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Conserved domains on  [gi|118572908|sp|Q07DY6|]
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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 4.22e-39

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.17  E-value: 4.22e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  53 AMTIGDVSLIQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDSGA--NASfEKDKQTILITACsARGSEEqilk 130
Cdd:COG0666   94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAdvNAQ-DNDGNTPLHLAA-ANGNLE---- 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908 131 CVELLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKML 210
Cdd:COG0666  168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 118572908 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 1.61e-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: 90.42  E-value: 1.61e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118572908 272 SYTAFGDLEVFLHGIGLEHLTDLLKERDITLRHLLTMREDEFTKNGITSE-DQQKILATLKELQ 334
Cdd:cd09521    1 SYSKLDDLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQPgDQKKILDAIKEVH 64
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-250 4.22e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.17  E-value: 4.22e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  53 AMTIGDVSLIQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDSGA--NASfEKDKQTILITACsARGSEEqilk 130
Cdd:COG0666   94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAdvNAQ-DNDGNTPLHLAA-ANGNLE---- 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908 131 CVELLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKML 210
Cdd:COG0666  168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 118572908 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 1.61e-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: 90.42  E-value: 1.61e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118572908 272 SYTAFGDLEVFLHGIGLEHLTDLLKERDITLRHLLTMREDEFTKNGITSE-DQQKILATLKELQ 334
Cdd:cd09521    1 SYSKLDDLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQPgDQKKILDAIKEVH 64
Ank_2 pfam12796
Ankyrin repeats (3 copies);
129-211 3.78e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 3.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  129 LKCVELLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHgAEVNTQDeNGYTALTWAARQGHKNIVLKLLELGANK 208
Cdd:pfam12796  10 LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADI 87


                  ...
gi 118572908  209 MLQ 211
Cdd:pfam12796  88 NVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 65-281 9.60e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.02  E-value: 9.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  65 LLDSGISVDSTFQYGWTPLMYAASV-----ANAELVRVLLDSGANASFEKDKQT--ILITACSARGSeeqiLKCVELLLS 137
Cdd:PHA03100  54 LLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGItpLLYAISKKSNS----YSIVEYLLD 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908 138 RNADPNVACRRLMTPIMYAARDGH--TQVVALLVAHGAEVN----------------TQDENGYTALTWAARQGHKNIVL 199
Cdd:PHA03100 130 NGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINaknrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFVK 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908 200 KLLELGANKMLQTKDGKMPSEIAKRNKHHEIFNLLS---------------FTLNPLEGKLQQLTKEDTICKILTTDSDR 264
Cdd:PHA03100 210 YLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLnngpsiktiietllyFKDKDLNTITKIKMLKKSIMYMFLLDPGF 289

                        250
                 ....*....|....*...
gi 118572908 265 EKDH-IFSSYTAFGDLEV 281
Cdd:PHA03100 290 YKNRkLIENSKSLKDVIN 307
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 57-169 6.89e-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: 45.39  E-value: 6.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  57 GDVSLIQELLDSGISV--------------DSTFQYGWTPLMYAASVANAELVRVLLDSGANA----SFEKDKQTILITA 118
Cdd:cd22192  100 QNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIraqdSLGNTVLHILVLQ 179

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 118572908 119 CSARGSEEQIlkcvELLLSRNADPNVAC------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 9.41e-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: 40.33  E-value: 9.41e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 118572908  282 FLHGIGLEHLTDLLKERDITLRHLLTMREDEFTKNGITSE-DQQKILATLKEL 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 2.17e-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: 2.17e-04
                           10        20
                   ....*....|....*....|....*..
gi 118572908    78 YGWTPLMYAASVANAELVRVLLDSGAN 104
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-250 4.22e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.17  E-value: 4.22e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  53 AMTIGDVSLIQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDSGA--NASfEKDKQTILITACsARGSEEqilk 130
Cdd:COG0666   94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGAdvNAQ-DNDGNTPLHLAA-ANGNLE---- 167

