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Conserved domains on  [gi|90110652|sp|Q2QLH1|]
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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 1.19e-38

Ankyrin repeat [Signal transduction mechanisms];


:

Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.02  E-value: 1.19e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  53 ALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASVANVELVRVLLDRGANASF-DKDKQTILITACSARGLEeqilkC 131
Cdd:COG0666  94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAqDNDGNTPLHLAAANGNLE-----I 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652 132 VELLLSRNADPNVACRRLMTPIMYAARDGHPQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNVVLKLLELGANKMLQ 211
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 90110652 212 TKDGKIPSEIAKRNKHLEIFNFLSLTLNPLEGNLQQLTK 250
Cdd:COG0666 249 DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 272-333 1.10e-21

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: 88.11  E-value: 1.10e-21
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90110652 272 SYTAFGDLEIFLHGLGLEHMTDLLKEKDITLRHLLTMRKDEFTKNGIND-KDQQKILSALKEL 333
Cdd:cd09521   1 SYSKLDDLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQpGDQKKILDAIKEV 63
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-250 1.19e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.02  E-value: 1.19e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  53 ALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASVANVELVRVLLDRGANASF-DKDKQTILITACSARGLEeqilkC 131
Cdd:COG0666  94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAqDNDGNTPLHLAAANGNLE-----I 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652 132 VELLLSRNADPNVACRRLMTPIMYAARDGHPQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNVVLKLLELGANKMLQ 211
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 90110652 212 TKDGKIPSEIAKRNKHLEIFNFLSLTLNPLEGNLQQLTK 250
Cdd:COG0666 249 DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 272-333 1.10e-21

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: 88.11  E-value: 1.10e-21
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90110652 272 SYTAFGDLEIFLHGLGLEHMTDLLKEKDITLRHLLTMRKDEFTKNGIND-KDQQKILSALKEL 333
Cdd:cd09521   1 SYSKLDDLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQpGDQKKILDAIKEV 63
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 59-234 1.09e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 85.10  E-value: 1.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   59 ISLVQELLDSGISVDSSFRYGWTPLMYAASV-----ANVELVRVLLDRGANASFDKDKQT----ILITACSARgleeqiL 129
Cdd:PHA03100  48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGItpllYAISKKSNS------Y 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  130 KCVELLLSRNADPNVACRRLMTPIMYAARDGHP--QVVALLVAHGAEVN----------------TQDENGYTALTWAAR 191
Cdd:PHA03100 122 SIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINaknrvnyllsygvpinIKDVYGFTPLHYAVY 201

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 90110652  192 QGHKNVVLKLLELGANKMLQTKDGKIPSEIAKRNKHLEIFNFL 234
Cdd:PHA03100 202 NNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
129-211 3.20e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.69  E-value: 3.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   129 LKCVELLLSRNADPNVACRRLMTPIMYAARDGHPQVVALLVAHgAEVNTQDeNGYTALTWAARQGHKNVVLKLLELGANK 208
Cdd:pfam12796  10 LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADI 87


                  ...
gi 90110652   209 MLQ 211
Cdd:pfam12796  88 NVK 90
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
272-334 3.41e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 44.57  E-value: 3.41e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90110652   272 SYTAFGDLEIFLHGLGLEHMTDLLKEKDIT-LRHLLTMRKDEFTKNGINDK-DQQKILSALKELE 334
Cdd:pfam07647   2 ESWSLESVADWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLKRLGITSVgHRRKILKKIQELK 66
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 53-169 3.73e-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: 46.16  E-value: 3.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  53 ALTTGDISLVQELLDSGISVDSS------FR--------YGWTPLMYAASVANVELVRVLLDRGANA----SFDKDKQTI 114
Cdd:cd22192  96 AVVNQNLNLVRELIARGADVVSPratgtfFRpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIraqdSLGNTVLHI 175

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90110652 115 LITACSargleeQILKC--VELLLSRNADPNVAC------RRLMTPIMYAARDGHPQVVALLV 169
Cdd:cd22192 176 LVLQPN------KTFACqmYDLILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQHLV 232
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 78-104 1.07e-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: 39.11  E-value: 1.07e-04
                           10        20
                   ....*....|....*....|....*..
gi 90110652     78 YGWTPLMYAASVANVELVRVLLDRGAN 104
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
 
Name Accession Description Interval E-value
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
53-250 1.19e-38

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 142.02  E-value: 1.19e-38
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  53 ALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASVANVELVRVLLDRGANASF-DKDKQTILITACSARGLEeqilkC 131
Cdd:COG0666  94 AARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAqDNDGNTPLHLAAANGNLE-----I 168

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652 132 VELLLSRNADPNVACRRLMTPIMYAARDGHPQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNVVLKLLELGANKMLQ 211
Cdd:COG0666 169 VKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAGADVNAKDNDGKTALDLAAENGNLEIVKLLLEAGADLNAK 248

                       170       180       190
                ....*....|....*....|....*....|....*....
gi 90110652 212 TKDGKIPSEIAKRNKHLEIFNFLSLTLNPLEGNLQQLTK 250
Cdd:COG0666 249 DKDGLTALLLAAAAGAALIVKLLLLALLLLAAALLDLLT 287
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
47-234 1.26e-37

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 139.32  E-value: 1.26e-37
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  47 NETFKKALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASVANVELVRVLLDRGAN-ASFDKDKQTILITACSARGLE 125
Cdd:COG0666  55 ALLLLAAALAGDLLVALLLLAAGADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADvNARDKDGETPLHLAAYNGNLE 134

