELVRVLLDRGANA-SFEKDKQSILITACSaHGSEelilKCVELL 135
Cdd:PHA02878 146 EAEITKLLLSYGADINmKDRHKGNTALHYATENKDQRLTELLLSYGANVnIPDKTNNSPLHHAVK-HYNK----PIVHIL 220

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572911 136 LSRNADPNVACRRLMTPIMYA-ARDGHTQVVALLVAHGAEVNTQDE-NGYTALTWAARQGHKnivLK-LLELGANKMLQT 212
Cdd:PHA02878 221 LENGASTDARDKCGNTPLHISvGYCKDYDILKLLLEHGVDVNAKSYiLGLTALHSSIKSERK---LKlLLEYGADINSLN 297

                        170       180
                 ....*....|....*....|...
gi 118572911 213 KDGKMP-SEIAKRNKHHEIFNLL 234
Cdd:PHA02878 298 SYKLTPlSSAVKQYLCINIGRIL 320
 
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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