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908 131 CVELLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKML 210
Cdd:COG0666  168 IVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNA 247

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|
gi 118572908 211 QTKDGKMPSEIAKRNKHHEIFNLLSFTLNPLEGKLQQLTK 250
Cdd:COG0666  248 KDKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-234 4.54e-39

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 143.17  E-value: 4.54e-39
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  53 AMTIGDVSLIQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDSGAN-ASFEKDKQTILITACsARGSEEqilkC 131
Cdd:COG0666   61 AALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADvNARDKDGETPLHLAA-YNGNLE----I 135

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908 132 VELLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKMLQ 211
Cdd:COG0666  136 VKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAK 215

                        170       180
                 ....*....|....*....|...
gi 118572908 212 TKDGKMPSEIAKRNKHHEIFNLL 234
Cdd:COG0666  216 DNDGKTALDLAAENGNLEIVKLL 238
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 272-334 1.61e-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: 90.42  E-value: 1.61e-22
                         10        20        30        40        50        60
                 ....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118572908 272 SYTAFGDLEVFLHGIGLEHLTDLLKERDITLRHLLTMREDEFTKNGITSE-DQQKILATLKELQ 334
Cdd:cd09521    1 SYSKLDDLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQPgDQKKILDAIKEVH 64
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
59-234 1.31e-20

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 91.94  E-value: 1.31e-20
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  59 VSLIQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDSGANASFEKDKQTILITACSARGSEEQILkcveLLLSR 138
Cdd:COG0666    1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVAL----LLLAA 76

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908 139 NADPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKMLQTKDGKMP 218
Cdd:COG0666   77 GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP 156

                        170
                 ....*....|....*.
gi 118572908 219 SEIAKRNKHHEIFNLL 234
Cdd:COG0666  157 LHLAAANGNLEIVKLL 172
Ank_2 pfam12796
Ankyrin repeats (3 copies);
129-211 3.78e-18

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 79.00  E-value: 3.78e-18
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  129 LKCVELLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHgAEVNTQDeNGYTALTWAARQGHKNIVLKLLELGANK 208
Cdd:pfam12796  10 LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADI 87


                  ...
gi 118572908  209 MLQ 211
Cdd:pfam12796  88 NVK 90
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 65-281 9.60e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 82.02  E-value: 9.60e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  65 LLDSGISVDSTFQYGWTPLMYAASV-----ANAELVRVLLDSGANASFEKDKQT--ILITACSARGSeeqiLKCVELLLS 137
Cdd:PHA03100  54 LLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGItpLLYAISKKSNS----YSIVEYLLD 129

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908 138 RNADPNVACRRLMTPIMYAARDGH--TQVVALLVAHGAEVN----------------TQDENGYTALTWAARQGHKNIVL 199
Cdd:PHA03100 130 NGANVNIKNSDGENLLHLYLESNKidLKILKLLIDKGVDINaknrvnyllsygvpinIKDVYGFTPLHYAVYNNNPEFVK 209

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908 200 KLLELGANKMLQTKDGKMPSEIAKRNKHHEIFNLLS---------------FTLNPLEGKLQQLTKEDTICKILTTDSDR 264
Cdd:PHA03100 210 YLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLLLnngpsiktiietllyFKDKDLNTITKIKMLKKSIMYMFLLDPGF 289

                        250
                 ....*....|....*...
gi 118572908 265 EKDH-IFSSYTAFGDLEV 281
Cdd:PHA03100 290 YKNRkLIENSKSLKDVIN 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
83-179 8.97e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 72.46  E-value: 8.97e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908   83 LMYAASVANAELVRVLLDSGANASF-EKDKQTILITACSaRGSEEqilkCVELLLSrNADPNVACRRlMTPIMYAARDGH 161
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLqDKNGRTALHLAAK-NGHLE----IVKLLLE-HADVNLKDNG-RTALHYAARSGH 73