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652 126 eqilkCVELLLSRNADPNVACRRLMTPIMYAARDGHPQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNVVLKLLELG 205
Cdd:COG0666 135 -----IVKLLLEAGADVNAQDNDGNTPLHLAAANGNLEIVKLLLEAGADVNARDNDGETPLHLAAENGHLEIVKLLLEAG 209

                       170       180
                ....*....|....*....|....*....
gi 90110652 206 ANKMLQTKDGKIPSEIAKRNKHLEIFNFL 234
Cdd:COG0666 210 ADVNAKDNDGKTALDLAAENGNLEIVKLL 238
SAM_ASZ1 cd09521
SAM domain of ASZ1 subfamily; SAM (sterile alpha motif) domain of ASZ1 (Ankyrin, SAM, leucine ...
 272-333 1.10e-21

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: 88.11  E-value: 1.10e-21
                        10        20        30        40        50        60
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90110652 272 SYTAFGDLEIFLHGLGLEHMTDLLKEKDITLRHLLTMRKDEFTKNGIND-KDQQKILSALKEL 333
Cdd:cd09521   1 SYSKLDDLELFLHGLELGHLTPLFKEHDVTFSQLLKMTEEDLEKIGITQpGDQKKILDAIKEV 63
ANKYR COG0666
Ankyrin repeat [Signal transduction mechanisms];
59-234 1.43e-19

Ankyrin repeat [Signal transduction mechanisms];


Pssm-ID: 440430 [Multi-domain]  Cd Length: 289  Bit Score: 88.86  E-value: 1.43e-19
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  59 ISLVQELLDSGISVDSSFRYGWTPLMYAASVANVELVRVLLDRGANASFDKDKQTILITACSARGLEEQILkcveLLLSR 138
Cdd:COG0666   1 LLLLLLLLLLLLAALLLLLLLALLLLAAALLLLLLLLLLLLLALLALALADALGALLLLAAALAGDLLVAL----LLLAA 76

                        90       100       110       120       130       140       150       160
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652 139 NADPNVACRRLMTPIMYAARDGHPQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNVVLKLLELGANKMLQTKDGKIP 218
Cdd:COG0666  77 GADINAKDDGGNTLLHAAARNGDLEIVKLLLEAGADVNARDKDGETPLHLAAYNGNLEIVKLLLEAGADVNAQDNDGNTP 156

                       170
                ....*....|....*.
gi 90110652 219 SEIAKRNKHLEIFNFL 234
Cdd:COG0666 157 LHLAAANGNLEIVKLL 172
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 59-234 1.09e-17

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 85.10  E-value: 1.09e-17
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   59 ISLVQELLDSGISVDSSFRYGWTPLMYAASV-----ANVELVRVLLDRGANASFDKDKQT----ILITACSARgleeqiL 129
Cdd:PHA03100  48 IDVVKILLDNGADINSSTKNNSTPLHYLSNIkynltDVKEIVKLLLEYGANVNAPDNNGItpllYAISKKSNS------Y 121

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  130 KCVELLLSRNADPNVACRRLMTPIMYAARDGHP--QVVALLVAHGAEVN----------------TQDENGYTALTWAAR 191
Cdd:PHA03100 122 SIVEYLLDNGANVNIKNSDGENLLHLYLESNKIdlKILKLLIDKGVDINaknrvnyllsygvpinIKDVYGFTPLHYAVY 201

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|...
gi 90110652  192 QGHKNVVLKLLELGANKMLQTKDGKIPSEIAKRNKHLEIFNFL 234
Cdd:PHA03100 202 NNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEIFKLL 244
Ank_2 pfam12796
Ankyrin repeats (3 copies);
129-211 3.20e-17

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 76.69  E-value: 3.20e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   129 LKCVELLLSRNADPNVACRRLMTPIMYAARDGHPQVVALLVAHgAEVNTQDeNGYTALTWAARQGHKNVVLKLLELGANK 208
Cdd:pfam12796  10 LELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKD-NGRTALHYAARSGHLEIVKLLLEKGADI 87


                  ...
gi 90110652   209 MLQ 211
Cdd:pfam12796  88 NVK 90
Ank_2 pfam12796
Ankyrin repeats (3 copies);
83-179 3.99e-16

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 73.61  E-value: 3.99e-16
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652    83 LMYAASVANVELVRVLLDRGANASF-DKDKQTILITACSARGLEeqilkCVELLLSrNADPNVACRRlMTPIMYAARDGH 161
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLqDKNGRTALHLAAKNGHLE-----IVKLLLE-HADVNLKDNG-RTALHYAARSGH 73

                          90
                  ....*....|....*...
gi 90110652   162 PQVVALLVAHGAEVNTQD 179
Cdd:pfam12796  74 LEIVKLLLEKGADINVKD 91
Ank_2 pfam12796
Ankyrin repeats (3 copies);
57-144 1.55e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 66.29  E-value: 1.55e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652    57 GDISLVQELLDSGISVDSSFRYGWTPLMYAASVANVELVRVLLDRgANASFDKDKQTILITACSARGLEeqilkCVELLL 136
Cdd:pfam12796   8 GNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEH-ADVNLKDNGRTALHYAARSGHLE-----IVKLLL 81


                  ....*...
gi 90110652   137 SRNADPNV 144
Cdd:pfam12796  82 EKGADINV 89
PHA03100 PHA03100
ankyrin repeat protein; Provisional
 56-207 2.15e-13

ankyrin repeat protein; Provisional


Pssm-ID: 222984 [Multi-domain]  Cd Length: 422  Bit Score: 71.62  E-value: 2.15e-13
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   56 TGDISLVQELLDSGISVDSSFRYGWTPLMYAAS--VANVELVRVLLDRGANASFDKDKQTILITACSARGLEEqiLKCVE 133
Cdd:PHA03100  83 TDVKEIVKLLLEYGANVNAPDNNGITPLLYAISkkSNSYSIVEYLLDNGANVNIKNSDGENLLHLYLESNKID--LKILK 160

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  134 LLLSRNADPNVACR----------------RLMTPIMYAARDGHPQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNV 197
Cdd:PHA03100 161 LLIDKGVDINAKNRvnyllsygvpinikdvYGFTPLHYAVYNNNPEFVKYLLDLGANPNLVNKYGDTPLHIAILNNNKEI 240

                        170
                 ....*....|
gi 90110652  198 VLKLLELGAN 207
Cdd:PHA03100 241 FKLLLNNGPS 250
Ank_2 pfam12796
Ankyrin repeats (3 copies);
153-234 8.97e-13

Ankyrin repeats (3 copies);


Pssm-ID: 463710 [Multi-domain]  Cd Length: 91  Bit Score: 63.98  E-value: 8.97e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   153 IMYAARDGHPQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNVVLKLLELGANKMlqTKDGKIPSEIAKRNKHLEIFN 232
Cdd:pfam12796   1 LHLAAKNGNLELVKLLLENGADANLQDKNGRTALHLAAKNGHLEIVKLLLEHADVNL--KDNGRTALHYAARSGHLEIVK 78


                  ..
gi 90110652   233 FL 234
Cdd:pfam12796  79 LL 80
PHA03095 PHA03095
ankyrin-like protein; Provisional
 65-240 1.63e-12

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 69.28  E-value: 1.63e-12
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   65 LLDSGISVDSSFRYGWTPL-MYAASV-ANVELVRVLLDRGANAsFDKD--KQTIL-ITACSARGLEeqilKCVELLLSRN 139
Cdd:PHA03095 138 LLRKGADVNALDLYGMTPLaVLLKSRnANVELLRLLIDAGADV-YAVDdrFRSLLhHHLQSFKPRA----RIVRELIRAG 212

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  140 ADPNVACRRLMTPIMYAARDGHPQ--VVALLVAHGAEVNTQDENGYTALTWAARQGHKNVVLKLLELGANKMLQTKDGKI 217
Cdd:PHA03095 213 CDPAATDMLGNTPLHSMATGSSCKrsLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADINAVSSDGNT 292

                        170       180
                 ....*....|....*....|....
gi 90110652  218 PSEIAKRNKHLEIFN-FLSLTLNP 240
Cdd:PHA03095 293 PLSLMVRNNNGRAVRaALAKNPSA 316
Ank_4 pfam13637
Ankyrin repeats (many copies);
150-202 1.80e-11

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 59.21  E-value: 1.80e-11
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 90110652   150 MTPIMYAARDGHPQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNVVLKLL 202
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 41-218 1.47e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 63.06  E-value: 1.47e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   41 LPIEEKNETFKKALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASVANVELVRVLLDRGANASfdkdkqtILITACS 120
Cdd:PHA02874  30 ISVDETTTPLIDAIRSGDAKIVELFIKHGADINHINTKIPHPLLTAIKIGAHDIIKLLIDNGVDTS-------ILPIPCI 102

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  121 ARGLEEQILKCvelllsrNADPNVACRRLMTPIMYAARDGHPQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNVVLK 200
Cdd:PHA02874 103 EKDMIKTILDC-------GIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKL 175

                        170
                 ....*....|....*...
gi 90110652  201 LLELGANKMLQTKDGKIP 218
Cdd:PHA02874 176 LLEKGAYANVKDNNGESP 193
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 53-207 3.89e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.55  E-value: 3.89e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   53 ALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASVANVELVRVLLDRGA----------------------------- 103
Cdd:PHA02875   9 AILFGELDIARRLLDIGINPNFEIYDGISPIKLAMKFRDSEAIKLLMKHGAipdvkypdieselhdaveegdvkaveell 88

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  104 ------NASFDKDKQTILITACSARGLEeqILKcveLLLSRNADPNVACRRLMTPIMYAARDGHPQVVALLVAHGAEVNT 177
Cdd:PHA02875  89 dlgkfaDDVFYKDGMTPLHLATILKKLD--IMK---LLIARGADPDIPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDI 163

                        170       180       190
                 ....*....|....*....|....*....|
gi 90110652  178 QDENGYTALTWAARQGHKNVVLKLLELGAN 207
Cdd:PHA02875 164 EDCCGCTPLIIAMAKGDIAICKMLLDSGAN 193
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 53-207 5.04e-10

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 61.16  E-value: 5.04e-10
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   53 ALTTGDISLVQELLDSGISVDSSF-RYGWTPLMYAASVANVELVRVLLDRGANASF-DKDKQTILITACSARGLeeqilK 130
Cdd:PHA02875  75 AVEEGDVKAVEELLDLGKFADDVFyKDGMTPLHLATILKKLDIMKLLIARGADPDIpNTDKFSPLHLAVMMGDI-----K 149