                          90
                  ....*....|....*...
gi 118572908  162 TQVVALLVAHGAEVNTQD 179
Cdd:pfam12796  74 LEIVKLLLEKGADINVKD 91
PHA03095 PHA03095
ankyrin-like protein; Provisional
 58-232 2.03e-14

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 75.06  E-value: 2.03e-14
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  58 DVSLIQELLDSGISVDSTFQYGWTPL-MYAASV-ANAELVRVLLDSGANAsFEKD--KQTIL-ITACSARGSEeqilKCV 132
Cdd:PHA03095 131 NPKVIRLLLRKGADVNALDLYGMTPLaVLLKSRnANVELLRLLIDAGADV-YAVDdrFRSLLhHHLQSFKPRA----RIV 205

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908 133 ELLLSRNADPNVACRRLMTPIMYAARDGHTQ--VVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKML 210
Cdd:PHA03095 206 RELIRAGCDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINA 285

                        170       180
                 ....*....|....*....|..
gi 118572908 211 QTKDGKMPSEIAKRNKHHEIFN 232
Cdd:PHA03095 286 VSSDGNTPLSLMVRNNNGRAVR 307
Ank_2 pfam12796
Ankyrin repeats (3 copies);
57-144 1.98e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 65.91  E-value: 1.98e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908   57 GDVSLIQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDSgANASFEKDKQTILITACSARgseeqILKCVELLL 136
Cdd:pfam12796   8 GNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSG-----HLEIVKLLL 81


                  ....*...
gi 118572908  137 SRNADPNV 144
Cdd:pfam12796  82 EKGADINV 89
Ank_2 pfam12796
Ankyrin repeats (3 copies);
153-234 1.92e-12

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 62.83  E-value: 1.92e-12
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  153 IMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKMlqTKDGKMPSEIAKRNKHHEIFN 232
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78


                  ..
gi 118572908  233 LL 234
Cdd:pfam12796  79 LL 80
Ank_4 pfam13637
Ankyrin repeats (many copies);
150-202 5.92e-12

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 60.37  E-value: 5.92e-12
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 118572908  150 MTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLL 202
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 53-218 2.21e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 62.29  E-value: 2.21e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  53 AMTIGDVSLIQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDSGANASfekdkqtILITACSARGSEEQILKCv 132
Cdd:PHA02874  42 AIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTS-------ILPIPCIEKDMIKTILDC- 113

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908 133 elllsrNADPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKMLQT 212
Cdd:PHA02874 114 ------GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKD 187


                 ....*.
gi 118572908 213 KDGKMP 218
Cdd:PHA02874 188 NNGESP 193
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 53-207 4.29e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.55  E-value: 4.29e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  53 AMTIGDVSLIQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVL---------------------------------L 99
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLmkhgaipdvkypdieselhdaveegdvkaveelL 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908 100 DSG--ANASFEKDKQTILITAcsargSEEQILKCVELLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNT 177
Cdd:PHA02875  89 DLGkfADDVFYKDGMTPLHLA-----TILKKLDIMKLLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163

                        170       180       190
                 ....*....|....*....|....*....|
gi 118572908 178 QDENGYTALTWAARQGHKNIVLKLLELGAN 207
Cdd:PHA02875 164 EDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 53-207 1.42e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 60.00  E-value: 1.42e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  53 AMTIGDVSLIQELLDSGISVDSTF-QYGWTPLMYAASVANAELVRVLLDSGANASFEK-DKQTILITACSARGseeqiLK 130
Cdd:PHA02875  75 AVEEGDVKAVEELLDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIPNtDKFSPLHLAVMMGD-----IK 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118572908 131 CVELLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENG-YTALTWAARQGHKNIVLKLLELGAN 207
Cdd:PHA02875 150 GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGAD 227
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 57-234 3.60e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 58.82  E-value: 3.60e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  57 GDVSLIQELLDS-----GISVDSTFqygwTPLMYAASVANAELVRVLLDSGANASFEKDK-QTILITACSARGSeeqilK 130
Cdd:PHA02874  12 GDIEAIEKIIKNkgnciNISVDETT----TPLIDAIRSGDAKIVELFIKHGADINHINTKiPHPLLTAIKIGAH-----D 82