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90110652  131 CVELLLSRNADPNVACRRLMTPIMYAARDGHPQVVALLVAHGAEVNTQDENG-YTALTWAARQGHKNVVLKLLELGAN 207
Cdd:PHA02875 150 GIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDYFGKNGcVAALCYAIENNKIDIVRLFIKRGAD 227
PHA03095 PHA03095
ankyrin-like protein; Provisional
 62-234 1.06e-09

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 60.42  E-value: 1.06e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   62 VQELLDSGISVDSSFRYGWTPLMYAASVANVE-LVRVLLDRGANASF-DKDKQTILITACSARGLEEQIlkcVELLLSRN 139
Cdd:PHA03095  66 VRLLLEAGADVNAPERCGFTPLHLYLYNATTLdVIKLLIKAGADVNAkDKVGRTPLHVYLSGFNINPKV---IRLLLRKG 142

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  140 ADPNVACRRLMTP--IMYAARDGHPQVVALLVAHGAEVNTQDENGYTALTWAARQGHKN--VVLKLLELGANKMLQTKDG 215
Cdd:PHA03095 143 ADVNALDLYGMTPlaVLLKSRNANVELLRLLIDAGADVYAVDDRFRSLLHHHLQSFKPRarIVRELIRAGCDPAATDMLG 222

                        170       180
                 ....*....|....*....|..
gi 90110652  216 KIPSEIAK---RNKHLEIFNFL 234
Cdd:PHA03095 223 NTPLHSMAtgsSCKRSLVLPLL 244
PHA02875 PHA02875
ankyrin repeat protein; Provisional
 41-154 2.33e-09

ankyrin repeat protein; Provisional


Pssm-ID: 165206 [Multi-domain]  Cd Length: 413  Bit Score: 59.23  E-value: 2.33e-09
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   41 LPIEEKNETFKKALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASVANVELVRVLLDRGANASFdKDKQTILITACS 120
Cdd:PHA02875 130 IPNTDKFSPLHLAVMMGDIKGIELLIDHKACLDIEDCCGCTPLIIAMAKGDIAICKMLLDSGANIDY-FGKNGCVAALCY 208

                         90       100       110
                 ....*....|....*....|....*....|....
gi 90110652  121 ArgLEEQILKCVELLLSRNADPNVacrrlMTPIM 154
Cdd:PHA02875 209 A--IENNKIDIVRLFIKRGADCNI-----MFMIE 235
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 43-207 1.11e-08

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 57.38  E-value: 1.11e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   43 IEEKNETFKKALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASVANV-ELVRVLLDRGA--NASFDKDKQTILITAC 119
Cdd:PHA02876 237 INKNDLSLLKAIRNEDLETSLLLYDAGFSVNSIDDCKNTPLHHASQAPSLsRLVPKLLERGAdvNAKNIKGETPLYLMAK 316

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  120 SARGLEEqilkcVELLLSRNADPNVACRRLMTPIMYAAR-DGHPQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNVV 198
Cdd:PHA02876 317 NGYDTEN-----IRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAAVRNNVVII 391


                 ....*....
gi 90110652  199 LKLLELGAN 207
Cdd:PHA02876 392 NTLLDYGAD 400
Ank_5 pfam13857
Ankyrin repeats (many copies);
134-186 2.59e-08

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 50.04  E-value: 2.59e-08
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 90110652   134 LLLSRNADPNVACRRLMTPIMYAARDGHPQVVALLVAHGAEVNTQDENGYTAL 186
Cdd:pfam13857   1 LLEHGPIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTAL 53
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 55-207 4.42e-08

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 55.64  E-value: 4.42e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   55 TTGDISLVQELLDSGISVDSSFRYGWTPLMYAASVANVELVRVLLDRGANASF-DKDKQTILITACSARglEEQILKcVE 133
Cdd:PLN03192 534 STGNAALLEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIrDANGNTALWNAISAK--HHKIFR-IL 610

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....
gi 90110652  134 LLLSRNADPNVACRRLMTpimyAARDGHPQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNVVLKLLELGAN 207
Cdd:PLN03192 611 YHFASISDPHAAGDLLCT----AAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLLIMNGAD 680
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 141-235 4.46e-08

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 55.67  E-value: 4.46e-08
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  141 DPNVAcRRLMTPIMYAARDGHPQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNVVLKLLELGANKMLQTKDGKIPSE 220
Cdd:PTZ00322  75 DPVVA-HMLTVELCQLAASGDAVGARILLTGGADPNCRDYDGRTPLHIACANGHVQVVRVLLEFGADPTLLDKDGKTPLE 153

                         90
                 ....*....|....*
gi 90110652  221 IAKRNKHLEIFNFLS 235
Cdd:PTZ00322 154 LAEENGFREVVQLLS 168
PHA03095 PHA03095
ankyrin-like protein; Provisional
 73-207 1.20e-07

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 53.88  E-value: 1.20e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   73 DSSFRYgwtpLMYAASVaNVELVRVLLDRGANASFDKDKQTILITACSARGLEeQILKCVELLLSRNADPNVACRRLMTP 152
Cdd:PHA03095  13 AALYDY----LLNASNV-TVEEVRRLLAAGADVNFRGEYGKTPLHLYLHYSSE-KVKDIVRLLLEAGADVNAPERCGFTP 86