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908 131 CVELLLSRNADPNVacrrLMTPimyaarDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKML 210
Cdd:PHA02874  83 IIKLLIDNGVDTSI----LPIP------CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNI 152

                        170       180
                 ....*....|....*....|....
gi 118572908 211 QTKDGKMPSEIAKRNKHHEIFNLL 234
Cdd:PHA02874 153 EDDNGCYPIHIAIKHNFFDIIKLL 176
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 118572908 141 DPNVAcRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKMLQTKDGKMPSE 220
Cdd:PTZ00322  75 DPVVA-HMLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153

                         90
                 ....*....|....*
gi 118572908 221 IAKRNKHHEIFNLLS 235
Cdd:PTZ00322 154 LAEENGFREVVQLLS 168
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 53-255 4.72e-09

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 58.73  E-value: 4.72e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  53 AMTIGDVSLIQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDSGANASFeKDKQ--TILITACSARgsEEQILK 130
Cdd:PLN03192 532 VASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHI-RDANgnTALWNAISAK--HHKIFR 608

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908 131 cVELLLSRNADPNVACRRLMTpimyAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKML 210
Cdd:PLN03192 609 -ILYHFASISDPHAAGDLLCT----AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGADVDK 683

                        170       180       190       200       210
                 ....*....|....*....|....*....|....*....|....*....|
gi 118572908 211 QTKDGKMPSE-----IAKRNKHHEIFNLLSFTLNPLEGKLQQLTKEDTIC 255
Cdd:PLN03192 684 ANTDDDFSPTelrelLQKRELGHSITIVDSVPADEPDLGRDGGSRPGRLQ 733
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 53-154 6.92e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 57.69  E-value: 6.92e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  53 AMTIGDVSLIQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDSGANASFeKDKQTILITACSArgSEEQILKCV 132
Cdd:PHA02875 142 AVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDY-FGKNGCVAALCYA--IENNKIDIV 218

                         90       100
                 ....*....|....*....|..
gi 118572908 133 ELLLSRNADPNVacrrlMTPIM 154
Cdd:PHA02875 219 RLFIKRGADCNI-----MFMIE 235
Ank_5 pfam13857
Ankyrin repeats (many copies);
134-186 3.21e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.04  E-value: 3.21e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 118572908  134 LLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTAL 186
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 65-207 7.45e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 55.07  E-value: 7.45e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  65 LLDSGISVDSTFQYGWTPLMYAASVAN-AELVRVLLDSGA--NASFEKDKQTILITACSARGSEEqilkcVELLLSRNAD 141
Cdd:PHA02876 259 LYDAGFSVNSIDDCKNTPLHHASQAPSlSRLVPKLLERGAdvNAKNIKGETPLYLMAKNGYDTEN-----IRTLIMLGAD 333

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 118572908 142 PNVACRRLMTPIMYAAR-DGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGAN 207
Cdd:PHA02876 334 VNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGAD 400
Ank_5 pfam13857
Ankyrin repeats (many copies);
168-222 7.53e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 48.88  E-value: 7.53e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 118572908  168 LVAHG-AEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKMLQTKDGKMPSEIA 222
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA03095 PHA03095
ankyrin-like protein; Provisional
 87-207 4.05e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 52.33  E-value: 4.05e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  87 ASVANAELVRVLLDSGANASFEKDKQTILITACsARGSEEQILKCVELLLSRNADPNVACRRLMTPIMYAARDGHT-QVV 165
Cdd:PHA03095  22 ASNVTVEEVRRLLAAGADVNFRGEYGKTPLHLY-LHYSSEKVKDIVRLLLEAGADVNAPERCGFTPLHLYLYNATTlDVI 100

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|....
gi 118572908 166 ALLVAHGAEVNTQDENGYTAL-TWAARQG-HKNIVLKLLELGAN 207
Cdd:PHA03095 101 KLLIKAGADVNAKDKVGRTPLhVYLSGFNiNPKVIRLLLRKGAD 144
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 61-218 8.87e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 51.12  E-value: 8.87e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  61 LIQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDSGANASFEKDKQTILITACSARGSEEQIlkcvELLLSRNA 140
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDII----KLLLEKGA 181

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118572908 141 DPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARqgHKNIVLKLLELGANKMLQTKDGKMP 218
Cdd:PHA02874 182 YANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTP 257
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 278-332 1.11e-06

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: 45.69  E-value: 1.11e-06
                         10        20        30        40        50
                 ....*....|....*....|....*....|....*....|....*....|....*.
gi 118572908 278 DLEVFLHGIGLEHLTDLLKERDITLRHLLTMREDEFTKNGITSE-DQQKILATLKE 332
Cdd:cd09487    1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPgHRKKILRAIQR 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 58-234 2.39e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 50.06  E-value: 2.39e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  58 DVSLIQE-LLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDSGANASF--------------EKDKQTI-------- 114
Cdd:PHA02876 156 DELLIAEmLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIialddlsvlecavdSKNIDTIkaiidnrs 235

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908 115 --------LITACSARGSEEQIL-----------------------------KCVELLLSRNADPNVACRRLMTPIMYAA 157
Cdd:PHA02876 236 ninkndlsLLKAIRNEDLETSLLlydagfsvnsiddckntplhhasqapslsRLVPKLLERGADVNAKNIKGETPLYLMA 315

                        170       180       190       200       210       220       230
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 118572908 158 RDGH-TQVVALLVAHGAEVNTQDENGYTALTWAAR-QGHKNIVLKLLELGANKMLQTKDGKMPSEIAKRNKHHEIFNLL 234
Cdd:PHA02876 316 KNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTL 394
PHA03095 PHA03095
ankyrin-like protein; Provisional
 58-204 3.11e-06

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 49.64  E-value: 3.11e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  58 DVSLIQELLDSGISVDSTFQYGWTPL---MYAASVANAELVRVLLDSGANA-SFEKDKQTILIT-ACSArgSEEQILKcv 132
Cdd:PHA03095  26 TVEEVRRLLAAGADVNFRGEYGKTPLhlyLHYSSEKVKDIVRLLLEAGADVnAPERCGFTPLHLyLYNA--TTLDVIK-- 101

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 118572908 133 eLLLSRNADPNVACRRLMTPI-MYAARDG-HTQVVALLVAHGAEVNTQDENGYTALtwAARQGHKNIVLKLLEL 204
Cdd:PHA03095 102 -LLIKAGADVNAKDKVGRTPLhVYLSGFNiNPKVIRLLLRKGADVNALDLYGMTPL--AVLLKSRNANVELLRL 172
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 61-218 4.53e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.81  E-value: 4.53e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  61 LIQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDSGANASFE-KDKQTILITACSARGSeeqilkCVELLLSrN 139
Cdd:PHA02874 172 IIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKcKNGFTPLHNAIIHNRS------AIELLIN-N 244

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908 140 ADPNVACRRLMTPIMYAAR-DGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKllELGANKMLQTKDGKMP 218
Cdd:PHA02874 245 ASINDQDIDGSTPLHHAINpPCDIDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIK--DIIANAVLIKEADKLK 322
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 58-234 4.93e-06

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 48.72  E-value: 4.93e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  58 DVSLIQELLDSGISVDSTFQYGWTPLMYAASVAN----AELVRVLL-DSGANA---------------------SFEKDK 111
Cdd:PHA02878  49 NLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNklgmKEMIRSINkCSVFYTlvaikdafnnrnveifkiiltNRYKNI 128

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908 112 QTILITACSARGSEEQI-LKCVELLLSRNADPNVACR-RLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWA 189
Cdd:PHA02878 129 QTIDLVYIDKKSKDDIIeAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKTNNSPLHHA 208