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*...
gi 90110652  153 IMYAARDGH-PQVVALLVAHGAEVNTQDENGYTAL-TWAARQG-HKNVVLKLLELGAN 207
Cdd:PHA03095  87 LHLYLYNATtLDVIKLLIKAGADVNAKDKVGRTPLhVYLSGFNiNPKVIRLLLRKGAD 144
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 56-234 1.86e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 53.43  E-value: 1.86e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   56 TGDISLVQELLDS-----GISVDSSFrygwTPLMYAASVANVELVRVLLDRGANASFDKDK-QTILITACSARGLeeqil 129
Cdd:PHA02874  11 SGDIEAIEKIIKNkgnciNISVDETT----TPLIDAIRSGDAKIVELFIKHGADINHINTKiPHPLLTAIKIGAH----- 81

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  130 KCVELLLSRNADPNVacrrLMTPimyaarDGHPQVVALLVAHGAEVNTQDENGYTALTWAARQGHKNVVLKLLELGANKM 209
Cdd:PHA02874  82 DIIKLLIDNGVDTSI----LPIP------CIEKDMIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVN 151

                        170       180
                 ....*....|....*....|....*
gi 90110652  210 LQTKDGKIPSEIAKRNKHLEIFNFL 234
Cdd:PHA02874 152 IEDDNGCYPIHIAIKHNFFDIIKLL 176
Ank_5 pfam13857
Ankyrin repeats (many copies);
168-222 5.73e-07

Ankyrin repeats (many copies);


Pssm-ID: 433530 [Multi-domain]  Cd Length: 56  Bit Score: 46.19  E-value: 5.73e-07
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 90110652   168 LVAHG-AEVNTQDENGYTALTWAARQGHKNVVLKLLELGANKMLQTKDGKIPSEIA 222
Cdd:pfam13857   1 LLEHGpIDLNRLDGEGYTPLHVAAKYGALEIVRVLLAYGVDLNLKDEEGLTALDLA 56
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 45-234 5.98e-07

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 51.99  E-value: 5.98e-07
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   45 EKNETFKKALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASVANVELVRVLLDRGANASF--------------DKD 110
Cdd:PHA02876 144 EYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIialddlsvlecavdSKN 223

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  111 KQTI----------------LITACSARGLEEQIL-----------------------------KCVELLLSRNADPNVA 145
Cdd:PHA02876 224 IDTIkaiidnrsninkndlsLLKAIRNEDLETSLLlydagfsvnsiddckntplhhasqapslsRLVPKLLERGADVNAK 303

                        170       180       190       200       210       220       230       240
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  146 CRRLMTPIMYAARDGH-PQVVALLVAHGAEVNTQDENGYTALTWAAR-QGHKNVVLKLLELGANKMLQTKDGKIPSEIAK 223
Cdd:PHA02876 304 NIKGETPLYLMAKNGYdTENIRTLIMLGADVNAADRLYITPLHQASTlDRNKDIVITLLELGANVNARDYCDKTPIHYAA 383

                        250
                 ....*....|.
gi 90110652  224 RNKHLEIFNFL 234
Cdd:PHA02876 384 VRNNVVIINTL 394
SAM_superfamily cd09487
SAM (Sterile alpha motif ); SAM (Sterile Alpha Motif) domain is a module consisting of ...
 278-332 7.36e-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: 46.08  E-value: 7.36e-07
                        10        20        30        40        50
                ....*....|....*....|....*....|....*....|....*....|....*.
gi 90110652 278 DLEIFLHGLGLEHMTDLLKEKDITLRHLLTMRKDEFTKNGINDK-DQQKILSALKE 332
Cdd:cd09487   1 DVAEWLESLGLEQYADLFRKNEIDGDALLLLTDEDLKELGITSPgHRKKILRAIQR 56
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 61-218 1.68e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 50.35  E-value: 1.68e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   61 LVQELLDSGISVDSSFRYGWTPLMYAASVANVELVRVLLDRGANASFDKDKQTILITACSARGLEEQIlkcvELLLSRNA 140
Cdd:PHA02874 106 MIKTILDCGIDVNIKDAELKTFLHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDII----KLLLEKGA 181

                         90       100       110       120       130       140       150
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 90110652  141 DPNVACRRLMTPIMYAARDGHPQVVALLVAHGAEVNTQDENGYTALTWAARqgHKNVVLKLLELGANKMLQTKDGKIP 218
Cdd:PHA02874 182 YANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTP 257
PLN03192 PLN03192
Voltage-dependent potassium channel; Provisional
 132-234 2.52e-06

Voltage-dependent potassium channel; Provisional


Pssm-ID: 215625 [Multi-domain]  Cd Length: 823  Bit Score: 50.25  E-value: 2.52e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  132 VELLLSRNADPNVACRRLMTPIMYAARDGHPQVVALLVAHGAEVNTQDENGYTALtW----------------------- 188
Cdd:PLN03192 541 LEELLKAKLDPDIGDSKGRTPLHIAASKGYEDCVLVLLKHACNVHIRDANGNTAL-Wnaisakhhkifrilyhfasisdp 619

                         90       100       110       120       130
                 ....*....|....*....|....*....|....*....|....*....|....*
gi 90110652  189 ---------AARQGHKNVVLKLLELGANKMLQTKDGKIPSEIAKRNKHLEIFNFL 234
Cdd:PLN03192 620 haagdllctAAKRNDLTAMKELLKQGLNVDSEDHQGATALQVAMAEDHVDMVRLL 674
SAM_2 pfam07647
SAM domain (Sterile alpha motif);
272-334 3.41e-06