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|....*.
gi 118572908 190 ARQGHKNIVLKLLELGANKMLQTKDGKMPSEIA-KRNKHHEIFNLL 234
Cdd:PHA02878 209 VKHYNKPIVHILLENGASTDARDKCGNTPLHISvGYCKDYDILKLL 254
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 53-222 9.36e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.04  E-value: 9.36e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  53 AMTIGDVSLIQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDSGANASFEKDKQTILITACSARGSeeqiLKCV 132
Cdd:PHA02874 131 AIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVKDNNGESPLHNAAEYGD----YACI 206

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908 133 ELLLSRNADPNVACRRLMTPIMYAARdgHTQVVALLVAHGAEVNTQDENGYTALTWAARQG-HKNIVLKLLELGANKMLQ 211
Cdd:PHA02874 207 KLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILLYHKADISIK 284

                        170
                 ....*....|.
gi 118572908 212 TKDGKMPSEIA 222
Cdd:PHA02874 285 DNKGENPIDTA 295
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 101-189 9.98e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 48.14  E-value: 9.98e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908 101 SGANASFEKDKQTILITACSARGSEEQILKCVELLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDE 180
Cdd:PHA02876 130 SGNDIHYDKINESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIAL 209


                 ....*....
gi 118572908 181 NGYTALTWA 189
Cdd:PHA02876 210 DDLSVLECA 218
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 65-199 4.54e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 45.82  E-value: 4.54e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  65 LLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDSGAN-ASFEKDKQTILITACSARGSeeqiLKCVELLLSRNADPN 143
Cdd:PHA02876 361 LLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADiEALSQKIGTALHFALCGTNP----YMSVKTLIDRGANVN 436

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 118572908 144 VACRRLMTPIMYAARDG-HTQVVALLVAHGAEVNTQD-ENGYTALTWAARQGHKNIVL 199
Cdd:PHA02876 437 SKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINiQNQYPLLIALEYHGIVNILL 494
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 57-169 6.89e-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: 45.39  E-value: 6.89e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  57 GDVSLIQELLDSGISV--------------DSTFQYGWTPLMYAASVANAELVRVLLDSGANA----SFEKDKQTILITA 118
Cdd:cd22192  100 QNLNLVRELIARGADVvspratgtffrpgpKNLIYYGEHPLSFAACVGNEEIVRLLIEHGADIraqdSLGNTVLHILVLQ 179

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*..
gi 118572908 119 CSARGSEEQIlkcvELLLSRNADPNVAC------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 9.41e-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: 40.33  E-value: 9.41e-05
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 118572908  282 FLHGIGLEHLTDLLKERDITLRHLLTMREDEFTKNGITSE-DQQKILATLKEL 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 2.17e-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: 2.17e-04
                           10        20
                   ....*....|....*....|....*..
gi 118572908    78 YGWTPLMYAASVANAELVRVLLDSGAN 104
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 150-180 2.80e-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: 2.80e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 118572908  150 MTPIMYAA-RDGHTQVVALLVAHGAEVNTQDE 180
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
SAM_ANKS3 cd09519
SAM domain of ANKS3 subfamily; SAM (sterile alpha motif) domain of ANKS3 subfamily is a ...
 273-319 4.59e-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: 38.24  E-value: 4.59e-04
                         10        20        30        40
                 ....*....|....*....|....*....|....*....|....*..
gi 118572908 273 YTAFGDLEVFLHGIGLEHLTDLLKERDITLRHLLTMREDEFTKNGIT 319
Cdd:cd09519    1 YTGPKDLSELLEQIGCSKYLPIFEEQDIDLRIFLTLTESDLKEIGIT 47
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 95-182 4.98e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.58  E-value: 4.98e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  95 VRVLLDSGANA-SFEKDKQTILITACsARGSeeqiLKCVELLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHGA 173
Cdd:PTZ00322  98 ARILLTGGADPnCRDYDGRTPLHIAC-ANGH----VQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172