SAM domain (Sterile alpha motif);


Pssm-ID: 429573  Cd Length: 66  Bit Score: 44.57  E-value: 3.41e-06
                          10        20        30        40        50        60
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90110652   272 SYTAFGDLEIFLHGLGLEHMTDLLKEKDIT-LRHLLTMRKDEFTKNGINDK-DQQKILSALKELE 334
Cdd:pfam07647   2 ESWSLESVADWLRSIGLEQYTDNFRDQGITgAELLLRLTLEDLKRLGITSVgHRRKILKKIQELK 66
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 61-199 3.66e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 49.68  E-value: 3.66e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   61 LVQELLDSGISVDSSFRYGWTPLMYAASVANVELVRVLLDRGAN-ASFDKDKQTILITACSArgleEQILKCVELLLSRN 139
Cdd:PHA02876 357 IVITLLELGANVNARDYCDKTPIHYAAVRNNVVIINTLLDYGADiEALSQKIGTALHFALCG----TNPYMSVKTLIDRG 432

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 90110652  140 ADPNVACRRLMTPIMYAARDG-HPQVVALLVAHGAEVNTQD-ENGYTALTWAARQGHKNVVL 199
Cdd:PHA02876 433 ANVNSKNKDLSTPLHYACKKNcKLDVIEMLLDNGADVNAINiQNQYPLLIALEYHGIVNILL 494
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 46-222 5.99e-06

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 48.42  E-value: 5.99e-06
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   46 KNETF-KKALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASVANVELVRVLLDRGANASF-DKDKQTILITAcsarg 123
Cdd:PHA02874 123 ELKTFlHYAIKKGDLESIKMLFEYGADVNIEDDNGCYPIHIAIKHNFFDIIKLLLEKGAYANVkDNNGESPLHNA----- 197

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  124 LEEQILKCVELLLSRNADPNVACRRLMTPIMYAARdgHPQVVALLVAHGAEVNTQDENGYTALTWAARQG-HKNVVLKLL 202
Cdd:PHA02874 198 AEYGDYACIKLLIDHGNHIMNKCKNGFTPLHNAII--HNRSAIELLINNASINDQDIDGSTPLHHAINPPcDIDIIDILL 275

                        170       180
                 ....*....|....*....|
gi 90110652  203 ELGANKMLQTKDGKIPSEIA 222
Cdd:PHA02874 276 YHKADISIKDNKGENPIDTA 295
Ank_4 pfam13637
Ankyrin repeats (many copies);
47-99 6.67e-06

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 43.42  E-value: 6.67e-06
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 90110652    47 NETFKKALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASVANVELVRVLL 99
Cdd:pfam13637   2 LTALHAAAASGHLELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
PHA02876 PHA02876
ankyrin repeat protein; Provisional
 102-207 1.15e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165207 [Multi-domain]  Cd Length: 682  Bit Score: 47.75  E-value: 1.15e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  102 GANASFDKDKQTILITACSARGLEEQILKCVELLLSRNADPNVACRRLMTPIMYAARDGHPQVVALLVAHGAEVNTQDEN 181
Cdd:PHA02876 131 GNDIHYDKINESIEYMKLIKERIQQDELLIAEMLLEGGADVNAKDIYCITPIHYAAERGNAKMVNLLLSYGADVNIIALD 210

                         90       100
                 ....*....|....*....|....*.
gi 90110652  182 GYTALTWAARQGHKNVVLKLLELGAN 207
Cdd:PHA02876 211 DLSVLECAVDSKNIDTIKAIIDNRSN 236
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 50-222 2.92e-05

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 46.41  E-value: 2.92e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   50 FKKALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASVANVELVRVLL-----------DRGANASFD---------- 108
Cdd:PHA02878  41 LHQAVEARNLDVVKSLLTRGHNVNQPDHRDLTPLHIICKEPNKLGMKEMIrsinkcsvfytLVAIKDAFNnrnveifkii 120

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  109 -----KDKQTILITACSARGLEEQI-LKCVELLLSRNADPNVACR-RLMTPIMYAARDGHPQVVALLVAHGAEVNTQDEN 181
Cdd:PHA02878 121 ltnryKNIQTIDLVYIDKKSKDDIIeAEITKLLLSYGADINMKDRhKGNTALHYATENKDQRLTELLLSYGANVNIPDKT 200

                        170       180       190       200
                 ....*....|....*....|....*....|....*....|.
gi 90110652  182 GYTALTWAARQGHKNVVLKLLELGANKMLQTKDGKIPSEIA 222
Cdd:PHA02878 201 NNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHIS 241
TRPV5-6 cd22192
Transient Receptor Potential channel, Vanilloid subfamily (TRPV), types 5 and 6; TRPV5 and ...
 53-169 3.73e-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: 46.16  E-value: 3.73e-05
                        10        20        30        40        50        60        70        80
                ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  53 ALTTGDISLVQELLDSGISVDSS------FR--------YGWTPLMYAASVANVELVRVLLDRGANA----SFDKDKQTI 114
Cdd:cd22192  96 AVVNQNLNLVRELIARGADVVSPratgtfFRpgpknliyYGEHPLSFAACVGNEEIVRLLIEHGADIraqdSLGNTVLHI 175

                        90       100       110       120       130       140
                ....*....|....*....|....*....|....*....|....*....|....*....|...
gi 90110652 115 LITACSargleeQILKC--VELLLSRNADPNVAC------RRLMTPIMYAARDGHPQVVALLV 169
Cdd:cd22192 176 LVLQPN------KTFACqmYDLILSYDKEDDLQPldlvpnNQGLTPFKLAAKEGNIVMFQHLV 232
PHA02874 PHA02874
ankyrin repeat protein; Provisional
 61-218 4.33e-05

ankyrin repeat protein; Provisional


Pssm-ID: 165205 [Multi-domain]  Cd Length: 434  Bit Score: 45.72  E-value: 4.33e-05
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   61 LVQELLDSGISVDSSFRYGWTPLMYAASVANVELVRVLLDRGANASFD-KDKQTILITAcsargleeqIL---KCVELLL 136
Cdd:PHA02874 172 IIKLLLEKGAYANVKDNNGESPLHNAAEYGDYACIKLLIDHGNHIMNKcKNGFTPLHNA---------IIhnrSAIELLI 242

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  137 SrNADPNVACRRLMTPIMYAARdgHP---QVVALLVAHGAEVNTQDENGYTALTWAARQGHKNVVLKllELGANKMLQTK 213
Cdd:PHA02874 243 N-NASINDQDIDGSTPLHHAIN--PPcdiDIIDILLYHKADISIKDNKGENPIDTAFKYINKDPVIK--DIIANAVLIKE 317


                 ....*
gi 90110652  214 DGKIP 218
Cdd:PHA02874 318 ADKLK 322
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 78-104 1.07e-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: 39.11  E-value: 1.07e-04
                           10        20
                   ....*....|....*....|....*..
gi 90110652     78 YGWTPLMYAASVANVELVRVLLDRGAN 104
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 78-104 1.22e-04

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


Pssm-ID: 463933 [Multi-domain]  Cd Length: 30  Bit Score: 39.16  E-value: 1.22e-04
                          10        20
                  ....*....|....*....|....*..
gi 90110652    78 YGWTPLMYAASVANVELVRVLLDRGAN 104
Cdd:pfam13606   1 DGNTPLHLAARNGRLEIVKLLLENGAD 27
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 47-158 2.88e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 43.33  E-value: 2.88e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   47 NETFKKALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAAS-VANVELVRVLLDRGANASFdkdKQTIL-ITACSARGL 124
Cdd:PHA02878 202 NSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGyCKDYDILKLLLEHGVDVNA---KSYILgLTALHSSIK 278

                         90       100       110
                 ....*....|....*....|....*....|....
gi 90110652  125 EEQILKcveLLLSRNADPNVACRRLMTPIMYAAR 158
Cdd:PHA02878 279 SERKLK---LLLEYGADINSLNSYKLTPLSSAVK 309
SAM_1 pfam00536
SAM domain (Sterile alpha motif); It has been suggested that SAM is an evolutionarily ...
 282-333 3.99e-04

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


Pssm-ID: 425739  Cd Length: 64  Bit Score: 38.40  E-value: 3.99e-04
                          10        20        30        40        50
                  ....*....|....*....|....*....|....*....|....*....|...
gi 90110652   282 FLHGLGLEHMTDLLKEKDITLRHLLTMRKDEFTKNGINDK-DQQKILSALKEL 333
Cdd:pfam00536  11 WLESIGLGQYIDSFRAGYIDGDALLQLTEDDLLKLGVTLLgHRKKILYAIQRL 63
PHA03095 PHA03095
ankyrin-like protein; Provisional
 60-173 4.43e-04

ankyrin-like protein; Provisional


Pssm-ID: 222980 [Multi-domain]  Cd Length: 471  Bit Score: 42.70  E-value: 4.43e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   60 SLVQELLDSGISVDSSFRYGWTPLMYAASVANVELVRVLLDRGANASfdkdkqtiLITACSARGLEEQILKC----VELL 135
Cdd:PHA03095 238 SLVLPLLIAGISINARNRYGQTPLHYAAVFNNPRACRRLIALGADIN--------AVSSDGNTPLSLMVRNNngraVRAA 309

                         90       100       110       120
                 ....*....|....*....|....*....|....*....|.
gi 90110652  136 LSRNADPNVACR---RLMTPIMYAARDGHPQVVALLVAHGA 173
Cdd:PHA03095 310 LAKNPSAETVAAtlnTASVAGGDIPSDATRLCVAKVVLRGA 350
PHA02878 PHA02878
ankyrin repeat protein; Provisional
 53-192 4.49e-04

ankyrin repeat protein; Provisional


Pssm-ID: 222939 [Multi-domain]  Cd Length: 477  Bit Score: 42.56  E-value: 4.49e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   53 ALTTGDISLVQELLDSGISVDSSFRYGWTPLMYAASVANVELVRVLLDRGANASFDKDKQTILITACSARGLEEQILKcv 132
Cdd:PHA02878 175 ATENKDQRLTELLLSYGANVNIPDKTNNSPLHHAVKHYNKPIVHILLENGASTDARDKCGNTPLHISVGYCKDYDILK-- 252

                         90       100       110       120       130       140
                 ....*....|....*....|....*....|....*....|....*....|....*....|.
gi 90110652  133 eLLLSRNADPNVACRRL-MTPIMYAARDghPQVVALLVAHGAEVNTQDENGYTALTWAARQ 192
Cdd:PHA02878 253 -LLLEHGVDVNAKSYILgLTALHSSIKS--ERKLKLLLEYGADINSLNSYKLTPLSSAVKQ 310
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 150-180 4.72e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 37.65  E-value: 4.72e-04
                          10        20        30
                  ....*....|....*....|....*....|..
gi 90110652   150 MTPIMYAA-RDGHPQVVALLVAHGAEVNTQDE 180
Cdd:pfam00023   3 NTPLHLAAgRRGNLEIVKLLLSKGADVNARDK 34
PTZ00322 PTZ00322
6-phosphofructo-2-kinase/fructose-2,6-biphosphatase; Provisional
 95-182 7.61e-04