                 ....*....
gi 118572908 174 EVNTQDENG 182
Cdd:PTZ00322 173 CHFELGANA 181
Ank_4 pfam13637
Ankyrin repeats (many copies);
57-99 5.40e-04

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 38.02  E-value: 5.40e-04
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|...
gi 118572908   57 GDVSLIQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLL 99
Cdd:pfam13637  12 GHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 139-234 7.15e-04

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 42.16  E-value: 7.15e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908 139 NADPNVACRrlmtpIMYAARDGHTQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNIVLKLLELGANKMLQTKDGKMP 218
Cdd:PLN03192 520 HDDPNMASN-----LLTVASTGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTA 594

                         90
                 ....*....|....*.
gi 118572908 219 SEIAKRNKHHEIFNLL 234
Cdd:PLN03192 595 LWNAISAKHHKIFRIL 610
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 78-104 9.12e-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: 36.47  E-value: 9.12e-04
                          10        20
                  ....*....|....*....|....*..
gi 118572908   78 YGWTPLMYAASVANAELVRVLLDSGAN 104
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 181-207 1.15e-03

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


Pssm-ID: 197603 [Multi-domain]  Cd Length: 30  Bit Score: 36.41  E-value: 1.15e-03
                           10        20
                   ....*....|....*....|....*..
gi 118572908   181 NGYTALTWAARQGHKNIVLKLLELGAN 207
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank_4 pfam13637
Ankyrin repeats (many copies);
129-169 1.76e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.48  E-value: 1.76e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 118572908  129 LKCVELLLSRNADPNVACRRLMTPIMYAARDGHTQVVALLV 169
Cdd:pfam13637  14 LELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02946 PHA02946
ankyin-like protein; Provisional
 58-262 1.80e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 40.81  E-value: 1.80e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908  58 DVSLIQELLDSGISVDSTFQYGWTPLMYAASVANAELVRVLLDSGA--NASFEKDKQTILITAcsarGSEEQILKCVELL 135
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGAdpNACDKQHKTPLYYLS----GTDDEVIERINLL 126

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 118572908 136 LSRNADPNVACRRLMTPIMYAARDGHTQVVALLVAHGAEVNTQDENGYTAL--TWAARQGHKNIVLKLLELGANKMLQTK 213
Cdd:PHA02946 127 VQYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDH 206

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 118572908 214 DGKMPSEI--AKRNKHHEIFNLL----------SFTLNPLEGKLQQLTKEDTICKILTTDS 262
Cdd:PHA02946 207 DGNTPLHIvcSKTVKNVDIINLLlpstdvnkqnKFGDSPLTLLIKTLSPAHLINKLLSTSN 267
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 78-104 2.25e-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: 35.73  E-value: 2.25e-03
                          10        20
                  ....*....|....*....|....*...
gi 118572908   78 YGWTPLMYAA-SVANAELVRVLLDSGAN 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 2.96e-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: 35.26  E-value: 2.96e-03
                           10        20
                   ....*....|....*....|....*..
gi 118572908   150 MTPIMYAARDGHTQVVALLVAHGAEVN 176
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 150-177 6.33e-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: 6.33e-03
                          10        20
                  ....*....|....*....|....*...
gi 118572908  150 MTPIMYAARDGHTQVVALLVAHGAEVNT 177
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02884 PHA02884
ankyrin repeat protein; Provisional
 81-158 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
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 118572908  81 TPLMYAASVANAELVRVLLDSGANASFEKDKQTILITACSARGSEeqiLKCVELLLSRNADPNVACRRLMTPIMYAAR 158
Cdd:PHA02884  72 NPLIYAIDCDNDDAAKLLIRYGADVNRYAEEAKITPLYISVLHGC---LKCLEILLSYGADINIQTNDMVTPIELALM 146
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 181-207 9.95e-03

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 33.77  E-value: 9.95e-03
                          10        20
                  ....*....|....*....|....*..
gi 118572908  181 NGYTALTWAARQGHKNIVLKLLELGAN 207
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
 
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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