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


Pssm-ID: 140343 [Multi-domain]  Cd Length: 664  Bit Score: 42.19  E-value: 7.61e-04
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   95 VRVLLDRGANA-SFDKDKQTILITACsARGLeeqiLKCVELLLSRNADPNVACRRLMTPIMYAARDGHPQVVALLVAHGA 173
Cdd:PTZ00322  98 ARILLTGGADPnCRDYDGRTPLHIAC-ANGH----VQVVRVLLEFGADPTLLDKDGKTPLELAEENGFREVVQLLSRHSQ 172


                 ....*....
gi 90110652  174 EVNTQDENG 182
Cdd:PTZ00322 173 CHFELGANA 181
Ank pfam00023
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 78-104 7.87e-04

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


Pssm-ID: 459634 [Multi-domain]  Cd Length: 34  Bit Score: 36.88  E-value: 7.87e-04
                          10        20
                  ....*....|....*....|....*...
gi 90110652    78 YGWTPLMYAA-SVANVELVRVLLDRGAN 104
Cdd:pfam00023   1 DGNTPLHLAAgRRGNLEIVKLLLSKGAD 28
Ank_4 pfam13637
Ankyrin repeats (many copies);
129-169 1.38e-03

Ankyrin repeats (many copies);


Pssm-ID: 372654 [Multi-domain]  Cd Length: 54  Bit Score: 36.87  E-value: 1.38e-03
                          10        20        30        40
                  ....*....|....*....|....*....|....*....|.
gi 90110652   129 LKCVELLLSRNADPNVACRRLMTPIMYAARDGHPQVVALLV 169
Cdd:pfam13637  14 LELLRLLLEKGADINAVDGNGETALHFAASNGNVEVLKLLL 54
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 181-207 1.61e-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: 1.61e-03
                           10        20
                   ....*....|....*....|....*..
gi 90110652    181 NGYTALTWAARQGHKNVVLKLLELGAN 207
Cdd:smart00248   1 DGRTPLHLAAENGNLEVVKLLLDKGAD 27
ANK smart00248
ankyrin repeats; Ankyrin repeats are about 33 amino acids long and occur in at least four ...
 150-176 2.41e-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: 2.41e-03
                           10        20
                   ....*....|....*....|....*..
gi 90110652    150 MTPIMYAARDGHPQVVALLVAHGAEVN 176
Cdd:smart00248   3 RTPLHLAAENGNLEVVKLLLDKGADIN 29
Ank_3 pfam13606
Ankyrin repeat; Ankyrins are multifunctional adaptors that link specific proteins to the ...
 150-177 3.54e-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: 34.93  E-value: 3.54e-03
                          10        20
                  ....*....|....*....|....*...
gi 90110652   150 MTPIMYAARDGHPQVVALLVAHGAEVNT 177
Cdd:pfam13606   3 NTPLHLAARNGRLEIVKLLLENGADINA 30
PHA02946 PHA02946
ankyin-like protein; Provisional
 114-188 4.26e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 39.27  E-value: 4.26e-03
                         10        20        30        40        50        60        70
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 90110652  114 ILITACSARGLEEQIlkcVELLLSRNADPNVACRRLMTPIMYAARDGHPQVVALLVAHGAEVNTQDENGYTALTW 188
Cdd:PHA02946  40 ILHAYCGIKGLDERF---VEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPNACDKQHKTPLYY 111
PHA02946 PHA02946
ankyin-like protein; Provisional
 58-262 8.62e-03

ankyin-like protein; Provisional


Pssm-ID: 165256 [Multi-domain]  Cd Length: 446  Bit Score: 38.50  E-value: 8.62e-03
                         10        20        30        40        50        60        70        80
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652   58 DISLVQELLDSGISVDSSFRYGWTPLMYAASVANVELVRVLLDRGANA-SFDKDKQTILITacsARGLEEQILKCVELLL 136
Cdd:PHA02946  51 DERFVEELLHRGYSPNETDDDGNYPLHIASKINNNRIVAMLLTHGADPnACDKQHKTPLYY---LSGTDDEVIERINLLV 127

                         90       100       110       120       130       140       150       160
                 ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  137 SRNADPNVACRRLMTPIMYAARDGHPQVVALLVAHGAEVNTQDENGYTAL--TWAARQGHKNVVLKLLELGANKMLQTKD 214
Cdd:PHA02946 128 QYGAKINNSVDEEGCGPLLACTDPSERVFKKIMSIGFEARIVDKFGKNHIhrHLMSDNPKASTISWMMKLGISPSKPDHD 207

                        170       180       190       200       210       220
                 ....*....|....*....|....*....|....*....|....*....|....*....|
gi 90110652  215 GKIPSEI--AKRNKHLEIFNFL--SLTLN--------PLEGNLQQLTKEETICKLLTTES 262
Cdd:PHA02946 208 GNTPLHIvcSKTVKNVDIINLLlpSTDVNkqnkfgdsPLTLLIKTLSPAHLINKLLSTSN 267
 
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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